ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
B3E0Z6 | MHQLGIEWNKLIAQIINFVIVLWVLNRFAFKPVLKILEERRKKIAESLQNAEKIKQELAEAEEARKEILRKANEQASFIVAEAQKVASYQGEKKIQEAVEEAKRVLKKAEESAKLEREKAKEEMRREILNLVIEITSKVVGKTLTLDDQERLKNEVLSKLPQKEGHEAYSRN | 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... |
B0JWU9 | MIIDTILLLATEAKEAAAEGFGINTDILGTNLFNLSILLGLIIFYGRKVLGQILGERQSKIAEALAEAENRKNIAATALAEEQKKLALAKQEAEKIIDNSRSRAKAVTADIAAQAELDIQRMRESAAKDLSAEQDRVLVELRQRITALALANVESQLSTGLEESVQQTLIDRSLANLGGK | 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... |
P80285 | MISNGLILAAAEGANPLIPNPWEILVVVVGFALLMFIVIKFIVPTLEKSYQDRVEAIEGGLAKAEKAQAEANAMMADYESQLADARTEANRIREDARTEAAEIVAEARERATAEATRVFEQAQAQIAAERQQAAAQLKREVGSLATTLAGKIVGESLEDDARSQRVVDRFLADLDRHQSAGVAE | 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... |
Q2RFX5 | MQAIFQALNFNPWTFLFQTLNLLVVMGLLYVFLYKPLGKVLADREARIEGNLNDAAAAREKAENILAEYRQQLQGARQEAQAILDRATKMAEETRAEIINRAREEAERTLAQARREIEGEKSKALAAIRSEAASLAILAAGKVLERSLTPDDQERLAREAIAEVERLQ | 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... |
A5IYE1 | MNLFYNLSLKANTLLSAQSGGIKDELKDKFKTLFPTWPMFLATLIAFILVVLILWFLLHKPIKKAMKARQDYIQKNIDEAKLTNDISKQKLNEANKRLAEAYSEADELIKNAKIHGESVIDEYTHKAKNKSKRIIEKAHMEIESERQKMVDDSKSNIAKAAIEISKKIMQKEVTKESQDEVIKNFLKDK | 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... |
P33256 | MWSTRVKKLLLLSFNFLIISAIVSSCSIPEELQAKTIVNEFFPNFWVFVAHTIALSIIILLGIFLLWKPTKRFLAKRSELIQAEINNANEIKKQAQFLLDNAKKQKQNAELQAREIINLATNQAYRLKNDLETDAKRKANRIIENAHAEIIKQESILKRELEGRIVDVALEATSTLIQKNVAKEDHERLVNELLRNLD | 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... |
A8M2J7 | MFFLAAEGGETSHSPILPVWQEIVVGLVAFGLLAFVLMKFVFPRMEQTFQARVDAIEGGIKRAEAAQAEANQLLEQYRAQLSEARSDAAKIRDDARADAEGIRQDILAKAREESDRIIAAGKEQLVAERATIVRELRTEVGTLAVDLASKIVGESLADEARRAGTVDRFLDGLESAGAR | 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... |
Q2S434 | MTALFAQSLVTPSVGLIFWKTVAFLIFLYILYRFGWGPITESLEEREEEIEHSIQRAEEALEEAKAIQAENEEARREAEQKAQQILREARDSAEELREEEKAKTRREIQEMKEQAQAEIEREKQAALQELRDEVADLAIEAAQKIIENDLDADRHRQLVDDALDDFPTN | 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... |
A4XAW6 | MFLAAEGSHNPILPIWQELVVGTIAFALLVFVLLKFVMPRMETMYQARVDAIEGGLKRAEAAQAEANQLLEQYRAQLAEVRTEAARIRDDARADAEGIRQDILAKAREESDRIIAAGKEQLVAERTTIVRELRTEVGTLAVDLAGKIVGESLADEARRAGTVDRFLNGLESAGAR | 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... |
Q2GGH2 | MANLKALLLRIKSVKSIQKTTKVMQMISAAKLHRVQQKLENAKKHLLELSSIVDYVPSDGVHNCASIAKKERVLLVVMSSDRGLCGNFNNLIVKFTKSYVEKLESSNKEVKLIFFGKKAYDMMYSQYSDKILNVFSNTKSITDFLYFKLFVYNSGIDFDQFDNVMILFNKFYTTILQKPDAQQLIPCNLGIPMLLKEVYQYEPTYVDVLSTISLGYVLNLMYIAFLENSASEHCSRMVAMESANRNTKDMLNRLALEYNRSRQASITTDLIEIISGFESLN | 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): 32170
Sequence Length: 281
Subcellular... |
B2KEX2 | MESLKDIRDNIKSVQSTQQVMVTMKMISSARIKKAQNAMLNARPFSLGLEGVIDDLRKDILDENNSFKDPDLSKFFKKPDMEKKNIGVLFITADKGLAGAFNALLLRAALNFIKENQDKNIYFFIIGKKGRDFLSRLKQPNVHIVYDAVGIFPKVGYVHADILGEEIINNFLKLDLCEVRVLYNDFKSMGSQKLENQRLIPFDFEIAQGHTEFGEEEHGFLFEPGKEMIFKLLLYRHIKAGLYRILLESQAAELAARMNAMDSASKNAGEIIDTLKVKLNKVRQSSITNEITEIVGAVEALNK | 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): 34307
Sequence Length: 303
Subcellular... |
C0QTG6 | MAKLSPRDIKRKIQGIKNTQRITKAMKAVSAAKLNKAKAKLNATRPYSERLYDLINDLAMFVDRDIHPLLKIRDEHKVDIVVVTADRGLAGAFNSYVIKTTLGKVKELQEAGKDVNLILIGRKAVQFFKNKGFNIIAEYEDIYRDHMNLSFTSQVGGIIAERYENEKTDAVYLINNELITTATYETKVRKLFPIEPELDYTKLSEISRYNIEPSSEEVLEQLLKRYINFQLYRALVESSTAEHAARMIAMDNATRNAGEAIKRWTIIFNKARQEAITTELIDIINASNAIE | 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): 33202
Sequence Length: 291
Subcellular... |
Q41075 | MRSFCIAALLAVASAFTTQPTSFTVKTANVGERASGVFPEQSSAHRTRKATIVMDGKANAIRDRITSVKNTRKITMAMKLVRAAPKVRRAQDAVLATRPFSETLQSVFGGLIQRLGGESVDLPLLTEREVKKVTLLVITGDRGLCGGYNSFMIKKAEARFNELKKNGVEADLILVGKKGIAYFERRGFPIRKKYETGQNPTAKQALAIAEEVSSTFLSGESDAVELLYTKFVSLIASSPSIRTLVPFSASDITAKGDEVFQLTSESGQFGVERTELDVAAPQEFPNDMIFEQDPIQIVNAILPLYLNGQILRTLQESVAS... | 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): 40217
Sequence Length: 370
Subcellular... |
A1VIV1 | MAAGKEIRGKIKSVENTRKITKAMEMVAASKMRKAQERMRAARPYSDKIRNIAAHLSQANPEYTHPFMESNDAKTTGFIVVTTDKGLCGGLNTNVLRLLTTKLKDMQAAGEDAQAVAIGNKGLGFLNRIGVKVAAHATQLGDKPHLDKLIGPVKVLLDAYSEGKIKAVYLCYTRFINTMKQESVVEQLLPLTADRMQPDKTEHSWDYIYEPDAQTVIDELLVRYVEALVFQAVAENMASEQSARMVAMKSATDNAGSVIGELKLIYNKTRQAAITKELSEIVAGAAAV | 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): 31558
Sequence Length: 288
Subcellular... |
B7GTY8 | MDIITLAEVAGNLSVIGYGIGTLGPGIGLGILFGKAMESTARQPEMSGKIQTIMFIGLALVEVLALIGFVAALIIR | 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... |
Q494C8 | MEHLNFDMLYIAAAIMMGLAAIGAAIGIGILGSKFLEGAARQPDLIPILRTQFFIVMGLVDAIPMITVGLGLYVMFSAV | 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... |
Q89B44 | MDNVSMDMLYIAVAVMIGLAAIGAAVGIGILGSKFLEGVARQPDLTSLLRTQFFVVMGLVDAIPMIAVGLGLYMLFAVI | 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... |
B9MS73 | MTALAAGIAMLAGLGVGIGIGIATGKASESIGRQPEAFGRIFPLFLIGAALAEAVAIYSLVIAFMLISKI | 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... |
Q4AAW2 | MNSIVNFSQQLIQNFQEVSQRTAADSSNLKAFAYLGAGLAMIGVIGVGAGQGYAAGKACDAIARNPEAQKQVFRVLVIGTAISETSSIYALLVALILIFVG | 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... |
B3PLV3 | METIVNGFNQPNAQASPLAYGLTMVAAGLAIMGAGVVSVGQGMAVAKAVEAIGRNPEATSKIRSTLIMGLAIVETASIYCFIIALLIIFV | 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... |
C5CA73 | MELHGSLNMIGYGLAAIGSAIGVGLIFAAYINGVARQPEAQRILQPIALLGFALAEALAILGLVFAFVIGA | 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... |
Q2RFX4 | MATIGFIGVGLAIGLAALGSGLGQGIASRGALEGMARQPEASGDIRTTLLLALAFMEALTLFSFVIAILMWTKL | 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... |
A5IYE0 | MEKGLIAIGIGISMISGLGVGLGQGLAAGKAAEAVGRNPEAASKIRTMMLVGQAVAESAAIYALVISILLMFAFN | 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... |
P63692 | MDPTIAAGALIGGGLIMAGGAIGAGIGDGVAGNALISGVARQPEAQGRLFTPFFITVGLVEAAYFINLAFMALFVFATPVK | 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... |
P33258 | MNIFLVIHELINQADQVNVTLTNHVGAYIGAGMAMTAAAGVGVGQGFASGLCATALARNPELLPKIQLFWIVGSAIAESSAIYGLIIAFILIFVAR | 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... |
P47644 | MEHVNEILATVGVILQQTQTTQDVNASAKLGAYIGAGVTMIAGSTVGIGQGYIFGKAVEAIARNPEVEKQVFKLIFIGSAVSESTAIYGLLISFILIFVAGA | 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... |
Q73HW2 | MDLVALKFIAIGLAVFGMLGAGLGIANIFSAMLNGIARNPESEGKMKSYVYIGAAMVEIMGLLAFVLAMLLIFAA | 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... |
A1JTD2 | MENLNMDLLYMAAAIMMGLAAIGAAIGIGILGGKFLEGAARQPDLIPLLRTQFFIVMGLVDAIPMIAVGLGLYVMFAVA | 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... |
Q3ZBI7 | MAGPEADAQFHFTGIKKYFNSYTLTGRMNCVLATYGSIALIVLYFKLRSKKTPAVKAT | 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... |
Q9VR93 | MSDHFNFNEAFNSQTMRGRANVAKATWASLGLVYVLVKMHRRNTKRRETKLYCKGCQQAMLHG | 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... |
Q96IX5 | MAGPESDAQYQFTGIKKYFNSYTLTGRMNCVLATYGSIALIVLYFKLRSKKTPAVKAT | 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... |
Q9JJW3 | MAGPESDGQFQFTGIKKYFNSYTLTGRMNCVLATYGGIALLVLYFKLRPKKTPAVKAT | 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... |
P65076 | MTDLITVKKLGSRIGAQIDGVRLGGDLDPAAVNEIRAALLAHKVVFFRGQHQLDDAEQLAFAGLLGTPIGHPAAIALADDAPIITPINSEFGKANRWHTDVTFAANYPAASVLRAVSLPSYGGSTLWANTAAAYAELPEPLKCLTENLWALHTNRYDYVTTKPLTAAQRAFRQVFEKPDFRTEHPVVRVHPETGERTLLAGDFVRSFVGLDSHESRVLFEVLQRRITMPENTIRWNWAPGDVAIWDNRATQHRAIDDYDDQHRLMHRVTLMGDVPVDVYGQASRVISGAPMEIAG | Function: Alpha-ketoglutarate-dependent sulfate ester dioxygenase, which oxidizes medium-chain alkyl-sulfate esters. Thus, catalyzes the oxygenolytic cleavage of 2-ethylhexyl sulfate (2-EHS), leading to the formation of succinate and 2-ethylhexanal. Has likely a role in sulfate scavenging in vivo.
Catalytic Activity: 2... |
Q9WWU5 | MSNAALATAPHALELDVHPVAGRIGAEIRGVKLSPDLDAATVEAIQAALVRHKVIFFRGQTHLDDQSQEGFAKLLGEPVAHPTVPVVDGTRYLLQLDGAQGQRANSWHTDVTFVEAYPKASILRSVVAPASGGDTVWANTAAAYQELPEPLRELADKLWAVHSNEYDYASLKPDIDPAKLERHRKVFTSTVYETEHPVVRVHPISGERALQLGHFVKRIKGYSLADSQHLFAVLQGHVTRLENTVRWRWEAGDVAIWDNRATQHYAVDDYGTQPRIVRRVTLAGEVPVGVDGQLSRTTRKG | Function: Catalyzes the oxygenolytic cleavage of 2-ethylhexyl sulfate (2-EHS) in the presence of alpha-ketoglutarate to yield 2-ethyl-hexanal and succinate, the decarboxylated form of alpha-ketoglutarate. It can accept a wide range of alpha-keto acids including 2-oxo-valerate, 2-oxo-adipate, 2-oxo-octanoate, 3-methyl-2... |
Q5W7F3 | MESSVATHWLSAFVILCSFITTQSLNNKIHEHMTIDELRNVFHVEHHSRVPEYHLVQLTHHLARRNIPTSHPANSNSADSGKTPHLKTEKVTKGGYKAPSLLNDEMFVEAKKRIEDVDIMGDPNSTVSVDFKVQSSEFGDSESLSDKEHSAESQEDGVHKIDLEAFGRQLKLVLKKQEGLIKKDGLKVWKALKNETQPHGVDYEEMITEDDEEFGDLYQDEENGAALLIRRHPKHGKLVVEGSIGHDLVIRPIPDTMTSPAQDDEMFMDPSSMADMVSIDTGLPIMKRKKEEQDRLQEALNGAQHVIIKRDPAEVDHMSD... | Cofactor: Binds 1 zinc ion per subunit.
Function: Involved in larval molting and metamorphosis. May degrade extracellular matrix (ECM) and basement membrane (BM) during the development of organs to allow degeneration and remodeling of tissues.
Sequence Mass (Da): 77840
Sequence Length: 693
Subcellular Location: Secrete... |
Q2T0V9 | MSRVKWRNEKIIVALGSLWILGFAAWAFLLFDLLGTSVKEGILEGPREGVFWTAAQYRNSFSRFERQLILYATRQDRDFDNVLLQLDSLEASFGFLERPSEVSAYWLSIPKARDDIAELSRFMATLRRDVPALGARAGDSRRVLEDVARHWPKVNALANYFRAIEMEQRDFTFHQLKEKRRAIVMLGGVLGVILGALFLLLFYTIRTRGSLLEQQQAALDAQRKASDRAFEMIAAKNAFLGMVSHELRTPLQAICGSIEVLLARPQSDANMKTIKRLQNSAASLEAQVKDLTDYIKLRSTNRSVQSDPVEIAPLLADVLD... | Function: Member of a two-component regulatory system involved in control of gene expression; inhibits synthesis of (at least) the polyketide antibiotic thailandamide. Its two-component partner may be BTH_I0635.
Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
Location Topology: Mult... |
P07893 | MPAAIVHSADPSSTSILVEVEGMKCAGCVAAVERRLQQTAGVEAVSVNLITRLAKVDYDAALIEDPTVLTTEITGLGFRAQLRQDDNPLTLPIAEIPPLQQQRLQLAIAAFLLIVSSWGHLGHWLDHPLPGTDQLWFHALLAIWALLGPGRSILQAGWQGLRCGAPNMNSLVLLGTGSAYLASLVALLWPQLGWVCFLDEPVMLLGFILLGRTLEEQARFRSQAALQNLLALQPETTQLLTAPSSIAPQDLLEAPAQIWPVAQLRAGDYVQVLPGVRIPVDGCIVAGQSTLDTAMLTGEPLPQPCQVGDRVCAGTLNLSH... | Function: Involved in copper transport.
Catalytic Activity: ATP + Cu(2+)(in) + H2O = ADP + Cu(2+)(out) + H(+) + phosphate
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 83657
Sequence Length: 790
Subcellular Location: Cell membrane
EC: 7.2.2.9
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P01513 | MFGKIVFLLLVALCAGVQSRYLIVSEPVYYIEHYEEPELLASSRVRRDAHGALTLNSDGTSGAVVKVPFAGNDKNIVSAIGSVDLTDRQKLGAATAGVALDNINGHGLSLTDTHIPGFGDKMTAAGKVNVFHNDNHDITAKAFATRNMPDIANVPNFNTVGGGIDYMFKDKIGASASAAHTDFINRNDYSLDGKLNLFKTPDTSIDFNAGFKKFDTPFMKSSWEPNFGFSLSKYF | Function: Hemolymph antibacterial protein.
PTM: Attacin F appears to be derived by proteolytic digestion of attacin E.
Sequence Mass (Da): 25438
Sequence Length: 235
Subcellular Location: Secreted
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Q93703 | MQTLMSHSRITPLPGAITKEEIKNQLLVHERRFLSKPNRKDQWNVLPQSAHSKNTVNPVRKIADACAVPPHPEKKVIKLHLGDPSVGGKLPPSEIAVQAMHESVSSHMFDGYGPAVGALAAREAIVERYSSADNVFTADDVVLASGCSHALQMAIEAVANAGENILVPHPGFPLYSTLCRPHNIVDKPYKIDMTGEDVRIDLSYMATIIDDNTKAIIVNNPGNPTGGVFTKEHLEEILAFAHQYKLIIIADEIYGDLVYNGATFYPLASLSPKVPIITCDGIAKRWMVPGWRLGWLIIHNHFGVLTDVKNGIVALSQKIV... | Function: Transaminase involved in tyrosine breakdown . Converts tyrosine to p-hydroxyphenylpyruvate . Has no transaminase activity towards phenylalanine . Plays protective role against oxidative stress, metabolizing meta-tyrosine and negatively regulating its accumulation . Plays a role in modulating the daf-2/insulin... |
Q54HG7 | MIKHLIKNVSNSVKYNNVTSNNILFSTSSSLKFGRKFTTETQQECILERLEGENKGISVISFNRGHVKNALGKNLMNQFRSHLNELRFCPDTRVVIVRSLVDGVFCSGADLKERALMSQVEASQFVHSLRSSFTELETLQMPTIAAIEGVAVGGGTEMVLACDFRVASKSSKMGLPETGLAIIPGAGGTQRLPRLIGIPRAKELIFTGAILDSKRALEIGLVQYETEKGEAFDKAIEIAKQIIPKGPIAIRMAKQAIDRGMNVDQASGMIIEQASYAQVIPTKDRIEGLTAFKEKRKPIYKGE | Function: Catalyzes the conversion of 3-methylglutaconyl-CoA to 3-hydroxy-3-methylglutaryl-CoA.
Catalytic Activity: (3S)-hydroxy-3-methylglutaryl-CoA = 3-methyl-(2E)-glutaconyl-CoA + H2O
Sequence Mass (Da): 33245
Sequence Length: 303
Pathway: Amino-acid degradation; L-leucine degradation; (S)-3-hydroxy-3-methylglutaryl... |
Q13825 | MAAAVAAAPGALGSLHAGGARLVAACSAWLCPGLRLPGSLAGRRAGPAIWAQGWVPAAGGPAPKRGYSSEMKTEDELRVRHLEEENRGIVVLGINRAYGKNSLSKNLIKMLSKAVDALKSDKKVRTIIIRSEVPGIFCAGADLKERAKMSSSEVGPFVSKIRAVINDIANLPVPTIAAIDGLALGGGLELALACDIRVAASSAKMGLVETKLAIIPGGGGTQRLPRAIGMSLAKELIFSARVLDGKEAKAVGLISHVLEQNQEGDAAYRKALDLAREFLPQGPVAMRVAKLAINQGMEVDLVTGLAIEEACYAQTIPTKD... | Function: Catalyzes the fifth step in the leucine degradation pathway, the reversible hydration of 3-methylglutaconyl-CoA (3-MG-CoA) to 3-hydroxy-3-methylglutaryl-CoA (HMG-CoA) . Can catalyze the reverse reaction but at a much lower rate in vitro . HMG-CoA is then quickly degraded by another enzyme (such as HMG-CoA lya... |
G3XSI3 | TADNMLNALFYFLLRNPQCLKRLEEEVSCVGATVNELSDDRLAKLPYLNACINETFRIAPAFNGGILQRVSCGATVDGVYVPPGVAVSVDHYTLGHDPQYWVKPDVFNPERWIDPDCKDNFKASRPFLIGARQCPGRQMAYQMFRVCVAKLVYLYTFEL | Function: Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of aurasperone B, a dimeric gamma-naphthopyrone . The first step in the biosynthesis of aurasperone B is the production of gamma-naphthopyrone precursor YWA1 by the non-reducing polyketide synthase albA, via condensation of... |
A2QBE9 | MSDTARISGGSFTSPPGRDVELNSFKEASQTRLYPYSSRKEEEGREDEQQRPEREEDTGALTGYKLVLVTVGLCFCIFCTSLDNTIVATAVPRITQQFHSLDDVGWYASAYLLTTCAVTLPFGRLYTFFPIKWVYLSALFVFELGSFICGITPSSLGLILGRAVAGLGGGGLFSGSLLIITQCVPLRRRPAFSGFIMSIFAVASVIAPLMGGAFTDHISWRWCFYINLPFGLVSAVVIFFTFQTTKPVVQASLREKAAGLDPLGTATFLPAIVCLLLATQWGGAQYPWGDGRIIALFTLFGVLLACFVGLQLWARERATL... | Function: Efflux pump; part of the gene cluster that mediates the biosynthesis of aurasperone B, a dimeric gamma-naphthopyrone.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 60824
Sequence Length: 565
Subcellular Location: Cell membrane
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Q54WX4 | MSYPNNKENSNNIGGGSFSVPSKQPQRVLQQQNTNINNHQTTSTVKSTITKPTTTGATTSTNTSTIPPTTTASSSSSSSSSSSSSSSSSSSSSSSSSQSVPKKKWCIDDFDIGKLLGMGRFGHVYLAREKKSQFIVALKVLFKNQLQTHNIEHQLRREIEIQSHLRHPNILRLFGYFYDDKRVFLIIEFAKGGECFKELQKVGSFNEQTAATYTLQIADALRYCHSKHVIHRDIKPENLLIGVGGEIKIADFGWSVHAPNTKRSTFCGTLEYLPPEVIEKKGYDQTADVWSLGILIFEFLVGRSPFTSDEEKNIFHNIQE... | Function: Part of a chromosomal passenger complex.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 42918
Sequence Length: 384
Subcellular Location: Cytoplasm
EC: 2.7.11.1
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E2RTQ7 | MPQHLVPHTGTGKRTTIEDFEIGRFLGRGKYGLVYLAREQSSKLVVALKVLYKSYIKSERVEGQVRRELDIHLNVRHINIIRLYTWFQDETRVFLVLEVAPYGELYQRLQQFGKFPLPVVSKIIRDVAQAIQYLHRKNIFHRDLKAENILICKGKETKEHTDAHNSDDSISVHEHELVRMAHYTYKIADFGWSVHHPTHGGRRRTQCGTLDYLPPEVMLGQSYDKACDIWSLGALCYELICGTAPFYHDEIKITRQNIANVEYSFTKDFSPASKDFIQRMLIRSPEARISIEDILRHPFLRQTDHRSKVPK | Function: Involved in regulation of the cell cycle. Required for mitotic cell division and cytokinesis. Based on its localization to centrosomes and spindle microtubules, as well as to various cytoskeletal components such as the median body, parental attachment disk, and anterior and posterior-lateral paraflagellar den... |
D7UQM5 | MTPTGPSHHSMAPKRVLPAASQSNMYGNIRSASTTSTTASTSSQALRLLQNAKTSKNADNRIAHAERQGPPSAHPAAMQKPAARVAPSNENRPDPAARQHQHQQQLQQQKATGHDRVLKESQAGNSTTTTMTSTQSKEANKWSLANFDIGRPLGKGKFGNVYLAREKKSKFIVALKVLFKSQLQKAKVEHQLRREIEIQSHLRHDHILRLYGYFYDDTRVYLILEYAARGELYKEMQAQKAGHFDEDRSAVYIYQLAKALLYCHEKKVIHRDIKPENLLLDLKGDLKIADFGWSVHAPSSRRATLCGTLDYLPPEMIEGK... | Function: Serine/threonine protein kinase that contributes to the regulation of cell cycle progression. Involved in meiotic apparatus formation and polar body extrusion. Contributes to Plk1 activation and phosphorylation of histone H3 at 'Ser-10' during meiosis I. Required for accurate progression of early embryonic M ... |
I1RF64 | MLFRFLALLPFVAGAFAEYKVHDDTFKPDYVLEATLDDIKINCVSRSSIVFNGTSPGPTIYLQEEQTTWIRVYNKIPDNNVTVHWHGLSQRAAPFSDGTPLVSQWPIPAGQFFDYEIRPEIGDAGSYFYHSHVGFQIVTAFGALIVRDARKPEYKYDGDIPLLVGDNYAAEDEVIEQGLLADPFKWSGEPQAITIQGNSGNKSFYEAPDSSCMPHVVHVDPGKTYRLRFISATALSMIKLGIEDHENLTVIEADGSYTKPAKIDHVQVSPGQRYSYLMKTKTSKEVCGGDKSQYWIRYESRDRPKVISGYALLKYRCDKN... | Function: Multicopper oxidase; part of the gene cluster that mediates the biosynthesis of aurofusarin, a red mycelium pigment which is acting as a mycotoxin . The first step is performed by the polyketide synthase which condenses one acetyl-CoA and 6 malonyl-CoA units to form the first intermediate, the cyclic heptaket... |
I1RF55 | MINSFSLFAHITPIIRSSLHSRYSVISSRKAMSSLAAAPYRHVMMPFSPAQDAQVHGNSALTKLTDAIPDLKIYTRSSPHYESLRGVYNKLITAQPLAICRPTSVAQVQAIVKTVSGLGIPLGVRGGGHDVFGRGCIADSVTIDMRELDTQELSQDKKTVKVGGGITSKNLVGFLGSHNLCTSNGFAGEAGWTSWASWGGYGPLGDYVGLGVDNIVGAKIVTASGDVVDAKGDSELLWALRGGGGNFGVIAETDVRVYPMSTIQAGFIVYPWPETADVLLRLQALLDSGVPDKLCLQAGFTKGEWGLGMAITYIWPEAET... | Function: FAD-linked oxidoreductase; part of the gene cluster that mediates the biosynthesis of aurofusarin, a red mycelium pigment which is acting as a mycotoxin . The first step is performed by the polyketide synthase which condenses one acetyl-CoA and 6 malonyl-CoA units to form the first intermediate, the cyclic he... |
I1RF63 | MSKQKPSLWRALRALSFIISIPLLIQYLVLKWYSTSQNTPTPVFHEPNHETNLTVWEVLSNDDRVSKFVDVIGKLPDIVRGLSAPQARFTVYAPVNEAFDSFYFPPDPPPFFGLFIAGCHMGPGPVPAERLPSMGTVSSFVNGDIFFTYKQRISVQKDKSGLTLNRAARVLPVNASQSIAVNGFVHHIDTVLELPNSTAHALRTRPELSKLRRGLEATKLSESIYDTNAHVSQTIFAPTNAAFDRLGKTATKFLFSHGGRPYLRALLKYHVVANKTLFSDSYWPHGGAKLMDLSLIPNKDSHQFDLPTLHNNLTLQVESR... | Function: Part of the gene cluster that mediates the biosynthesis of aurofusarin, a red mycelium pigment which is acting as a mycotoxin . The first step is performed by the polyketide synthase which condenses one acetyl-CoA and 6 malonyl-CoA units to form the first intermediate, the cyclic heptaketide and yellow pigmen... |
I1RF56 | MTDNTDMEKLDRATTPTPIPNEAPPTSEPSESKPEEAEDESKYPHGLKLAAIILSNMVAMFLVALDRTIIATAIPRITDDFNALGDISWYASAYLITSSATQLLWGRIFTFYPTKTVYLVAIFFFELGSLLCGVAPNSVAFIIGRAIAGAGSAGIYSGSTILITTVTPLSKRAGYVGMMGAVFGIASVIAPLIGGAFTDHVTWRWCFYINLPVGGAAVACLILLFPKFPVNEPVSVKQQIKQLDPWGNLVFLPGVICLILALQWGGEKYAWDSGRIVALLVLACVLLLVFIGIQIWQQENATVPPRLFKIRNVWLGTIFA... | Function: Rubrofusarin-specific efflux pump; part of the gene cluster that mediates the biosynthesis of aurofusarin, a red mycelium pigment which is acting as a mycotoxin . The first step is performed by the polyketide synthase which condenses one acetyl-CoA and 6 malonyl-CoA units to form the first intermediate, the c... |
I1RF59 | MSPHSDTQETSHEATVTGQPDTLVCLTITAYKKPSLSEKEYRHHMTKVHAKLVSPLMEEYGIVRYTMTHNTKETRPMLYQLYDPQFSNQSDYDCIVQFIFKDIKDFLRMKADPRFLEKVAPDHVNFADTKRSTMTVGYYEEFVNDGKVVPKD | Function: Dehydratase; part of the gene cluster that mediates the biosynthesis of aurofusarin, a red mycelium pigment which is acting as a mycotoxin . The first step is performed by the polyketide synthase which condenses one acetyl-CoA and 6 malonyl-CoA units to form the first intermediate, the cyclic heptaketide and ... |
Q5ATK1 | MAKLYYMPYIFNEGMPLASGPPTLPEDFTPEKSGFRVLVEVRRMKGHFPAQKWRKRNQEWQCINNETLLPDHVRNGHLAKNVPYRPYRPVYVPFAMTVSPTTDAMGTSEETRSKQTKGSNDDILSAKIAGRVARPVYHCTSARLHDLAYDPWPITTIDTHGLSSLKAPSTHTRILIIGAGFGGLLFAVRLLQAGFSRDDLLLVDSAGGFGGTWYWNRYPGLMCDIESYIYMPLLEETGHMPSRKYVPGEELRTHAEGIAAKWELEQRALFRTTIRTLEWDEGGNQWIAHAEQLGVFTDAKQGGNGGGGPLTFTATFAIIA... | Cofactor: Binds 1 FAD per subunit.
Function: FAD-binding monooxygenase; part of the gene cluster A that mediates the biosynthesis of austinol and dehydroaustinol, two fungal meroterpenoids . The first step of the pathway is the synthesis of 3,5-dimethylorsellinic acid by the polyketide synthase ausA . 3,5-dimethylorsel... |
C8VE79 | MYASNKTYPSSRALPCLVEKVEAQHVDGAIRVRITTLEQKDWRQAKAAAVEAKYEAEREIQLRAHGNVKDIEITRESAFEHFATDPWAQHVGVDIEAQRERLLAEPGSRKILIIGAGFGGLLFAVRLIQTGRFTAEDITMIDSAAGFGGTWYWNRYPGLMCDTESYIYMPLLEETGYMPRNKYASGNEIREHAERIAQTYGLATRAMFRTVVEKLDWNEAEKVWTVAGSMLGIANNGQRDNMMSFQMVSQFTIMASGSFASPRVPDYPNIFDYKGKLFHTARWDYNYTGGSVENPKMLGLADKTVAIIGTGASAVQIVPQ... | Cofactor: Binds 1 FAD per subunit.
Function: FAD-binding monooxygenase; part of the gene cluster A that mediates the biosynthesis of austinol and dehydroaustinol, two fungal meroterpenoids . The first step of the pathway is the synthesis of 3,5-dimethylorsellinic acid by the polyketide synthase ausA . 3,5-dimethylorsel... |
P0C1T7 | MSALKFVLICGLVLLLIETIPGVSLNLMRATNRHQCDTNDDCEEDECCVLVGGNVNNPGVQTRICLACSRK | Function: Elicits an uncoordinated twisting syndrome when injected into C.elegans, but has no effect on mice.
Sequence Mass (Da): 7722
Sequence Length: 71
Domain: The presence of a 'disulfide through disulfide knot' structurally defines this protein as a knottin.
Subcellular Location: Secreted
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Q92194 | MLLSTHLLFVITTLVTSLLHPIDGHAVKRSGSLQQVTDFGDNPTNVGMYIYVPNNLASNPGIVVAIHYCTGTGPGYYGDSPYATLSEQYGFIVIYPSSPYSGGCWDVSSQATLTHNGGGNSNSIANMVTWTISKYGADSSKVFVTGSSSGAMMTNVMAATYPELFAAATVYSGVSAGCFYSNTNQVDGWNSTCAQGDVITTPEHWASIAEAMYSGYSGSRPRMQIYHGSIDTTLYPQNYYETCKQWAGVFGYDYSAPEKTEANTPQTNYETTIWGDSLQGIFATGVGHTVPIHGDKDMEWFGFA | Function: Acetylxylan esterase involved in the hydrolysis of xylan, a major structural heterogeneous polysaccharide found in plant biomass representing the second most abundant polysaccharide in the biosphere, after cellulose. Degrades acetylated xylans by cleaving acetyl side groups from the hetero-xylan backbone.
Cat... |
Q75P26 | MILLSYLLTYLLCALTCSARAIHNGRSLIPRAGSLEQVTDFGDNPSNVKMYIYVPTNLASNPGIIVAIHYCTGTAQAYYQGSPYAQLAETHGFIVIYPESPYEGTCWDVSSQATLTHNGGGNSNSIANMVTWTTKQYNADSSKVFVTGTSSGAMMTNVMAATYPNLFAAGVAYAGVPAGCFLSTADQPDAWNSTCAQGQSITTPEHWASIAEAMYPDYSGSRPKMQIYHGNVDTTLYPQNYEETCKQWAGVFGYNYDAPESTESNTPEANWSRTTWGPNLQGILAGGVGHNIQIHGDEDMKWFGFTN | Function: Acetylxylan esterase involved in the hydrolysis of xylan, a major structural heterogeneous polysaccharide found in plant biomass representing the second most abundant polysaccharide in the biosphere, after cellulose. Degrades acetylated xylans by cleaving acetyl side groups from the hetero-xylan backbone. Dis... |
A8PB24 | MVFSPRLSAFVALVALTNAATAVPMYGQCGGSGYTGPTQCDPGLVCVKLNDWYSQCQSGGAQPPVTTTSSPPVTVSPPPSTTTVAPPVATGPPAPEIPAGQLTQLRSFGNNPSNISMFVYKPQNVKNRPGLLVALHPCGGTAQQYFSGFPGFRQHADQRGFIVLYGQSPPGSSNCWDIISTASLTREGGDDSTGIASAVKYALQNWNVDPEKVFVTGTSSGAMMTNIMAATYPDLFKAGAVWAGTAVGCLSANTPQFPPDPCQSGTVIRTPQEWGDRVRRAYPGYNGPWPRMQIWHGTNDFALDHKNLAEQMKQWTNVHN... | Function: Acetylxylan esterase involved in the hydrolysis of xylan, a major structural heterogeneous polysaccharide found in plant biomass representing the second most abundant polysaccharide in the biosphere, after cellulose. Degrades acetylated xylans by cleaving acetyl side groups from the hetero-xylan backbone.
PTM... |
Q81UB2 | MNKTLIINAHPKVDDTSSVSIKVFKHFLESYKELISNNETIEQINLYDDVVPMIDKTVLSAWEKQGNGQELTREEQKVTERMSEILQQFKSANTYVIVLPLHNFNIPSKLKDYMDNIMIARETFKYTETGSVGLLKDGRRMLVIQASGGIYTNDDWYTDVEYSHKYLKAMFNFLGIEDYQIVRAQGTAVLDPTEVLQNAYKEVEEAASRLANKYIFSLEE | 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): 25369
Sequence Length: 220
EC: 1.6.5.-
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O35022 | MSTVLFVKSSDRTAEEGVSTKLYEAFLAAYKENNPNDEVVELDLHKENLPYLGRDMINGTFKAGQGMEMTEDEKKQAAIADKYLNQFVKADKVVFAFPLWNFTVPAVLHTYVDYLSRAGVTFKYTQEGPVGLMGGKKVALLNARGGVYSEGPMAALEMSLNFMKTVLGFWGVQDLHTVVIEGHNAAPDQAQEIVEKGLQEAKDLAAKF | Cofactor: Binds 1 FMN per subunit.
Function: Quinone reductase that provides resistance to thiol-specific stress caused by electrophilic quinones (Probable). Contributes to resistance to 2-methylhydroquinone (2-MHQ) and catechol .
Catalytic Activity: 2 a quinone + H(+) + NADH = 2 a 1,4-benzosemiquinone + NAD(+)
Sequenc... |
Q89PW2 | MAKLLHLSCSPRPDSESSAGARVFLDGFRQMRPDWDIDVMDLWRERMPEFAGPIVEAKYARMKAEAFDDAQRDSFAEAERMATRLSLAERVLISTPMWNFGIPYKLKQWFDIIVQPGLTFRYDPASGYLPLLKDRPTLVILASGSDFVTGMNRGRTDMATPYLREALRFIGISDVRFVPIGPTTGPADPILAARETAYRRLREIATWF | 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): 23682
Sequence Length: 208
EC: 1.6.5.-
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Q97LF7 | MKKLLYISVNTKPEGMSASKTVGREFVDRFVQNYPEYQLIEHDICNEYIPELDHRFLNDNGDIVSGNDYNLLSDNDKKIVDRINDLCNEFVSADVYVIAYPMWSSLFPPRLKMYIDCIVQNGKTIKISEDESSGLLSDKERSVLCIQSSGGVYPKIISWKINHGINYLHDIFRHLGIKKFEKLLVEGVDVQDIGKEKAVEKAFDEIDELIDKMQVRDFVKQ | 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): 25504
Sequence Length: 221
EC: 1.6.5.-
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Q0KBB2 | MNILQIDSSVLGDNSVSRSLTASVVADLVAATPDAKVTVRDLDQDAPAHLSGNLLPVLGGPKEGLSAIQEAELQRTEQWLAEFLAADVLVVGVPQYNFSIPSQLKAWIDRIAQAGRTFKYTENGPVGLAGGKRVIVVSSRGGVRQDANELDLHEKTVDIVFRFLGITDITYVRAHGLAMGPQFREAGLASARTEIAALNDASRLAA | 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): 21945
Sequence Length: 206
EC: 1.6.5.-
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Q6ALS1 | MSKLLYIEASPRKNKSFSTRVAQSFINTFLDADPANRIETLDLWDFPLPEVDGSYLSAKYKILHWQDPTEAEARAWTEIANIVSQFKDADSYLFSIPMWNFSIPYKLKHFIDIITQPGLTFMFSPESGYQGLVTGKACTVIYARGAQYRGTKGSTLDFQKTYMELLLSFIGFENIHSIRVEPTLTDSASRERVLATAKLEAISLAKELYSLI | 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): 24075
Sequence Length: 212
EC: 1.6.5.-
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Q728Q5 | MATILYIKASPRGERSHSVTVADAFVKAYSEANPGDVVRVLDVFEADLPAFGTDAVVARYLSGQGDPLSPAQEAAWAAVKRQVEDFKTADKYVIALPMWNFSIPWRLKQFFDIIIQPGLTFSYDEQGYHGLVTGRPVLVSYARGGAYPAGTPAEGWDFQKRYLEHILGFIGFTDIRSVVVEPTLAGGPDTAQAKRAEAVEQARRMALEF | 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): 22989
Sequence Length: 209
EC: 1.6.5.-
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Q8X9S9 | MSKVLVLKSSILAGYSQSNQLSDYFVEQWREKHSADEITVRDLAANPIPVLDGELVGALRPSDAPLTTRQQEALALSDELIAELKAHDVIVIAAPMYNFNISTQLKNYFDLVARAGVTFRYTENGPEGLVTGKKAIVITSRGGIHKDGPTDLVTPYLSTFLGFIGITDVKFVFAEGIAYGPEMAAKAQSDAKAAIDSIVAA | 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): 21646
Sequence Length: 201
EC: 1.6.5.-
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Q8FHN0 | MSKVLVLKSSILAGYSQSNQLSDYFVEQWREKHSADEITVRDLATNPIPVLDGELVGALRPSDAPLTPRQQEALALSDELIAELKAHDVIVIAAPMYNFNISTQLKNYFDLVARAGVTFRYTEKGPEGLVTGKKAIVITSRGGIHKDGPTDLVTPYLSTFLGFIGITDVKFVFAEGIAYGPEMAAKAQSDAKAAIDSIVAE | 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): 21744
Sequence Length: 201
EC: 1.6.5.-
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Q831B2 | MSKLLVVKAHPLTKEESRSVRALETFLASYRETNPSDEIEILDVYAPETNMPEIDEELLSAWGALRAGAAFETLSENQQQKVARFNELTDQFLSADKVVIANPMWNLNVPTRLKAWVDTINVAGKTFQYTAEGPKPLTSGKKALHIQSNGGFYEGKDFASQYIKAILNFIGVDQVDGLFIEGIDHFPDRAEELLNTAMTKATEYGKTF | 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): 23221
Sequence Length: 208
EC: 1.6.5.-
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Q2N970 | MSTILHITASIRGDESISRALSSKLVERLSGTDTKVITRDLSQNDIPYVDADRFAANLSPYTERSPEQQELAAIADTLIEELQAADTIVLGVPIYNFSVPATVKAWADTVARAGTTFEYTPTGPKGKLDGKKAYITVASGGTPVGSEVDFMSPWLKFFLGFLGISEVEVVATADGIMGEGGEEKIASAHKQVEQVAA | 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): 20997
Sequence Length: 197
EC: 1.6.5.-
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C4L0W8 | MTKVLYVSANPKPTELSYSKQVAETFVSTLKAENASIEVEAIELYDVDVQEIDGDVLSAWGKFASGEALTDVEAKKVGTMSGMLEKFMEADLYVFATPMWNFFFPARMKMFLDSVLMAGKTFRYTEQGPVGLLENKQAIHIQGTGGIYTGTDLNFADAYLRQALAFVGVSEVTTVAVEGMNQYPDKIEEIVADAKAKAEALAKEVAGAVTV | 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): 22966
Sequence Length: 211
EC: 1.6.5.-
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Q9M9U5 | MPATDFQGSFGRSLLSLRRDQVDSSTVVSGSSSHHEPSTMEVELDSFQRQVAEKFIDLNASSNDLLSLEWIGKLLDSFLCCQEEFRAIVFNHRSQISKSPMDRLISDYFERSIKALDVCNAIRDGIEQIRQWEKLADIVISALDSHRPIGEGQLRRAKKALIDLAIGMLDEKDHPSGTNLAHRNRSFGRVKDSHHRSIGHFRSLSWSVSRSWSASKQLQALASNLATPRPNDVVASNGLAVPVYTMTSVLLFVMWVLVAAIPCQDRGLQVNFFVPRHFQWAAPVMSLHDKIVEESKRRDRKNCCGLLKEIDRIEKSSRLM... | Function: Together with TRANSTHYRETIN-LIKE protein (TTL), prevents plant growth and development, but by opposition to TTL, regulates positively cold tolerance, probably in a brassinosteroid (BR) and allantoin-dependent manner . Controls lateral root initiation by modulating exocytic vesicular trafficking-mediated PIN-F... |
C0JB40 | WIMGHMVNDISLVDEYLNQGANSLELDVSFNSEGIAEKLYHGYPCDCLRSCTKTVAFSTYLDYIRNITTPGDPKFRNELVLLMLDLKLKQIAPEAAYWAGFDTAEKLLDYYWQNGQSGARAYIILSIEILTHYEFVTGFKHQLQNKGHEEYSAKIGWDFSGNENLEEIHKVMSDLDLKEHIWQGDGITNCLPRGDDRLKEALFRRNTDWYKYIDKVYTWSIDKKSSIRNALRLGVDGVMTNYPERVVEVLQEPEFSSKLRLATYEDDPWARTVL | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Dermonecrotic toxins cleave the phosphodiester linkage between the phosphate and headgroup of certain phospholipids (sphingolipid and lysolipid substrates), forming an alcohol (often choline) and a cyclic phosphate (By similarity). This toxin acts on sphingomyelin (SM... |
Q1W694 | MQLFIILCLAGSAVQLEGTELDGVERADNRRPIWNIAHMVNDKGLIDEYLDDGANSVESDVSFDSNGKPEKMLHGSPCDCGRSCKRQMSFADYLDYMRQLTTPGDPKFRENLILVMLDLKLKKLSSEQAYSAGQEVASQMLDKYWKRGESGARAYIVLSIPTITRVTFVNGFYDKLHSEGFDQYREKVGVDFSGNEDLEDTGKILKSRDILDHIWQSDGITNCLFRIMKRLKAAIRKRDSNGYMVKVYTWSVDKYTTMRKALRAGADGMITNFPKRLVSVLNEREFSGKFRLATYNDNPWERYTG | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Dermonecrotic toxins cleave the phosphodiester linkage between the phosphate and headgroup of certain phospholipids (sphingolipid and lysolipid substrates), forming an alcohol (often choline) and a cyclic phosphate (By similarity). This toxin acts on sphingomyelin (SM... |
C0JB51 | FALAHMVNDLEMVDEFVGKGANGLEIDVTFSSAGQPEYTYHGVPCDCFRNCKRREDFDTYIKYIRHLATPGDPKFRSNLIMLIFDLKLNGLSQDALRSAGKEMADKLVGNYWQDLAEARAYIVLSMPSIEQADFVTAFKDELKDFGYDKNLDRIGYDFSGNEDLGETAKVYEKLNIHEHIWQADGITNCLPRGDSRLKEAISKRDTPGYQYINKVYTWTIDKSGSIANALRLGVDGVMTNYPERVIDALNDSEFSGKLRLATYEDNPWETFKG | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Dermonecrotic toxins cleave the phosphodiester linkage between the phosphate and headgroup of certain phospholipids (sphingolipid and lysolipid substrates), forming an alcohol (often choline) and a cyclic phosphate (By similarity). This toxin acts on sphingomyelin (SM... |
Q96Q91 | MEMKLPGQEGFEASSAPRNIPSGELDSNPDPGTGPSPDGPSDTESKELGVPKDPLLFIQLNELLGWPQALEWRETGSSSASLLLDMGEMPSITLSTHLHHRWVLFEEKLEVAAGRWSAPHVPTLALPSLQKLRSLLAEGLVLLDCPAQSLLELVEQVTRVESLSPELRGQLQALLLQRPQHYNQTTGTRPCWGSTHPRKASDNEEAPLREQCQNPLRQKLPPGAEAGTVLAGELGFLAQPLGAFVRLRNPVVLGSLTEVSLPSRFFCLLLGPCMLGKGYHEMGRAAAVLLSDPQFQWSVRRASNLHDLLAALDAFLEEVT... | Function: Electroneutral Cl(-)/HCO3(-) antiporter that favors chloride ion entry and efflux of hydrogencarbonate and sodium ion across the basolateral membrane and may participate in salivary secretion . Also mediates Cl(-)/HCO3(-) exchange activity in the presence of K(+) as well as Cs(+), Li(+), and Rb(+) (By similar... |
A0A494BA31 | MKLPGQGDFESSDAHENAHSEEPDSGLGPGPGLNGPSGIDIGESQVSKDPLLFIQLNELLGWPQALEWRETGRWLLFEEKLDMGAGRWSAPHVPTLELPSLQKLRSLLAEGIVLLDCQAQSLLELVEQVVSGESLSPELRGQLQALLLQRPQHHIQTMGIRPCRESNAFRKASRDEDAPLKHQNPLRQKLPAGAEAAAVLAGELGFLEQPLGAFVRLRNPIVLEPLTEMILPSRFFCLLLGPPTLGRSYHEMGRAAAVLLSDPQFQWSVRRASHLPDLLAALDAFLQEVTALPPGRWDRTARIPPPKYLPSQHKRFPSKL... | Function: Electroneutral Cl(-)/HCO3(-) antiporter that favors chloride ion entry and efflux of hydrogencarbonate and sodium ion across the basolateral membrane and may participate in salivary secretion . Also mediates Cl(-)/HCO3(-) exchange activity in the presence of K(+) as well as Cs(+), Li(+), and Rb(+) . Does not ... |
Q9GKY1 | MKLPGQEELEAACACENVPVGQLDSGPSSGPCPDDPSDTGSRELGPPEDPPLFLQLNELLGWPQTLEWREMGRWVLFEEKLEVDAGRWSAPHVPTLALPSLQNLRSLLAEGLVLLDCPAQNLLELVEQVTRVESLSPELRGQLQALLLQRPQHHTQTTGSRPCWGPAQSRKAAHNKEAPMQQQCQSPLRQKLPPGAEAGAVLAGELGFLAQPLAAFVRLRDPVWLGPLTEVPLPSRFFCLLLGPPMLGKGYHELGRAAAVLLSDPHFQWSVRRASNLHDLLTALDAFLEEVTVLPPGRWDPTARIPPPRCLPSRHKRPPL... | Function: Electroneutral Cl(-)/HCO3(-) antiporter that favors chloride ion entry and efflux of hydrogencarbonate and sodium ion across the basolateral membrane and may participat in salivary secretion . Also mediates Cl(-)/HCO3(-) exchange activity in the presence of K(+) as well as Cs(+), Li(+), and Rb(+). Does not co... |
P15575 | MEGPGQDTEDALRRSLDPEGYEDTKGSRTSLGTMSNPLVSDVDLEAAGSRQPTAHRDTYEGYVELHELVLDSRKDPCWMEAGRWLHLEESMEPGGAWGSHLPLLTYHSLLELHRAFAKGVVLLDVAANSLAAVAHVLLDQLIYEGQLKPQHRDDVLRALLLRHKHPSEAESVWTLPAAQLQCSDGEQKDADERALLRDQRAVEMRELHGAGQSPSRAQLGPQLHQQLPEDTEATLVLVACAAFLEQPLLALVRLGAPCPDAVLAVPLPVRFVLTVLGPDSPRLSYHEIRRAAATVMADRVFRRDAYLCGGRAELLGGLQG... | Function: Functions both as a transporter that mediates electroneutral anion exchange across the cell membrane and as a structural protein. Major integral membrane glycoprotein of the erythrocyte membrane; required for normal flexibility and stability of the erythrocyte membrane and for normal erythrocyte shape via the... |
P02730 | MEELQDDYEDMMEENLEQEEYEDPDIPESQMEEPAAHDTEATATDYHTTSHPGTHKVYVELQELVMDEKNQELRWMEAARWVQLEENLGENGAWGRPHLSHLTFWSLLELRRVFTKGTVLLDLQETSLAGVANQLLDRFIFEDQIRPQDREELLRALLLKHSHAGELEALGGVKPAVLTRSGDPSQPLLPQHSSLETQLFCEQGDGGTEGHSPSGILEKIPPDSEATLVLVGRADFLEQPVLGFVRLQEAAELEAVELPVPIRFLFVLLGPEAPHIDYTQLGRAAATLMSERVFRIDAYMAQSRGELLHSLEGFLDCSLV... | Function: Functions both as a transporter that mediates electroneutral anion exchange across the cell membrane and as a structural protein . Component of the ankyrin-1 complex of the erythrocyte membrane; required for normal flexibility and stability of the erythrocyte membrane and for normal erythrocyte shape via the ... |
P04919 | MGDMRDHEEVLEIPDRDSEEELENIIGQIAYRDLTIPVTEMQDPEALPTEQTATDYVPSSTSTPHPSSGQVYVELQELMMDQRNQELQWVEAAHWIGLEENLREDGVWGRPHLSYLTFWSLLELQKVFSKGTFLLGLAETSLAGVANHLLDCFIYEDQIRPQDREELLRALLLKRSHAEDLGNLEGVKPAVLTRSGGASEPLLPHQPSLETQLYCGQAEGGSEGPSTSGTLKIPPDSETTLVLVGRANFLEKPVLGFVRLKEAVPLEDLVLPEPVGFLLVLLGPEAPHVDYTQLGRAAATLMTERVFRITASMAHNREEL... | Function: Functions both as a transporter that mediates electroneutral anion exchange across the cell membrane and as a structural protein. Component of the ankyrin-1 complex of the erythrocyte membrane; required for normal flexibility and stability of the erythrocyte membrane and for normal erythrocyte shape via the i... |
P32847 | MENDLSFGEDVMSYEEESDSAFPSPIRPTPPGHSGNYDLEQSRQEEDSNQAIQSIVVHTDPEAYLNLNTNANTRGDAQAYVELNELMGNSWQETGRWVGYEENFNPGTGKWGPSHVSYLTFKSLIQLRKIMSTGAIILDLQASSLSAVAEKVVDELRTKGEIRAADRDGLLRALLQRRSQSEGAVAQPLGGDIEMQTFSVTKQRDTTDSVEASIVLSGVMDSLEKPAVAFVRLGDSVVIEGALEAPVPVRFVFVLVGPSQGGVDYHESGRAMAALMADWVFSLEAYLAPTNKELTNAIADFMDCGIVIPPTEIQDEGMLQ... | Function: Functions both as a transporter that mediates electroneutral anion exchange across the cell membrane and as a structural protein. Major integral membrane glycoprotein of the erythrocyte membrane; required for normal flexibility and stability of the erythrocyte membrane and for normal erythrocyte shape via the... |
Q9VTG7 | MKGGNYTSLGTCSGINVSGNVAGTRKMSLGKSIKMYLTIFILTTCIYMALYQYHISREPFAASEVVKHQEKSSSYIASYLWSPISLLMANSSSNTNNNSTTTSTTTTTAPTTPTTTTTTTVGSVGQKLGASSISSIRMVSLAATIPSFKSTLSESRSVSLGGHQKTATVKTSTTITTRTTASGLATTKLSATTRTTAKTSAKLSAATTPTASHMENGYKTRPTFVAASLPPPLYIITPTYRRPEQLAELTRLGYTLKHVVNLLWLVIEDANKTNPLVGHTLDRIGVPYEYMVAPMPEKYKQTKKAKPRGVSNRNRGLEYL... | Function: Involved in the biosynthesis of L2/HNK-1 carbohydrate epitope on both glycolipids and glycoproteins. Enzyme has a broad specificity.
Catalytic Activity: 3-O-(beta-D-galactosyl-(1->3)-beta-D-galactosyl-(1->4)-beta-D-xylosyl)-L-seryl-[protein] + UDP-alpha-D-glucuronate = 3-O-(beta-D-GlcA-(1->3)-beta-D-Gal-(1->3... |
Q53461 | PMILLALGLLADTDIASLFTAITMDIGMCVTGLAAALITSSHLLRWVFYGISCAFFVAVLYVLLVQWPADAEAAGTSEIFGTLKILTVVLWLGYPILWALGSEGVALLSVGVTSWGYSGLDILAKYVFAFI | Function: Light-driven chloride pump.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 13951
Sequence Length: 131
Subcellular Location: Cell membrane
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P33970 | IALAGLSILLFVYMGRNVEDPRAQLIFVATLMVPLVSISSYTGLVSGLTVGFLEMPAGHALAGMGAGPEGGVFTPWGRYLTWAFSTPMILIALGLLAGSNMSKLFTAVVADVGMCITGLAAALTTSSYLLRWVWYGISCAFFVVVLYILLAEWAKDAEVAGTADIFNTLKVLTVVLWLGYPIFWALGAEGLAVLDIAITSWAYSGM | Function: Light-driven chloride pump.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 21871
Sequence Length: 206
Subcellular Location: Cell membrane
|
B0R2U4 | MSITSVPGVVDAGVLGAQSAAAVRENALLSSSLWVNVALAGIAILVFVYMGRTIRPGRPRLIWGATLMIPLVSISSYLGLLSGLTVGMIEMPAGHALAGEMVRSQWGRYLTWALSTPMILLALGLLADVDLGSLFTVIAADIGMCVTGLAAAMTTSALLFRWAFYAISCAFFVVVLSALVTDWAASASSAGTAEIFDTLRVLTVVLWLGYPIVWAVGVEGLALVQSVGVTSWAYSVLDVFAKYVFAFILLRWVANNERTVAVAGQTLGTMSSDD | Function: Light-driven chloride pump.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 28874
Sequence Length: 274
Subcellular Location: Cell membrane
|
O93742 | MMETAADALASGTVPLEMTQTQIFEAIQGDTLLASSLWINIALAGLSILLFVYMGRNLEDPRAQLIFVATLMVPLVSISSYTGLVSGLTVSFLEMPAGHALAGQEVLTPWGRYLTWALSTPMILVALGLLAGSNATKLFTAVTADIGMCVTGLAAALTTSSYLLRWVWYVISCAFFVVVLYVLLAEWAEDAEVAGTAEIFNTLKLLTVVLWLGYPIFWALGAEGLAVLDVAVTSWAYSGMDIVAKYLFAFLLLRWVVDNERTVAGMAAGLGAPLARCAPADD | Function: Light-driven chloride pump.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 30143
Sequence Length: 282
Subcellular Location: Cell membrane
|
O00154 | MKLLARALRLCEFGRQASSRRLVAGQGCVGPRRGCCAPVQVVGPRADLPPCGACITGRIMRPDDANVAGNVHGGTILKMIEEAGAIISTRHCNSQNGERCVAALARVERTDFLSPMCIGEVAHVSAEITYTSKHSVEVQVNVMSENILTGAKKLTNKATLWYVPLSLKNVDKVLEVPPVVYSRQEQEEEGRKRYEAQKLERMETKWRNGDIVQPVLNPEPNTVSYSQSSLIHLVGPSDCTLHGFVHGGVTMKLMDEVAGIVAARHCKTNIVTASVDAINFHDKIRKGCVITISGRMTFTSNKSMEIEVLVDADPVVDSSQ... | Function: Catalyzes the hydrolysis of acyl-CoAs into free fatty acids and coenzyme A (CoASH), regulating their respective intracellular levels . Preferentially hydrolyzes palmitoyl-CoA, but has a broad specificity acting on other fatty acyl-CoAs with chain-lengths of C8-C18 . May play an important physiological functio... |
P69051 | MDPIALTAAVGADLLGDGRPETLWLGIGTLLMLIGTFYFIVKGWGVTDKEAREYYSITILVPGIASAAYLSMFFGIGLTEVQVGSEMLDIYYARYADWLFTTPLLLLDLALLAKVDRVSIGTLVGVDALMIVTGLVGALSHTPLARYTWWLFSTICMIVVLYFLATSLRAAAKERGPEVASTFNTLTALVLVLWTAYPILWIIGTEGAGVVGLGIETLLFMVLDVTAKVGFGFILLRSRAILGDTEAPEPSAGAEASAAD | Function: Light-driven proton pump. It may interact with bacterioruberin in the claret membrane.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 27852
Sequence Length: 260
Subcellular Location: Cell membrane
|
P32370 | MDMKHSRLFSPLQIGSLTLSNRVGMAPMSMDYEAADGTVPKRLADVFVRRAEGGTGYVMIDAVTIDSKYPYMGNTTALDRDELVPQFKEFADRVKEAGSTLVPQIIHPGPESVCGYRHIAPLGPSANTNANCHVSRSISIDEIHDIIKQFGQAARRAEEAGCGAISLHCAHAYMLPGSFLSPLRNKRMDEYGGSLDNRARFVIEMIEEARRNVSPDFPIFLRISGDERMVGGNSLEDMLYLAPKFEAAGVSMLEVSGGTQYEGLEHIIPCQNKSRGVNVYEASEIKKVVGIPVYAVGKINDIRYAAEIVERGLVDGVAMG... | Function: NADH-dependent flavin oxidoreductase . Stereo-specific NAD(H)-dependent 3-oxo-delta4-cholenoic acid oxidoreductase involved in bile acid 7beta-dehydroxylation .
Catalytic Activity: 7beta-hydroxy-3-oxochol-24-oyl-CoA + NAD(+) = 7beta-hydroxy-3-oxochol-4-en-24-oyl-CoA + H(+) + NADH
Sequence Mass (Da): 72029
Seq... |
B0NAQ4 | MNRIGIIGGGASGIVAAIAAARSDGDAQVFILEQKENIGKKILATGNGRCNLTNEAMDASCYHGEDPEFARNVLKQFGYGETLEFFASLGLFTKSRGGYIYPRSDQAASVLELLEMELRRQKVKIYTGVRVEALKLSAKGFVIRADGQRFPADRVILACGGKASKSLGSDGSGYALARSMGHTLSPVVPALVQLKVKKHPFAKAAGVRTDAKVAALLGRQVLAEDTGEMQITAYGISGIPVFQISRHIAKGLYEGKEMKVRVDFLPEMEASQVRKAFNTHLDKCPYATCQEFLTGIFPKKLIPRLLELSHIRQNFPASEL... | Function: Involved in the secondary bile acid metabolism. Catalyzes two subsequent reductions of the double bonds within the bile acid A/B rings of 3-oxochol-4,6-dien-24-oyl-CoA and 12alpha-hydroxy-3-oxochol-4,6-dien-24-oyl-CoA to yield 3-oxocholan-24-oyl-CoA and 12alpha-hydroxy-3-oxocholan-24-oyl-CoA, respectively.
Ca... |
Q9UQB8 | MSLSRSEEMHRLTENVYKTIMEQFNPSLRNFIAMGKNYEKALAGVTYAAKGYFDALVKMGELASESQGSKELGDVLFQMAEVHRQIQNQLEEMLKSFHNELLTQLEQKVELDSRYLSAALKKYQTEQRSKGDALDKCQAELKKLRKKSQGSKNPQKYSDKELQYIDAISNKQGELENYVSDGYKTALTEERRRFCFLVEKQCAVAKNSAAYHSKGKELLAQKLPLWQQACADPSKIPERAVQLMQQVASNGATLPSALSASKSNLVISDPIPGAKPLPVPPELAPFVGRMSAQESTPIMNGVTGPDGEDYSPWADRKAAQ... | Function: Adapter protein that links membrane-bound small G-proteins to cytoplasmic effector proteins. Necessary for CDC42-mediated reorganization of the actin cytoskeleton and for RAC1-mediated membrane ruffling. Involved in the regulation of the actin cytoskeleton by WASF family members and the Arp2/3 complex. Plays ... |
Q6GMN2 | MSLSRSEEMHRLTENVYKTIMEQFNPSLRNFIAMGKNYEKALAGVTFAAKGYFDALVKMGELASESQGSKELGDVLFQMAEVHRQIQNQLEEMLKAFHNELLTQLEQKVELDSRYLSAALKKYQTEQRSKGDALDKCQAELKKLRKKSQGSKNPQKYSDKELQYIDAISNKQGELENYVSDGYKTALTEERRRFCFLVEKQCAVAKNSAAYHSKGKELLAQKLPLWQQACADPNKIPDRAAQLMQQMANSNGSILPSALSASKSNLVISDPIPGAKPLPVPPELAPFVGRMSAQENVPVMNGVAGADSEDYNPWADRKAA... | Function: Adapter protein that links membrane-bound small G-proteins to cytoplasmic effector proteins. Necessary for CDC42-mediated reorganization of the actin cytoskeleton and for RAC1-mediated membrane ruffling. Involved in the regulation of the actin cytoskeleton by WASF family members and the Arp2/3 complex. Plays ... |
Q94F62 | MERRLMIPCFFWLILVLDLVLRVSGNAEGDALSALKNSLADPNKVLQSWDATLVTPCTWFHVTCNSDNSVTRVDLGNANLSGQLVMQLGQLPNLQYLELYSNNITGTIPEQLGNLTELVSLDLYLNNLSGPIPSTLGRLKKLRFLRLNNNSLSGEIPRSLTAVLTLQVLDLSNNPLTGDIPVNGSFSLFTPISFANTKLTPLPASPPPPISPTPPSPAGSNRITGAIAGGVAAGAALLFAVPAIALAWWRRKKPQDHFFDVPAEEDPEVHLGQLKRFSLRELQVASDNFSNKNILGRGGFGKVYKGRLADGTLVAVKRLK... | Function: Dual specificity kinase acting on both serine/threonine- and tyrosine-containing substrates. Controls the expression of genes associated with innate immunity in the absence of pathogens or elicitors. Involved in brassinosteroid (BR) signal transduction. Phosphorylates BRI1. May be involved in changing the equ... |
Q6Z4U4 | MAAHRWAVWAVLLLRLLVPAARVLANMEGDALHSLRTNLVDPNNVLQSWDPTLVNPCTWFHVTCNNDNSVIRVDLGNAALSGTLVPQLGQLKNLQYLELYSNNISGTIPSELGNLTNLVSLDLYLNNFTGPIPDSLGNLLKLRFLRLNNNSLSGSIPKSLTAITALQVLDLSNNNLSGEVPSTGSFSLFTPISFANNPSLCGPGTTKPCPGAPPFSPPPPYNPPTPVQSPGSSSSTGAIAGGVAAGAALLFAIPAIGFAWYRRRKPQEHFFDVPAEEDPEVHLGQLKRFSLRELQVATDTFSNKNILGRGGFGKVYKGRL... | Function: LRR receptor kinase involved in defense response . Does not seem to be required specifically for XA21-mediated immunity or basal resistance to Xanthomonas oryzae pv. oryzae (Xoo), or immunity to Magnaporthe oryzae . Involved in brassinosteroid (BR) signaling pathway. Acts as coreceptor of BRI1. Forms at the p... |
Q6ZNE5 | MASPSGKGARALEAPGCGPRPLARDLVDSVDDAEGLYVAVERCPLCNTTRRRLTCAKCVQSGDFVYFDGRDRERFIDKKERLSRLKSKQEEFQKEVLKAMEGKWITDQLRWKIMSCKMRIEQLKQTICKGNEEMEKNSEGLLKTKEKNQKLYSRAQRHQEKKEKIQRHNRKLGDLVEKKTIDLRSHYERLANLRRSHILELTSVIFPIEEVKTGVRDPADVSSESDSAMTSSTVSKLAEARRTTYLSGRWVCDDHNGDTSISITGPWISLPNNGDYSAYYSWVEEKKTTQGPDMEQSNPAYTISAALCYATQLVNILSHI... | Function: Required for both basal and inducible autophagy. Determines the localization of the autophagy-specific PI3-kinase complex PI3KC3-C1 . Plays a role in autophagosome formation and MAP1LC3/LC3 conjugation to phosphatidylethanolamine . Promotes BECN1 translocation from the trans-Golgi network to autophagosomes . ... |
Q8CDJ3 | MASPSGKGSWTPEAPGFGPRALARDLVDSVDDAEGLYVAVERCPLCNTTRRRLTCAKCVQSGDFVYFDGRDRERFIDKKERLSQLKNKQEEFQKEVLKAMEGKRLTDQLRWKIMSCKMRIEQLKQTICKGNEEMKKNSEGLLKNKEKNQKLYSRAQRHQEKKEKIQRHNRKLGDLVEKKTIDLKSHYERLARLRRSHILELTSIIFPIDEVKTSGRDPADVSSETDSAMTSSMVSKLAEARRTTYLSGRWVCDDHNGDTSISITGPWISLPNNGDYSAYYNWVEEKKTTQGPDMEHNNPAYTISAALGYATQLVNIVSHI... | Function: Required for both basal and inducible autophagy . Determines the localization of the autophagy-specific PI3-kinase complex PI3KC3-C1 (By similarity). Plays a role in autophagosome formation and MAP1LC3/LC3 conjugation to phosphatidylethanolamine . Promotes BECN1 translocation from the trans-Golgi network to a... |
D4A4K3 | MASPSGKGSWTPEAPGFGPRALAPDLVDSVDDAEGLYVAVERCPLCNTTRRRLTCAKCVQSGDFVYFDGRDRERFIDKKERLSQLKNKQEEFQKEVLKAMEGKRLTDQLRWKIMSCKMRIEQLKQTICKGNEEMKKNSEGLLKNKEKNQKLYSRAQRHQEKKEKIQRHNRKLGDLVEKKTSDLREHYDRLACLRRLHILELTSVIFPMDEVKTSGRDPADVSSETDSAMTSSMVSKLAEARRTTYLSGRWVCDDHNGDTSISITGPWISLPNNGDYSAYYNWVEEKKTTQGPDMEHNNPAYTISAALGYATQLVNIVSHI... | Function: Required for both basal and inducible autophagy. Determines the localization of the autophagy-specific PI3-kinase complex. Plays a role in autophagosome formation and MAP1LC3/LC3 conjugation to phosphatidylethanolamine. Promotes BECN1 translocation from the trans-Golgi network to autophagosomes. Enhances PIK3... |
Q16611 | MASGQGPGPPRQECGEPALPSASEEQVAQDTEEVFRSYVFYRHQQEQEAEGVAAPADPEMVTLPLQPSSTMGQVGRQLAIIGDDINRRYDSEFQTMLQHLQPTAENAYEYFTKIATSLFESGINWGRVVALLGFGYRLALHVYQHGLTGFLGQVTRFVVDFMLHHCIARWIAQRGGWVAALNLGNGPILNVLVVLGVVLLGQFVVRRFFKS | Function: Plays a role in the mitochondrial apoptotic process. Upon arrival of cell death signals, promotes mitochondrial outer membrane (MOM) permeabilization by oligomerizing to form pores within the MOM. This releases apoptogenic factors into the cytosol, including cytochrome c, promoting the activation of caspase 9... |
O08734 | MASGQGPGPPKVGCDESPSPSEQQVAQDTEEVFRSYVFYLHQQEQETQGAAAPANPEMDNLPLEPNSILGQVGRQLALIGDDINRRYDTEFQNLLEQLQPTAGNAYELFTKIASSLFKSGISWGRVVALLGFGYRLALYVYQRGLTGFLGQVTCFLADIILHHYIARWIAQRGGWVAALNFRRDPILTVMVIFGVVLLGQFVVHRFFRS | Function: In the presence of an appropriate stimulus, accelerates programmed cell death by binding to, and antagonizing the anti-apoptotic action of BCL2.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 23295
Sequence Length: 209
Domain: Intact BH3 motif is required by BIK, BID, BAK, BAD and BAX for... |
Q961J5 | MDFDEVLREVGSFGLYQKVIICSVLLPAALPCAFHAYSQLFIAATPQHFCRVPELEPWTQDYVQLVKNLSIPRNRNGAYAECSMYSRNYTDIVRYLEYRPPPDLLRQQAEDLLKLQPDTTQVVPCQHGWHYDKSIYSSTVVQEWNLVCDRSFLVTLALVVFGVGGLLGNYVFGYLVDLWGRRPSFYAYLLLEIIACAASAFAWNYYTWLGLRFVVGLTVPAILASPYVLAIELVGPERRVFCTIVSNIAYSLGLVVLAGVIYIVRDWRELSLAVSMPLLMLFSCFFVLPESPRWLMAVGKTRRAIKILKVMARVNGVRVN... | Function: Beta-alanine transporter required for the uptake of beta-alanine by the glia . Required for the recycling process of the neurotransmitter histamine in photoreceptor neurons of the compound eye and therefore for photoreceptor synaptic transmission . Following histamine release from photoreceptors and its uptak... |
F4JPW1 | MGVISPTETLFLKSQHRLLQPRNYSYALAFHSTRRVANFPRNSFSSLGSCSVDFPLRSNPISQNSKSIHPWRRYVSESDSNELYHKKVSSIMETLKQAYSFIPHGILLSTILALVYPPSFTWFKPRYFVPGLGFMMFAVGINSNERDFLEALKRPDAIFAGYIGQYLIKPLLGYIFGVIAVSLFNLPTSIGAGIMLVSCVSGAQLSNYTTFLTDPSLAALSIVMTSISTATAVLVTPMLSLLLIGKKLPVDVFGMISSILQVVITPIAAGLLLNRLFPRLSNAIKPFLPALTVIDMSCCIGAPLALNIDSILSPFGATIL... | Function: Plastidic transporter involved in the biosynthesis of aliphatic glucosinolates by translocating the biosynthetic intermediates of Met-derived glucosinolates across chloroplast membranes. Transports short chain (C2) alpha-keto acids, such as 4-methylsulfanyl-2-oxobutanoic acid, from the cytosol to the chloropl... |
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