ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
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... |
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... |
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... |
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... |
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 extramemb... |
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... |
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... |
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... |
Q92G87 | MSNLKQLRTRIKSVKSTQKITKAMQLVSASKMAKIKSQIANSNFYIEAVSKMMSAILSIDMYELSIEEQKFFNTVPNKANLLIVMTSQRGLCGTFNYSIIKQVKNDIKELENKGEQIKLIIIGKKGYEALKRQYVNYIDSYFELPKIHDENLMLQVKQKIMSAVENLEVSNCVIYFNKFKNAMTQIMTRQQILPVAKYQDDSMIDNPIVNLVGFGYKERGVKPINNRRATSDIVGESKSIDYNYEYEGESLISNLINLYVNSQINYALLQSRASEEGARMTAMENATNNANDLISKLVLKLNRSRQAIITTELIEIIAGS... | 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... |
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 c... |
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 c... |
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 | MALEEISERLQVSDFPTLGMAANYDLRRHKFESLANDGSHEMRADVRRWVGNPSDFGGCNPINGHIIALTMPMIKPDRVKIAGYIYECWFLYSWDLTTTLTGADGFFHDDILEGTNEGVSDTDAFGLGTADQDAKARDGRKQIQAKMMYLLETTDKACAKHLQKVWSNMLVTTIQHKSRDFETLKEYIDFRIRDCGALFGEGVMLFGMGLALTEKDREDVASTIYPCYAALGLTNDYFSFDREWEEAKRTGEAKFSNAVRLFMDWQSTGAAAAKEVVRKAIIEYEREFLELREKFVKANPKAERLHKFLEAMVYQISGHV... | 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 Baeye... |
A0A084R1J2 | MNVADIAMDLFRGAKGETISIFAIAKVTVTGVSRGLSKLVFGVVDQANLVNLGQYVVYSVVSMIYNITLHPLASFPGPVFWGASRWPSIWRLFKGRLVHDVHALHGQYGHVVRIAPNELAFSSAQAWKDIYGHKRGNNSMEEMPKFHKFYSGISKTPSIVSEPTRDGHRFIRRILSPAFSDKNLRELEPIVQGYISQFIDQLRSHCEDSTGSKVPLDLVSWYNSATFDIVGDLTFGRPFGSLEQGEEDPFIKDINHFAAVGGAMLIFTSHFPGRGILRFLASLGKVFQNGQEKHVTKMEESLVDRMKNKSSRPDIIDGLV... | 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 ATR... |
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... |
P13090 | MGNQSLVVLTESKGEYENETELPVKKSSRDNNIGESLTATAFTQSEDEMVDSNQKWQNPNYFKYAWQEYLFIFTCMISQLLNQAGTTQTLSIMNILSDSFGSEGNSKSWLMASFPLVSGSFILISGRLGDIYGLKKMLLVGYVLVIIWSLICGITKYSGSDTFFIISRAFQGLGIAFVLPNVLGIIGNIYVGGTFRKNIVISFVGAMAPIGATLGCLFAGLIGTEDPKQWPWAFYAYSIAAFINFVLSIYAIPSTIPTNIHHFSMDWIGSVLGVIGLILLNFVWNQAPISGWNQAYIIVILIISVIFLVVFIIYEIRFAK... | 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: ... |
A0A084R1M6 | MAVISLFRIIVDKWHVVLACSACLGALLFQALRRQSNSTKDVPFIGMELGSAEKRRKAYMTDARSLFRDGYQQFKDRVFGITTTSENLVVVVPPRFLDELGRLPDEVLSASMAVADISQDKYTKMEITDPIISHAVRGNLTMSLSRLNDAILEELRKALSLLLPTCDEWTSVNISEKLQRIVAVISGRVFVGPELCGSDAYLDAAIHIAHEASAAVQSISTLPPWKRPFLSARLPELRALRERQDKVHSVLRPVLEKRIQMNEEDRPDDMLTWIISSQKKHGERSIETMAKVQTALHLAAIGTTSEMATNAFYNLAAMPE... | 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 ATR... |
A0A8F4SN83 | MALLDTIELFSNFSLSGVFAGLVLASLLTTTYCIWNIFYNIYLHPLKGYPGPKFLTTSRLPYLKWMFSGTLVPNFQRLHEQYGPVVRVAPNELSYINPEALKTIYGHRQPGEGFRKNPAFFQPATNGVHSILTSEGDAHSSVRRKILPAFSDKALAEQQDILQHFTDLLIRKLRERVEASKSSEPVDMFEWYIWTTFDLIGDLAFGEPFNCLEAASFTEWVALVFNAFKTFAFINISKQLAPLDKLVRLMIPKSMKARQDKVFSLNVAKVDRRIASKADRPDFLSYIIKGKDGVAMALPELYANSTLLVLAGSESTASGL... | 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... |
A0A084R1J1 | METLSQRITSMESVQLQGIAVAFVTASALYYVLPAAISHIQLSALPMLGKTEVVVIPPKLLSELSKSPRTLSAEIAGNEFIAGKYTKVKALTPILLHSITKYLIPSLGRNAVVMSEEVSNAVRLGIPTCNDWTGVNIYPKIMRMVTVSTGRFLVGSELNRSEDYIDTVHNYALDVSSAQSAVHKMHPWIRPLLAEWLPEIRRLRKRTEEAFALFESLIKERMKMQRELSESELPDDLLQWMIANRHNYNNEDAHDLVYSQLGLTFTANHSTASTITNALYTLATMGDLIDVIRDDITQALAESGGQFTSKALDSMWKFDS... | 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 ATR... |
A0A8F4PN06 | MTSVDTMPPPMVRLESQPDDLMGSSDVADVSDLLPGHTNGLEDEVKIPATNGLKSHPVVTTGTEKTGVMPPLQPESKKNNKGVPWYHASPNDIDPVTRGLLENYSKIPSDQVQQHVIAIREKAWDVYPYPCIGQFLFLNLTINLSPYYPSLVSRLRDQNQTLLDLGCCFAQDVRKLVSDGAPSQNIYGADLYGEFMDLGFELFRDRKTLKSTFFPTDILNERDLLLKGLDGEMDVVYLGLFLHHFDFETCVKVCTRVTRLLKPKPGSLVMGVQVGSLVGDTKPIPIPSGGILWRHDIASLERVWEEVGALTGTKWKVEAR... | 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 methy... |
A0A084R1M7 | MRLDLLGPVATRIITYLDSLTWVGMALPLFSLCWAISYARGKAYPTVPGAPVYGYNSRFEPSFMLKSRTYTGFYDILSNGYKMLKDVPFVIPRHDTNINILPIKYLDEIRLMPKHILNSHLVLISQMTPKWTWLQPAADSDLVTRVLLTKLNPDLQKYVDITRLELDSAFKSDFPRHDEEWTEVDFQPLIRRVLTRISAKIFLGEPACLNEDWLRIAIGYTAGALEVTKDLHKFPSWTHFLVAPLLPSRRRLRRELDIAMKIVEKQIQLHEQAEKDGLKNYDTLLDWMLDNCSDKESSVEAMTIFQCFIAMASIHTTEFS... | 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 ATR... |
A0A8F4PNE5 | MEDPKSLSAPLTAFNADTTTADETPAAQKKYEDDNGQKAGSESSENTKNSDHGDATEVNTPKSADLEANALRNSSVSRSNQEQEKSEEAIDPNIVDWDGPNDPSNPLNWPTWKIKTHIFLVSSITFISPLGSSILATGIPQILAEFRSTNAELGSLVVSVYLLGFAAGPLVIAPLSELYGRMPLYHICNILFAILTVGCALGPTLNSEIGLRFLQGCAGSAPLAIGGGTISDLIPQERRGKYMGIYALGPTLGPIFGPVAGGFLTGAKGWRWLMWLLLMIEGSVTLVNFVVMRETYGVVIMARKTRALQKQTGNMSLRSR... | 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: ... |
M4C699 | MRLISPALVVSTAIQARHVNSSAPVDSAMTEANPLASAHPPDVGYDGVPAGRVRNPDDPTTEERTPGESFMEAINFKIFKLVQEAQGRILGLPEQPRGDMEWLERYGQDAILHYLETGDKDPSQLEKKYDQLLDELKNAPNLEVEILESIHALFLAYMEEVAKPAVQTTPKLNEQPDKFAWAMINKARRNAKPGIRNPYKSLNIPLVENYIKKYNAFIELRQRELTLLDTFSCAFNHNTVKLAKFLAMVDTFSPKRTFVLAMRIELSEIWIEEKRTIAEVASILGISTITGYAKNRLSAGTFVRFIYQLAKTNEQLGPDI... | 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 ide... |
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 cycla... |
A0A084R1J7 | MAVEKVQAFEKVSIPTEKQPGSEDLGFDPAELQKKYEAERNLRIQNGGVSQYRSAWKSGFGYYLEDPNADANFSRDPISARYDVVIMGGGFSGLLVAARLVQQGITNFTILDKSADFGGTWYWSRYPGAQCDVDSTIYLPLLEEVGYIPKEKYSFGPEILEHAQRIAKHFGLYPKALFQTEVKTCHWSEEDSLWTVQTDRGDNLRAQFIVSAFGISHMPKLPGISGIENFQGKSFHASRWDYNYTGGDSTGNMTKLADKRVGIIGTGATAIQVVPKLAESAKELYVFQRTPSSVDVRNNRPTDAEWAKTLRPGWQQERID... | 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 p... |
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 cycla... |
P54253 | MKSNQERSNECLPPKKREIPATSRSSEEKAPTLPSDNHRVEGTAWLPGNPGGRGHGGGRHGPAGTSVELGLQQGIGLHKALSTGLDYSPPSAPRSVPVATTLPAAYATPQPGTPVSPVQYAHLPHTFQFIGSSQYSGTYASFIPSQLIPPTANPVTSAVASAAGATTPSQRSQLEAYSTLLANMGSLSQTPGHKAEQQQQQQQQQQQQHQHQQQQQQQQQQQQQQHLSRAPGLITPGSPPPAQQNQYVHISSSPQNTGRTASPPAIPVHLHPHQTMIPHTLTLGPPSQVVMQYADSGSHFVPREATKKAESSRLQQAIQA... | 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, in... |
G5ED29 | MSTPTGLPALNGDVLSAINDMIGRVIIINTTDKKRYSGVLGAVSQDFDFGMQCVVEITKENENNLLRTESECRDKMVFHYSDIVDFAYVTQEIKKQHAVSKFVTDRQYHGDTPIEGEELQEWNGGEEDGLGGSIEDDVVVAGGQTAARRSNNHNNGTGWSVNDMFAANEKMNVVSTFKEDLTQYTTVEVVGTDEDRARAERLAREIESNSSSKFMANLENDDDERDLDKITRQEDFENGNGRKRNNNSFNQQQQQRRNPNIAPNGQPVNRRAEGLRGDRRNSGSSSANNSRYGAPAAAQQNYSQNQQQQQGQKGYRRQNE... | 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 . Requi... |
P31414 | MVAPALLPELWTEILVPICAVIGIAFSLFQWYVVSRVKLTSDLGASSSGGANNGKNGYGDYLIEEEEGVNDQSVVAKCAEIQTAISEGATSFLFTEYKYVGVFMIFFAAVIFVFLGSVEGFSTDNKPCTYDTTRTCKPALATAAFSTIAFVLGAVTSVLSGFLGMKIATYANARTTLEARKGVGKAFIVAFRSGAVMGFLLAASGLLVLYITINVFKIYYGDDWEGLFEAITGYGLGGSSMALFGRVGGGIYTKAADVGADLVGKIERNIPEDDPRNPAVIADNVGDNVGDIAGMGSDLFGSYAEASCAALVVASISSFG... | 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 aux... |
Q56ZN6 | MMMDEDVEQASLMSFNDRPRAFPNMRSKTYSPLIFRIIRKLNVRVLSIILLFCFGAIFYMGASTSPIIVFVFTVCIISFLLSIYLTKWVLAKDEGPPEMVEISDAIRDGAEGFFRTQYSTISKMAILLAFVILCIYLFRSLTPQQEAAGLGRAMSAYITVAAFLLGALCSGIAGYVGMWVSVRANVRVSSAARRSAREALQIAVRAGGFSALVVVGMAVIGIAILYSTFYVWLGVGSPGSMNVTDLPLLLVGYGFGASFVALFAQLGGGIYTKGADVGADLVGKVEQGIPEDDPRNPAVIADLVGDNVGDCAARGADLFE... | 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... |
Q06572 | MAILGELGTEILIPVCGVIGIVFAVAQWFIVSKVKVTPGAASAAAGAKNGYGDYLIEEEEGLNDHNVVVKCAEIQTAISEGATSFLFTMYQYVGMFMVVFAAIIFLFLGSIEGFSTKGQPCTYSKGTCKPALYTALFSTASFLLGAITSLVSGFLGMKIATYANARTTLEARKGVGKAFITAFRSGAVMGFLLSSSGLVVLYITINVFKMYYGDDWEGLFESITGYGLGGSSMALFGRVGGGIYTKAADVGADLVGKVERNIPEDDPRNPAVIADNVGDNVGDIAGMGSDLFGSYAESSCAALVVASISSFGINHDFTAM... | 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 ... |
P21616 | MGAAILPDLGTEILIPVCAVIGIAFALFQWLLVSKVKLSAVRDASPNAAAKNGYNDYLIEEEEGINDHNVVVKCAEIQNAISEGATSFLFTEYKYVGIFMVAFAILIFLFLGSVEGFSTSPQACSYDKTKTCKPALATAIFSTVSFLLGGVTSLVSGFLGMKIATYANARTTLEARKGVGKAFITAFRSGAVMGFLLAANGLLVLYIAINLFKIYYGDDWGGLFEAITGYGLGGSSMALFGRVGGGIYTKAADVGADLVGKVERNIPEDDPRNPAVIADNVGDNVGDIAGMGSDLFGSYAESSCAALVVASISSFGLNHE... | 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 + ... |
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 hos... |
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 hallm... |
Q28043 | MGAAAKLAFAVFLISCSSGAILGRSETQECIFYNANWERDRTNRTGVESCYGDKDKRRHCFATWKNISGSIEIVKQGCWLDDINCYDRTDCIEKKDSPEVYFCCCEGNMCNERFSYFPEMEVTQPTSNPVTPKPPYYNILLYSLVPLMLIAGIVICAFWVYRHHKMAYPPVLVPTQDPGPPPPSPLLGLKPLQLLEVKARGRFGCVWKAQLLNEYVAVKIFPIQDKQSWQNEYEVYSLPGMKHENILQFIGAEKRGTSVDVDLWLITAFHEKGSLSDFLKANVVSWNELCHIAETMARGLAYLHEDIPGLKDGHKPAISH... | 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 inhi... |
P27038 | MGAAAKLAFAVFLISCSSGAILGRSETQECLFFNANWERDRTNQTGVEPCYGDKDKRRHCFATWKNISGSIEIVKQGCWLDDINCYDRTDCIEKKDSPEVYFCCCEGNMCNEKFSYFPEMEVTQPTSNPVTPKPPYYNILLYSLVPLMLIAGIVICAFWVYRHHKMAYPPVLVPTQDPGPPPPSPLLGLKPLQLLEVKARGRFGCVWKAQLLNEYVAVKIFPIQDKQSWQNEYEVYSLPGMKHENILQFIGAEKRGTSVDVDLWLITAFHEKGSLSDFLKANVVSWNELCHIAETMARGLAYLHEDIPGLKDGHKPAISH... | 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 inhi... |
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.-
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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.-
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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.-
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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.-
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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... |
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.-
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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.-
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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.-
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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.-
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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.-
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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.-
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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.-
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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.-
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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.-
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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 prog... |
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 involve... |
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-ap... |
Q91Z92 | MKVFRRAWRHRVALGLGGLAFCGTTLLYLARCASEGETPSASGAARPRAKAFLAVLVASAPRAVERRTAVRSTWLAPERRGGPEDVWARFAVGTGGLGSEERRALELEQAQHGDLLLLPALRDAYENLTAKVLAMLTWLDERVDFEFVLKADDDSFARLDAILVDLRAREPARRRRLYWGFFSGRGRVKPGGRWREAAWQLCDYYLPYALGGGYVLSADLVHYLRLSREYLRAWHSEDVSLGTWLAPVDVQREHDPRFDTEYKSRGCNNQYLVTHKQSPEDMLEKQQMLLHEGRLCKHEVQLRLSYVYDWSAPPSQCCQR... | 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 towa... |
Q6NQB7 | MKHKVSKRVISLKWVPFLCISFFALGAIFTSRSWEPSSDSGSQLISQHHRDHELQIVSDDCAHNKKATQEKDVTGEVLRTHEAIQDDRSLDKSVSTLSSTRSSQEMVDGSETNPRKKVFMVMGINTAFSSRKRRDSVRETWMPQGEKLERLEQEKGIVIKFMIGHSATSNSILDRAIDSEDAQHKDFLRLEHVEGYHELSAKTKIFFSTAVAKWDAEFYIKVDDDVHVNLGMLASTLARHRSKPRVYIGCMKSGPVLAQNLLNCFRTVKYHEPEYWKFGEDGNKYFRHATGQIYAISKDLANYISINQPILHKYANEDVS... | 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 ap... |
Q9C809 | MRAKAASGKAIIVLCLASFLAGSLFMSRTLSRSYIPEEEDHHLTKHLSKHLEIQKDCDEHKRKLIESKSRDIIGEVSRTHQAVKSLERTMSTLEMELAAARTSDRSSEFWSERSAKNQSRLQKVFAVIGINTAFSSKKRRDSVRQTWMPTGEKLKKIEKEKGIVVRFVIGHSATPGGVLDKAIDEEDSEHKDFLRLKHIEGYHQLSTKTRLYFSTATAMYDAEFYVKVDDDVHVNLGMLVTTLARYQSRPRIYIGCMKSGPVLSQKGVKYHEPEFWKFGEEGNKYFRHATGQIYAISKDLATYISTNQGILHRYANEDVS... | 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 ap... |
Q5XEZ1 | MESLPTTVPSKSERRARSSKFSQSSSKPSVIMAFFSCVAWLYVAGRLWQDAENRVVLNNILKKSYDQKPKVLTVDDKLMVLGCKDLERRIVETEMELTLAKSQGYLKNLKSGSSSGKKLLAVIGVYSGFGSHLRRNTFRGSYMPQGDALRKLEERGIVIRFVIGRSPNRGDSLDRKIDEENQARKDFLILENHEEAQEELAKKVKFFFSAAVQNWDAEFYIKVDDNIDLDLEGLIGLLESRRGQDAAYIGCMKSGEVVAEEGGKWYEPEWWKFGDEKSYFRHAAGSLLILSKTLAQYVNINSGSLKTYAFDDTSIGSWMI... | 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 resid... |
A8MXE2 | MQVTFCRLRTHQWCFILFNVILFHALLFGTDFVEEYFLHSLPYIDVKVLEIKNKARKLNIEPLRSNLSKYYVLSQSEICKGKNIFLLSLIFSSPGNGTRRDLIRKTWGNVTSVQGHPILTLFALGMPVSVTTQKEINKESCKNNDIIEGIFLDSSENQTLKIIAMIQWAVAFCPNALFILKVDEETFVNLPSLVDYLLNLKEHLEDIYVGRVLHQVTPNRDPQNRDFVPLSEYPEKYYPDYCSGEAFIMSQDVARMMYVVFKEVPMMVPADVFVGICAKFIGLIPIHSSRFSGKRHIRYNRCCYKFIFTSSEIADPEMPL... | 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.-
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Q94A05 | MESLPTTVSGKSDRRGRFSKSQNTSKPSLILAFFSCLAWLYVAGRLWQDAQYRAALNTVLKMNYDQRPKVLTVEDKLVVLGCKDLERRIVETEMELAQAKSQGYLKKQKSVSSSGKKMLAVIGVYTGFGSHLKRNKFRGSWMPRDDALKKLEERGVVIRFVIGRSANRGDSLDRKIDEENRATKDFLILENHEEAQEELPKKVKFFYSAAVQNWDAEFYVKVDDNVDLDLEGMIALLESRRSQDGAYIGCMKSGDVITEEGSQWYEPEWWKFGDDKSYFRHATGSLVILSKNLAQYVNINSGLLKTYAFDDTTIGSWMIG... | 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 resid... |
Q94F27 | MARKGSSIRLSSSRISTLLLFMFATFASFYVAGRLWQESQTRVHLINELDRVTGQGKSAISVDDTLKIIACREQKKTLAALEMELSSARQEGFVSKSPKLADGTETKKRPLVVIGIMTSLGNKKKRDAVRQAWMGTGASLKKLESEKGVIARFVIGRSANKGDSMDKSIDTENSQTDDFIILDDVVEAPEEASKKVKLFFAYAADRWDAQFYAKAIDNIYVNIDALGTTLAAHLENPRAYIGCMKSGEVFSEPNHKWYEPEWWKFGDKKAYFRHAYGEMYVITHALARFVSINRDILHSYAHDDVSTGSWFVGLDVKHVD... | 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 resid... |
Q66GS2 | MPLFSHRFTTASSSSPASPSYYNKPSSKTHKPNSSSSSYTSSRIHVAIIFFSLVSVFIGVAGTIFALSSTGPASVYRCGGSKDTSRVVSASRKLGGDGGNNGVVVERRKLLGFVGIQTGFDSGDRRTALRSTWFPSDPDSLLRLEQATGLAFRFVIGKSKDAKKMAELEKEIKEYRDFVLLDTEEEYIRLPYKTLAFFKAAFKLFEADYYVKADDDIYLRPDRLATLLANERLHSQTYIGCMKKGPVITDPKLKWYEKQGNLIGNEYFLHAYGPIYVLSAEIVASLAAARNGSLRMFNNEDVTIGSWMLAMDVHHEDNRA... | 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 ap... |
Q8L7M1 | MHSPRKLFHARSSLATRRSTALVVLTSLAIGIAGFTFGLAVILIPGLRLTGRNCLTNTPPKTVRVVWDVAGNSNGVVSGEKKRHKVMGFVGIQTGFGSAGRRRSLRKTWMPSDPEGLRRLEESTGLAIRFMIGKTKSEEKMAQLRREIAEYDDFVLLDIEEEYSKLPYKTLAFFKAAYALYDSEFYVKADDDIYLRPDRLSLLLAKERSHSQTYLGCLKKGPVFTDPKLKWYEPLSHLLGKEYFLHAYGPIYALSADVVASLVALKNNSFRMFNNEDVTIGAWMLAMNVNHENHHILCEPECSPSSVAVWDIPKCSGLCN... | 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 ap... |
Q8L7F9 | MKRFYGGLLVVSMCMFLTVYRYVDLNTPVEKPYITAAASVVVTPNTTLPMEWLRITLPDFMKEARNTQEAISGDDIAVVSGLFVEQNVSKEEREPLLTWNRLESLVDNAQSLVNGVDAIKEAGIVWESLVSAVEAKKLVDVNENQTRKGKEELCPQFLSKMNATEADGSSLKLQIPCGLTQGSSITVIGIPDGLVGSFRIDLTGQPLPGEPDPPIIVHYNVRLLGDKSTEDPVIVQNSWTASQDWGAEERCPKFDPDMNKKVDDLDECNKMVGGEINRTSSTSLQSNTSRGVPVAREASKHEKYFPFKQGFLSVATLRVG... | 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 prot... |
Q9ASW1 | MKQFMSVVRFKFGFTSVRMRDWSVGVSIMVLTLIFIIRYEQSDHTHTVDDSSIEGESVHEPAKKPHFMTLEDLDYLFSNKSFFGEEEVSNGMLVWSRMRPFLERPDALPETAQGIEEATLAMKGLVLEINREKRAYSSGMVSKEIRRICPDFVTAFDKDLSGLSHVLLELPCGLIEDSSITLVGIPDEHSSSFQIQLVGSGLSGETRRPIILRYNVNFSKPSIVQNTWTEKLGWGNEERCQYHGSLKNHLVDELPLCNKQTGRIISEKSSNDDATMELSLSNANFPFLKGSPFTAALWFGLEGFHMTINGRHETSFAYRE... | 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 ga... |
Q8GXG6 | MKKSKLDNSSSQIRFGLVQFLLVVLLFYFLCMSFEIPFIFRTGSGSGSDDVSSSSFADALPRPMVVGGGSREANWVVGEEEEADPHRHFKDPGRVQLRLPERKMREFKSVSEIFVNESFFDNGGFSDEFSIFHKTAKHAISMGRKMWDGLDSGLIKPDKAPVKTRIEKCPDMVSVSESEFVNRSRILVLPCGLTLGSHITVVATPHWAHVEKDGDKTAMVSQFMMELQGLKAVDGEDPPRILHFNPRIKGDWSGRPVIEQNTCYRMQWGSGLRCDGRESSDDEEYVDGEVKCERWKRDDDDGGNNGDDFDESKKTWWLNR... | 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 ga... |
Q8RX55 | MKKPKLSKVEKIDKIDLFSSLWKQRSVRVIMAIGFLYLVIVSVEIPLVFKSWSSSSVPLDALSRLEKLNNEQEPQVEIIPNPPLEPVSYPVSNPTIVTRTDLVQNKVREHHRGVLSSLRFDSETFDPSSKDGSVELHKSAKEAWQLGRKLWKELESGRLEKLVEKPEKNKPDSCPHSVSLTGSEFMNRENKLMELPCGLTLGSHITLVGRPRKAHPKEGDWSKLVSQFVIELQGLKTVEGEDPPRILHFNPRLKGDWSKKPVIEQNSCYRMQWGPAQRCEGWKSRDDEETVDSHVKCEKWIRDDDNYSEGSRARWWLNRL... | 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 ga... |
Q9LV16 | MRKPKLSKLERLEKFDIFVSLSKQRSVQILMAVGLLYMLLITFEIPFVFKTGLSSLSQDPLTRPEKHNSQRELQERRAPTRPLKSLLYQESQSESPAQGLRRRTRILSSLRFDPETFNPSSKDGSVELHKSAKVAWEVGRKIWEELESGKTLKALEKEKKKKIEEHGTNSCSLSVSLTGSDLLKRGNIMELPCGLTLGSHITVVGKPRAAHSEKDPKISMLKEGDEAVKVSQFKLELQGLKAVEGEEPPRILHLNPRLKGDWSGKPVIEQNTCYRMQWGSAQRCEGWRSRDDEETVDGQVKCEKWARDDSITSKEEESSK... | 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 ga... |
A7XDQ9 | MKRVKSESFRGVYSSRRFKLSHFLLAIAGFYLVFLAFKFPHFIEMVAMLSGDTGLDGALSDTSLDVSLSGSLRNDMLNRKLEDEDHQSGPSTTQKVSPEEKINGSKQIQPLLFRYGRISGEVMRRRNRTIHMSPFERMADEAWILGSKAWEDVDKFEVDKINESASIFEGKVESCPSQISMNGDDLNKANRIMLLPCGLAAGSSITILGTPQYAHKESVPQRSRLTRSYGMVLVSQFMVELQGLKTGDGEYPPKILHLNPRIKGDWNHRPVIEHNTCYRMQWGVAQRCDGTPSKKDADVLVDGFRRCEKWTQNDIIDMVD... | 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 ga... |
P0DUT8 | MASEMNASPEYTGYRLEVFIAVFTPLTIIAVALRFYARSLTSKKIDSGDWLIIAALVGQIVAGGIAIGAVKQAGVGHHAAYLAETNPETLVAFFKYLVAMSTWYATTEGLAKLAVCILYKRLFPQRGIHMVINTTMLVLVGASVGGGLADLFGCTPFSAHWGTAEEQAAHCIDTEALFVWGSFPNIVTDVVLLVLPMPIVWGLHASVRLRLVLVLTFLFGSIFGELIGGDSGLITSVLRFIAFYNKSSFIDPTFHAVELIIWTVCEPGVYLIAACLLVYRPLLEKIGIPLVGGVSSRGGNRQEPTELAFQKPSRPRNGAV... | 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 ... |
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 | MIQLTATPVSALVDEPVHIRATGLIPFQMVSFQASLEDENGDMFYSQAHYRANEFGEVDLNHASSLGGDYMGVHPMGLFWSLKPEKLLTRLLKRDVMNRPFQVQVKLYDLELIVNNKVASAPKASLTLERWYVAPGVTRIKVREGRLRGALFLPPGEGLFPGVIDLFGGLGGLLEFRASLLASRGFASLALAYHNYEDLPRKPEVTDLEYFEEAANFLLRHPKVFGSGVGVVSVCQGVQIGLSMAIYLKQVTATVLINGTNFPFGIPQVYHGQIHQPLPHSAQLISTNALGLLELYRTFETTQVGASQYLFPIEEAQGQF... | 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 . Th... |
Q91X34 | MAKLTAVPLSALVDEPVHIQVTGLAPFQVVCLQASLKDEKGNLFSSQAFYRASEVGEVDLEHDPSLGGDYMGVHPMGLFWSLKPEKLLGRLIKRDVMNSPYQIHIKACHPYFPLQDIVVSPPLDSLTLERWYVAPGVKRIQVKESRIRGALFLPPGEGPFPGVIDLFGGAGGLMEFRASLLASRGFATLALAYWNYDDLPSRLEKVDLEYFEEGVEFLLRHPKVLGPGVGILSVCIGAEIGLSMAINLKQIRATVLINGPNFVSQSPHVYHGQVYPPVPSNEEFVVTNALGLVEFYRTFQETADKDSKYCFPIEKAHGHF... | 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 ... |
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 rec... |
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 ... |
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-... |
A7Z4Y0 | MISFVFPGQGSQRIGMGEDLFGRYPELTAKADHILGYSIQELCRDGERLNQTQFTQPALYVVNALSYLKKTEETGLKPDFTAGHSLGEYNALYASGAFDFEEGLQLVKKRGELMSRAKGGGMAAVIGLTHEQVTDVLRENHLDMIDIANMNTPQQIVISGYKEDIEKAASVFEAVNGVKMVHRLNVSGAFHSRYMLEAKEEFSRFIESFHFKPLSIPVISNVTARPYEQRELKETLTGQITGSVNWTDSIRFLMGRKNMSFEEIGPGKVLTGLIQRITAEAEPITDEIKVPAEAGKSSITAASLGNEEFKRDYQLKYAYL... | 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-Co... |
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 | MKFWRPGITGKLFLAIFATCIVLLISMHWAVRISFERGFIDYIKHGNEQRLQLLSDALGEQYAQHGNWRFLRNNDRFVFQILRSFEHDNSEDKPGPGMPPHGWRTQFWVVDQNNKVLVGPRAPIPPDGTRRPILVNGAEVGAVIASPVERLTRNTDINFDKQQRQTSWLIVALATLLAALATFLLARGLLAPVKRLVDGTHKLAAGDFTTRVTPTSEDELGKLAQDFNQLASTLEKNQQMRRDFMADISHELRTPLAVLRGELEAIQDGVRKFTPETVASLQAEVGTLTKLVDDLHQLSMSDEGALAYQKAPVDLIPLLE... | 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 t... |
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-induce... |
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 i... |
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 | MMLLKRCNRRALVALAAVLLLAACGGARELPDLSDVGDGVATETLWTASTGSGSASSAYALVPAVEGGRVYAADSNGRVTAWDAESGERLWRVDTGRELAAGPGAGGGLVLVGARDGRLLALDAENGEERWVSGLSSEILAVPQIARNIVVARSGDGRVYGLDGLTGRRLWIHDRSVPVLTLRGSSSPVVVGNRVVVGQDNGRLVTLNLQDGEVIWEAPVSIPRGRSDLERMVDLHADPLVFRGVAYAQAYQGELAAVGMGDGRERWSRDIPGHTGMAADSRQLYVVDDQSRLWALDRNNGATVWRQDRLQGLRLTAPVV... | 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 | MFHNTCGRKGRFARAMGMALAISVTLSGCSTVSDWFADEEELEIRRLKPIDAKFTPSVKWDRDIGDGVDHYFSRLRPVYAYENLYAADRHGSVVAMNPENGDVLWERDFAVFEGDGWWDSIARLWRSGASARIGGISVADRLLFVGTENGVVMALDYETGETKWEASVPGEVLAAPSADEGILVVNTGAGTLFGFDTRTGEQLWRHEGDTPPLTLRGISGPVAANGGALIGTPTGKLQVNLLESGILAWETVIATPTGATELERIVDLDTTPVLFGGTIYTVSYNGTLAAVELRSGRIIWKREYGSYRNLSIEGNSIFVV... | 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 | MMRNSRPGRAWRGAVVLTGLLALSGCSMFSSDDDRYKPAELTQYAPGMSVRTAWTASVGSGSGLGFAPTVLGESIYAATPDGSVGKFDLLSGRAIWKSSADAKLSAGAGSDGQTTAVATPDGEVIAFDDTGKIKWRARATSDVAIPPVVGYGVVVVRSGDYRIQAFNAENGERMWSMQRPGPALALRSAAQMVLAEGLVISGLPGGKLLAINSATGNVQWEGTVATPRGASDLERLTDVVGAPRIAGRLMCAVAYQGRIVCFDVSAGGRPIWAKDFSSASGMVIDDRFAYAPDQGSVVSAFALDSGNNVWKQAELKNRLL... | 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 | MNLLKRYAAPVACAAAVLVFAACSSTKDARRVPTPLTEFKPVLDVQQVWTASVGKGGRYSFSPVAVGDAVYVAGANGSVEKIDAKTGQQVWRTKIGSDLSAGVGSDGNLTAVGALKGGVFVLGPDGKQLWKATVQGEIFSPPLVGNGLVIVRTIDGQVIAFAAQTGEQKWTYRNRAVPLNLRVSAGMTFAGDAAVLAGFPGGGLVALNLQTGEPFWQTPVSFPKGVTEVERINDVTGAPTLVGAETCAVTFQGQLGCFDANSGRPLWEKPFSSRSGVAQDDTVVVGGDDWSVVSAYDVATGKALWRNDKLKSRDVGVPYL... | 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 | MQLRKLLLPGLLSVTLLSGCSLFNSEEDVVKMSPLPTVENQFTPTTAWSTSVGSGIGNFYSNLHPALADNVVYAADRAGLVKALNADDGKEIWSVSLAEKDGWFSKEPALLSGGVTVSGGHVYIGSEKAQVYALNTSDGTVAWQTKVAGEALSRPVVSDGLVLIHTSNGQLQALNEADGAVKWTVNLDMPSLSLRGESAPTTAFGAAVVGGDNGRVSAVLMEQGQMIWQQRISQATGSTEIDRLSDVDTTPVVVNGVVFALAYNGNLTALDLRSGQIMWKRELGSVNDFIVDGNRIYLVDQNDRVMALTIDGGVTLWTQS... | 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... |
F8GAQ8 | MKKLFLVIVPLLLSLLATSCSTSNVPPPTPLAEKPPKEAKVKVKWSRKTGNGNGGLPIYNVSPTYANNTVFVPNQNGVAYGLSITDGKIVWKHDTGTILSSQPNTIANAVIFGSVKGVLTAVDQKDGKILWRTDAPSSIFSQPTIYSNHLYTHTHDGSVTSFDATNGSKVWNVTNNIPEITLPSDSSPIILNDTVMVGSAFGTVLGFTLESGDRTINLPVAIAHGSSPADKMVDITANPMLYGNYLIFAAFQGAIVALDKDTGKMLWAKKASIINNMAINNGVIFTAQANSELKAYDIQTGDTVWTQSTLEWRKITAPIY... | 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
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C7R5S3 | MILGWTQRIFTLLVVVTLLAACADEVVNPPKELADIEEKFSVQSSWVEVIGQGDEEKFNSLSPALWQDKIITADVDGLITAFDIKSGKVIWETNLKQPLSGGVTANAGLVAVGTKNAQVHVLDVNDGKQLWHVNVTTEVLAKPAISDGRLVVRTPDGRIFAYSLATQKQEWFYDRIIPNLTLRGTSAAVATSGVVITGFANGKMAAFNLRTGDMLWEQSISAPRGSSEISRIVDVDSTPVVYSNYLYAAGFNGFAIAMDLTNGRYLWREDASVTEELLVDARRVYLVDTKGRIVALDRITGEEVWTQEGLLYRKPTGAAD... | 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 | MKIRILVLILCALTQGCTYVDDYMLGKDNTPQPKELKEIQPKVKMAQSWTTPVGKAHKTNEYLNIKPAIRGDVIYTADASGLVQAVNRKDGQIKWSTALKNNIVSGPTVAAGYVAVGTNASTLVLLNQSDGKEIWQNKVSAEVLAPPAISHQKVIAKTIDGKVYAIDAVNGKQLWVADHGAPSLVLKASSSPIIVDDLVLVGFSDGKLDALELQTGRLIWQRSIAYGTGASDVERLVDIDSDPIISNNVAYLATYQGYVGALSLSNGQFIWRKPASVYKNMLLSHNNLYFTDSNDVLWSLNSSTGQVNWKQTSLKARGLT... | 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 | MPVLRDRIPRRGFFLGLALLAALSGCSSTDTFEQPVPVPEIEASVEFERVWSMSVGDGHDGDFLYLAPLVTGDLIYAASADGELYAVATETGEVAWESEFEDRIFSGLGGDGQNLYLTTENADLVALSREDGSEVWRTSLPTEVLSSPQSNGSLVVAQTTDGKVLGFSATDGEKLWQYDGSVPVLSMRAAAAPLVGGDVVIASFASGKLIALTAASGQPMWQYEVGQPQGRTELERLVDVTGQPLVIETAVMVVGYQGKLALVDIRTGQEIWSRKASSLYSPMIGGGQIYLAAADGEIIALRGSDRREVWTQDRLAWRQL... | 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 | MAGNILLLILDYVFHAGSRTLRVCILSLLILLSGCANLSDLGGGHLTDLFSSEEDEVEIDEAEIVALQTLAPINPLWQVKLAESKTAVFLPVYDNGALYVADEDGRLVKLDPVTGREIWRVETKSQLSGGVGAGGGMILLGTYKGEVLAFDEAGNALWQSRVPGEVLSPPKTDSGIVVVRTGDSKLFGLNATDGKRIWSYQSVTPPLTVRSFVGVSITRGAVFAGFPGGKLIALDLLTGNVGWEETVSQPHGVTELERMTDISSLPIVDENQVCAVAYRGRAACFEISSGNQIWARDASSSMGMVIDNHHVYISEEHGIV... | 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 | MVQWKHAALLALALAVVGCSSNSKKELPPAELTDFKEEVVLSKQWSRSVGDGQGDLYNLLEPAVDGSTIYAASAEGRVMAIQRETGDVLWKKDLERPVSGGVGVGYGLVLVGTLRGDVIALDEATGKKKWTKRVNSEVLSAPATNGDVVVVQTQDDKLIGLDAASGDQRWIYESTVPVLTLRGTGAPLIAGNMALAGLASGKVVAVDVQRGLPIWEQRVAIPQGRSELDRVVDIDGGLLLSGDTLYVVSYQGRAAALDVNSGRLLWQREASSYVGVAEGFGNIYVSQASGSVEGLDSRGASSLWNNDALARRQLSAPAVF... | 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 | MIHALEQGGVARGIAQAARVAVLALAATAVLGGCSLFSSKNKHEPAKLMEVQQVLAVRQVWSVSVGKSGRYVMQPAVAGNNVYVSAAGGTVTALDGATGRTVWQGKADVDLTTGPGSDGTLTAVAGEKGAVIAFDEKGAQKWKVAVNGEVLTAPLVGQGLVIVRTTDGRVLGLDPSNGERKWIYQRSPSALNLRSSLPMIFAGDNIILGFAGGKLGALSASNGALRWEAAVSYPRGVSEIERLNDVTGAPSVNGSQVCAASFQGRVACFDMSTGAPRWGRDFSSPTGVTQDDGGLFAADEKSVVYGFNAQNGADLWKNDA... | 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
|
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