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Synthyra 5

A1BJF4

MPTLKDIRVRIKGVKSTQQVTKAMKMVAAAKLRRAQERAIMARPYARKLKEMLGSLSDKVDTSLNPLLSNRSEVNKVVVILITADRGLCGAFNTNIVKLAYKLIHEDYAAQHSKNGVSLICAGSRGFDFFRKRGYNIIKGYPGVFQRLDFSFAKEIAETVSGMYLRGEADRVVVVYNEFKSVLAPVLKFETLLPITPEASGKDGGSDYIYEPSPESIIDVLVPKHLNTQVWRVMLESNAAEQAARMSAMDSATENAKELLRTLNISYNRARQAAITKELSEIVGGADALKG

Function: Produces ATP from ADP in the presence of a proton gradient across the membrane. The gamma chain is believed to be important in regulating ATPase activity and the flow of protons through the CF(0) complex. Location Topology: Peripheral membrane protein Sequence Mass (Da): 32175 Sequence Length: 291 Subcellular Location: Cell inner membrane

Q8KAW9

MPTLKDIRIRLKGVKSTQQVTKAMKMVAAAKLRRAQDRAIQARPYAGKLKEMLASLSTKVDTSVNPLLSPREEVNNVLVILVTSDRGLCGGFNANIIKMAQRLIHEEYAALHAKGGVTMICAGTKGTEFFRKRGYKLAAAYPGVFQNLSFDSAREIADKASKMYLSGEVDRVVLVYNEFKSVLAPNLRTEQLLPITPEGGDAKTASSEYLYEPSPAAIIDELVPKHLNTQLWRVMLESNAAEQAARMAAMDSATENAKELIRVLNISYNRARQAAITKELSEIVAGADALKQ

Function: Produces ATP from ADP in the presence of a proton gradient across the membrane. The gamma chain is believed to be important in regulating ATPase activity and the flow of protons through the CF(0) complex. Location Topology: Peripheral membrane protein Sequence Mass (Da): 32053 Sequence Length: 292 Subcellular Location: Cell inner membrane

A0M6G3

MANLKELRSRITSVSSTMQITKAMKMVSASKLSKAQDAITQMRPYSEKLTQLLQDLSATLDDDAGSKYAEEREVKNVLIVAISSNKGLAGAFNTNIIKAVKYKAKNDYKAKNIDIYTVGKKANDILKKEYDIHKNNNEIYDDLSFENASAIAEELMQLFLDEKYDKIVLVYNQFKNAATQIVQHEQFLPIEQFDSEENKQLDYIFEPSKLEIVKDLIPKSLKMQLFKALRDSFASEHGARMTAMHKATENATELRDDLKLSYNKARQASITNEILEIVGGAEALNG

Function: Produces ATP from ADP in the presence of a proton gradient across the membrane. The gamma chain is believed to be important in regulating ATPase activity and the flow of protons through the CF(0) complex. Location Topology: Peripheral membrane protein Sequence Mass (Da): 32304 Sequence Length: 286 Subcellular Location: Cell inner membrane

Q7VJ22

MGGNLKNIKRQISSTKNTQKTTKAMKLVSSSKLKKAEELARRSKVYAKQLSAVFHDVVAKIRVRGLDNINSRYFAKSEGREIKKLDIIFITADKGLCGGFNITTIKEVLRLMETYKQQGIKVRLRGIGKTGISFFAFNDIEVLDKAIGLSAAPTFEKAEAFIENVVEDFLNGATDEVIIVHNGFKNMISQELESQAILPLTINIKQNEQPSVLNIEPEDEENIILDELAKKYVQYNMYYALVDSLAAEHSARIQAMDAATNNAGDLVKSLTISLNKARQEAITTELVEINAGAEAIK

Function: Produces ATP from ADP in the presence of a proton gradient across the membrane. The gamma chain is believed to be important in regulating ATPase activity and the flow of protons through the CF(0) complex. Location Topology: Peripheral membrane protein Sequence Mass (Da): 32956 Sequence Length: 297 Subcellular Location: Cell inner membrane

P36542

MFSRAGVAGLSAWTLQPQWIQVRNMATLKDITRRLKSIKNIQKITKSMKMVAAAKYARAERELKPARIYGLGSLALYEKADIKGPEDKKKHLLIGVSSDRGLCGAIHSSIAKQMKSEVATLTAAGKEVMLVGIGDKIRGILYRTHSDQFLVAFKEVGRKPPTFGDASVIALELLNSGYEFDEGSIIFNKFRSVISYKTEEKPIFSLNTVASADSMSIYDDIDADVLQNYQEYNLANIIYYSLKESTTSEQSARMTAMDNASKNASEMIDKLTLTFNRTRQAVITKELIEIISGAAALD

Function: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(1) domain and the central stalk which is part of the complex rotary element. The gamma subunit protrudes into the catalytic domain formed of alpha(3)beta(3). Rotation of the central stalk against the surrounding alpha(3)beta(3) subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits. Location Topology: Peripheral membrane protein Sequence Mass (Da): 32996 Sequence Length: 298 Subcellular Location: Mitochondrion inner membrane

B4U6A3

MPKLSPRDIKSKIAGIKNTMRITNAMKVVSAAKLRKAQEAIFKARPYSDKLYELMAHLFAHIDTYSHPLFKRRELKNVDLVIISADRGLAGAFNTNLFKKVDSYLKSCPSQRINLHIVGKKANQYYSKRSYHIVSSYQDVFKKEINFDIVKELGAKLISRYKEEETDHIVLFNNEMITKATYAPKERRFLPITYEDVHIQEPKLDHNTIYNIEGNETDILDGIISIYMNYQLYRAMLESNAAEHFARMVAMDNATRNASDLIKKWTLIFNKARQESITAELIDIVTAAEAMD

Function: Produces ATP from ADP in the presence of a proton gradient across the membrane. The gamma chain is believed to be important in regulating ATPase activity and the flow of protons through the CF(0) complex. Location Topology: Peripheral membrane protein Sequence Mass (Da): 33691 Sequence Length: 292 Subcellular Location: Cell inner membrane

Q7UFB6

MANARALDKRRKSIRNIRKITRTMELIATARYKKAMDRAAAATAYTEQITKIVSRLADAGLDVQHPLLEQREKINTTRVLVLASNRGLCGGYNASILRTALPRIKSLRESIPNVIVDASGKRGVNGLKFRGIETEQRFLQFEDQPAYDDVEKIAEGYLAEYITGKIDRLDVVYTKFISTSKQEAVIETLLPLGSLGDESDSASDGSDDTNAEYEFLPSAESILEEVVPTSFKVKLFKCFLDAAVSEQVARMIAMKGATESAGDMIKQLSMTYNRARQSQITGEIMEIIGGVEALEG

Function: Produces ATP from ADP in the presence of a proton gradient across the membrane. The gamma chain is believed to be important in regulating ATPase activity and the flow of protons through the CF(0) complex. Location Topology: Peripheral membrane protein Sequence Mass (Da): 32680 Sequence Length: 296 Subcellular Location: Cell inner membrane

P72246

MPSLKDLKNRIVSVKNTRKITKAMQMVAAANIRRAQESAEAARPYAERMNAVMSSLAGAVGSTDGAPRLLAGTGSDKVHLLVIMTGERGLCGGFNANIAKLAKAKAMELLAQGKTVKILTVGKKGRDALRRDLGQYYIDHIDLSDVKKLSYPVAQKISQNIIDRFEAGEYDVATIFFSVFQSVISQVPTAKQVIPAQFETDAASASAVYDYEPGDQEILTALLPRAVATAIFAALLENNASFNGAQMSAMDNATRNAGDMIDRLTIEYNRSRQAAITKELIEIISGAEAL

Function: Produces ATP from ADP in the presence of a proton gradient across the membrane. The gamma chain is believed to be important in regulating ATPase activity and the flow of protons through the CF(0) complex. Location Topology: Peripheral membrane protein Sequence Mass (Da): 31243 Sequence Length: 290 Subcellular Location: Cellular chromatophore membrane

Q92G87

MSNLKQLRTRIKSVKSTQKITKAMQLVSASKMAKIKSQIANSNFYIEAVSKMMSAILSIDMYELSIEEQKFFNTVPNKANLLIVMTSQRGLCGTFNYSIIKQVKNDIKELENKGEQIKLIIIGKKGYEALKRQYVNYIDSYFELPKIHDENLMLQVKQKIMSAVENLEVSNCVIYFNKFKNAMTQIMTRQQILPVAKYQDDSMIDNPIVNLVGFGYKERGVKPINNRRATSDIVGESKSIDYNYEYEGESLISNLINLYVNSQINYALLQSRASEEGARMTAMENATNNANDLISKLVLKLNRSRQAIITTELIEIIAGSEVV

Function: Produces ATP from ADP in the presence of a proton gradient across the membrane. The gamma chain is believed to be important in regulating ATPase activity and the flow of protons through the CF(0) complex. Location Topology: Peripheral membrane protein Sequence Mass (Da): 36735 Sequence Length: 323 Subcellular Location: Cell inner membrane

Q70Y12

MNPLISAASVIAAGLAVGLASIGPGVGQGTAAGQAVEGIARQPEAEGKIRGTLLLSLAFMEALTIYGLVVALALLFANPFV

Function: F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Location Topology: Multi-pass membrane protein Sequence Mass (Da): 7990 Sequence Length: 81 Subcellular Location: Plastid

B0YPM3

MNPLIPAASVIAAGLAVGLASIGPGIGQGTAAGQAVEGIARQPEAEGKIRGTLLSSPASMEALTIYGLVVALALSFANPFI

Function: F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Location Topology: Multi-pass membrane protein Sequence Mass (Da): 7900 Sequence Length: 81 Subcellular Location: Plastid membrane

Q40607

MFFSLAAVEVGTHLYWEIGGLEVHGQVLLITWLVLAIILTLAILGTLKLEQVPKGVQNFLESVFEYVSGIAKDQIGEYHYRPWVPFVGTLFLFIFVANWLGALIPWKLIHLPEGELAAPTNDINTTVALSLLTSISYFYAGFKEKGLGFFARYISPTPIFLPINILEDFTKPLSLSFRLFGNILADEIVVSVLCLLVPLLIPLPVMVLGIFASSVQALVFSTLSAAYIGESIE

Function: Key component of the proton channel; it plays a direct role in the translocation of protons across the membrane. Location Topology: Multi-pass membrane protein Sequence Mass (Da): 25721 Sequence Length: 233 Subcellular Location: Plastid

A0A084R1K7

MALEEISERLQVSDFPTLGMAANYDLRRHKFESLANDGSHEMRADVRRWVGNPSDFGGCNPINGHIIALTMPMIKPDRVKIAGYIYECWFLYSWDLTTTLTGADGFFHDDILEGTNEGVSDTDAFGLGTADQDAKARDGRKQIQAKMMYLLETTDKACAKHLQKVWSNMLVTTIQHKSRDFETLKEYIDFRIRDCGALFGEGVMLFGMGLALTEKDREDVASTIYPCYAALGLTNDYFSFDREWEEAKRTGEAKFSNAVRLFMDWQSTGAAAAKEVVRKAIIEYEREFLELREKFVKANPKAERLHKFLEAMVYQISGHVVWSINCPRYNPSFRYDPNSGVENQVLAERRGKSSSKKPSVMIEEIDEKSHLASETGPAMIA

Function: Terpene cyclase; part of the core atranone cluster (CAC) which products are predicted to catalyze most or all steps of mycotoxin atranone synthesis, starting from geranylgeranyl pyrophosphate (GGPP) . The initial cyclization of GGPP to dolabellane is probably performed by the terpene cyclase ATR13 . The Baeyer-Villiger oxidation near the end of the atranone synthesis, which converts atranones D and E to atranones F and G is predicted to be catalyzed by the monooxygenase ATR8 . Of the CAC's other predicted gene products, the reducing PKS ATR6 might synthesize a polyketide chain . This polyketide is probably transferred onto the atranone backbone by the polyketide transferase ATR5 (By similarity). Other predicted CAC products include 4 oxygenases (ATR2, ATR3, ATR4, and ATR14), 3 short-chain reductases (ATR7, ATR9, and ATR10), and a methyltransferase (ATR12) . These may all be involved in the various steps of atranone biosynthesis, although their specific roles must await experimental determination . Sequence Mass (Da): 43218 Sequence Length: 381 Pathway: Mycotoxin biosynthesis. EC: 4.2.3.-

A0A084R1J2

MNVADIAMDLFRGAKGETISIFAIAKVTVTGVSRGLSKLVFGVVDQANLVNLGQYVVYSVVSMIYNITLHPLASFPGPVFWGASRWPSIWRLFKGRLVHDVHALHGQYGHVVRIAPNELAFSSAQAWKDIYGHKRGNNSMEEMPKFHKFYSGISKTPSIVSEPTRDGHRFIRRILSPAFSDKNLRELEPIVQGYISQFIDQLRSHCEDSTGSKVPLDLVSWYNSATFDIVGDLTFGRPFGSLEQGEEDPFIKDINHFAAVGGAMLIFTSHFPGRGILRFLASLGKVFQNGQEKHVTKMEESLVDRMKNKSSRPDIIDGLVKEKDGFQIDYDRVLENAAAITMAGSETTASQLSGLTALLLQNPNCLERLKKEVRSAFKSDKDITSTSSLVGVWQYSANHSPRNFTYPDEFRPDRWLDDRDQKEYEHDHGDAMQPFSVGPRDCPSQK

Function: Cytochrome P450 monooxygenase; part of the core atranone cluster (CAC) which products are predicted to catalyze most or all steps of mycotoxin atranone synthesis, starting from geranylgeranyl pyrophosphate (GGPP) . The initial cyclization of GGPP to dolabellane is probably performed by the terpene cyclase ATR13 . The Baeyer-Villiger oxidation near the end of the atranone synthesis, which converts atranones D and E to atranones F and G is predicted to be catalyzed by the monooxygenase ATR8 . Of the CAC's other predicted gene products, the reducing PKS ATR6 might synthesize a polyketide chain . This polyketide is probably transferred onto the atranone backbone by the polyketide transferase ATR5 (By similarity). Other predicted CAC products include 4 oxygenases (ATR2, ATR3, ATR4, and ATR14), 3 short-chain reductases (ATR7, ATR9, and ATR10), and a methyltransferase (ATR12) . These may all be involved in the various steps of atranone biosynthesis, although their specific roles must await experimental determination . Sequence Mass (Da): 49993 Sequence Length: 446 Pathway: Mycotoxin biosynthesis. EC: 1.-.-.-

M4B6G6

MRVCYFVLVPSVALAVIATESSETSGTIVHVFPLRDVADHRNDALINRALRAQTALDDDEERWPFGPSAVEALIETIDRHGRVSLNDEAKMKKVVRTWKKLIERDDLIGEIGKHYFEAPGPLHDTYDEALATRLVTTYSDRGVARAILHTRPSDPLSKKAGQAHRLEEAVASLWKGRGYTSDNVVSSIATGHDVDFFAPTAFTFLVKCVESEDDANNAIFEYFGSNPSRYFSAVLHAMEKPDADSRVLESSKKWMFQCYAQKQFPTPVFERTLAAYQSEDYAIRGARNHYEKLSLSQIEELVEEYSRIYSV

Function: Secreted effector that acts as an elicitor of hypersensitive response (HR) specifically on plants carrying both defense protein RPP1 from several ecotypes including RPP1-NdA, RPP1-WsB, RPP1-EstA and RPP1-ZdrA. Sequence Mass (Da): 35102 Sequence Length: 311 Domain: The RxLR-dEER motif acts to carry the protein into the host cell cytoplasm through binding to cell surface phosphatidylinositol-3-phosphate (PIP). However ATR1 does not bind to PIPs, even though it harbors the RxLR-dEER motif at the N-terminus, suggesting that the RxLR-dEER motif is insufficient for PIP binding. Subcellular Location: Secreted

P13090

MGNQSLVVLTESKGEYENETELPVKKSSRDNNIGESLTATAFTQSEDEMVDSNQKWQNPNYFKYAWQEYLFIFTCMISQLLNQAGTTQTLSIMNILSDSFGSEGNSKSWLMASFPLVSGSFILISGRLGDIYGLKKMLLVGYVLVIIWSLICGITKYSGSDTFFIISRAFQGLGIAFVLPNVLGIIGNIYVGGTFRKNIVISFVGAMAPIGATLGCLFAGLIGTEDPKQWPWAFYAYSIAAFINFVLSIYAIPSTIPTNIHHFSMDWIGSVLGVIGLILLNFVWNQAPISGWNQAYIIVILIISVIFLVVFIIYEIRFAKTPLLPRAVIKDRHMIQIMLALFFGWGSFGIFTFYYFQFQLNIRQYTALWAGGTYFMFLIWGIIAALLVGFTIKNVSPSVFLFFSMVAFNVGSIMASVTPVHETYFRTQLGTMIILSFGMDLSFPASSIIFSDNLPMEYQGMAGSLVNTVVNYSMSLCLGMGATVETQVNSDGKHLLKGYRGAQYLGIGLASLACMISGLYMVESFIKGRRARAAAEYDCTVA

Function: Putative component of the machinery responsible for pumping aminotriazole (and possibly other toxic compounds) out of the cell. Probable ATP-dependent export permease. Appears to confer resistance only to aminotriazole. Location Topology: Multi-pass membrane protein Sequence Mass (Da): 59983 Sequence Length: 542 Domain: Deletion of the C-terminal 34 residues abolishes ATR1 activity, while deletion of the C-terminal 23 residues have a minor effect. Subcellular Location: Membrane

A0A084R1M6

MAVISLFRIIVDKWHVVLACSACLGALLFQALRRQSNSTKDVPFIGMELGSAEKRRKAYMTDARSLFRDGYQQFKDRVFGITTTSENLVVVVPPRFLDELGRLPDEVLSASMAVADISQDKYTKMEITDPIISHAVRGNLTMSLSRLNDAILEELRKALSLLLPTCDEWTSVNISEKLQRIVAVISGRVFVGPELCGSDAYLDAAIHIAHEASAAVQSISTLPPWKRPFLSARLPELRALRERQDKVHSVLRPVLEKRIQMNEEDRPDDMLTWIISSQKKHGERSIETMAKVQTALHLAAIGTTSEMATNAFYNLAAMPELVPELREEIRTVLEEHDGVVSTKSLQAMKKLDSFLKETARLYPPFLAAFERKVLRTFTLSNGQVIPAGALIKVPSQAIMTDPALFPDPDRFDAFRFYDLQQQKNILKDGSVSVGASVNQFVNSNKNSLVFGYGRHACPGRFLAADELKMILVYFLQAYEIRLEEGESRRYRNLEFAAFSIPDPTKTIQMKKLQ

Function: Cytochrome P450 monooxygenase; part of the core atranone cluster (CAC) which products are predicted to catalyze most or all steps of mycotoxin atranone synthesis, starting from geranylgeranyl pyrophosphate (GGPP) . The initial cyclization of GGPP to dolabellane is probably performed by the terpene cyclase ATR13 . The Baeyer-Villiger oxidation near the end of the atranone synthesis, which converts atranones D and E to atranones F and G is predicted to be catalyzed by the monooxygenase ATR8 . Of the CAC's other predicted gene products, the reducing PKS ATR6 might synthesize a polyketide chain . This polyketide is probably transferred onto the atranone backbone by the polyketide transferase ATR5 (By similarity). Other predicted CAC products include 4 oxygenases (ATR2, ATR3, ATR4, and ATR14), 3 short-chain reductases (ATR7, ATR9, and ATR10), and a methyltransferase (ATR12) . These may all be involved in the various steps of atranone biosynthesis, although their specific roles must await experimental determination . Sequence Mass (Da): 57679 Sequence Length: 513 Pathway: Mycotoxin biosynthesis. EC: 1.-.-.-

A0A8F4SN83

MALLDTIELFSNFSLSGVFAGLVLASLLTTTYCIWNIFYNIYLHPLKGYPGPKFLTTSRLPYLKWMFSGTLVPNFQRLHEQYGPVVRVAPNELSYINPEALKTIYGHRQPGEGFRKNPAFFQPATNGVHSILTSEGDAHSSVRRKILPAFSDKALAEQQDILQHFTDLLIRKLRERVEASKSSEPVDMFEWYIWTTFDLIGDLAFGEPFNCLEAASFTEWVALVFNAFKTFAFINISKQLAPLDKLVRLMIPKSMKARQDKVFSLNVAKVDRRIASKADRPDFLSYIIKGKDGVAMALPELYANSTLLVLAGSESTASGLAGITFELLKHREAQKKAVEEIRSAFKTEDEIVPESVKRLPYLAAMVSEGLRMYPPFPEGLPRLTPRQGAQICGQWVPGGTYVQFSTHAAHRASANFTDPNVFAPERWLGDTKFASDIKEASQPFSIGPRSCIGRNLAYLEMRLILARMLWSFDMQLTPECEDWDDQNSWIQWDKKPLMVKLSLVKR

Function: Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of atranorin, a depside of polyketide origin that accumulates in the cortical or medullary layers of lichen thalli . Atr2 performs the oxidation at the C-9 position of 4-O-demethylbarbatic acid to yield proatranorin III via proatranorin II . Atr2 is also able to oxidize the atr3 product proatranorin I to produce the final compound atranorin . The first step in the pathway is performed by the non-reducing polyketide synthase atr1 that produces 4-O-demethylbarbatic acid composed of two 3-methylorsellinic acid (3MOA) moieties. The pathway continues with the actions of the cytochrome P450 monooygenase atr2 that catalizes the oxidation of c-9 and the O-methyltransferase atr3 that performs the methylation of the carboxyl group to yield atranorin, via the proatranorin II and III intermediates if atr2 acts first, or the proatranorin I intermediate if atr3 acts first . Catalytic Activity: 4-O-demethylbarbatate + O2 + reduced [NADPH--hemoprotein reductase] = H(+) + H2O + oxidized [NADPH--hemoprotein reductase] + proatranorin II Location Topology: Single-pass membrane protein Sequence Mass (Da): 57240 Sequence Length: 506 Pathway: Secondary metabolite biosynthesis; terpenoid biosynthesis. Subcellular Location: Membrane EC: 1.-.-.-

A0A084R1J1

METLSQRITSMESVQLQGIAVAFVTASALYYVLPAAISHIQLSALPMLGKTEVVVIPPKLLSELSKSPRTLSAEIAGNEFIAGKYTKVKALTPILLHSITKYLIPSLGRNAVVMSEEVSNAVRLGIPTCNDWTGVNIYPKIMRMVTVSTGRFLVGSELNRSEDYIDTVHNYALDVSSAQSAVHKMHPWIRPLLAEWLPEIRRLRKRTEEAFALFESLIKERMKMQRELSESELPDDLLQWMIANRHNYNNEDAHDLVYSQLGLTFTANHSTASTITNALYTLATMGDLIDVIRDDITQALAESGGQFTSKALDSMWKFDSFIKETVRMNPLVMSVAVRKVVEPIKLPSGQVIPTGVTLETPLVAVNLDDQIFPNADVFDPMRFYNLREKDRKQGDAREAEFNQLISSSTSHMSWGFGKHTCPGRAFAAQQIKMILAHIILRYDIKLVGDSTDRYENIPKGHLSLPDPTKDILMKRREI

Function: Cytochrome P450 monooxygenase; part of the core atranone cluster (CAC) which products are predicted to catalyze most or all steps of mycotoxin atranone synthesis, starting from geranylgeranyl pyrophosphate (GGPP) . The initial cyclization of GGPP to dolabellane is probably performed by the terpene cyclase ATR13 . The Baeyer-Villiger oxidation near the end of the atranone synthesis, which converts atranones D and E to atranones F and G is predicted to be catalyzed by the monooxygenase ATR8 . Of the CAC's other predicted gene products, the reducing PKS ATR6 might synthesize a polyketide chain . This polyketide is probably transferred onto the atranone backbone by the polyketide transferase ATR5 (By similarity). Other predicted CAC products include 4 oxygenases (ATR2, ATR3, ATR4, and ATR14), 3 short-chain reductases (ATR7, ATR9, and ATR10), and a methyltransferase (ATR12) . These may all be involved in the various steps of atranone biosynthesis, although their specific roles must await experimental determination . Location Topology: Single-pass membrane protein Sequence Mass (Da): 53631 Sequence Length: 478 Pathway: Mycotoxin biosynthesis. Subcellular Location: Membrane EC: 1.-.-.-

A0A8F4PN06

MTSVDTMPPPMVRLESQPDDLMGSSDVADVSDLLPGHTNGLEDEVKIPATNGLKSHPVVTTGTEKTGVMPPLQPESKKNNKGVPWYHASPNDIDPVTRGLLENYSKIPSDQVQQHVIAIREKAWDVYPYPCIGQFLFLNLTINLSPYYPSLVSRLRDQNQTLLDLGCCFAQDVRKLVSDGAPSQNIYGADLYGEFMDLGFELFRDRKTLKSTFFPTDILNERDLLLKGLDGEMDVVYLGLFLHHFDFETCVKVCTRVTRLLKPKPGSLVMGVQVGSLVGDTKPIPIPSGGILWRHDIASLERVWEEVGALTGTKWKVEARLERGKGFGEKWQLEGTRRLGFEVYRL

Function: O-methyltransferase; part of the gene cluster that mediates the biosynthesis of atranorin, a depside of polyketide origin that accumulates in the cortical or medullary layers of lichen thalli . Atr3 methylates the carboxyl group of 4-O-demethylbarbatic acid to yield proatranorin I . Atr3 is also able to methylate the atr2 product proatranorin III to produce the final compound atranorin . The first step in the pathway is performed by the non-reducing polyketide synthase atr1 that produces 4-O-demethylbarbatic acid composed of two 3-methylorsellinic acid (3MOA) moieties. The pathway continues with the actions of the cytochrome P450 monooygenase atr2 that catalizes the oxidation of c-9 and the O-methyltransferase atr3 that performs the methylation of the carboxyl group to yield atranorin, via the proatranorin II and III intermediates if atr2 acts first, or the proatranorin I intermediate if atr3 acts first . Catalytic Activity: 4-O-demethylbarbatate + S-adenosyl-L-methionine = proatranorin I + S-adenosyl-L-homocysteine Sequence Mass (Da): 38717 Sequence Length: 346 Pathway: Secondary metabolite biosynthesis; terpenoid biosynthesis. EC: 2.1.3.-

A0A084R1M7

MRLDLLGPVATRIITYLDSLTWVGMALPLFSLCWAISYARGKAYPTVPGAPVYGYNSRFEPSFMLKSRTYTGFYDILSNGYKMLKDVPFVIPRHDTNINILPIKYLDEIRLMPKHILNSHLVLISQMTPKWTWLQPAADSDLVTRVLLTKLNPDLQKYVDITRLELDSAFKSDFPRHDEEWTEVDFQPLIRRVLTRISAKIFLGEPACLNEDWLRIAIGYTAGALEVTKDLHKFPSWTHFLVAPLLPSRRRLRRELDIAMKIVEKQIQLHEQAEKDGLKNYDTLLDWMLDNCSDKESSVEAMTIFQCFIAMASIHTTEFSLANVLFDLCAHPEWFPVLREELDEVIRVHGNIGHRLPAKQWLQKLEKMDSLLAETLRLCPTMLTSIQRLALEKVQLKDGTVIPKGSRLAWASLHHVTDPEVDGTLAAWDPMRNYRKRHSGSGENLTKFVAGQINESTLGFGYGNQACPGRYFAVNEIKMMLARLLLEFEFKFPEGKSRPKVFFIGEIACLDHDATLMMRNVRTC

Function: Cytochrome P450 monooxygenase; part of the core atranone cluster (CAC) which products are predicted to catalyze most or all steps of mycotoxin atranone synthesis, starting from geranylgeranyl pyrophosphate (GGPP) . The initial cyclization of GGPP to dolabellane is probably performed by the terpene cyclase ATR13 . The Baeyer-Villiger oxidation near the end of the atranone synthesis, which converts atranones D and E to atranones F and G is predicted to be catalyzed by the monooxygenase ATR8 . Of the CAC's other predicted gene products, the reducing PKS ATR6 might synthesize a polyketide chain . This polyketide is probably transferred onto the atranone backbone by the polyketide transferase ATR5 (By similarity). Other predicted CAC products include 4 oxygenases (ATR2, ATR3, ATR4, and ATR14), 3 short-chain reductases (ATR7, ATR9, and ATR10), and a methyltransferase (ATR12) . These may all be involved in the various steps of atranone biosynthesis, although their specific roles must await experimental determination . Location Topology: Single-pass membrane protein Sequence Mass (Da): 60146 Sequence Length: 524 Pathway: Mycotoxin biosynthesis. Subcellular Location: Membrane EC: 1.-.-.-

A0A8F4PNE5

MEDPKSLSAPLTAFNADTTTADETPAAQKKYEDDNGQKAGSESSENTKNSDHGDATEVNTPKSADLEANALRNSSVSRSNQEQEKSEEAIDPNIVDWDGPNDPSNPLNWPTWKIKTHIFLVSSITFISPLGSSILATGIPQILAEFRSTNAELGSLVVSVYLLGFAAGPLVIAPLSELYGRMPLYHICNILFAILTVGCALGPTLNSEIGLRFLQGCAGSAPLAIGGGTISDLIPQERRGKYMGIYALGPTLGPIFGPVAGGFLTGAKGWRWLMWLLLMIEGSVTLVNFVVMRETYGVVIMARKTRALQKQTGNMSLRSRYDQGLTTRRLWRNTLIRPAKMLVYSPIIFLLSLFMAMVYGYLYLLFTTFPVVFGEYYHFSIGITGLVYLGLGIGNIIGLVIFGVFSDKILLAKAASGELKPEYRLLPMVWTSFTVPIGLFIYGWSARYAVHWIVPIIGTVFFGIGLLVTLVCTLTYIVDAFTEYAASATAANAVMRSVVGATLPLAGPSMYQALGIGWGNSLLAFIALAGCPIPWVFYVYGERIRKSSKATY

Function: MFS-type transporter; part of the gene cluster that mediates the biosynthesis of atranorin, a depside of polyketide origin that accumulates in the cortical or medullary layers of lichen thalli. Location Topology: Multi-pass membrane protein Sequence Mass (Da): 59981 Sequence Length: 552 Subcellular Location: Cell membrane

M4C699

MRLISPALVVSTAIQARHVNSSAPVDSAMTEANPLASAHPPDVGYDGVPAGRVRNPDDPTTEERTPGESFMEAINFKIFKLVQEAQGRILGLPEQPRGDMEWLERYGQDAILHYLETGDKDPSQLEKKYDQLLDELKNAPNLEVEILESIHALFLAYMEEVAKPAVQTTPKLNEQPDKFAWAMINKARRNAKPGIRNPYKSLNIPLVENYIKKYNAFIELRQRELTLLDTFSCAFNHNTVKLAKFLAMVDTFSPKRTFVLAMRIELSEIWIEEKRTIAEVASILGISTITGYAKNRLSAGTFVRFIYQLAKTNEQLGPDIVKDLVKTFGPDRTTELLTRMKTVSPRMFTILKDHMDVRLKETGVTPN

Function: Secreted effector that acts as an elicitor of hypersensitive response (HR) specifically on plants carrying defense protein RPP5. Sequence Mass (Da): 41475 Sequence Length: 367 Domain: Has the canonical EER motif, but lacks the canonical translocation motif RxLR, which characterizes most oomycete effectors identified so far. The EER motif is not required to trigger an RPP5-dependent immune response. Subcellular Location: Secreted

A0A084R1K1

MSTLTIDPTSIPPLEGKTAVVTATPLVPGGASGIGLAAAKIMLQKGATVYALDRQEPIEAVPGLKFRRCDVTSWSALREVFDEIQQVHLAFANAGICDKSPESYYDDVCDNGNLQEPDYSMIDVNLKAVLNFVKLARHSMRRHQVQGSIVITASSTGLVPEQSAPVYSSTKFAVIGLVRTLRSVLIQENITINAVAPFVTTTGMAPAEAMVPLKNLGVQTSPADFVGLALVYSAVARQTRRVEAYGKETEEDILEHGRWNGRVILTLGDKYTEVEEEFSKSRPLWTGGEVLQSIRLQQAVLDFRHGGVAIKSNRPSNQLN

Function: Short-chain dehydrogenase/reductase; part of the core atranone cluster (CAC) which products are predicted to catalyze most or all steps of mycotoxin atranone synthesis, starting from geranylgeranyl pyrophosphate (GGPP) . The initial cyclization of GGPP to dolabellane is probably performed by the terpene cyclase ATR13 . The Baeyer-Villiger oxidation near the end of the atranone synthesis, which converts atranones D and E to atranones F and G is predicted to be catalyzed by the monooxygenase ATR8 . Of the CAC's other predicted gene products, the reducing PKS ATR6 might synthesize a polyketide chain . This polyketide is probably transferred onto the atranone backbone by the polyketide transferase ATR5 (By similarity). Other predicted CAC products include 4 oxygenases (ATR2, ATR3, ATR4, and ATR14), 3 short-chain reductases (ATR7, ATR9, and ATR10), and a methyltransferase (ATR12) . These may all be involved in the various steps of atranone biosynthesis, although their specific roles must await experimental determination . Sequence Mass (Da): 34765 Sequence Length: 320 Pathway: Mycotoxin biosynthesis. EC: 1.-.-.-

A0A084R1J7

MAVEKVQAFEKVSIPTEKQPGSEDLGFDPAELQKKYEAERNLRIQNGGVSQYRSAWKSGFGYYLEDPNADANFSRDPISARYDVVIMGGGFSGLLVAARLVQQGITNFTILDKSADFGGTWYWSRYPGAQCDVDSTIYLPLLEEVGYIPKEKYSFGPEILEHAQRIAKHFGLYPKALFQTEVKTCHWSEEDSLWTVQTDRGDNLRAQFIVSAFGISHMPKLPGISGIENFQGKSFHASRWDYNYTGGDSTGNMTKLADKRVGIIGTGATAIQVVPKLAESAKELYVFQRTPSSVDVRNNRPTDAEWAKTLRPGWQQERIDNFYAITTGENVTEDLIDDGWTEIFRLVAAPFFASADIEQSLENRMEQVQIADFKKMESVRARVDSLVKDPATAASLKPWYNQFCKRPCFHDEYLQAFNHPNVTLVDTRGHGVDAVTTKGVLAQGKEYELDCLIYSTGYEWYTEWEQRTRSQVYGRNGLTITKKWSQGITTYHGWGVHGFPNFMVLSSAQVNNVPNYTHMVGYLSRHLAYIVRTCKDRGIKSVEPTATAESKWVQQVVEQGAARRDQMKLCTPGYLNHEGDITEKTDRLYSYNGSGDSKFQIILDKWRDDGKLVGLSIDCATEADL

Cofactor: Binds 1 FAD per subunit. Function: Baeyer-Villiger monooxygenase; part of the core atranone cluster (CAC) which products are predicted to catalyze most or all steps of mycotoxin atranone synthesis, starting from geranylgeranyl pyrophosphate (GGPP) . The initial cyclization of GGPP to dolabellane is probably performed by the terpene cyclase ATR13 . The Baeyer-Villiger oxidation near the end of the atranone synthesis, which converts atranones D and E to atranones F and G is predicted to be catalyzed by the monooxygenase ATR8 . Of the CAC's other predicted gene products, the reducing PKS ATR6 might synthesize a polyketide chain . This polyketide is probably transferred onto the atranone backbone by the polyketide transferase ATR5 (By similarity). Other predicted CAC products include 4 oxygenases (ATR2, ATR3, ATR4, and ATR14), 3 short-chain reductases (ATR7, ATR9, and ATR10), and a methyltransferase (ATR12) . These may all be involved in the various steps of atranone biosynthesis, although their specific roles must await experimental determination . Sequence Mass (Da): 70493 Sequence Length: 625 Pathway: Mycotoxin biosynthesis. EC: 1.14.13.-

A0A084R1K2

MPTIRGQSILIIGGSSGIGAAVAKYACGDGVKVSVASSNKGRVEKALKKIQALVPASEILGFTVDLSQYDLESRLEKLFKEVVDATGGPLDHVVMTAGTGNMVSLSEYTAKAFQESAPLHFIAPLMVGKVAPRFMNRHWKSSITFTSGAFGKKPAKGYCVIASAVGALDAATRALALELAPIRVNAVSPGPTVTEMFGPPSEALDKAVAAMGAQSLLGKLGRPEDVAEAYIYLMRDANTTGTIVDSNGGAFLQ

Function: Short-chain dehydrogenase/reductase; part of the core atranone cluster (CAC) which products are predicted to catalyze most or all steps of mycotoxin atranone synthesis, starting from geranylgeranyl pyrophosphate (GGPP) . The initial cyclization of GGPP to dolabellane is probably performed by the terpene cyclase ATR13 . The Baeyer-Villiger oxidation near the end of the atranone synthesis, which converts atranones D and E to atranones F and G is predicted to be catalyzed by the monooxygenase ATR8 . Of the CAC's other predicted gene products, the reducing PKS ATR6 might synthesize a polyketide chain . This polyketide is probably transferred onto the atranone backbone by the polyketide transferase ATR5 (By similarity). Other predicted CAC products include 4 oxygenases (ATR2, ATR3, ATR4, and ATR14), 3 short-chain reductases (ATR7, ATR9, and ATR10), and a methyltransferase (ATR12) . These may all be involved in the various steps of atranone biosynthesis, although their specific roles must await experimental determination . Sequence Mass (Da): 26317 Sequence Length: 253 Pathway: Mycotoxin biosynthesis. EC: 1.-.-.-

P54253

MKSNQERSNECLPPKKREIPATSRSSEEKAPTLPSDNHRVEGTAWLPGNPGGRGHGGGRHGPAGTSVELGLQQGIGLHKALSTGLDYSPPSAPRSVPVATTLPAAYATPQPGTPVSPVQYAHLPHTFQFIGSSQYSGTYASFIPSQLIPPTANPVTSAVASAAGATTPSQRSQLEAYSTLLANMGSLSQTPGHKAEQQQQQQQQQQQQHQHQQQQQQQQQQQQQQHLSRAPGLITPGSPPPAQQNQYVHISSSPQNTGRTASPPAIPVHLHPHQTMIPHTLTLGPPSQVVMQYADSGSHFVPREATKKAESSRLQQAIQAKEVLNGEMEKSRRYGAPSSADLGLGKAGGKSVPHPYESRHVVVHPSPSDYSSRDPSGVRASVMVLPNSNTPAADLEVQQATHREASPSTLNDKSGLHLGKPGHRSYALSPHTVIQTTHSASEPLPVGLPATAFYAGTQPPVIGYLSGQQQAITYAGSLPQHLVIPGTQPLLIPVGSTDMEASGAAPAIVTSSPQFAAVPHTFVTTALPKSENFNPEALVTQAAYPAMVQAQIHLPVVQSVASPAAAPPTLPPYFMKGSIIQLANGELKKVEDLKTEDFIQSAEISNDLKIDSSTVERIEDSHSPGVAVIQFAVGEHRAQVSVEVLVEYPFFVFGQGWSSCCPERTSQLFDLPCSKLSVGDVCISLTLKNLKNGSVKKGQPVDPASVLLKHSKADGLAGSRHRYAEQENGINQGSAQMLSENGELKFPEKMGLPAAPFLTKIEPSKPAATRKRRWSAPESRKLEKSEDEPPLTLPKPSLIPQEVKICIEGRSNVGK

Function: Chromatin-binding factor that repress Notch signaling in the absence of Notch intracellular domain by acting as a CBF1 corepressor. Binds to the HEY promoter and might assist, along with NCOR2, RBPJ-mediated repression. Binds RNA in vitro. May be involved in RNA metabolism . In concert with CIC and ATXN1L, involved in brain development (By similarity). PTM: Ubiquitinated by UBE3A, leading to its degradation by the proteasome. The presence of expanded poly-Gln repeats in spinocerebellar ataxia 1 (SCA1) patients impairs ubiquitination and degradation, leading to accumulation of ATXN1 in neurons and subsequent toxicity. Sequence Mass (Da): 86923 Sequence Length: 815 Domain: The AXH domain is required for interaction with CIC. Subcellular Location: Cytoplasm

G5ED29

MSTPTGLPALNGDVLSAINDMIGRVIIINTTDKKRYSGVLGAVSQDFDFGMQCVVEITKENENNLLRTESECRDKMVFHYSDIVDFAYVTQEIKKQHAVSKFVTDRQYHGDTPIEGEELQEWNGGEEDGLGGSIEDDVVVAGGQTAARRSNNHNNGTGWSVNDMFAANEKMNVVSTFKEDLTQYTTVEVVGTDEDRARAERLAREIESNSSSKFMANLENDDDERDLDKITRQEDFENGNGRKRNNNSFNQQQQQRRNPNIAPNGQPVNRRAEGLRGDRRNSGSSSANNSRYGAPAAAQQNYSQNQQQQQGQKGYRRQNEENDWQMAKGKGQNQGHDHSFRQQQKQMLDPRPNNNVKPADDKAQSATTATAAAGGSRVTDLKNWGNEFSIATAPKDQAPAVPAGNSGSAWNRGPPSSLVAKGSSNESTPPPTTNGEEAETKKEEAPSTSVDVAAAPVQNVQNDAEKHQEDDNVSVTSENDSVITSKSSSFKFNINAPEFKPRVAPATPTATTPVQNEYHPQQQPHPAMMAPQQGPPAPGMGMVPPHMGGPQNQGQPPMMMWQQTGQQQQGGGGYPQNHQFPIQHVPMQGVPGQMYGPGAATPVTVAQQPNQQHQVPTSAAGGQNHQLRDGEYREKQPLYMPYGPPQMVPVTSQQFYHSQYQGQMQQAAPYQMKMMPQQAPQGAYQQRYQQPQVYMMPPQGQQQQPRYQGPPPPQQQQQQQPQQQQFSGEQSRPQSHPNSQPTTPGPRGELPKMSGAPQNGNMQAESSSNASHSGSTSSQSGQRSGSPPGAVPPPPPPQQQHQQQQHPPHHAPPHVGAPPPQMMQQQQQHIQQYMVMQGPHQMHPQIPNYYQQPQQVFYPMIMPQQMPMQQNQHPQQSLMGERSDQGFPTSGYFDYRTMPNYQQQQQQQQQQMHRQNSLPQQFQGNQGVNPSGQQSGPPPPPPPSQQGTPRDQQHSQSPP

Function: Probable RNA-binding protein that negatively regulates the translation of targets . Functions with RNA-binding protein szy-20 to ensure embryonic cell division, and to this end, plays a role in the regulation of centrosome assembly, position and size, and in astral microtubule outgrowth and nucleation . Required for gonad development, germ cell proliferation and for the production of oocytes . Regulates whole body growth and fat accumulation in response to food availability, and this may be through the mTOR pathway, upstream of daf-15 and rheb-1 . Sequence Mass (Da): 106041 Sequence Length: 959 Domain: The C-terminal part is necessary for interaction with szy-20. Subcellular Location: Cytoplasm

P31414

MVAPALLPELWTEILVPICAVIGIAFSLFQWYVVSRVKLTSDLGASSSGGANNGKNGYGDYLIEEEEGVNDQSVVAKCAEIQTAISEGATSFLFTEYKYVGVFMIFFAAVIFVFLGSVEGFSTDNKPCTYDTTRTCKPALATAAFSTIAFVLGAVTSVLSGFLGMKIATYANARTTLEARKGVGKAFIVAFRSGAVMGFLLAASGLLVLYITINVFKIYYGDDWEGLFEAITGYGLGGSSMALFGRVGGGIYTKAADVGADLVGKIERNIPEDDPRNPAVIADNVGDNVGDIAGMGSDLFGSYAEASCAALVVASISSFGINHDFTAMCYPLLISSMGILVCLITTLFATDFFEIKLVKEIEPALKNQLIISTVIMTVGIAIVSWVGLPTSFTIFNFGTQKVVKNWQLFLCVCVGLWAGLIIGFVTEYYTSNAYSPVQDVADSCRTGAATNVIFGLALGYKSVIIPIFAIAISIFVSFSFAAMYGVAVAALGMLSTIATGLAIDAYGPISDNAGGIAEMAGMSHRIRERTDALDAAGNTTAAIGKGFAIGSAALVSLALFGAFVSRAGIHTVDVLTPKVIIGLLVGAMLPYWFSAMTMKSVGSAALKMVEEVRRQFNTIPGLMEGTAKPDYATCVKISTDASIKEMIPPGCLVMLTPLIVGFFFGVETLSGVLAGSLVSGVQIAISASNTGGAWDNAKKYIEAGVSEHAKSLGPKGSEPHKAAVIGDTIGDPLKDTSGPSLNILIKLMAVESLVFAPFFATHGGILFKYF

Function: Contributes to the transtonoplast (from cytosol to vacuole lumen) H(+)-electrochemical potential difference. It establishes a proton gradient of similar and often greater magnitude than the H(+)-ATPase on the same membrane. In addition, facilitates auxin transport by modulating apoplastic pH and regulates auxin-mediated developmental processes. Confers tolerance to NaCl and to drought by increasing ion retention. Catalytic Activity: diphosphate + H(+)(in) + H2O = 2 H(+)(out) + 2 phosphate Location Topology: Multi-pass membrane protein Sequence Mass (Da): 80820 Sequence Length: 770 Domain: Has 16 transmembrane helices and a cytoplasmic domain that contains the active site. Subcellular Location: Vacuole membrane EC: 7.1.3.1

Q56ZN6

MMMDEDVEQASLMSFNDRPRAFPNMRSKTYSPLIFRIIRKLNVRVLSIILLFCFGAIFYMGASTSPIIVFVFTVCIISFLLSIYLTKWVLAKDEGPPEMVEISDAIRDGAEGFFRTQYSTISKMAILLAFVILCIYLFRSLTPQQEAAGLGRAMSAYITVAAFLLGALCSGIAGYVGMWVSVRANVRVSSAARRSAREALQIAVRAGGFSALVVVGMAVIGIAILYSTFYVWLGVGSPGSMNVTDLPLLLVGYGFGASFVALFAQLGGGIYTKGADVGADLVGKVEQGIPEDDPRNPAVIADLVGDNVGDCAARGADLFESIAAEIISAMILGGTMAKKCKIEDPSGFILFPLVVHSFDLIISSIGILSIKGTRDASVKSPVEDPMAVLQKGYSLTIILAVITFGASTRWLLYTEQAPSAWFNFALCGLVGIITAYIFVWISKYYTDYKHEPVRTLALASSTGHGTNIIAGVSLGLESTALPVLTISVAIISAYWLGNTSGLVDENGIPTGGLFGTAVATMGMLSTAAYVLTMDMFGPIADNAGGIVEMSQQPESVREITDLLDAVGNTTKATTKGFAIGSAALASFLLFSAYMDEVSAFANVSFKEVDIAIPEVFVGGLLGAMLIFLFSAWACAAVGRTAQEVVNEVRRQFIERPGIMEYKEKPDYSRCVAIVASAALREMIKPGALAIASPIVVGLVFRILGYYTGQPLLGAKVVASMLMFATVCGILMALFLNTAGGAWDNAKKYIETGALGGKGSEAHKAAVTGDTVGDPFKDTAGPSIHVLIKMLATITLVMAPVFL

Function: Pyrophosphatase active in both inorganic pyrophosphate hydrolysis and H(+) translocation. Catalytic Activity: diphosphate + H(+)(in) + H2O = 2 H(+)(out) + 2 phosphate Location Topology: Multi-pass membrane protein Sequence Mass (Da): 85133 Sequence Length: 802 Subcellular Location: Golgi apparatus membrane EC: 7.1.3.1

Q06572

MAILGELGTEILIPVCGVIGIVFAVAQWFIVSKVKVTPGAASAAAGAKNGYGDYLIEEEEGLNDHNVVVKCAEIQTAISEGATSFLFTMYQYVGMFMVVFAAIIFLFLGSIEGFSTKGQPCTYSKGTCKPALYTALFSTASFLLGAITSLVSGFLGMKIATYANARTTLEARKGVGKAFITAFRSGAVMGFLLSSSGLVVLYITINVFKMYYGDDWEGLFESITGYGLGGSSMALFGRVGGGIYTKAADVGADLVGKVERNIPEDDPRNPAVIADNVGDNVGDIAGMGSDLFGSYAESSCAALVVASISSFGINHDFTAMCYPLLVSSVGIIVCLLTTLFATDFFEIKAANEIEPALKKQLIISTALMTVGVAVISWLALPAKFTIFNFGAQKEVSNWGLFFCVAVGLWAGLIIGFVTEYYTSNAYSPVQDVADSCRTGAATNVIFGLALGYKSVIIPIFAIAVSIYVSFSIAAMYGIAMAALGMLSTMATGLAIDAYGPISDNAGGIAEMAGMSHRIRERTDALDAAGNTTAAIGKGFAIGSAALVSLALFGAFVSRAGVKVVDVLSPKVFIGLIVGAMLPYWFSAMTMKSVGSAALKMVEEVRRQFNTIPGLMEGTAKPDYATCVKISTDASIKEMIPPGALVMLTPLIVGTLFGVETLSGVLAGALVSGVQIAISASNTGGAWDNAKKYIEAGNSEHARSLGPKGSDCHKAAVIGDTIGDPLKDTSGPSLNILIKLMAVESLVFAPFFATYGGLLFKYI

Function: Contributes to the transtonoplast (from cytosol to vacuole lumen) H(+)-electrochemical potential difference. It establishes a proton gradient of similar and often greater magnitude than the H(+)-ATPase on the same membrane. Catalytic Activity: diphosphate + H(+)(in) + H2O = 2 H(+)(out) + 2 phosphate Location Topology: Multi-pass membrane protein Sequence Mass (Da): 79533 Sequence Length: 762 Domain: Has 16 transmembrane helices and a cytoplasmic domain that contains the active site. Subcellular Location: Vacuole membrane EC: 7.1.3.1

P21616

MGAAILPDLGTEILIPVCAVIGIAFALFQWLLVSKVKLSAVRDASPNAAAKNGYNDYLIEEEEGINDHNVVVKCAEIQNAISEGATSFLFTEYKYVGIFMVAFAILIFLFLGSVEGFSTSPQACSYDKTKTCKPALATAIFSTVSFLLGGVTSLVSGFLGMKIATYANARTTLEARKGVGKAFITAFRSGAVMGFLLAANGLLVLYIAINLFKIYYGDDWGGLFEAITGYGLGGSSMALFGRVGGGIYTKAADVGADLVGKVERNIPEDDPRNPAVIADNVGDNVGDIAGMGSDLFGSYAESSCAALVVASISSFGLNHELTAMLYPLIVSSVGILVCLLTTLFATDFFEIKAVKEIEPALKKQLVISTVLMTIGVAVVSFVALPTSFTIFNFGVQKDVKSWQLFLCVAVGLWAGLIIGFVTEYYTSNAYSPVQDVADSCRTGAATNVIFGLALGYKSVIIPIFAIAISIFVSFTFAAMYGIAVAALGMLSTIATGLAIDAYGPISDNAGGIAEMAGMSHRIRERTDALDAAGNTTAAIGKGFAIGSAALVSLALFGAFVSRASITTVDVLTPKVFIGLIVGAMLPYWFSAMTMKSVGSAALKMVEEVRRQFNTIPGLMEGTAKPDYATCVKISTDASIKEMIPPGALVMLTPLVVGILFGVETLSGVLAGSLVSGVQIAISASNTGGAWDNAKKYIEAGASEHARSLGPKGSDCHKAAVIGDTIGDPLKDTSGPSLNILIKLMAVESLVFAPFFATHGGLLFKIF

Function: Proton-translocating inorganic pyrophosphatase that contributes to the transtonoplast (from cytosol to vacuole lumen) H(+)-electrochemical potential difference. It establishes a proton gradient of similar and often greater magnitude than the H(+)-ATPase on the same membrane. Catalytic Activity: diphosphate + H(+)(in) + H2O = 2 H(+)(out) + 2 phosphate Location Topology: Multi-pass membrane protein Sequence Mass (Da): 80037 Sequence Length: 766 Domain: Has 16 transmembrane helices and a large cytoplasmic domain that contains the active site. Subcellular Location: Vacuole membrane EC: 7.1.3.1

D0NIW0

MRLSFIIFAISLLAGGSGAAEALHPASDVLTLRGTNQGASTGKRSLRYDNNAERAGEEDDEERAFPGAEELSRLANLAHTSKADSLGTSLKNFFKQLDKANVNPSNIHKYGFSGEEFDQLRKRFGTWYRHYKDIE

Function: Secreted effector that acts as an elicitor of hypersensitive response (HR) specifically on plants carrying defense protein R10 . Enhances P.infestans colonization of Nicotiana benthamiana leaves . Sequence Mass (Da): 14982 Sequence Length: 135 Domain: The RxLR-dEER motif acts to carry the protein into the host cell cytoplasm through binding to cell surface phosphatidylinositol-3-phosphate. Subcellular Location: Secreted

D0NVB5

MGLMHRVLLLATFALLCMHAKAAGFDHDKVPRTVERGGGARQLRTATMSDDEARVSKLPSFIESFVKNRKIESWIQNKVTDDFVLSELKLVRLPGTSLADDPNFKLFQKFKIGGWLEEKATTTKAWENLGLDSLPFDQVSKIDEFKTYTQYVTVLNKKASKLDIDQWHGLLSGGSPEELMAKAMILRTLGRDVLERRVMLGGHVVVPF

Function: Secreted effector that acts as an elicitor of hypersensitive response (HR) specifically on plants carrying defense protein R1, through its interaction with this protein . Acts also as a virulence factor that promotes colonization and suppresses cell death induced by CRN2 as well as callose deposition, a hallmark of basal defense . Interacts with host exocyst component Sec5 and thereby disturbs vesicle trafficking, a cellular process that is important for basal defense. By targeting and stabilizing Sec5 in the cytoplasm, the exocyst complex is thus out of balance and not able to mediate the focal secretion of PR-1 and callose . Sequence Mass (Da): 23420 Sequence Length: 208 Domain: The RxLR-dEER motif acts to carry the protein into the host cell cytoplasm through binding to cell surface phosphatidylinositol-3-phosphate. Subcellular Location: Secreted

Q28043

MGAAAKLAFAVFLISCSSGAILGRSETQECIFYNANWERDRTNRTGVESCYGDKDKRRHCFATWKNISGSIEIVKQGCWLDDINCYDRTDCIEKKDSPEVYFCCCEGNMCNERFSYFPEMEVTQPTSNPVTPKPPYYNILLYSLVPLMLIAGIVICAFWVYRHHKMAYPPVLVPTQDPGPPPPSPLLGLKPLQLLEVKARGRFGCVWKAQLLNEYVAVKIFPIQDKQSWQNEYEVYSLPGMKHENILQFIGAEKRGTSVDVDLWLITAFHEKGSLSDFLKANVVSWNELCHIAETMARGLAYLHEDIPGLKDGHKPAISHRDIKSKNVLLKNNLTACIADFGLALKFEAGKSAGDTHGQVGTRRYMAPEVLEGAINFQRDAFLRIDMYAMGLVLWELASRCTAADGPVDEYMLPFEEEIGQHPSLEDMQEVVVHKKKRPVLRDYWQKHAGMAMLCETIEECWDHDAEARLSAGCVGERITQMQRLTNIITTEDIVTVVTMVTNVDFPPKESSL

Function: On ligand binding, forms a receptor complex consisting of two type II and two type I transmembrane serine/threonine kinases. Type II receptors phosphorylate and activate type I receptors which autophosphorylate, then bind and activate SMAD transcriptional regulators. Receptor for activin A, activin B and inhibin A. Mediates induction of adipogenesis by GDF6. Catalytic Activity: ATP + L-threonyl-[receptor-protein] = ADP + H(+) + O-phospho-L-threonyl-[receptor-protein] Location Topology: Single-pass type I membrane protein Sequence Mass (Da): 57952 Sequence Length: 513 Subcellular Location: Cell membrane EC: 2.7.11.30

P27038

MGAAAKLAFAVFLISCSSGAILGRSETQECLFFNANWERDRTNQTGVEPCYGDKDKRRHCFATWKNISGSIEIVKQGCWLDDINCYDRTDCIEKKDSPEVYFCCCEGNMCNEKFSYFPEMEVTQPTSNPVTPKPPYYNILLYSLVPLMLIAGIVICAFWVYRHHKMAYPPVLVPTQDPGPPPPSPLLGLKPLQLLEVKARGRFGCVWKAQLLNEYVAVKIFPIQDKQSWQNEYEVYSLPGMKHENILQFIGAEKRGTSVDVDLWLITAFHEKGSLSDFLKANVVSWNELCHIAETMARGLAYLHEDIPGLKDGHKPAISHRDIKSKNVLLKNNLTACIADFGLALKFEAGKSAGDTHGQVGTRRYMAPEVLEGAINFQRDAFLRIDMYAMGLVLWELASRCTAADGPVDEYMLPFEEEIGQHPSLEDMQEVVVHKKKRPVLRDYWQKHAGMAMLCETIEECWDHDAEARLSAGCVGERITQMQRLTNIITTEDIVTVVTMVTNVDFPPKESSL

Function: On ligand binding, forms a receptor complex consisting of two type II and two type I transmembrane serine/threonine kinases. Type II receptors phosphorylate and activate type I receptors which autophosphorylate, then bind and activate SMAD transcriptional regulators. Receptor for activin A, activin B and inhibin A. Mediates induction of adipogenesis by GDF6 . Catalytic Activity: ATP + L-threonyl-[receptor-protein] = ADP + H(+) + O-phospho-L-threonyl-[receptor-protein] Location Topology: Single-pass type I membrane protein Sequence Mass (Da): 57890 Sequence Length: 513 Subcellular Location: Cell membrane EC: 2.7.11.30

Q2SMF5

MSQPITRILKIDSSARAESSMSRKLAQQLTEQLIAANPGAEVVSRDVSGGLPFVTEEWIGASYTPADQRTEAQNQALALSDSLIEEVQAADTLVIAVPMYNFSVPATLKAYIDQICRAQVTFRYTEQGPVGLLENKKAYVVTVTGGTPVNSAADFVSAYMRQVLGFIGIKDVTFINADRIMVDPESILADAQQQIAAATEVAAA

Cofactor: Binds 1 FMN per subunit. Function: Quinone reductase that provides resistance to thiol-specific stress caused by electrophilic quinones. Catalytic Activity: 2 a quinone + H(+) + NADH = 2 a 1,4-benzosemiquinone + NAD(+) Sequence Mass (Da): 21886 Sequence Length: 204 EC: 1.6.5.-

Q5QYY9

MKVLHLDSGIFLEQSVSRQVSQNIVNKLKEKQDITLFHRDLVANPVPHLAADELLAEEKPLIDELVQELLDADTLVIGAPMYNFTIPTQLKAWFDRVLQAGVTFKYTEQGPQGLVNGKKVYIASGRGGIYSQGEAQAMDHQESYLKQVLAFIGITDVTIIRAEGMNMGDEPRQQGFKEAEQEIETI

Cofactor: Binds 1 FMN per subunit. Function: Quinone reductase that provides resistance to thiol-specific stress caused by electrophilic quinones. Catalytic Activity: 2 a quinone + H(+) + NADH = 2 a 1,4-benzosemiquinone + NAD(+) Sequence Mass (Da): 20784 Sequence Length: 186 EC: 1.6.5.-

Q9CJ86

MTTLLIILAHPHTDDFSWSLATVEEFKKSYQESHPLDKIIIRDLFSEKVPALDNETFAAWKRNKYAPDTLSAEDKNLLHRHEEYLEEFLSADKYVFVNPMYNGFVTAELKQYIDVIAVPRKLFRYTENGPIGLLEGKKSLHIQSAGGFYHNEQDPTHMANDLGAAYIDQTMKMVGLTDENRQQLFVEGYARYPERADELKEKAFTSAENFGKAF

Cofactor: Binds 1 FMN per subunit. Function: Quinone reductase that provides resistance to thiol-specific stress caused by electrophilic quinones. Catalytic Activity: 2 a quinone + H(+) + NADH = 2 a 1,4-benzosemiquinone + NAD(+) Sequence Mass (Da): 24663 Sequence Length: 214 EC: 1.6.5.-

Q890E7

MTKTLIVNAHPDFRNAAHYSVQLEQAFLQLFQTRFPNDTVDVLNLYDTVIPQATVPELLGIWEKQAQHVNLSIEEQRLFAINQQLLQQFKAHHRIVIAMPLHNFNVPARLKDYIDNILVARETFRYTENGSVGLMTDNYRVMLLQASGSIYTRNDRYTPMEFSRLYLDKMFTEIMGFDRFEIVRAQGLQTNGVAVSQALKQAKMDLKAAFERFYD

Cofactor: Binds 1 FMN per subunit. Function: Quinone reductase that provides resistance to thiol-specific stress caused by electrophilic quinones. Catalytic Activity: 2 a quinone + H(+) + NADH = 2 a 1,4-benzosemiquinone + NAD(+) Sequence Mass (Da): 25011 Sequence Length: 215 EC: 1.6.5.-

Q8Y9C1

MTNVLFIKANGLPAERSVSVALYEIFLTEYKKSHPDDNVTELDLFEADLPYYDVTMMSGLHKEAAGETLSPEEKRLADIANSYLDQFLAADKIVMAFPLWNFSIPAQFLTYLFYLNQAGKTFKYTANGPVGLVADKKIALLNARGGIYSDGPMQSFEMSLNYVKNVLAHFGISEPEMVIVEGHNAKPDQAKDIISAGAKEAVELAKIF

Cofactor: Binds 1 FMN per subunit. Function: Quinone reductase that provides resistance to thiol-specific stress caused by electrophilic quinones. Catalytic Activity: 2 a quinone + H(+) + NADH = 2 a 1,4-benzosemiquinone + NAD(+) Sequence Mass (Da): 23025 Sequence Length: 208 EC: 1.6.5.-

Q6F271

MSKLLVINGSVIPSDKSNSHEMARIFLEEYKKVNPNDEIIELDLNKLVVGTNVLTTETFSTYWGEEEGMKYINQLKDVDKLLVIAPMYNFHVSGMLKNYIDHVALANQTFSYKYATKGASIGLLDKLKVQILATQGAPKGWYPWGDHVAYLKGTWEFMGAKVAEPILLAGVKVEPLSTQSPKEIVSSITSDLIAAAKKF

Cofactor: Binds 1 FMN per subunit. Function: Quinone reductase that provides resistance to thiol-specific stress caused by electrophilic quinones. Catalytic Activity: 2 a quinone + H(+) + NADH = 2 a 1,4-benzosemiquinone + NAD(+) Sequence Mass (Da): 22129 Sequence Length: 199 EC: 1.6.5.-

Q9I5F3

MSRILAVHASPRGERSQSRRLAEVFLAAYREAHPQARVARREVGRVPLPAVTEAFVAAAFHPQPEQRSLAMQADLALSDQLVGELFDSDLLVISTPMYNFSVPSGLKAWIDQIVRLGVTFDFVLDNGVAQYRPLLRGKRALIVTSRGGHGFGPGGENQAMNHADPWLRTALGFIGIDEVTVVAAEGEESGGRSFEDSCDEAEQRLLALARSA

Cofactor: Binds 1 FMN per subunit. Function: Quinone reductase that provides resistance to thiol-specific stress caused by electrophilic quinones . Shows a preference for benzoquinones . Catalytic Activity: 2 a quinone + H(+) + NADPH = 2 a 1,4-benzosemiquinone + NADP(+) Sequence Mass (Da): 23050 Sequence Length: 212 EC: 1.6.5.-

Q88IY3

MKLLHIDSSILGDNSASRQLSREVVEAWKAADPSVEVVYRDLAADAIAHFSAATLVAAGTPEDVRDAAQAFEAKLSAETLEEFLAADAVVIGAPMYNFTVPTQLKAWIDRVAVAGKTFRYTEAGPQGLCGNKKVVLVSTAGGLHAGQPTGAGHEDFLKVFLGFIGITDLEIVRAHGLAYGPEQRSQAIDAAQAQIASELFAAA

Cofactor: Binds 1 FMN per subunit. Function: Quinone reductase that provides resistance to thiol-specific stress caused by electrophilic quinones. Catalytic Activity: 2 a quinone + H(+) + NADH = 2 a 1,4-benzosemiquinone + NAD(+) Sequence Mass (Da): 21365 Sequence Length: 203 EC: 1.6.5.-

Q98QP9

MAKVLVIKTSMMGANSISNVLNDKFMEYYKEKNPNDEFIYMNLNDEKMASITMTSHNMKEYFVAEYSDKYINQLKKVDKVVMSVPMTNFNVNAVTKNYLDHISVADKTFSYKYSKKGEAIGLLDHLSVQILTTQGAPLGWYPWGNHSEYLKGHWRFLGAKVADHILVDSVKIGENSKKTPQEIIEKFDGEIKKAAYSF

Cofactor: Binds 1 FMN per subunit. Function: Quinone reductase that provides resistance to thiol-specific stress caused by electrophilic quinones. Catalytic Activity: 2 a quinone + H(+) + NADH = 2 a 1,4-benzosemiquinone + NAD(+) Sequence Mass (Da): 22673 Sequence Length: 198 EC: 1.6.5.-

Q4A6W2

MAKVLVLSGGLSEKEKSYSSQMLDLFVKTYKEVHPNDELEFVDLNTTKHAEVFLSRNTFATYWKDVESDKWIDKLKAADKVILSCSMTNFGPTAVVKNFIDSVAVANKTFSYKYSKKGDAVGLLDHLRVMIVTTQGAPKDWYLWGSHTNWLIGTWKFLGAKYVDTFELNGTKLSVFADKKPYDVVEEFRQDALEKAKQF

Cofactor: Binds 1 FMN per subunit. Function: Quinone reductase that provides resistance to thiol-specific stress caused by electrophilic quinones. Catalytic Activity: 2 a quinone + H(+) + NADH = 2 a 1,4-benzosemiquinone + NAD(+) Sequence Mass (Da): 22688 Sequence Length: 199 EC: 1.6.5.-

Q5YR63

MPTLLHLDASPRRRSISRDIGAAFADSWRATAPNGHYIHRDLAADPVPFIDAAWTEICDAVLAAGGTDLAALPTLVRTPAQAAAWRIVEPLLDELLAADVVLIGTPMYNYSIPAALKAWLDQVTFPRMSLAPRRFVVAAARGGSYSPGTPKAAFDHQERYLRDFFAGHFAVTDTVFVTAELANARQDPALAARRAEHDASYADALDTARRLGKEYR

Cofactor: Binds 1 FMN per subunit. Function: Quinone reductase that provides resistance to thiol-specific stress caused by electrophilic quinones. Catalytic Activity: 2 a quinone + H(+) + NADH = 2 a 1,4-benzosemiquinone + NAD(+) Sequence Mass (Da): 23541 Sequence Length: 216 EC: 1.6.5.-

Q8YV76

MANILHIDSSPRGDRSISRKLSYEFITSWKDTHPGDTVTYRDLGHNPVPHVDEPWIAAAFSSPESHTPELKTAIELSDTLIDEFLAADRLVFGVPMYNLNIPSTFKAYIDQIVRAGKTFTVDANGYKGLVDSSKKVLIITSRGGSYPPGTPYAAYDYQEPYLRAILGFMGLTDVTFIHAESLNMGEDAREKSLAGAKDAIAQAVANW

Cofactor: Binds 1 FMN per subunit. Function: Quinone reductase that provides resistance to thiol-specific stress caused by electrophilic quinones. Catalytic Activity: 2 a quinone + H(+) + NADH = 2 a 1,4-benzosemiquinone + NAD(+) Sequence Mass (Da): 22785 Sequence Length: 207 EC: 1.6.5.-

B1ZNL9

MKTLLVLNSSGRVTRSLTRRLTSRFAEAWSAVHHDAVVVQRDLTLNPPPTINEPWIVAAFAAPDTPATVREAVLRASDELLDELTAADAVVIGAPVYNFGLPAQLKAYVDQIVRVGRSFALTGDAAVPYRALLAPKPVVVMTAASDGVMLPGGALAHLNLVEPHLTAALGFIGLTDVRFVRVADSVADQAAHPHSLAAAERAIEMILPRLAAA

Cofactor: Binds 1 FMN per subunit. Function: Quinone reductase that provides resistance to thiol-specific stress caused by electrophilic quinones. Catalytic Activity: 2 a quinone + H(+) + NADH = 2 a 1,4-benzosemiquinone + NAD(+) Sequence Mass (Da): 22532 Sequence Length: 213 EC: 1.6.5.-

Q4FMI9

MKIYQIDSSARKEGSSSRALAKKLLNKIKKPGDEVIYRDLDDDMLFVSGLTESGMKIAEKDQTEEHKKMFELSDKLVSELKESDIIIISAPIYNYGPPATLKAWCDLAARIGETFKFKPNGRREGLLKNKQAYLVITSGGTKLNSSEDFLTPWLKFILNFFGIEKVEVISADQMALDYEKSIKEAEKQIENII

Cofactor: Binds 1 FMN per subunit. Function: Quinone reductase that provides resistance to thiol-specific stress caused by electrophilic quinones. Catalytic Activity: 2 a quinone + H(+) + NADH = 2 a 1,4-benzosemiquinone + NAD(+) Sequence Mass (Da): 21846 Sequence Length: 193 EC: 1.6.5.-

Q15SU5

MKNVLVLNASLQGENGNSSQLTSEFVTQLQQTESIKVEKVDLNTLNLPHLSAQEMQTWSMLSDNMTNDQAALAAYSNELLAQLERSDVIVVGMPMYNFTIPSTFKAWIDRVARAGRTFSYTSEGPKGHLQGKTVYIFAARGGIYQGTDNDTQTPYLKLVFGLMGITDVNFIYLEGLNMGEEYAQTSWQQARESLTTLLPATV

Cofactor: Binds 1 FMN per subunit. Function: Quinone reductase that provides resistance to thiol-specific stress caused by electrophilic quinones. Catalytic Activity: 2 a quinone + H(+) + NADH = 2 a 1,4-benzosemiquinone + NAD(+) Sequence Mass (Da): 22417 Sequence Length: 202 EC: 1.6.5.-

A1SUA7

MINFLALKSSILGDYSSSSKLIDELLAKYTPQQAIITEHDLAEQPLPVLDGEIAMAMRSPEQLNDKQRDALALSDKLISELVASDLLVIAAPMYNFMIPTQLKNWIDLVARAGKTFSYTEQGPQGLISGTRAIIVTTRGGMHKEQGTDQQVPYLKTVLNFMGISDIEVVYAESLAMGPETAELNLEQARKQLSVFTNDISTLNSQS

Cofactor: Binds 1 FMN per subunit. Function: Quinone reductase that provides resistance to thiol-specific stress caused by electrophilic quinones. Catalytic Activity: 2 a quinone + H(+) + NADH = 2 a 1,4-benzosemiquinone + NAD(+) Sequence Mass (Da): 22635 Sequence Length: 206 EC: 1.6.5.-

Q8XQG9

MQVLHLDSSILGDASASRILTAAIVDELRRDNPGATVIHRDLAVEAIPHLDGAIAAGFRATGADGFDAVTLAEHARSEALVGELLASDVIVVGAPMYNFSVPSQLKAWIDRVAQAGRTFKYTETGPVGLTGGKKVIVASTRGGMYSAGPTAAMDFQEAYLKTVFGFLGITDVQFVRAERLAMGPDARAQALEAAHAAMHDVVNQAIAA

Cofactor: Binds 1 FMN per subunit. Function: Quinone reductase that provides resistance to thiol-specific stress caused by electrophilic quinones. Catalytic Activity: 2 a quinone + H(+) + NADH = 2 a 1,4-benzosemiquinone + NAD(+) Sequence Mass (Da): 21773 Sequence Length: 208 EC: 1.6.5.-

Q98IF8

MSILLVTSSPRGAASHSTRIATEFAEKLLAADPSNTLVVRDLVANPLPHIDADYATGIYTPVEARTPRQAEVVGVSDVVLDELFAADTVILATGFINFNISSTLKSWVDHIARSGRSFAYGENGPKGLVTGKKVYIVLASGGIYSEGAAVQFDHAIPYLRGVLGFLGMTDVDVIRIEGVGMGPDAVTAALAKATAKVDAVVASQQAAAAA

Cofactor: Binds 1 FMN per subunit. Function: Quinone reductase that provides resistance to thiol-specific stress caused by electrophilic quinones. Catalytic Activity: 2 a quinone + H(+) + NADH = 2 a 1,4-benzosemiquinone + NAD(+) Sequence Mass (Da): 21813 Sequence Length: 210 EC: 1.6.5.-

P53563

MSQSNRELVVDFLSYKLSQKGYSWSQFSDVEENRTEAPEETEPERETPSAINGNPSWHLADSPAVNGATGHSSSLDAREVIPMAAVKQALREAGDEFELRYRRAFSDLTSQLHITPGTAYQSFEQVVNELFRDGVNWGRIVAFFSFGGALCVESVDKEMQVLVSRIASWMATYLNDHLEPWIQENGGWDTFVDLYGNNAAAESRKGQERFNRWFLTGMTVAGVVLLGSLFSRK

Function: Potent inhibitor of cell death. Inhibits activation of caspases. Appears to regulate cell death by blocking the voltage-dependent anion channel (VDAC) by binding to it and preventing the release of the caspase activator, CYC1, from the mitochondrial membrane. Also acts as a regulator of G2 checkpoint and progression to cytokinesis during mitosis. PTM: Proteolytically cleaved by caspases during apoptosis. The cleaved protein, lacking the BH4 motif, has pro-apoptotic activity (By similarity). Location Topology: Single-pass membrane protein Sequence Mass (Da): 26158 Sequence Length: 233 Domain: The BH4 motif is required for anti-apoptotic activity. The BH1 and BH2 motifs are required for both heterodimerization with other Bcl-2 family members and for repression of cell death. Subcellular Location: Mitochondrion inner membrane

Q1RMX3

MATPASAPDTRALVADFVGYKLRQKGYVCGAGPGEGPAADPLHQAMRAAGDEFETRFRRTFSDLAAQLHVTPGSAQQRFTQVSDELFQGGPNWGRLVAFFVFGAALCAESVNKEMEPLVGQVQEWMVAYLETRLADWIHSSGGWAEFTALYGDGALEEARRLREGNWASVRTVLTGAVALGALVTVGAFFASK

Function: Promotes cell survival. Blocks dexamethasone-induced apoptosis. Mediates survival of postmitotic Sertoli cells by suppressing death-promoting activity of BAX (By similarity). Location Topology: Peripheral membrane protein Sequence Mass (Da): 20774 Sequence Length: 193 Domain: The BH4 motif seems to be involved in the anti-apoptotic function. Subcellular Location: Mitochondrion membrane

Q92843

MATPASAPDTRALVADFVGYKLRQKGYVCGAGPGEGPAADPLHQAMRAAGDEFETRFRRTFSDLAAQLHVTPGSAQQRFTQVSDELFQGGPNWGRLVAFFVFGAALCAESVNKEMEPLVGQVQEWMVAYLETQLADWIHSSGGWAEFTALYGDGALEEARRLREGNWASVRTVLTGAVALGALVTVGAFFASK

Function: Promotes cell survival. Blocks dexamethasone-induced apoptosis. Mediates survival of postmitotic Sertoli cells by suppressing death-promoting activity of BAX. Location Topology: Peripheral membrane protein Sequence Mass (Da): 20746 Sequence Length: 193 Domain: The BH4 motif seems to be involved in the anti-apoptotic function. Subcellular Location: Mitochondrion membrane

Q91Z92

MKVFRRAWRHRVALGLGGLAFCGTTLLYLARCASEGETPSASGAARPRAKAFLAVLVASAPRAVERRTAVRSTWLAPERRGGPEDVWARFAVGTGGLGSEERRALELEQAQHGDLLLLPALRDAYENLTAKVLAMLTWLDERVDFEFVLKADDDSFARLDAILVDLRAREPARRRRLYWGFFSGRGRVKPGGRWREAAWQLCDYYLPYALGGGYVLSADLVHYLRLSREYLRAWHSEDVSLGTWLAPVDVQREHDPRFDTEYKSRGCNNQYLVTHKQSPEDMLEKQQMLLHEGRLCKHEVQLRLSYVYDWSAPPSQCCQRKEGVP

Function: Beta-1,3-galactosyltransferase that transfers galactose from UDP-galactose to substrates with a terminal beta-linked galactose residue. Has a preference for galactose-beta-1,4-xylose that is found in the linker region of glycosaminoglycans, such as heparan sulfate and chondroitin sulfate. Has no activity towards substrates with terminal glucosamine or galactosamine residues. Catalytic Activity: 3-O-(beta-D-galactosyl-(1->4)-beta-D-xylosyl)-L-seryl-[protein] + UDP-alpha-D-galactose = 3-O-(beta-D-galactosyl-(1->3)-beta-D-galactosyl-(1->4)-beta-D-xylosyl)-L-seryl-[protein] + H(+) + UDP Location Topology: Single-pass type II membrane protein Sequence Mass (Da): 37021 Sequence Length: 325 Pathway: Glycan metabolism; chondroitin sulfate biosynthesis. Subcellular Location: Golgi apparatus EC: 2.4.1.134

Q6NQB7

MKHKVSKRVISLKWVPFLCISFFALGAIFTSRSWEPSSDSGSQLISQHHRDHELQIVSDDCAHNKKATQEKDVTGEVLRTHEAIQDDRSLDKSVSTLSSTRSSQEMVDGSETNPRKKVFMVMGINTAFSSRKRRDSVRETWMPQGEKLERLEQEKGIVIKFMIGHSATSNSILDRAIDSEDAQHKDFLRLEHVEGYHELSAKTKIFFSTAVAKWDAEFYIKVDDDVHVNLGMLASTLARHRSKPRVYIGCMKSGPVLAQNLLNCFRTVKYHEPEYWKFGEDGNKYFRHATGQIYAISKDLANYISINQPILHKYANEDVSLGSWFIGLEVEHIDDRNFCCGTPPDCRWKAEAGDVCVASFEWSCSGICKSVERMKIVHEVCSEGEGAVWNTLL

Function: Beta-1,3-galactosyltransferase that transfers galactose from UDP-galactose to substrates with a terminal glycosyl residue. Location Topology: Single-pass type II membrane protein Sequence Mass (Da): 44675 Sequence Length: 393 Pathway: Protein modification; protein glycosylation. Subcellular Location: Golgi apparatus membrane EC: 2.4.1.-

Q9C809

MRAKAASGKAIIVLCLASFLAGSLFMSRTLSRSYIPEEEDHHLTKHLSKHLEIQKDCDEHKRKLIESKSRDIIGEVSRTHQAVKSLERTMSTLEMELAAARTSDRSSEFWSERSAKNQSRLQKVFAVIGINTAFSSKKRRDSVRQTWMPTGEKLKKIEKEKGIVVRFVIGHSATPGGVLDKAIDEEDSEHKDFLRLKHIEGYHQLSTKTRLYFSTATAMYDAEFYVKVDDDVHVNLGMLVTTLARYQSRPRIYIGCMKSGPVLSQKGVKYHEPEFWKFGEEGNKYFRHATGQIYAISKDLATYISTNQGILHRYANEDVSLGAWMLGLEVEHVDERSMCCGTPPDCQWKAQAGNVCAASFDWSCSGICKSVDRMARVHRACAEGDTPLANFRFFV

Function: Beta-1,3-galactosyltransferase that transfers galactose from UDP-galactose to substrates with a terminal glycosyl residue. Location Topology: Single-pass type II membrane protein Sequence Mass (Da): 44732 Sequence Length: 395 Pathway: Protein modification; protein glycosylation. Subcellular Location: Golgi apparatus membrane EC: 2.4.1.-

Q5XEZ1

MESLPTTVPSKSERRARSSKFSQSSSKPSVIMAFFSCVAWLYVAGRLWQDAENRVVLNNILKKSYDQKPKVLTVDDKLMVLGCKDLERRIVETEMELTLAKSQGYLKNLKSGSSSGKKLLAVIGVYSGFGSHLRRNTFRGSYMPQGDALRKLEERGIVIRFVIGRSPNRGDSLDRKIDEENQARKDFLILENHEEAQEELAKKVKFFFSAAVQNWDAEFYIKVDDNIDLDLEGLIGLLESRRGQDAAYIGCMKSGEVVAEEGGKWYEPEWWKFGDEKSYFRHAAGSLLILSKTLAQYVNINSGSLKTYAFDDTSIGSWMIGVQATYIDDNRLCCSSIRQDKVCSVA

Function: Possesses hydroxyproline O-galactosyltransferase activity. Transfers galactose from UDP-galactose to hydroxyproline residues in the arabinogalactan proteins (AGPs). Is specific for AGPs containing non-contiguous peptidyl hydroxyproline residues. The addition of galactose onto the peptidyl hydroxyproline residues in AGP core proteins represents the first committed step in arabinogalactan polysaccharide addition. AGP glycans play essential roles in both vegetative and reproductive plant growth. Location Topology: Single-pass type II membrane protein Sequence Mass (Da): 39059 Sequence Length: 346 Pathway: Protein modification; protein glycosylation. Subcellular Location: Golgi apparatus membrane EC: 2.4.1.-

A8MXE2

MQVTFCRLRTHQWCFILFNVILFHALLFGTDFVEEYFLHSLPYIDVKVLEIKNKARKLNIEPLRSNLSKYYVLSQSEICKGKNIFLLSLIFSSPGNGTRRDLIRKTWGNVTSVQGHPILTLFALGMPVSVTTQKEINKESCKNNDIIEGIFLDSSENQTLKIIAMIQWAVAFCPNALFILKVDEETFVNLPSLVDYLLNLKEHLEDIYVGRVLHQVTPNRDPQNRDFVPLSEYPEKYYPDYCSGEAFIMSQDVARMMYVVFKEVPMMVPADVFVGICAKFIGLIPIHSSRFSGKRHIRYNRCCYKFIFTSSEIADPEMPLAWKEINDGKECTLFETSYELISCKLLTYLDSFKRFHMGTIKNNLMYFAD

Function: Putative glycosyltransferase that could catalyze the transfer of galactose residues from UDP-alpha-D-galactose. Location Topology: Single-pass type II membrane protein Sequence Mass (Da): 42761 Sequence Length: 369 Subcellular Location: Golgi apparatus membrane EC: 2.4.1.-

Q94A05

MESLPTTVSGKSDRRGRFSKSQNTSKPSLILAFFSCLAWLYVAGRLWQDAQYRAALNTVLKMNYDQRPKVLTVEDKLVVLGCKDLERRIVETEMELAQAKSQGYLKKQKSVSSSGKKMLAVIGVYTGFGSHLKRNKFRGSWMPRDDALKKLEERGVVIRFVIGRSANRGDSLDRKIDEENRATKDFLILENHEEAQEELPKKVKFFYSAAVQNWDAEFYVKVDDNVDLDLEGMIALLESRRSQDGAYIGCMKSGDVITEEGSQWYEPEWWKFGDDKSYFRHATGSLVILSKNLAQYVNINSGLLKTYAFDDTTIGSWMIGVQATYIDDNRLCCSSTRQEKVCSMA

Function: Possesses hydroxyproline O-galactosyltransferase activity. Transfers galactose from UDP-galactose to hydroxyproline residues in the arabinogalactan proteins (AGPs). Is specific for AGPs containing non-contiguous peptidyl hydroxyproline residues. The addition of galactose onto the peptidyl hydroxyproline residues in AGP core proteins represents the first committed step in arabinogalactan polysaccharide addition. AGP glycans play essential roles in both vegetative and reproductive plant growth. Location Topology: Single-pass type II membrane protein Sequence Mass (Da): 39272 Sequence Length: 345 Pathway: Protein modification; protein glycosylation. Subcellular Location: Golgi apparatus membrane EC: 2.4.1.-

Q94F27

MARKGSSIRLSSSRISTLLLFMFATFASFYVAGRLWQESQTRVHLINELDRVTGQGKSAISVDDTLKIIACREQKKTLAALEMELSSARQEGFVSKSPKLADGTETKKRPLVVIGIMTSLGNKKKRDAVRQAWMGTGASLKKLESEKGVIARFVIGRSANKGDSMDKSIDTENSQTDDFIILDDVVEAPEEASKKVKLFFAYAADRWDAQFYAKAIDNIYVNIDALGTTLAAHLENPRAYIGCMKSGEVFSEPNHKWYEPEWWKFGDKKAYFRHAYGEMYVITHALARFVSINRDILHSYAHDDVSTGSWFVGLDVKHVDEGKFCCSAWSSEAICAGV

Function: Possesses hydroxyproline O-galactosyltransferase activity. Transfers galactose from UDP-galactose to hydroxyproline residues in the arabinogalactan proteins (AGPs). Is specific for AGPs containing non-contiguous peptidyl hydroxyproline residues. The addition of galactose onto the peptidyl hydroxyproline residues in AGP core proteins represents the first committed step in arabinogalactan polysaccharide addition. AGP glycans play essential roles in both vegetative and reproductive plant growth. Location Topology: Single-pass type II membrane protein Sequence Mass (Da): 37768 Sequence Length: 338 Pathway: Protein modification; protein glycosylation. Subcellular Location: Golgi apparatus membrane EC: 2.4.1.-

Q66GS2

MPLFSHRFTTASSSSPASPSYYNKPSSKTHKPNSSSSSYTSSRIHVAIIFFSLVSVFIGVAGTIFALSSTGPASVYRCGGSKDTSRVVSASRKLGGDGGNNGVVVERRKLLGFVGIQTGFDSGDRRTALRSTWFPSDPDSLLRLEQATGLAFRFVIGKSKDAKKMAELEKEIKEYRDFVLLDTEEEYIRLPYKTLAFFKAAFKLFEADYYVKADDDIYLRPDRLATLLANERLHSQTYIGCMKKGPVITDPKLKWYEKQGNLIGNEYFLHAYGPIYVLSAEIVASLAAARNGSLRMFNNEDVTIGSWMLAMDVHHEDNRALCDPHCSPKSIAVWDIPKCSGLCDPESRLKELHKTDMCSKSPTLPPDDIDQ

Function: Beta-1,3-galactosyltransferase that transfers galactose from UDP-galactose to substrates with a terminal glycosyl residue. Location Topology: Single-pass type II membrane protein Sequence Mass (Da): 41217 Sequence Length: 371 Pathway: Protein modification; protein glycosylation. Subcellular Location: Golgi apparatus membrane EC: 2.4.1.-

Q8L7M1

MHSPRKLFHARSSLATRRSTALVVLTSLAIGIAGFTFGLAVILIPGLRLTGRNCLTNTPPKTVRVVWDVAGNSNGVVSGEKKRHKVMGFVGIQTGFGSAGRRRSLRKTWMPSDPEGLRRLEESTGLAIRFMIGKTKSEEKMAQLRREIAEYDDFVLLDIEEEYSKLPYKTLAFFKAAYALYDSEFYVKADDDIYLRPDRLSLLLAKERSHSQTYLGCLKKGPVFTDPKLKWYEPLSHLLGKEYFLHAYGPIYALSADVVASLVALKNNSFRMFNNEDVTIGAWMLAMNVNHENHHILCEPECSPSSVAVWDIPKCSGLCNPEKRMLELHKQESCSKSPTLPSDDE

Function: Beta-1,3-galactosyltransferase that transfers galactose from UDP-galactose to substrates with a terminal glycosyl residue. Location Topology: Single-pass type II membrane protein Sequence Mass (Da): 38777 Sequence Length: 345 Pathway: Protein modification; protein glycosylation. Subcellular Location: Golgi apparatus membrane EC: 2.4.1.-

Q8L7F9

MKRFYGGLLVVSMCMFLTVYRYVDLNTPVEKPYITAAASVVVTPNTTLPMEWLRITLPDFMKEARNTQEAISGDDIAVVSGLFVEQNVSKEEREPLLTWNRLESLVDNAQSLVNGVDAIKEAGIVWESLVSAVEAKKLVDVNENQTRKGKEELCPQFLSKMNATEADGSSLKLQIPCGLTQGSSITVIGIPDGLVGSFRIDLTGQPLPGEPDPPIIVHYNVRLLGDKSTEDPVIVQNSWTASQDWGAEERCPKFDPDMNKKVDDLDECNKMVGGEINRTSSTSLQSNTSRGVPVAREASKHEKYFPFKQGFLSVATLRVGTEGMQMTVDGKHITSFAFRDTLEPWLVSEIRITGDFRLISILASGLPTSEESEHVVDLEALKSPTLSPLRPLDLVIGVFSTANNFKRRMAVRRTWMQYDDVRSGRVAVRFFVGLHKSPLVNLELWNEARTYGDVQLMPFVDYYSLISWKTLAICIFGTEVDSAKFIMKTDDDAFVRVDEVLLSLSMTNNTRGLIYGLINSDSQPIRNPDSKWYISYEEWPEEKYPPWAHGPGYIVSRDIAESVGKLFKEGNLKMFKLEDVAMGIWIAELTKHGLEPHYENDGRIISDGCKDGYVVAHYQSPAEMTCLWRKYQETKRSLCCREW

Function: Beta-1,3-galactosyltransferase that transfers galactose from UDP-galactose to substrates with a terminal beta-N-acetylglucosamine (beta-GlcNAc) residue. Involved in the biosynthesis of N-glycans containing Lewis a structures (with the combination of FUT13). Location Topology: Single-pass type II membrane protein Sequence Mass (Da): 72323 Sequence Length: 643 Pathway: Protein modification; protein glycosylation. Subcellular Location: Golgi apparatus membrane EC: 2.4.1.-

Q9ASW1

MKQFMSVVRFKFGFTSVRMRDWSVGVSIMVLTLIFIIRYEQSDHTHTVDDSSIEGESVHEPAKKPHFMTLEDLDYLFSNKSFFGEEEVSNGMLVWSRMRPFLERPDALPETAQGIEEATLAMKGLVLEINREKRAYSSGMVSKEIRRICPDFVTAFDKDLSGLSHVLLELPCGLIEDSSITLVGIPDEHSSSFQIQLVGSGLSGETRRPIILRYNVNFSKPSIVQNTWTEKLGWGNEERCQYHGSLKNHLVDELPLCNKQTGRIISEKSSNDDATMELSLSNANFPFLKGSPFTAALWFGLEGFHMTINGRHETSFAYREKLEPWLVSAVKVSGGLKILSVLATRLPIPDDHASLIIEEKLKAPSLSGTRIELLVGVFSTGNNFKRRMALRRSWMQYEAVRSGKVAVRFLIGLHTNEKVNLEMWRESKAYGDIQFMPFVDYYGLLSLKTVALCILGTKVIPAKYIMKTDDDAFVRIDELLSSLEERPSSALLYGLISFDSSPDREQGSKWFIPKEEWPLDSYPPWAHGPGYIISHDIAKFVVKGHRQRDLGLFKLEDVAMGIWIQQFNQTIKRVKYINDKRFHNSDCKSNYILVHYQTPRLILCLWEKLQKENQSICCE

Function: Possesses hydroxyproline O-galactosyltransferase activity. Transfers galactose from UDP-galactose to hydroxyproline residues in the arabinogalactan proteins (AGPs). Is specific for AGPs containing non-contiguous peptidyl hydroxyproline residues. Utilizes UDP-galactose solely as sugar donor. The addition of galactose onto the peptidyl hydroxyproline residues in AGP core proteins represents the first committed step in arabinogalactan polysaccharide addition. AGP glycans play essential roles in both vegetative and reproductive plant growth. Location Topology: Single-pass type II membrane protein Sequence Mass (Da): 70635 Sequence Length: 619 Pathway: Protein modification; protein glycosylation. Subcellular Location: Golgi apparatus membrane EC: 2.4.1.-

Q8GXG6

MKKSKLDNSSSQIRFGLVQFLLVVLLFYFLCMSFEIPFIFRTGSGSGSDDVSSSSFADALPRPMVVGGGSREANWVVGEEEEADPHRHFKDPGRVQLRLPERKMREFKSVSEIFVNESFFDNGGFSDEFSIFHKTAKHAISMGRKMWDGLDSGLIKPDKAPVKTRIEKCPDMVSVSESEFVNRSRILVLPCGLTLGSHITVVATPHWAHVEKDGDKTAMVSQFMMELQGLKAVDGEDPPRILHFNPRIKGDWSGRPVIEQNTCYRMQWGSGLRCDGRESSDDEEYVDGEVKCERWKRDDDDGGNNGDDFDESKKTWWLNRLMGRRKKMITHDWDYPFAEGKLFVLTLRAGMEGYHISVNGRHITSFPYRTGFVLEDATGLAVKGNIDVHSVYAASLPSTNPSFAPQKHLEMQRIWKAPSLPQKPVELFIGILSAGNHFAERMAVRKSWMQQKLVRSSKVVARFFVALHARKEVNVDLKKEAEYFGDIVIVPYMDHYDLVVLKTVAICEYGVNTVAAKYVMKCDDDTFVRVDAVIQEAEKVKGRESLYIGNINFNHKPLRTGKWAVTFEEWPEEYYPPYANGPGYILSYDVAKFIVDDFEQKRLRLFKMEDVSMGMWVEKFNETRPVAVVHSLKFCQFGCIEDYFTAHYQSPRQMICMWDKLQRLGKPQCCNMR

Function: Possesses hydroxyproline O-galactosyltransferase activity. Transfers galactose from UDP-galactose to hydroxyproline residues in the arabinogalactan proteins (AGPs). Is specific for AGPs containing non-contiguous peptidyl hydroxyproline residues. Utilizes UDP-galactose solely as sugar donor. The addition of galactose onto the peptidyl hydroxyproline residues in AGP core proteins represents the first committed step in arabinogalactan polysaccharide addition. AGP glycans play essential roles in both vegetative and reproductive plant growth. Location Topology: Single-pass type II membrane protein Sequence Mass (Da): 77037 Sequence Length: 673 Pathway: Protein modification; protein glycosylation. Subcellular Location: Golgi apparatus membrane EC: 2.4.1.-

Q8RX55

MKKPKLSKVEKIDKIDLFSSLWKQRSVRVIMAIGFLYLVIVSVEIPLVFKSWSSSSVPLDALSRLEKLNNEQEPQVEIIPNPPLEPVSYPVSNPTIVTRTDLVQNKVREHHRGVLSSLRFDSETFDPSSKDGSVELHKSAKEAWQLGRKLWKELESGRLEKLVEKPEKNKPDSCPHSVSLTGSEFMNRENKLMELPCGLTLGSHITLVGRPRKAHPKEGDWSKLVSQFVIELQGLKTVEGEDPPRILHFNPRLKGDWSKKPVIEQNSCYRMQWGPAQRCEGWKSRDDEETVDSHVKCEKWIRDDDNYSEGSRARWWLNRLIGRRKRVKVEWPFPFVEEKLFVLTLSAGLEGYHINVDGKHVTSFPYRTGFTLEDATGLTVNGDIDVHSVFVASLPTSHPSFAPQRHLELSKRWQAPVVPDGPVEIFIGILSAGNHFSERMAVRKSWMQHVLITSAKVVARFFVALHGRKEVNVELKKEAEYFGDIVLVPYMDSYDLVVLKTVAICEHGALAFSAKYIMKCDDDTFVKLGAVINEVKKVPEGRSLYIGNMNYYHKPLRGGKWAVTYEEWPEEDYPPYANGPGYVLSSDIARFIVDKFERHKLRLFKMEDVSVGMWVEHFKNTTNPVDYRHSLRFCQFGCVENYYTAHYQSPRQMICLWDKLLRQNKPECCNMR

Function: Possesses hydroxyproline O-galactosyltransferase activity. Transfers galactose from UDP-galactose to hydroxyproline residues in the arabinogalactan proteins (AGPs). Is specific for AGPs containing non-contiguous peptidyl hydroxyproline residues. Utilizes UDP-galactose solely as sugar donor. The addition of galactose onto the peptidyl hydroxyproline residues in AGP core proteins represents the first committed step in arabinogalactan polysaccharide addition. AGP glycans play essential roles in both vegetative and reproductive plant growth. Location Topology: Single-pass type II membrane protein Sequence Mass (Da): 77348 Sequence Length: 672 Pathway: Protein modification; protein glycosylation. Subcellular Location: Golgi apparatus membrane EC: 2.4.1.-

Q9LV16

MRKPKLSKLERLEKFDIFVSLSKQRSVQILMAVGLLYMLLITFEIPFVFKTGLSSLSQDPLTRPEKHNSQRELQERRAPTRPLKSLLYQESQSESPAQGLRRRTRILSSLRFDPETFNPSSKDGSVELHKSAKVAWEVGRKIWEELESGKTLKALEKEKKKKIEEHGTNSCSLSVSLTGSDLLKRGNIMELPCGLTLGSHITVVGKPRAAHSEKDPKISMLKEGDEAVKVSQFKLELQGLKAVEGEEPPRILHLNPRLKGDWSGKPVIEQNTCYRMQWGSAQRCEGWRSRDDEETVDGQVKCEKWARDDSITSKEEESSKAASWWLSRLIGRSKKVTVEWPFPFTVDKLFVLTLSAGLEGYHVSVDGKHVTSFPYRTGFTLEDATGLTINGDIDVHSVFAGSLPTSHPSFSPQRHLELSSNWQAPSLPDEQVDMFIGILSAGNHFAERMAVRRSWMQHKLVKSSKVVARFFVALHSRKEVNVELKKEAEFFGDIVIVPYMDSYDLVVLKTVAICEYGAHQLAAKFIMKCDDDTFVQVDAVLSEAKKTPTDRSLYIGNINYYHKPLRQGKWSVTYEEWPEEDYPPYANGPGYILSNDISRFIVKEFEKHKLRMFKMEDVSVGMWVEQFNNGTKPVDYIHSLRFCQFGCIENYLTAHYQSPRQMICLWDKLVLTGKPQCCNMR

Function: Possesses hydroxyproline O-galactosyltransferase activity. Transfers galactose from UDP-galactose to hydroxyproline residues in the arabinogalactan proteins (AGPs). Is specific for AGPs containing non-contiguous peptidyl hydroxyproline residues. Utilizes UDP-galactose solely as sugar donor. The addition of galactose onto the peptidyl hydroxyproline residues in AGP core proteins represents the first committed step in arabinogalactan polysaccharide addition. AGP glycans play essential roles in both vegetative and reproductive plant growth. Location Topology: Single-pass type II membrane protein Sequence Mass (Da): 77741 Sequence Length: 681 Pathway: Protein modification; protein glycosylation. Subcellular Location: Golgi apparatus membrane EC: 2.4.1.-

A7XDQ9

MKRVKSESFRGVYSSRRFKLSHFLLAIAGFYLVFLAFKFPHFIEMVAMLSGDTGLDGALSDTSLDVSLSGSLRNDMLNRKLEDEDHQSGPSTTQKVSPEEKINGSKQIQPLLFRYGRISGEVMRRRNRTIHMSPFERMADEAWILGSKAWEDVDKFEVDKINESASIFEGKVESCPSQISMNGDDLNKANRIMLLPCGLAAGSSITILGTPQYAHKESVPQRSRLTRSYGMVLVSQFMVELQGLKTGDGEYPPKILHLNPRIKGDWNHRPVIEHNTCYRMQWGVAQRCDGTPSKKDADVLVDGFRRCEKWTQNDIIDMVDSKESKTTSWFKRFIGREQKPEVTWSFPFAEGKVFVLTLRAGIDGFHINVGGRHVSSFPYRPGFTIEDATGLAVTGDVDIHSIHATSLSTSHPSFSPQKAIEFSSEWKAPPLPGTPFRLFMGVLSATNHFSERMAVRKTWMQHPSIKSSDVVARFFVALNPRKEVNAMLKKEAEYFGDIVILPFMDRYELVVLKTIAICEFGVQNVTAPYIMKCDDDTFIRVESILKQIDGVSPEKSLYMGNLNLRHRPLRTGKWTVTWEEWPEAVYPPYANGPGYIISSNIAKYIVSQNSRHKLRLFKMEDVSMGLWVEQFNASMQPVEYSHSWKFCQYGCTLNYYTAHYQSPSQMMCLWDNLLKGRPQCCNFR

Function: Possesses hydroxyproline O-galactosyltransferase activity. Transfers galactose from UDP-galactose to hydroxyproline residues in the arabinogalactan proteins (AGPs). Is specific for AGPs containing non-contiguous peptidyl hydroxyproline residues. Utilizes UDP-galactose solely as sugar donor. The addition of galactose onto the peptidyl hydroxyproline residues in AGP core proteins represents the first committed step in arabinogalactan polysaccharide addition. AGP glycans play essential roles in both vegetative and reproductive plant growth. Location Topology: Single-pass type II membrane protein Sequence Mass (Da): 77912 Sequence Length: 684 Pathway: Protein modification; protein glycosylation. Subcellular Location: Golgi apparatus membrane EC: 2.4.1.-

P0DUT8

MASEMNASPEYTGYRLEVFIAVFTPLTIIAVALRFYARSLTSKKIDSGDWLIIAALVGQIVAGGIAIGAVKQAGVGHHAAYLAETNPETLVAFFKYLVAMSTWYATTEGLAKLAVCILYKRLFPQRGIHMVINTTMLVLVGASVGGGLADLFGCTPFSAHWGTAEEQAAHCIDTEALFVWGSFPNIVTDVVLLVLPMPIVWGLHASVRLRLVLVLTFLFGSIFGELIGGDSGLITSVLRFIAFYNKSSFIDPTFHAVELIIWTVCEPGVYLIAACLLVYRPLLEKIGIPLVGGVSSRGGNRQEPTELAFQKPSRPRNGAVIKSIGSGSISESGFEYIGDDDQRPLRRQGGITATTNVEVTWAAGSAV

Function: Part of the gene cluster that mediates the biosynthesis of (2Z,4E,6E,10E)-9-hydroxydodeca-2,4,6,10-tetraenoic acid (BAA), (2E,4E,6E,10E)-9-hydroxydodeca-2,4,6,10-tetraenoic acid (BAB), and (2Z,4E,6E)-octa-2,4,6-trienedioic acid (PBA) . The highly reducing polyketide synthase Ba17a is sufficent to produce PBA and BAA . The still to be characterized protein Ba17b leads to an increased production of BAA as well as to the production of the new compound BAB . BAA does not possess insecticidal activity against G.mellonella larvae, however, both BAA and BAB increase the growth of Candida albicans and BAA can mitigate the fungicidal effects of fluconazole over C.albicans, suggesting that generalist pathogens such as M.anisopliae, can potentially manipulate the yeast microbiota found in arthropods (and anywhere else) by the activity of compounds as BAA and BAB . Location Topology: Multi-pass membrane protein Sequence Mass (Da): 39430 Sequence Length: 367 Pathway: Secondary metabolite biosynthesis. Subcellular Location: Membrane

Q8WXS3

MGCGGSRADAIEPRYYESWTRETESTWLTYTDSDAPPSAAAPDSGPEAGGLHSGMLEDGLPSNGVPRSTAPGGIPNPEKKTNCETQCPNPQSLSSGPLTQKQNGLQTTEAKRDAKRMPAKEVTINVTDSIQQMDRSRRITKNCVN

Function: May play a synaptic role at the postsynaptic lipid rafts possibly through interaction with CAMK2A. PTM: Palmitoylation and myristoylation target the protein to the lipid rafts. Sequence Mass (Da): 15551 Sequence Length: 145 Subcellular Location: Cytoplasm

Q8VHV1

MGCGGSRADAIEPRYYESWTRETESTWLTYTDSDALPSAAATDSGPEAGGLHAGVLEDGLSSNGVLRPAAPGGIANPEKKMNCGTQCPNSQNLSSGPLTQKQNGLWATEAKRDAKRMSAREVAINVTENIRQMDRSKRVTKNCIN

Function: May play a synaptic role at the postsynaptic lipid rafts possibly through interaction with CAMK2A. PTM: Palmitoylation and myristoylation target the protein to the lipid rafts. Sequence Mass (Da): 15515 Sequence Length: 145 Subcellular Location: Cytoplasm

Q8WNE9

MGCGGSRADAIEPRYYESWTRETESTWLTYTDSDAPPSNAAPDSGPEAGGLQAGVLEDGVSANGVPRSTAPGGTSNPEKKMSCGTQCPNPQSLGSGPLTQKQNGLRTTEAKRDAKRTSAKEVTINVTESIRQVDRNQRITKKCIN

Function: May play a synaptic role at the postsynaptic lipid rafts possibly through interaction with CAMK2A. PTM: Palmitoylation and myristoylation target the protein to the lipid rafts. Sequence Mass (Da): 15401 Sequence Length: 145 Subcellular Location: Cytoplasm

Q920K5

MGCGGSRADAIEPRYYESWTRETESTWLTYTDSDALPSAAATDSGPEAGGLHAGVLEDGPSSNGVLRPAAPGGIANPEKKMNCGTQCPNSQSLSSGPLTQKQNGLWTTEAKRDAKRMSAREVAISVTENIRQMDRSKRVTKNCIN

Function: May play a synaptic role at the postsynaptic lipid rafts possibly through interaction with CAMK2A. PTM: Palmitoylation and myristoylation target the protein to the lipid rafts. Sequence Mass (Da): 15475 Sequence Length: 145 Subcellular Location: Cytoplasm

Q14032

MIQLTATPVSALVDEPVHIRATGLIPFQMVSFQASLEDENGDMFYSQAHYRANEFGEVDLNHASSLGGDYMGVHPMGLFWSLKPEKLLTRLLKRDVMNRPFQVQVKLYDLELIVNNKVASAPKASLTLERWYVAPGVTRIKVREGRLRGALFLPPGEGLFPGVIDLFGGLGGLLEFRASLLASRGFASLALAYHNYEDLPRKPEVTDLEYFEEAANFLLRHPKVFGSGVGVVSVCQGVQIGLSMAIYLKQVTATVLINGTNFPFGIPQVYHGQIHQPLPHSAQLISTNALGLLELYRTFETTQVGASQYLFPIEEAQGQFLFIVGEGDKTINSKAHAEQAIGQLKRHGKNNWTLLSYPGAGHLIEPPYSPLCCASTTHDLRLHWGGEVIPHAAAQEHAWKEIQRFLRKHLIPDVTSQL

Function: Catalyzes the amidation of bile acids (BAs) with the amino acids taurine and glycine . More than 95% of the BAs are N-acyl amidates with glycine and taurine . Amidation of BAs in the liver with glycine or taurine prior to their excretion into bile is an important biochemical event in bile acid metabolism . This conjugation (or amidation) plays several important biological roles in that it promotes the secretion of BAs and cholesterol into bile and increases the detergent properties of BAs in the intestine, which facilitates lipid and vitamin absorption . May also act as an acyl-CoA thioesterase that regulates intracellular levels of free fatty acids . In vitro, catalyzes the hydrolysis of long- and very long-chain saturated acyl-CoAs to the free fatty acid and coenzyme A (CoASH), and conjugates glycine to these acyl-CoAs . Catalytic Activity: choloyl-CoA + glycine = CoA + glycocholate + H(+) Sequence Mass (Da): 46299 Sequence Length: 418 Subcellular Location: Cytoplasm EC: 2.3.1.65

Q91X34

MAKLTAVPLSALVDEPVHIQVTGLAPFQVVCLQASLKDEKGNLFSSQAFYRASEVGEVDLEHDPSLGGDYMGVHPMGLFWSLKPEKLLGRLIKRDVMNSPYQIHIKACHPYFPLQDIVVSPPLDSLTLERWYVAPGVKRIQVKESRIRGALFLPPGEGPFPGVIDLFGGAGGLMEFRASLLASRGFATLALAYWNYDDLPSRLEKVDLEYFEEGVEFLLRHPKVLGPGVGILSVCIGAEIGLSMAINLKQIRATVLINGPNFVSQSPHVYHGQVYPPVPSNEEFVVTNALGLVEFYRTFQETADKDSKYCFPIEKAHGHFLFVVGEDDKNLNSKVHANQAIAQLMKNGKKNWTLLSYPGAGHLIEPPYTPLCQASRMPILIPSLSWGGEVIPHAAAQEHSWKEIQKFLKQHLLPDLSSQL

Function: Catalyzes the amidation of bile acids (BAs) with the amino acid taurine . Selective for taurine conjugation of cholyl CoA and only taurine-conjugated BAs are found in bile . Amidation of BAs in the liver with taurine prior to their excretion into bile is an important biochemical event in bile acid metabolism (By similarity). This conjugation (or amidation) plays several important biological roles in that it promotes the secretion of BAs and cholesterol into bile and increases the detergent properties of BAs in the intestine, which facilitates lipid and vitamin absorption (By similarity). May also act as an acyl-CoA thioesterase that regulates intracellular levels of free fatty acids (By similarity). In vitro, catalyzes the hydrolysis of long- and very long-chain saturated acyl-CoAs to the free fatty acid and coenzyme A (CoASH), and conjugates glycine to these acyl-CoAs (By similarity). Catalytic Activity: choloyl-CoA + glycine = CoA + glycocholate + H(+) Sequence Mass (Da): 46482 Sequence Length: 420 Subcellular Location: Cytoplasm EC: 2.3.1.65

Q92934

MFQIPEFEPSEQEDSSSAERGLGPSPAGDGPSGSGKHHRQAPGLLWDASHQQEQPTSSSHHGGAGAVEIRSRHSSYPAGTEDDEGMGEEPSPFRGRSRSAPPNLWAAQRYGRELRRMSDEFVDSFKKGLPRPKSAGTATQMRQSSSWTRVFQSWWDRNLGRGSSAPSQ

Function: Promotes cell death. Successfully competes for the binding to Bcl-X(L), Bcl-2 and Bcl-W, thereby affecting the level of heterodimerization of these proteins with BAX. Can reverse the death repressor activity of Bcl-X(L), but not that of Bcl-2 (By similarity). Appears to act as a link between growth factor receptor signaling and the apoptotic pathways. PTM: Phosphorylated on one or more of Ser-75, Ser-99, Ser-118 and Ser-134 in response to survival stimuli, which blocks its pro-apoptotic activity. Phosphorylation on Ser-99 or Ser-75 promotes heterodimerization with 14-3-3 proteins. This interaction then facilitates the phosphorylation at Ser-118, a site within the BH3 motif, leading to the release of Bcl-X(L) and the promotion of cell survival. Ser-99 is the major site of AKT/PKB phosphorylation, Ser-118 the major site of protein kinase A (CAPK) phosphorylation. Phosphorylation at Ser-99 by PKB/AKT1 is almost completely blocked by the apoptotic C-terminus cleavage product of PKN2 generated by caspases-3 activity during apoptosis. Sequence Mass (Da): 18392 Sequence Length: 168 Domain: Intact BH3 motif is required by BIK, BID, BAK, BAD and BAX for their pro-apoptotic activity and for their interaction with anti-apoptotic members of the Bcl-2 family. Subcellular Location: Mitochondrion outer membrane

Q61337

MGTPKQPSLAPAHALGLRKSDPGIRSLGSDAGGRRWRPAAQSMFQIPEFEPSEQEDASATDRGLGPSLTEDQPGPYLAPGLLGSNIHQQGRAATNSHHGGAGAMETRSRHSSYPAGTEEDEGMEEELSPFRGRSRSAPPNLWAAQRYGRELRRMSDEFEGSFKGLPRPKSAGTATQMRQSAGWTRIIQSWWDRNLGKGGSTPSQ

Function: Promotes cell death. Successfully competes for the binding to Bcl-X(L), Bcl-2 and Bcl-W, thereby affecting the level of heterodimerization of these proteins with BAX. Can reverse the death repressor activity of Bcl-X(L), but not that of Bcl-2. Appears to act as a link between growth factor receptor signaling and the apoptotic pathways. PTM: Phosphorylated on one or more of Ser-112, Ser-136, Ser-155 and Ser-170 in response to survival stimuli, which blocks its pro-apoptotic activity. Phosphorylation on Ser-136 or Ser-112 promotes heterodimerization with 14-3-3 proteins. This interaction then facilitates the phosphorylation at Ser-155, a site within the BH3 motif, leading to the release of Bcl-X(L) and the promotion of cell survival. Ser-136 is the major site of AKT/PKB phosphorylation, Ser-155 the major site of protein kinase A (CAPK) phosphorylation. Sequence Mass (Da): 22080 Sequence Length: 204 Domain: Intact BH3 motif is required by BIK, BID, BAK, BAD and BAX for their pro-apoptotic activity and for their interaction with anti-apoptotic members of the Bcl-2 family. Subcellular Location: Mitochondrion outer membrane

A7Z4X8

MITYLFPGQGSQKQGMGSSLFDEFKDLTEQADETLGYSMKRLCLENPYSNLHKTQFTQPALYVVNVLSYLKKIQDNDIKPDYVAGHSLGEYNALFAAGAFDFITGLQLVRKRGELMSMATDGKMAAVMGLTAAQVSDALQTHGLHTIDIANMNSPHQVVISGRKEDIERAKSVFEGLKDVTMFHPLNVSGAFHSRYMSEAKQEFEKFLQSFHFSAISIPVISNVHARPYEQDGIHSVLADQIDHSVRWNDSIRYLLDKGRMEFEEVGPGHVLTGLIHRIKNETEASPAM

Function: Involved in some intermediate steps for the synthesis of the antibiotic polyketide bacillaene which is involved in secondary metabolism. It catalyzes the transfer of the malonyl-CoA group to the acyl-carrier-protein AcpK (Mal-AcpK) (By similarity). Catalytic Activity: holo-[ACP] + malonyl-CoA = CoA + malonyl-[ACP] Sequence Mass (Da): 32318 Sequence Length: 289 Pathway: Antibiotic biosynthesis; bacillaene biosynthesis. Subcellular Location: Cytoplasm EC: 2.3.1.39

A7Z4Y0

MISFVFPGQGSQRIGMGEDLFGRYPELTAKADHILGYSIQELCRDGERLNQTQFTQPALYVVNALSYLKKTEETGLKPDFTAGHSLGEYNALYASGAFDFEEGLQLVKKRGELMSRAKGGGMAAVIGLTHEQVTDVLRENHLDMIDIANMNTPQQIVISGYKEDIEKAASVFEAVNGVKMVHRLNVSGAFHSRYMLEAKEEFSRFIESFHFKPLSIPVISNVTARPYEQRELKETLTGQITGSVNWTDSIRFLMGRKNMSFEEIGPGKVLTGLIQRITAEAEPITDEIKVPAEAGKSSITAASLGNEEFKRDYQLKYAYLAGGMYRGISSKEMVVKLAEKGMMGFFGTGGLNIAHVEDAILSIQHELRDGGSFGINVVHNMKHTDSEEKMIDLLLKHGIQNLEASAFLTVTPALVRFRAKGLKRGAGGQIIARQRIIAKLSRPEVAEAFLSPAPDHILQKLAAENKITAEEASLMREIPVAHDICVEADSGGHTDGGVAYSLMPAIIRLRDDMMKKYRYGKTVRIGAAGGIGTPEAAMAAFMLGADFIVTGSINQCTVEAATSGLVKDLLQQMNVQDTAYAPAGDMFESGSKVQVLKKGLFFPTRASKLHELYQRHRSIEEIDEKTLRQIEEKYFKASVSSIYDKVKAHYSNEDISKAERNPKEKMALIFKWYFRQSSASAIKGDPDAKVDFQIHCGPALGAFNQWVKGTELESWKNRHADGIGMRLMEETASLLNQKLGSFLQTC

Function: Probably involved in some intermediate steps for the synthesis of the antibiotic polyketide bacillaene which is involved in secondary metabolism. Probably has an acyl transferase activity and could also have a flavin mononucleotide-dependent oxidoreductase activity. Catalytic Activity: holo-[ACP] + malonyl-CoA = CoA + malonyl-[ACP] Sequence Mass (Da): 82426 Sequence Length: 746 Pathway: Antibiotic biosynthesis; bacillaene biosynthesis. Subcellular Location: Cytoplasm

P69229

MTELPIDENTPRILIVEDEPKLGQLLIDYLRAASYAPTLISHGDQVLPYVRQTPPDLILLDLMLPGTDGLTLCREIRRFSDIPIVMVTAKIEEIDRLLGLEIGADDYICKPYSPREVVARVKTILRRCKPQRELQQQDAESPLIIDEGRFQASWRGKMLDLTPAEFRLLKTLSHEPGKVFSREQLLNHLYDDYRVVTDRTIDSHIKNLRRKLESLDAEQSFIRAVYGVGYRWEADACRIV

Function: Member of the two-component regulatory system BaeS/BaeR. Activates the mdtABCD operon (By similarity). PTM: Phosphorylated by BaeS. Sequence Mass (Da): 27656 Sequence Length: 240 Subcellular Location: Cytoplasm

P30847

MKFWRPGITGKLFLAIFATCIVLLISMHWAVRISFERGFIDYIKHGNEQRLQLLSDALGEQYAQHGNWRFLRNNDRFVFQILRSFEHDNSEDKPGPGMPPHGWRTQFWVVDQNNKVLVGPRAPIPPDGTRRPILVNGAEVGAVIASPVERLTRNTDINFDKQQRQTSWLIVALATLLAALATFLLARGLLAPVKRLVDGTHKLAAGDFTTRVTPTSEDELGKLAQDFNQLASTLEKNQQMRRDFMADISHELRTPLAVLRGELEAIQDGVRKFTPETVASLQAEVGTLTKLVDDLHQLSMSDEGALAYQKAPVDLIPLLEVAGGAFRERFASRGLKLQFSLPDSITVFGDRDRLMQLFNNLLENSLRYTDSGGSLQISAGQRDKTVRLTFADSAPGVSDDQLQKLFERFYRTEGSRNRASGGSGLGLAICLNIVEAHNGRIIAAHSPFGGVSITVELPLERDLQREV

Function: Member of the two-component regulatory system BaeS/BaeR which responds to envelope stress . Activates expression of periplasmic chaperone spy in response to spheroplast formation, indole and P pili protein PapG overexpression . Activates BaeR by phosphorylation which then activates the mdtABCD and probably the CRISPR-Cas casABCDE-ygbT-ygbF operons . PTM: Autophosphorylated. Location Topology: Multi-pass membrane protein Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine. Sequence Mass (Da): 51991 Sequence Length: 467 Subcellular Location: Cell inner membrane EC: 2.7.13.3

Q03565

MSTSVKHREFVGEPMGDKEVTCIAGIGPTYGTKLTDAGFDKAYVLFGQYLLLKKDEDLFIEWLKETAGVTANHAKTAFNCLNEWADQFM

Function: DNA-binding protein which plays an essential role in nuclear envelope formation . Required for normal chromosome segregation during mitosis . Associates with the nuclear lamina via its interaction with LEM domain containing proteins emr-1 and lem-2 . In association with lem-3, plays a role in radiation-induced DNA damage repair response . PTM: Phosphorylated by vrk-1. Phosphorylation by vrk-1 in mitosis is essential to achieve correct timing of recruitment of nuclear envelope components during nuclear envelope assembly. Dephosphorylated by protein phosphatase 2A (PP2A) following interaction with lem-4l during mitotic exit, leading to mitotic nuclear envelope reassembly. Sequence Mass (Da): 9954 Sequence Length: 89 Subcellular Location: Nucleus

Q6NTS2

MSSTSQKHRDFVAEPMGEKSVQCLAGIGEALGHRLEEKGFDKAYVVLGQFLVLKKDEELFKEWLKDICSANAKQSRDCYGCLKEWCDAFL

Function: Non-specific DNA-binding protein that plays key roles in mitotic nuclear reassembly, chromatin organization, DNA damage response, gene expression and intrinsic immunity against foreign DNA. Contains two non-specific double-stranded DNA (dsDNA)-binding sites which promote DNA cross-bridging. Plays a key role in nuclear membrane reformation at the end of mitosis by driving formation of a single nucleus in a spindle-independent manner. Transiently cross-bridges anaphase chromosomes via its ability to bridge distant DNA sites, leading to the formation of a dense chromatin network at the chromosome ensemble surface that limits membranes to the surface. Also acts as a negative regulator of innate immune activation by restricting CGAS activity toward self-DNA upon acute loss of nuclear membrane integrity. Outcompetes CGAS for DNA-binding, thereby preventing CGAS activation and subsequent damaging autoinflammatory responses. Also involved in DNA damage response; acts by inhibiting the ADP-ribosyltransferase activity of PARP1. Involved in the recognition of exogenous dsDNA in the cytosol: associates with exogenous dsDNA immediately after its appearance in the cytosol at endosome breakdown and is required to avoid autophagy. PTM: Phosphorylated during S and M phases. Sequence Mass (Da): 10206 Sequence Length: 90 Domain: Has a helix-hairpin-helix (HhH) structural motif conserved among proteins that bind non-specifically to DNA. Subcellular Location: Nucleus

Q8HYZ0

MDRHSSYIFVWLQLELCAMAVLLTKGEIRCYCDAAHCVATGYMCKSELSACFSRLLDPQNTNSPLTHGCLDSLASTADICQARQARNHSGSPLPSLECCHEDMCNYRGLQDVLTPPKGEASGQGNRYQHDGSRNLITKVQELTSSKELWFRAAVIAVPIAGGLILVLLIMLALRMLRSENKRLQEQRQQMLSRLHYSFHGHHSKKGQVAKLDLECMVPVSGHENCCLTCDKMRQADLSHDRILSLVHWGMYSGHGKLEFV

Function: Negatively regulates TGF-beta signaling. Location Topology: Single-pass type I membrane protein Sequence Mass (Da): 29116 Sequence Length: 260 Subcellular Location: Membrane

Q0A984

MMLLKRCNRRALVALAAVLLLAACGGARELPDLSDVGDGVATETLWTASTGSGSASSAYALVPAVEGGRVYAADSNGRVTAWDAESGERLWRVDTGRELAAGPGAGGGLVLVGARDGRLLALDAENGEERWVSGLSSEILAVPQIARNIVVARSGDGRVYGLDGLTGRRLWIHDRSVPVLTLRGSSSPVVVGNRVVVGQDNGRLVTLNLQDGEVIWEAPVSIPRGRSDLERMVDLHADPLVFRGVAYAQAYQGELAAVGMGDGRERWSRDIPGHTGMAADSRQLYVVDDQSRLWALDRNNGATVWRQDRLQGLRLTAPVVIGGHLVLADEEGYLNWIAPDNGDLVGRDRHGRQPIQRPPVPDGDVLYLLSADGRLAALRLVED

Function: Part of the outer membrane protein assembly complex, which is involved in assembly and insertion of beta-barrel proteins into the outer membrane. Location Topology: Lipid-anchor Sequence Mass (Da): 40918 Sequence Length: 383 Subcellular Location: Cell outer membrane

F5ZAY7

MFHNTCGRKGRFARAMGMALAISVTLSGCSTVSDWFADEEELEIRRLKPIDAKFTPSVKWDRDIGDGVDHYFSRLRPVYAYENLYAADRHGSVVAMNPENGDVLWERDFAVFEGDGWWDSIARLWRSGASARIGGISVADRLLFVGTENGVVMALDYETGETKWEASVPGEVLAAPSADEGILVVNTGAGTLFGFDTRTGEQLWRHEGDTPPLTLRGISGPVAANGGALIGTPTGKLQVNLLESGILAWETVIATPTGATELERIVDLDTTPVLFGGTIYTVSYNGTLAAVELRSGRIIWKREYGSYRNLSIEGNSIFVVDNNSNIYALDRRNGVELWSQGSLKSRSVTAATPVGEHIVVGDNWGFVHWIEQETGQIVARVDVGGDDEDDAIYDAPLNVDGVVVTMTRNGVVAAISTL

Function: Part of the outer membrane protein assembly complex, which is involved in assembly and insertion of beta-barrel proteins into the outer membrane. Location Topology: Lipid-anchor Sequence Mass (Da): 45336 Sequence Length: 418 Subcellular Location: Cell outer membrane

Q7VWL3

MMRNSRPGRAWRGAVVLTGLLALSGCSMFSSDDDRYKPAELTQYAPGMSVRTAWTASVGSGSGLGFAPTVLGESIYAATPDGSVGKFDLLSGRAIWKSSADAKLSAGAGSDGQTTAVATPDGEVIAFDDTGKIKWRARATSDVAIPPVVGYGVVVVRSGDYRIQAFNAENGERMWSMQRPGPALALRSAAQMVLAEGLVISGLPGGKLLAINSATGNVQWEGTVATPRGASDLERLTDVVGAPRIAGRLMCAVAYQGRIVCFDVSAGGRPIWAKDFSSASGMVIDDRFAYAPDQGSVVSAFALDSGNNVWKQAELKNRLLTAPALLGEAVAVGDFEGYVHFLSRSDGRLLARLSVGGGAIVSPPQTTSQGVLVQTGNGSLVMVRAN

Function: Part of the outer membrane protein assembly complex, which is involved in assembly and insertion of beta-barrel proteins into the outer membrane. Location Topology: Lipid-anchor Sequence Mass (Da): 40091 Sequence Length: 386 Subcellular Location: Cell outer membrane

Q63UT0

MNLLKRYAAPVACAAAVLVFAACSSTKDARRVPTPLTEFKPVLDVQQVWTASVGKGGRYSFSPVAVGDAVYVAGANGSVEKIDAKTGQQVWRTKIGSDLSAGVGSDGNLTAVGALKGGVFVLGPDGKQLWKATVQGEIFSPPLVGNGLVIVRTIDGQVIAFAAQTGEQKWTYRNRAVPLNLRVSAGMTFAGDAAVLAGFPGGGLVALNLQTGEPFWQTPVSFPKGVTEVERINDVTGAPTLVGAETCAVTFQGQLGCFDANSGRPLWEKPFSSRSGVAQDDTVVVGGDDWSVVSAYDVATGKALWRNDKLKSRDVGVPYLLGRAVVLGDYKGFVHFLSRDDGTFVARMKTDGSAIAAAPVLAGNTLVVLTQDGGVYGFRPR

Function: Part of the outer membrane protein assembly complex, which is involved in assembly and insertion of beta-barrel proteins into the outer membrane. Location Topology: Lipid-anchor Sequence Mass (Da): 39843 Sequence Length: 381 Subcellular Location: Cell outer membrane

P77774

MQLRKLLLPGLLSVTLLSGCSLFNSEEDVVKMSPLPTVENQFTPTTAWSTSVGSGIGNFYSNLHPALADNVVYAADRAGLVKALNADDGKEIWSVSLAEKDGWFSKEPALLSGGVTVSGGHVYIGSEKAQVYALNTSDGTVAWQTKVAGEALSRPVVSDGLVLIHTSNGQLQALNEADGAVKWTVNLDMPSLSLRGESAPTTAFGAAVVGGDNGRVSAVLMEQGQMIWQQRISQATGSTEIDRLSDVDTTPVVVNGVVFALAYNGNLTALDLRSGQIMWKRELGSVNDFIVDGNRIYLVDQNDRVMALTIDGGVTLWTQSDLLHRLLTSPVLYNGNLVVGDSEGYLHWINVEDGRFVAQQKVDSSGFQTEPVAADGKLLIQAKDGTVYSITR

Function: Part of the outer membrane protein assembly complex (Bam), which is involved in assembly and insertion of beta-barrel proteins into the outer membrane. Nonessential member of the complex, which may orient the flexible periplasmic domain of BamA for interaction with other Bam components, chaperones and nascent outer membrane proteins. Efficient substrate folding and insertion into the outer membrane requires all 5 subunits . A lateral gate may open between the first and last strands of the BamA beta-barrel that allows substrate to insert into the outer membrane; comparison of the structures of complete and nearly complete Bam complexes show there is considerable movement of all 5 proteins . Location Topology: Lipid-anchor Sequence Mass (Da): 41887 Sequence Length: 392 Subcellular Location: Cell outer membrane

F8GAQ8

MKKLFLVIVPLLLSLLATSCSTSNVPPPTPLAEKPPKEAKVKVKWSRKTGNGNGGLPIYNVSPTYANNTVFVPNQNGVAYGLSITDGKIVWKHDTGTILSSQPNTIANAVIFGSVKGVLTAVDQKDGKILWRTDAPSSIFSQPTIYSNHLYTHTHDGSVTSFDATNGSKVWNVTNNIPEITLPSDSSPIILNDTVMVGSAFGTVLGFTLESGDRTINLPVAIAHGSSPADKMVDITANPMLYGNYLIFAAFQGAIVALDKDTGKMLWAKKASIINNMAINNGVIFTAQANSELKAYDIQTGDTVWTQSTLEWRKITAPIYYKGLIVVADYQGFLHFFNSLNGDYLGRYKLTPKSDFFDYGISGQLVPTEKGILIEADSGTTYLVDAHSDRVIYENILGDYKVNRGKNVKFIYPLEQPKSGSIESSPKALPDKKVDSNKTSKNDTDSNPATTATSTKDIQNPANQEMINSTPVSNTSTKAEKNENTDSSIAEGVVTSNKVQPTPKGKNATIIIGDFSKGDSD

Function: Part of the outer membrane protein assembly complex, which is involved in assembly and insertion of beta-barrel proteins into the outer membrane. Location Topology: Lipid-anchor Sequence Mass (Da): 56221 Sequence Length: 521 Subcellular Location: Cell outer membrane

C7R5S3

MILGWTQRIFTLLVVVTLLAACADEVVNPPKELADIEEKFSVQSSWVEVIGQGDEEKFNSLSPALWQDKIITADVDGLITAFDIKSGKVIWETNLKQPLSGGVTANAGLVAVGTKNAQVHVLDVNDGKQLWHVNVTTEVLAKPAISDGRLVVRTPDGRIFAYSLATQKQEWFYDRIIPNLTLRGTSAAVATSGVVITGFANGKMAAFNLRTGDMLWEQSISAPRGSSEISRIVDVDSTPVVYSNYLYAAGFNGFAIAMDLTNGRYLWREDASVTEELLVDARRVYLVDTKGRIVALDRITGEEVWTQEGLLYRKPTGAADNQDYVVVGDFEGYLHWLDKSTGEFVARIHLDRYGIGGTPIVTDEHVIATTRYGYIHVLENPLATSSEE

Function: Part of the outer membrane protein assembly complex, which is involved in assembly and insertion of beta-barrel proteins into the outer membrane. Location Topology: Lipid-anchor Sequence Mass (Da): 42659 Sequence Length: 388 Subcellular Location: Cell outer membrane

Q5X521

MKIRILVLILCALTQGCTYVDDYMLGKDNTPQPKELKEIQPKVKMAQSWTTPVGKAHKTNEYLNIKPAIRGDVIYTADASGLVQAVNRKDGQIKWSTALKNNIVSGPTVAAGYVAVGTNASTLVLLNQSDGKEIWQNKVSAEVLAPPAISHQKVIAKTIDGKVYAIDAVNGKQLWVADHGAPSLVLKASSSPIIVDDLVLVGFSDGKLDALELQTGRLIWQRSIAYGTGASDVERLVDIDSDPIISNNVAYLATYQGYVGALSLSNGQFIWRKPASVYKNMLLSHNNLYFTDSNDVLWSLNSSTGQVNWKQTSLKARGLTAPALVGGNLAVGDKTGYLHILSTQTGELLGRSQLSGGVTVSPSVSGKNMYVLTNNGMLNQLSVS

Function: Part of the outer membrane protein assembly complex, which is involved in assembly and insertion of beta-barrel proteins into the outer membrane. Location Topology: Lipid-anchor Sequence Mass (Da): 41215 Sequence Length: 384 Subcellular Location: Cell outer membrane

E4PKG3

MPVLRDRIPRRGFFLGLALLAALSGCSSTDTFEQPVPVPEIEASVEFERVWSMSVGDGHDGDFLYLAPLVTGDLIYAASADGELYAVATETGEVAWESEFEDRIFSGLGGDGQNLYLTTENADLVALSREDGSEVWRTSLPTEVLSSPQSNGSLVVAQTTDGKVLGFSATDGEKLWQYDGSVPVLSMRAAAAPLVGGDVVIASFASGKLIALTAASGQPMWQYEVGQPQGRTELERLVDVTGQPLVIETAVMVVGYQGKLALVDIRTGQEIWSRKASSLYSPMIGGGQIYLAAADGEIIALRGSDRREVWTQDRLAWRQLTQPMVYEDYLVVGDFEGYLHALDREDGSLVGQREFDDEGIRVPAQRLANGNLLVFGNSGKMAVFQVKPQD

Function: Part of the outer membrane protein assembly complex, which is involved in assembly and insertion of beta-barrel proteins into the outer membrane. Location Topology: Lipid-anchor Sequence Mass (Da): 42166 Sequence Length: 390 Subcellular Location: Cell outer membrane

Q0AE45

MAGNILLLILDYVFHAGSRTLRVCILSLLILLSGCANLSDLGGGHLTDLFSSEEDEVEIDEAEIVALQTLAPINPLWQVKLAESKTAVFLPVYDNGALYVADEDGRLVKLDPVTGREIWRVETKSQLSGGVGAGGGMILLGTYKGEVLAFDEAGNALWQSRVPGEVLSPPKTDSGIVVVRTGDSKLFGLNATDGKRIWSYQSVTPPLTVRSFVGVSITRGAVFAGFPGGKLIALDLLTGNVGWEETVSQPHGVTELERMTDISSLPIVDENQVCAVAYRGRAACFEISSGNQIWARDASSSMGMVIDNHHVYISEEHGIVAAYDKSSGTAVWKRGKLGSRKLSGLMIVRGNRLVVGDDQGFVTLINRQDGSLLARSPTDGGIILSRAEYLPDGFVVQTLKGGVFAFSLQ

Function: Part of the outer membrane protein assembly complex, which is involved in assembly and insertion of beta-barrel proteins into the outer membrane. Location Topology: Lipid-anchor Sequence Mass (Da): 43737 Sequence Length: 409 Subcellular Location: Cell outer membrane

Q9HXJ7

MVQWKHAALLALALAVVGCSSNSKKELPPAELTDFKEEVVLSKQWSRSVGDGQGDLYNLLEPAVDGSTIYAASAEGRVMAIQRETGDVLWKKDLERPVSGGVGVGYGLVLVGTLRGDVIALDEATGKKKWTKRVNSEVLSAPATNGDVVVVQTQDDKLIGLDAASGDQRWIYESTVPVLTLRGTGAPLIAGNMALAGLASGKVVAVDVQRGLPIWEQRVAIPQGRSELDRVVDIDGGLLLSGDTLYVVSYQGRAAALDVNSGRLLWQREASSYVGVAEGFGNIYVSQASGSVEGLDSRGASSLWNNDALARRQLSAPAVFSSNVVVGDLEGYVHLLSQVDGRFVGRERVDSDGVRVRPLVVGSWMYVFGNGGKLVAYTIR

Function: Part of the outer membrane protein assembly complex, which is involved in assembly and insertion of beta-barrel proteins into the outer membrane. Location Topology: Lipid-anchor Sequence Mass (Da): 40397 Sequence Length: 380 Subcellular Location: Cell outer membrane

C6BGE7

MIHALEQGGVARGIAQAARVAVLALAATAVLGGCSLFSSKNKHEPAKLMEVQQVLAVRQVWSVSVGKSGRYVMQPAVAGNNVYVSAAGGTVTALDGATGRTVWQGKADVDLTTGPGSDGTLTAVAGEKGAVIAFDEKGAQKWKVAVNGEVLTAPLVGQGLVIVRTTDGRVLGLDPSNGERKWIYQRSPSALNLRSSLPMIFAGDNIILGFAGGKLGALSASNGALRWEAAVSYPRGVSEIERLNDVTGAPSVNGSQVCAASFQGRVACFDMSTGAPRWGRDFSSPTGVTQDDGGLFAADEKSVVYGFNAQNGADLWKNDALLWRDLGTPLAFGRAVIVGDSEGWLHFLSRDDGKFVARVKTDGSAIGAAPVVVGQTLVVQTRGGGVYGYLPK

Function: Part of the outer membrane protein assembly complex, which is involved in assembly and insertion of beta-barrel proteins into the outer membrane. Location Topology: Lipid-anchor Sequence Mass (Da): 40617 Sequence Length: 392 Subcellular Location: Cell outer membrane