ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
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Q09905 | MIYAVFIFNNKGKPRLTKFYTPIDESIQQKLIGDIYAAVSTRPPTACNFLESNLIAGKNRIIYRQYATLYFVFVVDEGESELGILDLIQVFVEALDRCFNNVCELDLVFKFQEIHAILAEVVSGGLVLETNLNEIVLAAQNQMPKTKRSNAMPFSNTLSSFATRF | Function: Part of the AP-3 complex, an adaptor-related complex which is not clathrin-associated. The complex is associated with the Golgi region as well as more peripheral structures. It facilitates the budding of vesicles from the Golgi membrane and may be directly involved in trafficking to the vacuole (By similarity... |
P47064 | MIHAVLIFNKKCQPRLVKFYTPVDLPKQKLLLEQVYELISQRNSDFQSSFLVTPPSLLLSNENNNDEVNNEDIQIIYKNYATLYFTFIVDDQESELAILDLIQTFVESLDRCFTEVNELDLIFNWQTLESVLEEIVQGGMVIETNVNRIVASVDELNKAAESTDSKIGRLTSTGFGSALQAFAQGGFAQWATGQ | Function: Part of the AP-3 complex, an adaptor-related complex which is not clathrin-associated. The complex is associated with the Golgi region as well as more peripheral structures. It facilitates the budding of vesicles from the Golgi membrane and may be directly involved in trafficking to the vacuole. Required for ... |
P9WEP1 | MDIYVVGPFGHAMDLLPNPTRPFSGRLHELSALALQRPQLVITTLGALLLAAFYLLPSKDPYNLKRIPMVSRSRVLDAYRSGVWWRFILPRFYPYIHEGYLKYSTKDRPFRVWLAQFQIWVYILPLKYLPLVKNQGITELSLRDFIDKATSAQLSSGSFDTFEVQVGSKLLNGNLIDIKPIVQTRTEQILERVIGRPREWRRFNIRALSVQVVKHVSARIAFGEALADNPGFLDAMERYSLNVIPYTLVFRYFNLGPLRYPLLYLIHLRQRQTLAVATRYVTDLIAERQRKEKEHRLDGDERPVDCIQWSMDQDIPDEQK... | Function: Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of aspergiltriene A, aspergildienes A-D and aspergilols A-D . The bifunctional terpene synthase AuAS converts DMAPP and IPP into sesterterpenes . The C-terminal prenyltransferase (PT) domain of AuAS catalyzes formation of G... |
P54456 | MNREEALACVKQQLTEHRYIHTVGVMNTAIELAERFGADSKKAEIAAIFHDYAKFRPKEEMKQIIAREKMPAHLLDHNPELWHAPVGAYLVQREAGVQDEDILDAIRYHTSGRPGMTLLEKVIYVADYIEPNRAFPGVDEVRKLAETDLNQALIQSIKNTMVFLMKKNQPVFPDTFLTYNWLVSGS | Function: Hydrolyzes diadenosine 5',5'''-P1,P4-tetraphosphate (Ap4A) to yield ADP.
Catalytic Activity: H2O + P(1),P(4)-bis(5'-adenosyl) tetraphosphate = 2 ADP + 2 H(+)
Sequence Mass (Da): 21282
Sequence Length: 186
EC: 3.6.1.41
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Q88A48 | MAVYAVGDLQGCLEPLQCLLEHVRFDPVQDRLWLVGDLVNRGPQSLQTLRYLYSIRESLVCVLGNHDLHLLAVARKNELLKKGDTLREILEAPDRDELLRWVRQQKLMHYDAERNIAMVHAGIAPQWSVKKALKQAAEVEHALQDDQLYGAFLDGMYGNEPAKWNNDLQGVTRLRVITNYFTRMRFCTSDGKLDLKSKEGVGTAIPGYAPWFSHQNRKTRDVKIIFGHWAALEGRCDEPGVFALDSGCVWGGAMTLLNVDTLERHQCNCDAVGNAATGIIASAQPGNAHIQQIPAQEPKQ | Function: Hydrolyzes diadenosine 5',5'''-P1,P4-tetraphosphate to yield ADP.
Catalytic Activity: H2O + P(1),P(4)-bis(5'-adenosyl) tetraphosphate = 2 ADP + 2 H(+)
Sequence Mass (Da): 33622
Sequence Length: 300
EC: 3.6.1.41
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A1STS0 | MATYIVGDVHGCFDELQALLELAQFKKNKDQLWITGDLVGRGPKSLETLRFVKSLGDSAKIVLGNHDLHLLAIHQGIHSDKESDKLSALLNAPDCDELLTWLRFQPLFRRHPEFNFVMVHAGISPQWTIQQAQGYAQEVQNILQGNEFKKLLKNMYGNHPASWNDSSQGIKRLRFIINALTRMRYCLLDGSLEFYSKLAPEQTDSTIIKPWFEINTLDQSSDIIFGHWAALLGTGTKQGIYALDTGCVWGNSLSMLRWQDKKMFSFACQRQRVHSK | Function: Hydrolyzes diadenosine 5',5'''-P1,P4-tetraphosphate to yield ADP.
Catalytic Activity: H2O + P(1),P(4)-bis(5'-adenosyl) tetraphosphate = 2 ADP + 2 H(+)
Sequence Mass (Da): 31453
Sequence Length: 276
EC: 3.6.1.41
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Q8Y1K9 | MTVASIPPHAIGDLQGCCSPLQTLLTALPANAPLRFVGDLVNRGPDSLGTLRRVIMLCEGGRARAVLGNHDIHLLAVAAGVRKLGKRDTLDDILGAPDCDALIHWLRHQPLAIFENGFLMVHAGVLPQWTTGDVLELAGAVERELRSPHWKTFLTDAFGNQPAKWSSDLIGIDRLRLTINALTRLRFCTPDGAMEFETTDADGAPDGHVPWFDVPGRRTRGTPIAFGHWSTRGLVMRDDLLGLDTGCVWGGKLTAARMTLAPAGREVIQVACEQAQDPLAHKK | Function: Hydrolyzes diadenosine 5',5'''-P1,P4-tetraphosphate to yield ADP.
Catalytic Activity: H2O + P(1),P(4)-bis(5'-adenosyl) tetraphosphate = 2 ADP + 2 H(+)
Sequence Mass (Da): 30660
Sequence Length: 283
EC: 3.6.1.41
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Q21MT2 | MATYAVGDIQGCYRALKLLLKKVKFNADNDHLWVAGDLVNRGPESLKSLRYIKKLGPSATLVLGNHDLHLLAHAYGVRTLNPKDTLAPILTAKDSDELLEWLQAQPLLHYDAEFDAVLVHAGIPPIWSIENALNYALEVEQALSTTQTAAAFFVDMYGNQPDVWQPSLEGTARLRLITNYLTRMRFCSPTGKLELQTKNAPSLPPTGFAPWYTHKHNKWGNTKILFGHWAALMGETRSKQFIGLDTGCVWGGALTMMRLEDGQFFAVDCPC | Function: Hydrolyzes diadenosine 5',5'''-P1,P4-tetraphosphate to yield ADP.
Catalytic Activity: H2O + P(1),P(4)-bis(5'-adenosyl) tetraphosphate = 2 ADP + 2 H(+)
Sequence Mass (Da): 30183
Sequence Length: 271
EC: 3.6.1.41
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Q28IW8 | MDSEVLRDGRILDLIDDAWREDKLPYEDVTIPLNELPEPEQDNGGATESVKEQEMKWADLALQYLHENISSSGS | Function: Component of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin ligase that controls progression through mitosis and the G1 phase of the cell cycle. The APC/C complex acts by mediating ubiquitination and subsequent degradation of target proteins: it mainly mediates the forma... |
Q58DR0 | MAASSSSSSAGGVSGSSVAGSGFSVSDLAPPRKALFTYPKGAGEMLEDGSERFLCESVFSYQVASTLKQVKHDQQVARMEKLAGLVEELEADEWRFKPIEQLLGFTPSSG | Function: Component of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin ligase that controls progression through mitosis and the G1 phase of the cell cycle. The APC/C complex acts by mediating ubiquitination and subsequent degradation of target proteins: it mainly mediates the forma... |
Q96DE5 | MAASSSSSSAGGVSGSSVTGSGFSVSDLAPPRKALFTYPKGAGEMLEDGSERFLCESVFSYQVASTLKQVKHDQQVARMEKLAGLVEELEADEWRFKPIEQLLGFTPSSG | Function: Component of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin ligase that controls progression through mitosis and the G1 phase of the cell cycle. The APC/C complex acts by mediating ubiquitination and subsequent degradation of target proteins: it mainly mediates the forma... |
Q6DJQ9 | MAASSSSSSAGGVSGSSVTGSGFSVSDLAPPRKALFTCPKAAGEMLEADGSERFLCESVFSYQVASTLKQVKHDQQVSRMEKLAGLVEELEADEWRYTPIEQLLGFTPSSGGK | Function: Component of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin ligase that controls progression through mitosis and the G1 phase of the cell cycle. The APC/C complex acts by mediating ubiquitination and subsequent degradation of target proteins: it mainly mediates the forma... |
Q5ATG7 | MSSVRESSKDESIVHPPKAPESEPFPDGGARAWMVALGAGGVLFCTFGYVNAFGVYQDYYITHQLSNYSASDIAWIGSVQTFFLFGSGLVGGPLFDRYGAKVIWAPAVLVIFSVMMTSLCTKFYQFFLAQGILGGMSMGLSLAPALSSTAQYFQKKRAAAMGITIAGSSLGGVIFPIALEQMLYSSLGFAWAVRIVGFIILGVMSFAVLGIRARLPPKRQRFLKLEAFKKTHYVATLTAVFFLNVGIFTPFFYLPLYGQSHGMSTGLAFYLIAIQNASSFFGRLVPGVIADKIGPYNMLSTVSIITAIITFCWIRMTTNA... | Function: Efflux pump that may be involved in the secretion of aspyridones .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 52253
Sequence Length: 487
Subcellular Location: Cell membrane
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Q5ATG5 | MAEISSVPFAEPPYLRGLPSPYYNESHRRFQKACRAFLYENLLKHAMEWEKAGTVPEHVFSDFCKANMLLPNLPAPLPVAWLKRLGIHDILGVKVEEWDYLHTGIYSDEMARSGLSGPSGSLTAGFAFGTPPIIKYGSKELQEKFLPDLLTGKKRNCIAITEPDAGSDVAGITTTATKSADGKYYIVNGNKKWITNGIWSDYSTMAVRTGGPGAGGLSLLVVPLKNYPGVTMQRLKVSGQITGGTTYIELDEVKVPVENLIGLEGDGMKMIMNNFNHERLTIAVGVTRQARVALSTAFSYCLKREAFGKTLMDQPVVRHR... | Function: Acyl-CoA dehydrogenase; part of the gene cluster that mediates the biosynthesis of aspyridones . The polyketide-amino acid backbone preaspyridone A is first assembled by the PKS-NRPS hybrid apdA . The assembly of preaspyridone A is initiated by loading of malonyl-CoA onto apdA, followed by decarboxylation to ... |
Q5XF07 | MKRFFKPIEKENSPAAKKPCLSPEKRDGDGDGVEEEKNQNEPSKFMTWNANSFLLRVKNDWSQFSKFVSDFDPDVIAIQEVRMPAAGGKGKPKNHEELSDDTKVLREEKQILTRALSSPPFGNYGVWWSLADSKYAGTALLVKKCFKPRKVYFNLDKLASKHEPDGRVILAEFETFRLLNTYSPNNGWKDEENAFQRRRKWDKRIVEFLNKTSDKPLIWCGDLNVSHEEIDVSHPEFFATAKLNGYVPPNKEDCGQPGFTPSERGRFGATIKEGRLVDAYRYLHKEQEMESGFSWSGNPIGKYRGKRMRIDYFLVSEQLK... | Cofactor: Probably binds two magnesium ions per subunit.
Function: Apurinic/apyrimidinic (AP) endonuclease involved in active DNA demethylation and gene imprinting . According to a report, also displays an in vitro 3'-phosphatase activity . According to another report, has no in vitro 3'-phosphatase activity . Catalyze... |
O73942 | MDGYALFYLVGALRDGSVYRYSRNYYVIWYSSNKDYLERVIVSKLRILGFHNVRVYQYKRGAYRVRISSKQLFHILVNQFEHPLSTSSRKTPWPTPQRVKDGPLALQIEYVKGFVDAEGSVIKSSKGVQVDVSQQIMEPLKFLAQVLEKVGVKVTGIYLGSDGVWRLRIASLASLRRFAHYIGFRHPCKSKKLNELLGRPLPGPSKLKGIGGGAPQGVEPAA | Cofactor: 1-5 mM manganese gives higher cleavage activity than the same concentration of magnesium.
Function: Endonuclease involved in 16S rRNA intron I-alpha homing. Recognizes the minimal target 5'-GCAAGGCTGAAACTTAAAGG-3'; generates 4 base 3' protruding ends 5'-AAAC-3' and 5'-GTTT-3'.
Sequence Mass (Da): 25031
Sequen... |
Q97VF1 | MPNIEKYEIFLDFNGNEYEGVEKIYLNSEEEKLELDSVNLEIRSVKSDGKDTKFELKGEKLVIYGKIERELEIKFKGKASRDSILGIYVAPYDGKGMITTQFEAVYARRFIPCFDHPAMKARFKLSVRVQKGLKVISNMPVERIEEDVDGKVIYRFQETPKMSTYLLYLGIDEFEEISDNSKQPTVILATVPGKSKRGLFAINVARKVIEFYEKYFEIPYQLPKVHLIQVPEFAAGAMENWGAITFRETALLADDSSSISQKFRVAEVVAHELAHQWFGNLVTLKWWDDLWLNESFATFMSYKSIKHLFPQWDSEGHLIY... | Cofactor: Binds 1 zinc ion per subunit.
Sequence Mass (Da): 90143
Sequence Length: 784
Subcellular Location: Cytoplasm
EC: 3.4.11.-
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F4JNY0 | MKIVTYNVNGLRQRVSQFDSLLKLLDSFDADIICFQETKLRRQELTADLAIADGYESFFSCTRTSEKGRTGYSGVATFCRVKSASSSCETALPVTAEEGITGLVNSNSRGGKSETSTVAEGLEEYEKEELLMIDQEGRCVITDHGHFVVFNVYGPRAVADDADRIEFKHRFYGVLERRWECLLRQGRRVFVVGDLNIAPFAMDRCEAGPDFEKNEFRKWFRSLLVERGGSFSDVFRSKHPERKDAFTCWSSSSGAEQFNYGSRIDHILVAGSCLHQDEDKQGHSFLACHVKECDILTEYKRFKNENMPTRWKGGLVTKFK... | Cofactor: Probably binds two magnesium or manganese ions per subunit.
Function: Exhibits apurinic/apyrimidinic (AP) endonuclease activity in vitro . By contrast, another report show that APE2 has no biochemical activity . Unable to catalyze the conversion of 3'-phosphor-alpha,beta-unsaturated aldehyde (3'-PUA) to 3'-OH... |
Q59KZ1 | MASNNTSQRSGFSSFFCRLKTYFCNHFLCLFVLSFFPLSFRRLCLLCHLCEKSNLWLSSDNSASVVKQEREVLPTNVKPLHYDLTIEPIFDNFTFKGEETIDFQVNEKTNFITLNSLEIEVQEAKIDGKSVTDISFDAGKQTVTFKFDDDLSTGSIAKLYIKFTGELNDKMAGFYRASYQEDGKTKYMATTQMEPTDCRRAFPSYDEPAAKSKFTISLIADKELVCLSNSSEKETVSLDGNKKKVTFQTTPLMSTYLVAFIVGDLRYISNDNYRVPIRVYSTPGTEHLGEYSANIAAQTLKFFDQQFGIDYPYDKLDMVA... | Cofactor: Binds 1 zinc ion per subunit.
Function: Metalloprotease that specifically hydrolyzes peptides with N-terminal alanine, arginine and leucine residues.
Sequence Mass (Da): 104382
Sequence Length: 924
Subcellular Location: Secreted
EC: 3.4.11.-
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P95928 | MIKVNRYEIFLDFSFQTGDYKGYEKIEMESDEETVVLDAVGLKIVKAKVNGKEIEFSQDESRVNVKSGSFSGILEVEFEGKVTERKLVGIYKASYKDGYVISTQFEATHARDFIPCFDHPAMKARFKLTVRVDKGLKVISNMPVVREKEENGKVVYEFDETPKMSTYLLYLGIGNFEEIRDEGKIPTIIVATIPGKVQKGRFSMQISRNSIEFYEKYFEIPYQLPKVHLIAIPEFAYGAMENWGAITFRETALLADDSSSVYQKFRVAEVVAHELAHQWFGNLVTLKWWDDLWLNESFATFMSHKAISQLFPSWNFWDYF... | Cofactor: Binds 1 zinc ion per subunit.
Function: Preferentially acts as a leucyl-aminopeptidase, although it also has activity against other substrates.
PTM: Can be phosphorylated by cell extracts.
Catalytic Activity: Release of an N-terminal amino acid, Xaa-|-Yaa-, in which Xaa is preferably Leu, but may be other ami... |
P37302 | MHFSLKQLAVAAFYATNLGSAYVIPQFFQEAFQQEEPIENYLPQLNDDDSSAVAANIPKPHIPYFMKPHVESEKLQDKIKVDDLNATAWDLYRLANYSTPDYGHPTRVIGSKGHNKTMEYILNVFDDMQDYYDVSLQEFEALSGKIISFNLSDAETGKSFANTTAFALSPPVDGFVGKLVEIPNLGCEEKDYASVVPPRHNEKQIALIERGKCPFGDKSNLAGKFGFTAVVIYDNEPKSKEGLHGTLGEPTKHTVATVGVPYKVGKKLIANIALNIDYSLYFAMDSYVEFIKTQNIIADTKHGDPDNIVALGAHSDSVEE... | Cofactor: Binds 2 Zn(2+) ions per subunit.
Catalytic Activity: Preferentially, release of N-terminal lysine.
Sequence Mass (Da): 60137
Sequence Length: 537
Subcellular Location: Vacuole
EC: 3.4.11.15
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Q7SZP9 | MEPTSEYTETYDYYDTGYNDSGCDYSEWEPSYSLIPVLYMLIFILGLSGNGVVIFTVWRAKSKRRAADVYIGNLALADLTFVITLPLWAVYTALGYHWPFGVALCKISSYVVLVNMYASVFCLTCLSFDRYLAIVHSLSSGRLRSRATMLASLGAIWFLSCLLAVPTLLFRTTVDDTGSNRTTCAMDFSLVTLNQDHESLWIAGLSLSSSALGFLLPFLAMTVCYCFIGCTVTRHFSHLRKEDQKKRRLLKIITTLVVVFAFCWTPFHVLKSMDALSYLDLAPNSCGFLHFLLLAHPYATCLAYVNSCLNPFLYAFFDLR... | Function: Receptor for apelin receptor early endogenous ligand (apela) and apelin (apln) hormones coupled to G proteins that inhibit adenylate cyclase activity . Plays a key role in early development such as gastrulation, blood vessels formation and heart morphogenesis by acting as a receptor for apela hormone, promoti... |
P79960 | METEGLSPMLYEDDYYYGNETGLQPCDETDWDFSYSLLPVFYMIVFVLGLSGNGVVIFTVWKSKPKRRSADTYIGNLALADLAFVVTLPLWATYTALGFHWPFGSALCKLSSYLVLLNMFASVFCLTCLSFDRYLAIVHSLSSAKLRSRSSIIVSLAVIWLFSGLLALPSLILRDTRVEGNNTICDLDFSGVSSKENENFWIGGLSILTTVPGFLLPLLLMTIFYCFIGGKVTMHFQNLKKEEQKKKRLLKIIITLVVVFAICWLPFHILKTIHFLDLMGFLELSCSTQNIIVSLHPYATCLAYVNSCLNPFLYAFFDLR... | Function: Receptor for apelin receptor early endogenous ligand (apela) and apelin (apln) hormones coupled to G proteins that inhibit adenylate cyclase activity . Plays a key role in early development such as gastrulation, blood vessels formation and heart morphogenesis by acting as a receptor for apela hormone, promoti... |
A0T2N3 | MNAMDNMTADYSPDYFDDAVNSSMCEYDEWEPSYSLIPVLYMLIFILGLTGNGVVIFTVWRAQSKRRAADVYIGNLALADLTFVVTLPLWAVYTALGYHWPFGVALCKISSYVVLLNMYASVFCLTCLSLDRYMAIVHSLTSTQLRTRGHMRASLTAIWLLSGVLAAPTLLFRTTVYDVETNRTSCAMDFNLVVSQPGQETYWIAGLSISSTALGFLIPLLAMMVCYGFIGCTVTRHFNSLRKEDQRKRRLLKIITTLVVVFAACWMPFHVVKTMDALSYLNLAPDSCTFLNLLLLAHPYATCLAYVNSCLNPLLYAFFD... | Function: Receptor for apelin receptor early endogenous ligand (apela) and apelin (apln) hormones coupled to G proteins that inhibit adenylate cyclase activity . Plays a key role in early development such as gastrulation, blood vessels formation and heart morphogenesis by acting as a receptor for apela hormone, promoti... |
Q9WV08 | MEDDGYNYYGADNQSECDYADWKPSGALIPAIYMLVFLLGTTGNGLVLWTVFRTSREKRRSADIFIASLAVADLTFVVTLPLWATYTYREFDWPFGTFSCKLSSYLIFVNMYASVFCLTGLSFDRYLAIVRPVANARLRLRVSGAVATAVLWVLAALLAVPVMVFRSTDASENGTKIQCYMDYSMVATSNSEWAWEVGLGVSSTAVGFVVPFTIMLTCYFFIAQTIAGHFRKERIEGLRKRRRLLSIIVVLVVTFALCWMPYHLVKTLYMLGSLLHWPCDFDIFLMNVFPYCTCISYVNSCLNPFLYAFFDPRFRQACTS... | Function: Receptor for apelin receptor early endogenous ligand (APELA) and apelin (APLN) hormones coupled to G proteins that inhibit adenylate cyclase activity. Plays a key role in early development such as gastrulation, blood vessels formation and heart morphogenesis by acting as a receptor for APELA hormone . May pro... |
Q43295 | MIAAGAKSLLGLSMASPKGIFDSNSMSNSRSVVVVRACVSMDGSQTLSHNKNGSIPEVKSINGHTGQKQGPLSTVGNSTNIKWHECSVEKVDRQRLLDQKGCVIWVTGLSGSGKSTLACALNQMLYQKGKLCYILDGDNVRHGLNRDLSFKAEDRAENIRRVGEVAKLFADAGIICIASLISPYRTDRDACRSLLPEGDFVEVFMDVPLSVCEARDPKGLYKLARAGKIKGFTGIDDPYEPPLNCEISLGREGGTSPIEMAEKVVGYLDNKGYLQA | Function: Catalyzes the synthesis of activated sulfate. Essential for plant reproduction and viability. Required for the production of glucosinolates.
Catalytic Activity: adenosine 5'-phosphosulfate + ATP = 3'-phosphoadenylyl sulfate + ADP + H(+)
Sequence Mass (Da): 29787
Sequence Length: 276
Pathway: Sulfur metabolism... |
O49196 | MEGLAIRASRPSVFCSIPGLGGDSHRKPPSDGFLKLPASSIPADSRKLVANSTSFHPISAVNVSAQASLTADFPALSETILKEGRNNGKEKAENIVWHESSICRCDRQQLLQQKGCVVWITGLSGSGKSTVACALSKALFERGKLTYTLDGDNVRHGLNRDLTFKAEHRTENIRRIGEVAKLFADVGVICIASLISPYRRDRDACRSLLPDGDFVEVFMDVPLHVCESRDPKGLYKLARAGKIKGFTGIDDPYEAPVNCEVVLKHTGDDESCSPRQMAENIISYLQNKGYLEG | Function: Catalyzes the synthesis of activated sulfate. Essential for plant reproduction and viability. Required for the production of glucosinolates.
Catalytic Activity: adenosine 5'-phosphosulfate + ATP = 3'-phosphoadenylyl sulfate + ADP + H(+)
Sequence Mass (Da): 31977
Sequence Length: 293
Pathway: Sulfur metabolism... |
Q9SRW7 | MSTVGNSTNIFWQESPIGKTERQKLLNQKGCVVWITGLSGSGKSTLACSLSRELNNRGKLSYILDGDNLRHGLNKDLGFKAEDRVENIRRVGEVAKLFADAGLICIASLISPYRKDRDACREMIQNSSFIEVFMNMSLQLCEARDPKGLYKLARAGKIKGFTGIDDPYESPLNCEIELKEKEGECPSPVAMAEEVISYLEDKGFLQNE | Function: Catalyzes the synthesis of activated sulfate for the sulfation of secondary metabolites, including the glucosinolates . Essential for plant reproduction and viability .
Catalytic Activity: adenosine 5'-phosphosulfate + ATP = 3'-phosphoadenylyl sulfate + ADP + H(+)
Sequence Mass (Da): 23146
Sequence Length: 20... |
Q84JF0 | MDVAAMARCVGRCYVSPAFGESESHRLSERRFLKLSSSTNSDPAGSKSLKLRGKIHRRMSYFRPIMAKDESISSRSGETKQINGKQKNIVWHDCPVTKSDRQELIKQKGCVIWITGLSGSGKSSLACALSRALHNRGKLSYILDGDNVRHGLNSDLSFEADDRAENIRRVGEVAKLFADSGIICIASLISPYRIERAACRALLPQGDFIEVFMDVPLHVCEARDPKGLYKRARAGKIKGFTGVDDPYEAPLDCEIVIQNSRDKGLSSSSSSSSSPSSSSSSLCEMADIVVSYLDQNGYLKKHSTKSRNCM | Function: Catalyzes the phosphorylation of adenosine 5'-phosphosulfate to 3'-phosphoadenylyl sulfate, which is the activated sulfate form for sulfation reactions. Essential for plant reproduction and viability.
Catalytic Activity: adenosine 5'-phosphosulfate + ATP = 3'-phosphoadenylyl sulfate + ADP + H(+)
Sequence Mass... |
A1Z9X0 | MQKMPSQILNDGSSVSLNSASMNMANTPNSITVKTAYNGQIIITTINKNISYEELCYEIRNICRFPLDQPFTIKWVDEENDPCTISTKMELDEAIRLYEMNFDSQLVIHVFPNVPQAPGLSCDGEDRSIYRRGARRWRKLYRVNGHIFQAKRFNRRAFCAYCQDRIWGLGRQGFKCIQCKLLVHKKCHKLVQKHCTDQPEPLVKERAEESSDPIPVPLPPLPYEAMSGGAEACETHDHAHIVAPPPPEDPLEPGTQRQYSLNDFELIRVIGRGSYAKVLMVELRRTRRIYAMKVIKKALVTDDEDIDWVQTEKHVFETAS... | Function: Serine/threonine protein kinase which is required for apico-basal cell polarity in the germ line as well as in epithelial and neural precursor cells, for epithelial planar cell polarity and for cell proliferation. During oocyte development, required for the posterior translocation of oocyte specification fact... |
P02656 | MQPRVLLVVALLALLASARASEAEDASLLSFMQGYMKHATKTAKDALSSVQESQVAQQARGWVTDGFSSLKDYWSTVKDKFSEFWDLDPEVRPTSAVAA | Function: Component of triglyceride-rich very low density lipoproteins (VLDL) and high density lipoproteins (HDL) in plasma . Plays a multifaceted role in triglyceride homeostasis . Intracellularly, promotes hepatic very low density lipoprotein 1 (VLDL1) assembly and secretion; extracellularly, attenuates hydrolysis an... |
P33622 | MQPRTLLTVALLALLASARAEEVEGSLLLGSVQGYMEQASKTVQDALSSVQESDIAVVARGWMDNHFRFLKGYWSKFTDKFTGFWDSNPEDQPTPAIES | Function: Component of triglyceride-rich very low density lipoproteins (VLDL) and high density lipoproteins (HDL) in plasma. Plays a multifaceted role in triglyceride homeostasis. Intracellularly, promotes hepatic very low density lipoprotein 1 (VLDL1) assembly and secretion; extracellularly, attenuates hydrolysis and ... |
P53933 | MNSQGYDESSSSTAATSGPTSGDPRMGKKQRFMNLIRTTKDVYIPNLTSSISQKTMDGIRSTTNSFEGYNDLPMELPHNTTITYFPTYTTTNLVDPDGLSAPRKDFETTVRCAVSYPGNPTSRRNRWLLSLCKQYLRTGTAEADVAPVVPPHLEEDSGDLNDSQSSIESSLSSKSENRYSHMGIQEEDVLNERIQGFLSKKVPNTPVVVDLLPKDKLRGDTASFFGTTDSYGNLLIKAETDFLPSKINITLDTPIEGHADPISETFPANYVSPYGIGLISDIDDTIKHTGVTGDRRSMFRNVFIHDVQSWVIDGVPLWYK... | Function: Mg(2+)-dependent phosphatidate (PA) phosphatase which catalyzes the dephosphorylation of PA to yield diacylglycerol. May play a role in vesicular trafficking through its PAP activity at cortical actin patches . Can also utilize diacylglycerol pyrophosphate and lyso-PA as substrates with specificity constants ... |
P42061 | MKRRKTALMMLSVLMVLAIFLSACSGSKSSNSSAKKSAGKPQQGGDLVVGSIGEPTLFNSLYSTDDASTDIENMLYSFLTKTDEKLNVKLSLAESIKELDGGLAYDVKIKKGVKFHDGKELTADDVVFTYSVPLSKDYKGERGSTYEMLKSVEKKGDYEVLFKLKYKDGNFYNNALDSTAILPKHILGNVPIADLEENEFNRKKPIGSGPFKFKEWKQGQYIKLEANDDYFEGRPYLDTVTYKVIPDANAAVAQLQAGDINFFNVPATDYKTAEKFNNLKIVTDLALSYVYIGWNEKNELFKDKKVRQALTTALDRESIV... | Function: This protein is a component of an oligopeptide permease, a binding protein-dependent transport system. This APP system can completely substitute for the OPP system in both sporulation and genetic competence. AppA can bind and transport tetra- and pentapeptides but not tripeptides.
Location Topology: Lipid-anc... |
P42062 | MAAYIIRRTLMSIPILLGITILSFVIMKAAPGDPMTLMMDPKISQADREQFIEKYGLNDPQYVQYLKWLGNMVQGDFGTSIVRKGTPVSELIMARLPNTLLLMLVSTILALMISIPFGVLSAKRPYSKIDYGITFTSFIGLAIPNFWFGLILIMVLSVNLGWFPTGGVETLNTEFNIFDRIHHLILPAFVLATADMAGLTRYTRSNMLDVLNQDYIRTARAKGFKENRVLFKHGLRNALLPVITIFGLMIPSFIGGSVVVEQIFTWPGLGKLFVDSAFQRDYPVIMAMTVISAVLVVVGNLIADILYAIVDPRIEY | Function: This protein is a component of an oligopeptide permease, a binding protein-dependent transport system. This APP system can completely substitute for the OPP system in both sporulation and genetic competence, though, unlike OPP, is incapable of transporting tripeptides. Probably responsible for the translocati... |
P26458 | MFDYETLRFIWWLLIGVILVVFMISDGFDMGIGCLLPLVARNDDERRIVINSVGAHWEGNQVWLILAGGALFAAWPRVYAAAFSGFYVAMILVLCSLFFRPLAFDYRGKIADARWRKMWDAGLVIGSLVPPVVFGIAFGNLLLGVPFAFTPQLRVEYLGSFWQLLTPFPLLCGLLSLGMVILQGGVWLQLKTVGVIHLRSQLATKRAALLVMLCFLLAGYWLWVGIDGFVLLAQDANGPSNPLMKLVAVLPGAWMNNFVESPVLWIFPLLGFFCPLLTVMAIYRGRPGWGFLMASLMQFGVIFTAGITLFPFVMPSSVSP... | Cofactor: May bind up to 3 heme groups per complex.
Function: A terminal oxidase that catalyzes quinol-dependent, Na(+)-independent oxygen uptake. Prefers menadiol over other quinols although ubiquinol was not tested . Generates a proton motive force using protons and electrons from opposite sides of the membrane to ge... |
P42063 | MSELQTTPSPEIRLKENISKKPETMTKIFWEKFSKNKLAILGAVILFIIIMSAVFAPLIAPYPQEQQSLLDKYKAPGLEHLMGTDKFGRDIFSRILYGARVSLLVGFASVVGSILIGTVLGALAGYFRGIVDAVIMRVVDIVLSIPDIFLLITLVTIFKPGVDKLILIFCLTGWTTTARLVRGEFLSLRSREYVLAAKTIGTKTHKIIFSHILPNALGPIIVSATLKVGSVILAESALSYLGFGIQPPIASWGNMLQDAQNFTVMIQAWWYPLFPGLFILMTVLCFNFVGDGLRDALDPKNIK | Function: This protein is a component of an oligopeptide permease, a binding protein-dependent transport system. This APP system can completely substitute for the OPP system in both sporulation and genetic competence, though, unlike OPP, is incapable of transporting tripeptides. Probably responsible for the translocati... |
P26459 | MWDVIDLSRWQFALTALYHFLFVPLTLGLIFLLAIMETIYVVTGKTIYRDMTRFWGKLFGINFALGVATGLTMEFQFGTNWSFYSNYVGDIFGAPLAMEALMAFFLESTFVGLFFFGWQRLNKYQHLLVTWLVAFGSNLSALWILNANGWMQYPTGAHFDIDTLRMEMTSFSELVFNPVSQVKFVHTVMAGYVTGAMFIMAISAWYLLRGRERNVALRSFAIGSVFGTLAIIGTLQLGDSSAYEVAQVQPVKLAAMEGEWQTEPAPAPFHVVAWPEQDQERNAFALKIPALLGILATHSLDKPVPGLKNLMAETYPRLQR... | Cofactor: May bind up to 3 heme groups per complex.
Function: A terminal oxidase that catalyzes quinol-dependent, Na(+)-independent oxygen uptake. Prefers menadiol over other quinols although ubiquinol was not tested . Generates a proton motive force using protons and electrons from opposite sides of the membrane to ge... |
P42064 | MSTLLEVNNLKTYFFRKKEPIPAVDGVDFHISKGETVALVGESGSGKSITSLSIMGLVQSSGGKIMDGSIKLEDKDLTSFTENDYCKIRGNEVSMIFQEPMTSLNPVLTIGEQITEVLIYHKNMKKKEARQRAVELLQMVGFSRAEQIMKEYPHRLSGGMRQRVMIAIALSCNPKLLIADEPTTALDVTIQAQVLELMKDLCQKFNTSILLITHDLGVVSEAADRVIVMYCGQVVENATVDDLFLEPLHPYTEGLLTSIPVIDGEIDKLNAIKGSVPTPDNLPPGCRFAPRCPKAMDKCWTNQPSLLTHKSGRTVRCFLY... | Function: This protein is a component of an oligopeptide permease, a binding protein-dependent transport system. This APP system can completely substitute for the OPP system in both sporulation and genetic competence, though, unlike OPP, is incapable of transporting tripeptides. Probably responsible for energy coupling... |
P42065 | MTAANQETILELRDVKKYFPIRSGLFQRKVGDVKAVDGVSFSLKKGETLGIVGESGCGKSTAGRTMIRLYKPTEGQILFKGQDISNLSEEKLRKSVRKNIQMVFQDPFASLNPRKTLRSIIKEPFNTHNMYTMRERNEKVEELLARVGLHPSFAGRYPHEFSGGQRQRIGIARALTLNPELIIADEPVSALDVSIQAQVINLMEELQEEFNLTYLFISHDLSVVRHISDRVGVMYLGKMMELTGKHELYDNPLHPYTQALLSSVPVTRKRGSVKRERIVLKGELPSPANPPKGCVFHTRCPVAKPICKEQIPEFKEAAPS... | Function: This protein is a component of an oligopeptide permease, a binding protein-dependent transport system. This APP system can completely substitute for the OPP system in both sporulation and genetic competence, though, unlike OPP, is incapable of transporting tripeptides. Probably responsible for energy coupling... |
P24244 | MWYLLWFVGILLMCSLSTLVLVWLDPRLKS | Function: Might be part of cytochrome bd-II oxidase (appB and appC). Able to restore reductant resistance to a cydX deletion mutant upon overexpression. CydX and this protein may have some functional overlap.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 3597
Sequence Length: 30
Subcellular Locati... |
A2VEY9 | MNLLCCCCCSNMAPNQRVTRKWELFAGRNKFYCDGLLMSAPHTGVFYLTCILITGTSALFFAFDCPFLADSINPAIPIVGAVLYFFTMSSLLRTTFTDPGVIPRASNDEAAYIEKQIEVPNSLNSPTYRPPPRTKEVLVKGQTVKLKYCFTCKIFRPPRASHCSLCDNCVDRFDHHCPWVGNCVGKRNYRFFYLFLVSLAFLAVFIFSCSVTHLVLLMKKEHEVFNVIKAAPFTVIVVFICFFSIWSVIGLAGFHTYLTTSDQTTNEDLKGSFSSKGGPRTQNPYSRGNICLNCCHILCGPMTPSLIDRRGIATDEFIQQ... | Function: Palmitoylates Dlish which is required for the apical cell cortex localization, total cellular level and full activity of dachs.
Catalytic Activity: hexadecanoyl-CoA + L-cysteinyl-[protein] = CoA + S-hexadecanoyl-L-cysteinyl-[protein]
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 75008
Seq... |
O94353 | MSLTSVLWNFVAKLAVDHGLNTNPDQVFQTVENVGKSFEKYETSFLKSLFNGNLGLSLPSAINILTLIIVLYFSLVIVNKTTSIALALFKTLAVISFFLLIGCLFAYWFINNGSF | Function: Involved in the regulation of lipid homeostasis in the endoplasmic reticulum, thereby impacting nuclear pore complex biogenesis and localization, and nucleocytoplasmic mRNA transport.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 12762
Sequence Length: 115
Subcellular Location: Nucleus me... |
P40532 | MDATQPQYELSVVTQCLKSAIDVIQWLIPTITKFSQSHPLVFQLLFIFFTFYVFYKLLMNFITLVKRFLYLTLVVTCIGIYMRGSQQFLTVDLLNFYNFVMSNRYYAFKIYTLFINALEREINTVYHLAQMKMEQLLK | Function: Involved in the regulation of lipid homeostasis in the endoplasmic reticulum, thereby impacting nuclear pore complex biogenesis and localization, and nucleocytoplasmic mRNA transport.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 16508
Sequence Length: 138
Subcellular Location: Nucleus me... |
P92979 | MAMSVNVSSSSSSGIINSRFGVSLEPKVSQIGSLRLLDRVHVAPVSLNLSGKRSSSVKPLNAEPKTKDSMIPLAATMVAEIAEEVEVVEIEDFEELAKKLENASPLEIMDKALEKYGNDIAIAFSGAEDVALIEYAHLTGRPFRVFSLDTGRLNPETYRFFDAVEKHYGIRIEYMFPDSVEVQGLVRSKGLFSFYEDGHQECCRVRKVRPLRRALKGLKAWITGQRKDQSPGTRSEIPVVQVDPVFEGLDGGVGSLVKWNPVANVEGNDVWNFLRTMDVPVNTLHAAGYISIGCEPCTKAVLPGQHEREGRWWWEDAKAK... | Cofactor: Binds 1 [4Fe-4S] cluster.
Function: Reduces sulfate for Cys biosynthesis. Substrate preference is adenosine-5'-phosphosulfate (APS) >> 3'-phosphoadenosine-5'-phosphosulfate (PAPS). Uses glutathione or DTT as source of protons.
Catalytic Activity: AMP + glutathione disulfide + 2 H(+) + sulfite = adenosine 5'-p... |
Q2KUE4 | MQTDYAEVVRRTIRSVPDWPVPGVTFRDITPVLQDPRTFRALVDLFVYRYMRQRLDLVAGVDARGFILGSVLAYELNLGFVPVRKKGKLPYRTVAEEYSLEYGNATVEIHTDAVRTGQRVLLVDDLIATGGTMVAAIKLLQRLGANVVEAAAIIDLPYIGGSQHIAETGTPLYTVCQFSATD | Function: Catalyzes a salvage reaction resulting in the formation of AMP, that is energically less costly than de novo synthesis.
Catalytic Activity: AMP + diphosphate = 5-phospho-alpha-D-ribose 1-diphosphate + adenine
Sequence Mass (Da): 20131
Sequence Length: 182
Pathway: Purine metabolism; AMP biosynthesis via salva... |
O51718 | MKNKTEYYDQFISKIPNFPKKGVLFYDITSVLLKPEVYSSLINEVYSFYNFKKIDCIAVVESRGYLIGAPLSLKMQLPLVLIRKEGKLPREVFSEEYELEYGFGRIEVHKDDVRTYSNILLIDDILATGGTLKSSAILLERAGGKVKDIFCFIELCAINGRQSLESYEVNSLVRYN | Function: Catalyzes a salvage reaction resulting in the formation of AMP, that is energically less costly than de novo synthesis.
Catalytic Activity: AMP + diphosphate = 5-phospho-alpha-D-ribose 1-diphosphate + adenine
Sequence Mass (Da): 20173
Sequence Length: 176
Pathway: Purine metabolism; AMP biosynthesis via salva... |
Q56JW4 | MADPELQLVARRIRSFPNFPIPGVLFRDISPVLKDPTSFRASINLLANHLKKAHGGRIDYIAGLDSRGFLFGPSLAQELGLGCILIRKRGKLPGPTVCASYALEYGKGELEIQRDALEPGQKVVVVDDLLATGGTMCAACELLGQLRAEVLECVSLVELTSLKGREKLGAVPFFSLLQYE | Function: Catalyzes a salvage reaction resulting in the formation of AMP, that is energically less costly than de novo synthesis.
Catalytic Activity: AMP + diphosphate = 5-phospho-alpha-D-ribose 1-diphosphate + adenine
Sequence Mass (Da): 19537
Sequence Length: 180
Pathway: Purine metabolism; AMP biosynthesis via salva... |
Q89SB5 | MTFDHDLKASVRTIPDYPKPGIMFRDITTLLADARAFRRAVDELVNPWAGNKIDKVAGMEARGFIIGGAVAHQLSAGFVPIRKKGKLPHTTVRIAYSLEYGIDEMEMHVDAIQPGERVILVDDLIATGGTAEGAVKLLRQIGANVVAACFIIDLPELGGAAKLRAMDVPVRTLMTFEGH | Function: Catalyzes a salvage reaction resulting in the formation of AMP, that is energically less costly than de novo synthesis.
Catalytic Activity: AMP + diphosphate = 5-phospho-alpha-D-ribose 1-diphosphate + adenine
Sequence Mass (Da): 19406
Sequence Length: 179
Pathway: Purine metabolism; AMP biosynthesis via salva... |
C0QVL4 | MELKDYIRNIQDYPKKGILFRDITTLLQNKDAFKYAIDKMAEQISSEKIDYIVGAESRGFLIGSALAYKLNCGFIPVRKKGKLPYKTISEEYALEYGTDTLYMHEDAIKKGERVLIVDDLIATGGTALAMIKMVEKLEGIVVGSSFLIELKELNGRKEIEKYPVNVLIEY | Function: Catalyzes a salvage reaction resulting in the formation of AMP, that is energically less costly than de novo synthesis.
Catalytic Activity: AMP + diphosphate = 5-phospho-alpha-D-ribose 1-diphosphate + adenine
Sequence Mass (Da): 19298
Sequence Length: 170
Pathway: Purine metabolism; AMP biosynthesis via salva... |
Q038P1 | MTINFKDYIASVQDYPEPGIIFRDISPLMADGKAYAAATDEIAAYAQDKGVEMIVGPEARGFIVGCPVAYKLGIGFAPARKKGKLPRPTVKASYDLEYGEATLYLHKDAIKPGQRVLVCDDLLATGGTIAATIRLVEQLGGIVVGTAFLIELSDLHGRDKIKDYDMFTLMSYTGA | Function: Catalyzes a salvage reaction resulting in the formation of AMP, that is energically less costly than de novo synthesis.
Catalytic Activity: AMP + diphosphate = 5-phospho-alpha-D-ribose 1-diphosphate + adenine
Sequence Mass (Da): 18897
Sequence Length: 175
Pathway: Purine metabolism; AMP biosynthesis via salva... |
A3QF54 | MNTDKLALIKQSIKTIPDYPKPGIMFRDVTSLMEDPAAYQATIALFVERYKDLGVTKVVGTEARGFLFGAPLALELGVGFVPVRKPGKLPRETISESYELEYGHDMLEIHTDAIKPGDKVLVVDDLLATGGTIEATVKLIRQLGGEVEHAAFVISLPELGGEHRLAEMGLSLMTLCEFEGE | Function: Catalyzes a salvage reaction resulting in the formation of AMP, that is energically less costly than de novo synthesis.
Catalytic Activity: AMP + diphosphate = 5-phospho-alpha-D-ribose 1-diphosphate + adenine
Sequence Mass (Da): 19744
Sequence Length: 181
Pathway: Purine metabolism; AMP biosynthesis via salva... |
Q8EFG1 | MAMNTETLSLIKQSIKTIPNYPKEGILFRDVTSLLENATAYKATIDLLVEHYRSKGFTKIVGTEARGFLFGAPLALGLGIGFVPVRKPGKLPRATISQSYELEYGHDSLEIHTDAITANDKVLVVDDLLATGGTIEATVKLIRQLGGEVQDAAFVISLPDLGGEARLTALGLELVKLCEFEGE | Function: Catalyzes a salvage reaction resulting in the formation of AMP, that is energically less costly than de novo synthesis.
Catalytic Activity: AMP + diphosphate = 5-phospho-alpha-D-ribose 1-diphosphate + adenine
Sequence Mass (Da): 19746
Sequence Length: 183
Pathway: Purine metabolism; AMP biosynthesis via salva... |
P50635 | MAGRPGYSEVIFLYVVSVAVIARATDNMPVNKDVSKLFPLTLIHINDLHARFEETNMKSNVCTQKDQCIAGIARVYQKIKDLLKEYESKNPIYLNAGDNFQGTLWYNLLRWNVTADFIKKLKPAAMTLGNHEFDHTPKGLAPYLAELNKEGIPTIVANLVMNNDPDLKSSKIPKSIKLTVGKRKIGIIGVLYDKTHEIAQTGKVTLSNAVEAVRREAAALKKDNIDIIVVLSHCSYEEDKKIAAEAGDDIDVIVGAHSHSFLYSPDSKQPHDPKDKVEGPYPTLVESKNKRKIPIVQAKSFGKYVGRLTLYFDEEGEVKN... | Function: Facilitates hematophagy by preventing ADP-dependent platelet aggregation in the host. May reduce probing time by facilitating the speed of locating blood.
PTM: The N-terminus is blocked.
Catalytic Activity: a ribonucleoside 5'-triphosphate + 2 H2O = a ribonucleoside 5'-phosphate + 2 H(+) + 2 phosphate
Sequenc... |
O96559 | MRSSYRVGNPIRFQPTNVVGLLLLSLVLSFMLVQSYELGHASGETNANSKYPLTTPVEENLKVRFKIGVISDDDKNAVSKDESNTWVSTYLTGTLEWEKSTDKITVQWDKGNEKKVKSKYSYGGRGMELSELVTFNGNLLTFDDRTGLVYILKDDKVYPWVVLADGDGKNSKGFKSEWATEKAGNLYVGSSGKEWTTKEGTIENYNPMWVKMINKNGEVTSLNWQTNYEKIRSSMNITFPGYMWHEAACWSDKYNKWFFLPRALSQEAYDSKKFETQGANVIISCDDKFEKCEPTQIQGKTEDKRGFSNFKFVPTSEDKI... | Function: Inhibits platelet aggregation by the calcium-dependent hydrolysis of ATP and ADP.
Catalytic Activity: a ribonucleoside 5'-triphosphate + 2 H2O = a ribonucleoside 5'-phosphate + 2 H(+) + 2 phosphate
Sequence Mass (Da): 41474
Sequence Length: 364
EC: 3.6.1.5
|
P80595 | MLNQNSHFIFIILAIFLVLPLSLLSKNVNAQIPLRRHLLSHESEHYAVIFDAGSTGSRVHVFRFDEKLGLLPIGNNIEYFMATEPGLSSYAEDPKAAANSLEPLLDGAEGVVPQELQSETPLELGATAGLRMLKGDAAEKILQAVRNLVKNQSTFHSKDQWVTILDGTQEGSYMWAAINYLLGNLGKDYKSTTATIDLGGGSVQMAYAISNEQFAKAPQNEDGEPYVQQKHLMSKDYNLYVHSYLNYGQLAGRAEIFKASRNESNPCALEGCDGYYSYGGVDYKVKAPKKGSSWKRCRRLTRHALKINAKCNIEECTFNG... | Function: Catalyzes the hydrolysis of phosphoanhydride bonds of nucleoside tri- and di-phosphates.
PTM: The N-terminus is blocked.
Location Topology: Single-pass type II membrane protein
Catalytic Activity: a ribonucleoside 5'-triphosphate + 2 H2O = a ribonucleoside 5'-phosphate + 2 H(+) + 2 phosphate
Sequence Mass (Da... |
B3A0N5 | MFKITVFIYVLQLILPSKVHSSPVPDSDNGLREFPLSIVHINDFHARFEQTDELGGQCKPTAKCVGGYARLVTTVKKLKEEGQNTIFLNAADNYQGTLWYNLGKWNVTAYFMNLLPADAMTLGNHEFDDKIEGIVPFLEVIKTPIVVANIDDSLEPTFKGKYTKSVVLERGGRKIGIVGVIAQNTDNISSPGKLRFLDEIQSVKNESKRLREEEKVDIVIVLSHIGLDHDYDLAEQAGDYIDAIIGGHSHSFLWTGDNPPGKEKVVDAYPVEIVQTSGKKVLIVQASAFARYVGNITLYFGENNNLIRYAGAPVYLDSDV... | Function: Facilitates hematophagy by inhibiting ADP-dependent platelet aggregation in the host. Shows potential for antithrombotic activity. May reduce probing time by facilitating the speed of locating blood.
Catalytic Activity: a ribonucleoside 5'-triphosphate + 2 H2O = a ribonucleoside 5'-phosphate + 2 H(+) + 2 phos... |
A6NM10 | MAGLNVSLSFFFATFTLCEAARRASKALLPVGAYEVFAREAMRTLVELGPWAGDFGPDLLLTLLFLLFLAHGVTLDGASANPTVSLQEFLMAEESLPGTLLKLAAQGLGMQAACTLTRLCWAWELSDLHLLQSLMAQSCSSALRTSVPHGALVEAACAFCFHLTLLHLRHSPPAYSGPAVALLVTVTAYTAGPFTSAFFNPALAASVTFACSGHTLLEYVQVYWLGPLTGMVLAVLLHQGRLPHLFQRNLFYGQKNKYRAPRGKPAPASGDTQTPAKGSSVREPGRSGVEGPHSS | Function: Aquaporins facilitate the transport of water and small neutral solutes across cell membranes.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 31475
Sequence Length: 295
Domain: Aquaporins contain two tandem repeats each containing three membrane-spanning domains and a pore-forming loop with... |
A0A0G3FWY4 | MTANGDVRQPDARTYFTHQHPADYHADWKGYYERALVSRARSMERFAHELDIRYGTDPHQILNVFRAADTRSAPVIIYFHGGRWREGHPAFYDHLADTWAADGAVFVSAGYRLTPEHSIADSVADAWAVTDWVVRNIAAYGGDPSRITVAGHSSGGHLASMVALTDNCAVSIVGLVCMSAPVDLRTLGFWDDDTLSPHLQISRVPRRVVVSFGDPEPNRKGDDALRLTREGQMLADSLVAYGASLRTVVLPNADHVRTATAFADRQSPLFGAAHSVIFGDSTEDRSAPRSPHFQEEKQSCPE | Function: Involved in the degradation of the Pseudomonas aeruginosa quorum sensing signal molecules HHQ (2-heptyl-4-quinolone) and PQS (2-heptyl-3-hydroxy-4-quinolone) to anthranilic acid. Probably catalyzes the hydrolysis of N-octanoylanthranilic acid to anthranilic acid.
Catalytic Activity: H2O + N-octanoylanthranila... |
A0A0E4AET8 | MFQTVTAPTGVWRGRVTGDVTVFHGIQYARADRFAPPQRCEPQLQHLVEVPEPGPIAPQSPSRLEGVMGAPSSLKQSEACLTVTVTTPHLAQPGSLPVLVWLHGGAFLSGSGAWEQYGAEQLVRETGIVVVSVNYRLGVLGYLCAPGISSGNLGLLDQITALEWVRDNIEAFGGDNGRVTLDGQSAGAHSIVAMLGIDRARSLFSRAIIQSAPLGLGFHSVEQARRAAEIFEEELGSDPRRAVVTDILAAQARTAHRLAGRGAMNSAPPFLPVHGMAPLPFVGEWNGKVAANAARRKILIGNTRDEMAAFFGPHPVFSAM... | Function: Involved in the degradation of the Pseudomonas aeruginosa quorum sensing signal molecules HHQ (2-heptyl-4-quinolone) and PQS (2-heptyl-3-hydroxy-4-quinolone) to anthranilic acid. Probably catalyzes the hydrolysis of N-octanoylanthranilic acid to anthranilic acid.
Catalytic Activity: H2O + N-octanoylanthranila... |
A0A0E4AFG7 | MSGVAGHAEVVGGGIGGLSAAIALGKRGWTVRLHERNDEIRASGSGIYLWDNGLAALDYLGALDSTLVGAHFGARMQTRDAHNALVASSEVNRAGGPRVVTVARERLINALLASADAVGVEVVTGSTVTRVDAAGRIEFDNGHADADLIVVADGIGSRSRDQLGVKTRRRQLNQKCARVLLPREPGMVPSEWVDEYVTFYSGQRFLLYTPCSADLLYLALVCPSDDAPATGDPLPREAWIASFPQLAPLIDRIGPTPRWDEFEMLTLDSWSSGRVAILGDAAHAQPPSLGQGGGCAMLSALGLAHSLSKNYDLTTALGEW... | Function: Could be involved in the degradation of the Pseudomonas aeruginosa quorum sensing signal molecule HHQ (2-heptyl-4-quinolone) to anthranilic acid. May catalyze the hydroxylation of HHQ to PQS (2-heptyl-3-hydroxy-4-quinolone).
Catalytic Activity: 2-heptyl-4(1H)-quinolone + H(+) + NADH + O2 = 2-heptyl-3-hydroxy-... |
B1MFK1 | MSSGHAEVVGGGIGGLTAATALALRGWTVRLHERDTRIRTVGAGIYVWDNGLEALDTIGAAAEGLDDAYEAPAITVRASDGRPLYRIDVNQPGGARCVTLLRDRLIGALHVAAEHAGVEVCTGSAAVSATADGTVEFSTGTSTRADLVVAADGVHSLLRDRLGISYRRIRMRQGAARVMVSGERPFIPGMDVDQHHEFLGGRRRLLYTPCTATQTYLAFVADNDDTATVGPELDLAAWARAFPLLVPVFDAARGRALIRWDNFELIRLSTWSHGRVAVLGDAAHAQPPYVGQGGGTAMNSAVGLAAAVSESADVEDGLNR... | Function: Involved in the degradation pathway of the Pseudomonas aeruginosa quorum sensing signal molecule HHQ (2-heptyl-4(1H)-quinolone) to anthranilate. Catalyzes the hydroxylation of HHQ to PQS (2-heptyl-3-hydroxy-4(1H)-quinolone).
Catalytic Activity: 2-heptyl-4(1H)-quinolone + H(+) + NADH + O2 = 2-heptyl-3-hydroxy-... |
A0A0E4AE72 | MNMPQLSTIQIGDHELAYLDNKLTSAVTPTIVMLPGWCGDHHSFSELIPQLNDTHRVVAVNWRGHAPVPHDVSDFGYAEQAQDALAILDAIGVDEFLPVSASHGGWALVQLLVDAGPARARAGVVLDWLMRRPTPEFTAALLSLQDPEGWVDSCRALFHTWRPNDSDWVESRVERAKEFGFDMWARSGRVISGAYGEHGTPLEFMKTITPERHIRHLFSTPSDSDYVAPQEAFASENEWFSYALLGGTSHFPHLEMPDRVAAHIVELAKNTYQAGAMR | Function: Involved in the degradation of the Pseudomonas aeruginosa quorum sensing signal molecules HHQ (2-heptyl-4-quinolone) and PQS (2-heptyl-3-hydroxy-4-quinolone) to anthranilic acid. Catalyzes the cleavage of PQS to form N-octanoylanthranilic acid and carbon monoxide.
Catalytic Activity: 2-heptyl-3-hydroxy-4(1H)-... |
B1MFK2 | MITTKTVNGVQIAFDDQGHEPGPVFVTLSGWAHDLRAYDGMLPYLRAAQRTVRVCWRGHGPDRNLVGDFGIDEMAADTIGLLDALEVDSFVPIAHAHGGWAALEIADRLGAQRVPAVMILDLIMTPAPREFVAALHGIQDPERWKEGRDGLVQSWLAGTTNQAVLDHVRYDSGGHGFDMWARAGRVIDEAYRTWGSPMRRMEALAEPCAIRHVFSHPKIGEYDALHDDFAARHPWFSYRRLGGETHFPGIELPQQVAAEAIDLLAGARI | Function: Ring-cleaving dioxygenase involved in the degradation pathway of the Pseudomonas aeruginosa quorum sensing signal molecules HHQ (2-heptyl-4-quinolone) and PQS (2-heptyl-3-hydroxy-4(1H)-quinolone) to anthranilate. Catalyzes the cleavage of PQS to form N-octanoylanthranilate and carbon monoxide. Thus, leads to ... |
Q7MIV9 | MNKYLAELFGTFWLVLGGCGSAVLAAAFPDVGIGLLGVSLAFGLTVLTMAFAIGHISGCHLNPAVTIGLWAGGRFEAKEIVPYILAQVIGGVIAGGVLYTIASGQMGFDATSSGFASNGYGEHSPGGYSLTSALVTEIVMAMMFLLVILGATDQRAPQGFAPIAIGLCLTLIHLISIPVTNTSVNPARSTGVALYVGDWATAQLWLFWVAPILGALLGAVAYKLISGSNKD | Function: Channel that permits osmotically driven movement of water in both directions. It is involved in the osmoregulation and in the maintenance of cell turgor during volume expansion in rapidly growing cells. It mediates rapid entry or exit of water in response to abrupt changes in osmolarity.
Catalytic Activity: H... |
Q9NHW7 | MTESAGVKQLVGVADITENRNIWRMLVAEFLGTFFLVSIGIGSTMGWGGDYAPTMTQIAFTFGLVVATLAQAFGHVSGCHINPAVTIGLMITADISILKGAFYIVSQCVGAIAGAALIKAATPSDVIGGLGVTGIDPRLTAGQGVMIEALITFILVFVVHGVCDNRRSDIKGSAPLAIGLSITAGHLSAIKYTGASMNPARSFGPAVVMGNWTDQWVYWVGPIVGGILAGAVYRLFFKVRKGDEESYDF | Function: Forms a water-specific channel.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 26093
Sequence Length: 249
Domain: Aquaporins contain two tandem repeats each containing three membrane-spanning domains and a pore-forming loop with the signature motif Asn-Pro-Ala (NPA).
Subcellular Location: ... |
Q23808 | MAADKSVDNTKKIIGIDDITDTKTIWRCLAAELIGTLLLVLIGTGSCTGVQISEGDVVVRIALTFGFIIATMVQCIGHVSGCHINPAVTCGLLVTGHISILKAIFYIIVQCVGAIAGSAILKVITPAEFRGTLCMTSLAPGVTPPMGFLVEACITFVLILLVQSVCDDRRKNLGNAAPVAVGLAITCCHLAAIKYTGSSMNPARSFGPAVNGDDNWANHWVYWAGPIVGGVVAGITYRALFRARKPEEEASSYDF | Function: Forms a water-specific channel. May be involved in the transfer of excess sap dietary water from the initial midgut to the terminal midgut and the proximal part of the malpighian tubules.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 26885
Sequence Length: 255
Domain: Aquaporins contain t... |
Q9V5Z7 | MVEKTEMSKFVGVADITENKKIWRMLLGELVGTFFLIFVGVGSTTSGSVPQIAFTFGLTVATIAQGLGHLSGCHINPAVTLGFLIVGEISILKAAFYIIVQCVGAIAGAAVIKVALDGVAGGDLGVSSFDPSLNCAQAVLIEALITFILVFVVKAVSDPGRQDIKGSAPLAVGLAIAAGHLCAIKLSGASMNPARSFGPAVVQGVWTYHWVYWVGPIAGGLLAGIIYRLIFKVRKGDDETDSYDF | Function: Forms a water-specific channel.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 25575
Sequence Length: 245
Domain: Aquaporins contain two tandem repeats each containing three membrane-spanning domains and a pore-forming loop with the signature motif Asn-Pro-Ala (NPA).
Subcellular Location: ... |
Q8SRK2 | MTRETLKTLQSTFGEMVASFVFGFAVYSALLGSALTEQSAARVIVGLTVGFSGICVIYSFCDVTVAHFNPAITLAAILTCKLGVLRGIGYIVAQYIGFILAVCALLPCSPVGYKETLNIIRPTPSPFGGDNLNVFFTEFFLTAILVHVAFATAVNPYKPKTDTEGKFVDPDEEEPVDRRITAPLCIGLTLGFLAFLGLASSGGAFNPGLTLAPVIMSNTWNHFWAYFAGQYLGGFVGGLLQVLVLYKLSF | Function: Water channel required to facilitate the transport of water across membranes. Involved in osmotolerance.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 26795
Sequence Length: 250
Domain: Aquaporins contain two tandem repeats each containing three membrane-spanning domains and a pore-formin... |
B7XIC4 | MNTSTKLICQKLFAEMLCSCIFGFAVYSAILNTKASNSSISSTTVGLTVCFSSISLIYTFCDHSVAHFNPAITIAAICTGKLDILLGIGYVIAQLIGFILATLLTVVCFPYGYLKTMEFIASARISDDISTVNLFFTEFILSFILVFIAFEVGINAIREPGVTLFVGIKQIDRSKFAPLTIGITLGFLAFLASTTSGGAFNPGIVWGPAIMGGNFDDFVIYIISELSGGLLGAFIQVFLLFK | Function: Water channel required to facilitate the transport of water across membranes. Involved in osmotolerance (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 25999
Sequence Length: 242
Domain: Aquaporins contain two tandem repeats each containing three membrane-spanning domains a... |
C4VBN2 | MTRKWIKKLQSYIGEFFASFIFGFAVYTSIIGSAQTGQSAGPIIVALTIALSGVAIIYSFCDITVAHFNPAITFSAMCFRRLPFFGGIFIIIFQVAGFIIAGLASVAVLPGKYKNKLEIARPKRVADNVSRGRIFGTEFFLTAILVYVAFAVGVNPYTPPKDEHGDQLDPDEGLTEGRKITAPLAIGFTLGFCALLGIASSGGAFNPGIVLSPMILTGTWDFWWVYLLGQFSGGLLGGGLQRFLLYKIF | Function: Water channel required to facilitate the transport of water across membranes. Involved in osmotolerance (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 26936
Sequence Length: 249
Domain: Aquaporins contain two tandem repeats each containing three membrane-spanning domains a... |
P53943 | MSRSNSIYTEDIEMYPTHNEQHLTREYTKPDGQTKSEKLNFEGAYINSHGTLSKTTTREIEGDLDSETSSHSSDDKVDPTQQITAETKAPYTLLSYGQKWGMVAILTMCGFWSSLGSPIYYPALRQLEKQFNVDENMVNVTVVVYLLFQGISPTVSGGLADCFGRRPIILAGMLIYVIASIGLACAPSYGVIIFLRCIQSIGISPTIAISSGVVGDFTLKHERGTFVGATSGFVLLGQCFGSLIGAVLTARWDWRAIFWFLTIGCGSCFLIAFLILPETKRTIAGNLSIKPKRFINRAPIFLLGPVRRRFKYDNPDYETL... | Function: Probable transporter that confers resistance to short-chain monocarboxylic acids and quinidine.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 65296
Sequence Length: 586
Subcellular Location: Membrane
|
P0CD91 | MSSNDSNDTDKQHTRLDPTGVDDAYIPPEQPETKHHRFKISRDTLRDHFIAAVGEFCGTFMFLWCAYVICNVANHDVALVAAPDGSHPGQLIMIAIGFGFSVMFSIWCFAGVSGGALNPAMSLSLCLARAVSPTRCVVMWVSQIVAGMAAGGAASAMTPGEVLFANSLGLGCSRTRGLFLEMFGTAILCLTVLMTAVEKRETNFMAALPIGISLFIAHVALTAYTGTGVNPARSLGAAVAARYFPHYHWIYWIGTLLGSILAWSVWQLLQILDYTTYVTAEKAASTKEKAQKKGETSSSSAVAEV | Function: Water channel required to facilitate the transport of water across membranes. Involved in sporulation, freeze tolerance and osmotolerance (By similarity). Is non-functional in most laboratory strains.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 32713
Sequence Length: 305
Domain: Aquapor... |
Q49V87 | MTYSIGIDFGTGSGRVFLVNTENGEIIGQYVQTYAHGTIEGELNGHKLPQSYALQNANDYMEVIETGIPEILAKTNIDAKDIVGIGIDFTSSTVIFVDDQMEPMHNNPKFYNNPHAYVKLWKHHGAQAEADLLFNTAIEEKNRWLGYYGFNVSSEWMIPKIMEVNDKAPEVMTETADIMEAGDWIVNRLTGENVRSNCGLGFKSFWESSTGFHYDLFDKVDDNLSDIVRTKVEAPIVSIGESVGTVSAEMAHKLGLSPETVVSPFIIDAHSSLLGIGAEKDKEMTMVMGTSTCHLMLNKEQHKVPGISGSVKGAIIPDLY... | Catalytic Activity: ATP + D-ribulose = ADP + D-ribulose 5-phosphate + H(+)
Sequence Mass (Da): 60094
Sequence Length: 542
Pathway: Carbohydrate degradation; L-arabinose degradation via L-ribulose; D-xylulose 5-phosphate from L-arabinose (bacterial route): step 2/3.
EC: 2.7.1.16
|
B7GGV9 | MGKKYVIGIDYGTESGRAVLVDLEGNEIADHVTPYPHGVIDEVLPESNVQLEPDWALQHPGDYIEVLATAVPAVLQKSGVNPADVIGVGIDFTACTMLPIAGSGEPLCLKPEFKHRPHSWVKLWKHHAAQDEANLLNEMAAKRGEAFLPRYGGKISSEWMIAKIWQILNEDPDIYDQTDLFLEATDWVIFKMTGQLVRNSCTAGYKSIWHKQDGYPSKEFFRALDPRLEHVTETKLRGSIVPLGTRAGVLTKEMAAMMGLLPGTAVAVGNVDAHAAVPGVGVVEPGKMVMAMGTSICHMLLGTEEKYVEGMCGVVEDGII... | Catalytic Activity: ATP + D-ribulose = ADP + D-ribulose 5-phosphate + H(+)
Sequence Mass (Da): 61968
Sequence Length: 564
Pathway: Carbohydrate degradation; L-arabinose degradation via L-ribulose; D-xylulose 5-phosphate from L-arabinose (bacterial route): step 2/3.
EC: 2.7.1.16
|
P94524 | MAYTIGVDFGTLSGRAVLVHVQTGEELAAAVKEYRHAVIDTVLPKTGQKLPRDWALQHPADYLEVLETTIPSLLEQTGVDPKDIIGIGIDFTACTILPIDSSGQPLCMLPEYEEEPHSYVKLWKHHAAQKHADRLNQIAEEEGEAFLQRYGGKISSEWMIPKVMQIAEEAPHIYEAADRIIEAADWIVYQLCGSLKRSNCTAGYKAMWSEKAGYPSDDFFEKLNPSMKTITKDKLSGSIHSVGEKAGSLTEKMAKLTGLLPGTAVAVANVDAHVSVPAVGITEPGKMLMIMGTSTCHVLLGEEVHIVPGMCGVVDNGILP... | Catalytic Activity: ATP + D-ribulose = ADP + D-ribulose 5-phosphate + H(+)
Sequence Mass (Da): 61010
Sequence Length: 560
Pathway: Carbohydrate degradation; L-arabinose degradation via L-ribulose; D-xylulose 5-phosphate from L-arabinose (bacterial route): step 2/3.
EC: 2.7.1.16
|
P58541 | MAIAIGLDFGSDSVRALAVDCTTGEEIATSVEWYPRWQKGQFCDAPNNQFRHHPRDYIESMEAALKTVLAELSVEQRAAVVGIGVDSTGSTPAPIDADGNVLALRPEFAENPNAMFVLWKDHTAVEEAEEITRLCHAPGNVDYSRYIGGIYSSEWFWAKILHVTRQDSAVAQSAASWIELCDWVPALLSGTTRPQDIRRGRCSAGHKSLWHESWGGLPPASFFDELDPILNRHLPSPLFTDTWTADIPVGTLCPEWAQRLGLPESVVISGGAFDCHMGAVGAGAQPNALVKVIGTSTCDILIADKQSVGERAVKGICGQV... | Catalytic Activity: ATP + D-ribulose = ADP + D-ribulose 5-phosphate + H(+)
Sequence Mass (Da): 61228
Sequence Length: 566
Pathway: Carbohydrate degradation; L-arabinose degradation via L-ribulose; D-xylulose 5-phosphate from L-arabinose (bacterial route): step 2/3.
EC: 2.7.1.16
|
P94529 | MKPVKTGTVHPVPSAAKQSGWRDLFYSKKAAPYLFTAPFVLSFLVFFLYPIISVFIMSFQRILPGEVSFVGLSNYTALNNPTFYTALWNTLEYTFWTLIVLIPVPLLLAIFLNSKLVKFRNIFKSALFIPALTSTIVAGIIFRLIFGEMETSLANSILLKLGFSPQNWMNNEHTGMFLMVLLASWRWMGINILYFLAGLQNVPKELYEAADIDGANTMKKFLHITLPFLKPVTVYVLTISIIGGFRMFEESYVLWQNNSPGNIGLTLVGYLYQQGLAYNEMGYGAAIGIVLLIVILVVSLISLKLSGSFKGEG | Function: Part of the ABC transporter complex AraNPQ involved in the uptake of arabinooligosaccharides. Transports alpha-1,5-arabinooligosaccharides, at least up to four L-arabinosyl units . Responsible for the translocation of the substrate across the membrane (Probable).
Location Topology: Multi-pass membrane protein... |
P94530 | MLRHSPQFSVYRIALTLFFMMLSLLYLFPIFCLLLGSLKPSSELLRVGLNLDIDPKVMSFDNYTFLFNGGSIYFKWFFNSLVLGLFTTVLTLFFSSMIGYGLAVYDFKGRNIIFVLVLIIMMVPLEVMMLPLFKLTVGLHLIDSYTGVILPFIVSPVAVFFFRQYALGLPRDLLDSARMDGCTEFGIFFRIMAPLMKPAFGAMIILQSLNSWNNFLWPLIVLRSKEMFTLPIGLSSLLSPYGNNYDMLISGSVFAILPVIIIFLFFQKYFISGLTVGGVKG | Function: Part of the ABC transporter complex AraNPQ involved in the uptake of arabinooligosaccharides. Transports alpha-1,5-arabinooligosaccharides, at least up to four L-arabinosyl units . Responsible for the translocation of the substrate across the membrane (Probable).
Location Topology: Multi-pass membrane protein... |
O80885 | MLLNISSSPISHRNPHFLSNFNNPISYFPRRSKTHLSKSHFFPKFTPLSNQSLKNRVLFGNKRYPDGERFDFRSRAISGIDLGSFESVLEAIAVLTTIIVVHESGHFLAASLQGIHVSKFAIGFGPILAKFDYNNVEYSLRAFPLGGFVGFPDNDPDSEIPIDDENLLKNRPTLDRSIVVSAGIIANVIFAYAIIFVQVLSVGLPVQEAFPGVLVPEVKTFSAASRDGLLSGDVILAVDGTELSKTGPDAVSKIVDIVKRNPKSNVVFRIERGGEDFDIRVTPDKNFDGTGKIGVQLSPNVRITKVRPRNIPETFRFVGR... | Function: Metalloprotease essential for chloroplast and plant development. May be involved in regulated intramembrane proteolysis (RIP).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 48726
Sequence Length: 447
Subcellular Location: Plastid
EC: 3.4.24.-
|
H3ZPL1 | MELEKRLKEKLEAPTLDYEKYFSEKALGMKASEIRELLKLVETSDVISLAGGLPAPETFPVEIIGEITKEVLEKHAAQALQYGTTKGFTPLRLALAEWMRERYDIPISKVDIMTTSGSQQALDLIGRVFINPGDIIVVEAPTYLAALQAFKYYEPEFVQIPLDDEGMNVDLLEEKLQELEKEGKKVKIVYTIPTFQNPAGVTMNEKRRKRLLELASQYDFIIVEDNPYGELRYSGEPVKPIKAWDEEGRVIYLGTFSKILAPGFRIGWIAAEPHFIRKLEIAKQSVDLCTNTFSQVIAWKYVEGGYLDKHIPKIIEFYKP... | Function: Catalyzes the transamination of phenylalanine, tyrosine and tryptophan. Shows virtually no activity towards aspartic acid, alanine, valine or isoleucine.
Catalytic Activity: 2-oxoglutarate + an aromatic L-alpha-amino acid = an aromatic oxo-acid + L-glutamate
Sequence Mass (Da): 47610
Sequence Length: 417
EC: ... |
H3ZPU1 | MALSDRLEMVNPSEIRKLFDLAQGIEGIISLGIGEPDFDTPEHIKEYAKEALDKGLTHYSPNIGILELREAVAEKFKKHNGIDADPKTQIMITVGTNQQILMGLATFLKDNEEVLIPSPMFVSYAPAVILAGGKPVEVPTYEENEFRLSVDELEKYVTPKTRALIINTPNNPTGAVLTKKDLEEIADFAVEHDLMILSDEVYEYFVYDGVKNYSIASLDGMFERTITMNGFSKTFAMTGWRLGFLAAPEWVVEKMVRFQMYNATCPVTFIQYAAAKALRDERSWQAVEEMRREYERRRNLVWKRLNEMGLPTVKPKGAFY... | Function: Catalyzes the transamination of phenylalanine, tyrosine and tryptophan. Shows virtually no activity towards aspartic acid, alanine, valine or isoleucine.
Catalytic Activity: 2-oxoglutarate + an aromatic L-alpha-amino acid = an aromatic oxo-acid + L-glutamate
Sequence Mass (Da): 44105
Sequence Length: 389
EC: ... |
P40024 | MPPVSASKAKRDAKKAEREAKKAAAGKTIRKLGRKKEAAAEESEVDAAAREIKMMKLQQDKDGLSDRVVTGVLSSLETSRDIKLSSVSLLFHGKVLIQDSGLELNYGRRYGLLGENGCGKSTFLKALATREYPIPEHIDIYLLDEPAEPSELSALDYVVTEAQHELKRIEDLVEKTILEDGPESELLEPLYERMDSLDPDTFESRAAIILIGLGFNKKTILKKTKDMSGGWKMRVALAKALFVKPTLLLLDDPTAHLDLEACVWLEEYLKRFDRTLVLVSHSQDFLNGVCTNMIDMRAQKLTAYGGNYDSYHKTRSELET... | Function: ATPase that stimulates 40S and 60S ribosome biogenesis . Also involved in ribosome-associated quality control (RQC) pathway, a pathway that mediates ubiquitination and extraction of incompletely synthesized nascent chains for proteasomal degradation: localizes to the ribosomal E-site and stimulates VMS1-depen... |
P95470 | MPTHHPITRQHWHHSWLSALALLCASLACGAKQVDVHDPVMTREGDTWYLFSTGPGITIYSSKDRVNWRYSDRAFGTEPTWAKRVSPSFDGHLWAPDIYQHKGLFYLYYSVSAFGKNTSAIGVTVNKTLNPASPDYRWEDKGIVIESVPQRDLWNAIDPAIIADDHGQVWMSFGSFWGGLKLFKLNDDLTRPAEPQEWHSIAKLERSVLMDDSQAGSAQIEAPFILRKGDYYYLFASWGLCCRKGDSTYHLVVGRSKQVTGPYLDKTGRDMNQGGGSLLIKGNKRWVGLGHNSAYTWDGKDYLVLHAYEAADNYLQKLKI... | Function: Involved in the degradation of arabinan and is a key enzyme in the complete degradation of the plant cell wall. Catalyzes the cleavage of the terminal alpha-(1->5)-arabinofuranosyl bonds of linear arabinan and carboxymethylarabinan to produce almost exclusively arabinotriose.
Catalytic Activity: Hydrolysis of... |
P0C0B4 | MTAQTPIHVYSEIGKLKKVLLHRPGKEIENLMPDYLERLLFDDIPFLEDAQKEHDAFAQALRDEGIEVLYLETLAAESLVTPEIREAFIDEYLSEANIRGRATKKAIRELLMAIEDNQELIEKTMAGVQKSELPEIPASEKGLTDLVESNYPFAIDPMPNLYFTRDPFATIGTGVSLNHMFSETRNRETLYGKYIFTHHPIYGGGKVPMVYDRNETTRIEGGDELVLSKDVLAVGISQRTDAASIEKLLVNIFKQNLGFKKVLAFEFANNRKFMHLDTVFTMVDYDKFTIHPEIEGDLRVYSVTYDNEELHIVEEKGDLA... | PTM: Glycosylated.
Catalytic Activity: H2O + L-arginine = L-citrulline + NH4(+)
Sequence Mass (Da): 46297
Sequence Length: 411
Pathway: Amino-acid degradation; L-arginine degradation via ADI pathway; carbamoyl phosphate from L-arginine: step 1/2.
Subcellular Location: Cytoplasm
EC: 3.5.3.6
|
Q7LC44 | MELDHRTSGGLHAYPGPRGGQVAKPNVILQIGKCRAEMLEHVRRTHRHLLAEVSKQVERELKGLHRSVGKLESNLDGYVPTSDSQRWKKSIKACLCRCQETIANLERWVKREMHVWREVFYRLERWADRLESTGGKYPVGSESARHTVSVGVGGPESYCHEADGYDYTVSPYAITPPPAAGELPGQEPAEAQQYQPWVPGEDGQPSPGVDTQIFEDPREFLSHLEEYLRQVGGSEEYWLSQIQNHMNGPAKKWWEFKQGSVKNWVEFKKEFLQYSEGTLSREAIQRELDLPQKQGEPLDQFLWRKRDLYQTLYVDADEEE... | Function: Master regulator of synaptic plasticity that self-assembles into virion-like capsids that encapsulate RNAs and mediate intercellular RNA transfer in the nervous system. ARC protein is released from neurons in extracellular vesicles that mediate the transfer of ARC mRNA into new target cells, where ARC mRNA ca... |
C7R400 | MTETHNDPEELARRVASLSAQNERLAQILVEARSKIVGLQQQIDDLAQPPSTYATFIRSYSDGTADVMVQGRKMRLTSLPAAMVSTARPGQQVRLNEAMAIVETMTYDHTGELVTVKELIGTHRAMVVGRGDDERVVNLAGSLIGRDGPTIRTGDSVLVDLKAGYALEKIDKSEVEELVLEEVPRVAYEDIGGLSRQIDTIKDAVELPFLHPDLYREHGLKAPKGILLYGPPGCGKTLIAKAVAHSLAQTVGQGNNTPTDDTRGYFLNIKGPELLNKYVGETERQIRLIFTRARDKAAQGHPVVVFFDEMESLFRTRGTG... | Function: ATPase which is responsible for recognizing, binding, unfolding and translocation of pupylated proteins into the bacterial 20S proteasome core particle. May be essential for opening the gate of the 20S proteasome via an interaction with its C-terminus, thereby allowing substrate entry and access to the site o... |
Q9WV31 | MELDHMTTGGLHAYPAPRGGPAAKPNVILQIGKCRAEMLEHVRRTHRHLLTEVSKQVERELKGLHRSVGKLENNLDGYVPTGDSQRWKKSIKACLCRCQETIANLERWVKREMHVWREVFYRLERWADRLESMGGKYPVGSEPARHTVSVGVGGPEPYCQEADGYDYTVSPYAITPPPAAGELPEQESVEAQQYQSWGPGEDGQPSPGVDTQIFEDPREFLSHLEEYLRQVGGSEEYWLSQIQNHMNGPAKKWWEFKQGSVKNWVEFKKEFLQYSEGTLSREAIQRELELPQKQGEPLDQFLWRKRDLYQTLYVDAEEEE... | Function: Master regulator of synaptic plasticity that self-assembles into virion-like capsids that encapsulate RNAs and mediate intercellular RNA transfer in the nervous system (By similarity). ARC protein is released from neurons in extracellular vesicles that mediate the transfer of ARC mRNA into new target cells, w... |
A0QZ54 | MSESERSEGFPEGFAGAGSGSLSSEDAAELEALRREAAMLREQLENAVGPQSGLRSARDVHQLEARIDSLAARNAKLMDTLKEARQQLLALREEVDRLGQPPSGYGVLLATHDDDTVDVFTSGRKMRLTCSPNIEVKELKQGQTVRLNEALTVVEAGNFEAVGEISTLREILADGHRALVVGHADEERIVWLAEPLVAAKDLPDEPTDYFDDSRPRKLRPGDSLLVDTKAGYAFERIPKAEVEDLVLEEVPDVSYNDIGGLGRQIEQIRDAVELPFLHKDLYKEYSLRPPKGVLLYGPPGCGKTLIAKAVANSLAKKMAE... | Function: ATPase which is responsible for recognizing, binding, unfolding and translocation of pupylated proteins into the bacterial 20S proteasome core particle. May be essential for opening the gate of the 20S proteasome via an interaction with its C-terminus, thereby allowing substrate entry and access to the site o... |
Q9SKN5 | MEQEKSLDPQLWHACAGSMVQIPSLNSTVFYFAQGHTEHAHAPPDFHAPRVPPLILCRVVSVKFLADAETDEVFAKITLLPLPGNDLDLENDAVLGLTPPSSDGNGNGKEKPASFAKTLTQSDANNGGGFSVPRYCAETIFPRLDYSAEPPVQTVIAKDIHGETWKFRHIYRGTPRRHLLTTGWSTFVNQKKLIAGDSIVFLRSESGDLCVGIRRAKRGGLGSNAGSDNPYPGFSGFLRDDESTTTTSKLMMMKRNGNNDGNAAATGRVRVEAVAEAVARAACGQAFEVVYYPRASTPEFCVKAADVRSAMRIRWCSGMR... | Function: Auxin response factors (ARFs) are transcriptional factors that bind specifically to the DNA sequence 5'-TGTCTC-3' found in the auxin-responsive promoter elements (AuxREs). Could act as transcriptional activator or repressor. Formation of heterodimers with Aux/IAA proteins may alter their ability to modulate e... |
Q01K26 | MASSQEKAKTGVLRNAAALLDEMQLMGETQGAKKVINSELWHACAGPLVCLPQRGSLVYYFPQGHSEQVAATTRKIPNSRIPNYPNLPSQLLCQVHNITLHADKDTDEVYAQMTLQPVNSETDVFPIPTLGAYTKSKHPTEYFCKNLTASDTSTHGGFSVPRRAAEKLFPQLDYSMQPPNQELIVRDLHDNMWTFRHIYRGQPKRHLLTTGWSLFVGAKRLKAGDSVLFIRDEKSQLLLGVRRATRQQTMLSSSVLSTDSMHIGVLAAAAHAASSGSSFTIYYNPRTSPSPFVIPVARYNKATYMQPSVGMRFAMMFETE... | Function: Auxin response factors (ARFs) are transcriptional factors that bind specifically to the DNA sequence 5'-TGTCTC-3' found in the auxin-responsive promoter elements (AuxREs).
Sequence Mass (Da): 105224
Sequence Length: 955
Domain: Interactions between auxin response factors (ARFs) and Aux/IAA proteins occur thro... |
Q0J951 | MSSSSAASIGPPQPPPPPAPPEEEKKCLNSELWHACAGPLVCLPTVGTRVVYFPQGHSEQVAASTNKEVEGHIPNYPNLPAQLICQLHDVTMHADVETDEVYAQMTLQPLNPQEQNDAYLPAEMGIMSKQPTNYFCKTLTASDTSTHGGFSVPRRAAERVFPPLDFTQQPPAQELIARDIHDIEWKFRHIFRGQPKRHLLTTGWSVFVSAKRLVAGDSVLFIWNEKNQLLLGIRRASRPQTVMPSSVLSSDSMHIGLLAAAAHAAATNSRFTIFYNPRASPSEFVIPLSKYIKAVFHTRISVGMRFRMLFETEESSVRRY... | Function: Auxin response factors (ARFs) are transcriptional factors that bind specifically to the DNA sequence 5'-TGTCTC-3' found in the auxin-responsive promoter elements (AuxREs).
Sequence Mass (Da): 90901
Sequence Length: 818
Domain: Interactions between auxin response factors (ARFs) and Aux/IAA proteins occur throu... |
P53367 | MAQESPKNSAAEIPVTSNGEVDDSREHSFNRDLKHSLPSGLGLSETQITSHGFDNTKEGVIEAGAFQGSPAPPLPSVMSPSRVAASRLAQQGSDLIVPAGGQRTQTKSGPVILADEIKNPAMEKLELVRKWSLNTYKCTRQIISEKLGRGSRTVDLELEAQIDILRDNKKKYENILKLAQTLSTQLFQMVHTQRQLGDAFADLSLKSLELHEEFGYNADTQKLLAKNGETLLGAINFFIASVNTLVNKTIEDTLMTVKQYESARIEYDAYRTDLEELNLGPRDANTLPKIEQSQHLFQAHKEKYDKMRNDVSVKLKFLEE... | Function: Plays a role in controlling biogenesis of secretory granules at the trans-Golgi network . Mechanistically, binds ARF-GTP at the neck of a growing secretory granule precursor and forms a protective scaffold . Once the granule precursor has been completely loaded, active PRKD1 phosphorylates ARFIP1 and releases... |
Q5WEW9 | MATVVIKIGGSTLEALEEGFYEGVVKRASLGDKIMIVHGGGPAINNLLQAMAVESQFVNGLRKTTAEVLTAAETALSGQINKQLVRSLYQAGGKAIGLSGSDGHLLKTIPIDTDKLGFVGAVESVNVDVLFNVAKAGYIPVIAPIGMDANYQPYNINADTAAAAVAKASKAEELVFVTDVDGVQKDGKVIKEMDEVLAKHYIEEGVIYGGMVPKVNACLDSLSGALTKARIVNGKKAYHPSAGTAIVKQSNVLTSGA | Function: Catalyzes the ATP-dependent phosphorylation of N-acetyl-L-glutamate.
Catalytic Activity: ATP + N-acetyl-L-glutamate = ADP + N-acetyl-L-glutamyl 5-phosphate
Sequence Mass (Da): 26714
Sequence Length: 257
Pathway: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 2... |
A6TTJ1 | MNLSPNQKADVLIESLPYIKKFYNEIVVIKYGGSAMVNDELKESIIKDIVLMKYVGMHPVVVHGGGPEITNMLKVFDKESKFVDGLRVTDQATMEITEMVLLGKVCQEIVTRINQNGVRSIGICGKDGSMIKTVPKDPELGLVGGITSIDTDLIKTIIEKGYIPVISPIGCGPAGESHNINADEVAGKLAAALGAKKLMLITDVAGVLRDQHDEASLISDIKTNEIEEYIETGVIKGGMIPKISCCFDAVANGVERAHIIDGRKSHSMLLEIFTDQGVGTMITHGGDQNGNSKNNKQWKSIFNEHLWENAYSLPGR | Function: Catalyzes the ATP-dependent phosphorylation of N-acetyl-L-glutamate.
Catalytic Activity: ATP + N-acetyl-L-glutamate = ADP + N-acetyl-L-glutamyl 5-phosphate
Sequence Mass (Da): 34334
Sequence Length: 316
Pathway: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 2... |
B4S0H7 | MSVSPIVIKVGGALLDDAAAMTRLFLSVKDVQATRPVVVVHGGGPLVETLMASLGLKSTKIDGLRVTPDEHMPYICGALAGSANKQLCAAALASGLTPVGLSLLDGNMVVCEPLADQYGAVGVPSTADAAFLKSVLAQSTLPIISSIGSSPQGRLLNVNADQAATVIAELLNAELLLLSNVDGVLDGNKALISALNANSIAQYASEGVITDGMKVKVDAALASAESLSRPVYIASWAADITDILNKTTGTQIVPTTLAAENGNAGEI | Function: Catalyzes the ATP-dependent phosphorylation of N-acetyl-L-glutamate.
Catalytic Activity: ATP + N-acetyl-L-glutamate = ADP + N-acetyl-L-glutamyl 5-phosphate
Sequence Mass (Da): 27086
Sequence Length: 267
Pathway: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 2... |
O67848 | MNELIEKAKVLQEALPYIREFHGKVFVIKYGGSAMHDEELRESFARDVVLLKYVGINPVIVHGGGPQISKTLEKFGIKPKFVGGMRKTDEETMHVVEMVLSGDINKDIVALINRYSGEKIYAVGLSGRDGRLLKAKKLDKERYFSELGLPVPEEDIGFVGEIVDVNEELIFTLLSHNFIPVIAPVGVGEEGEAYNVNADLAASEIAGEIKAEKLIYLTDTKGVLDEKGELISSLSKDKAEELIKKGVIREGMIPKVRSALRALEKGVKKVHIIDGRVKHSILLEVFTKEGVGTEITLE | Function: Catalyzes the ATP-dependent phosphorylation of N-acetyl-L-glutamate.
Catalytic Activity: ATP + N-acetyl-L-glutamate = ADP + N-acetyl-L-glutamyl 5-phosphate
Sequence Mass (Da): 32908
Sequence Length: 298
Pathway: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 2... |
O28988 | MENVELLIEALPYIKDFHSTTMVIKIGGHAMVNDRILEDTIKDIVLLYFVGIKPVVVHGGGPEISEKMEKFGLKPKFVEGLRVTDKETMEVVEMVLDGKVNSKIVTTFIRNGGKAVGLSGKDGLLIVARKKEMRMKKGEEEVIIDLGFVGETEFVNPEIIRILLDNGFIPVVSPVATDLAGNTYNLNADVVAGDIAAALKAKKLIMLTDVPGILENPDDKSTLISRIRLSELENMRSKGVIRGGMIPKVDAVIKALKSGVERAHIIDGSRPHSILIELFTKEGIGTMVEP | Function: Catalyzes the ATP-dependent phosphorylation of N-acetyl-L-glutamate.
Catalytic Activity: ATP + N-acetyl-L-glutamate = ADP + N-acetyl-L-glutamyl 5-phosphate
Sequence Mass (Da): 31664
Sequence Length: 290
Pathway: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 2... |
B6YS18 | MERLTIVKVGGEIIRIPEVRDSFLKDFSIIAGYKILVHGGGSMLTELARNLDIETQMIDGRRVTTEKILKLAVMVYAGLINKEIVVGLQALGVDALGFTGADSNIICSEKRPIRDSIDYGLVGDIQEINVQLLNEFLNKGHTPIFAPITHNGGGQLLNTNADSIAGELAKVLVYDYNVRLVYCFDKKGVLYDEGDENSFISVLSYTDFQRYKENGIIGGGMLPKLDSAFNALSAGVKEVIITCASNIKHTGSGTHLKL | Function: Catalyzes the ATP-dependent phosphorylation of N-acetyl-L-glutamate.
Catalytic Activity: ATP + N-acetyl-L-glutamate = ADP + N-acetyl-L-glutamyl 5-phosphate
Sequence Mass (Da): 28108
Sequence Length: 258
Pathway: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 2... |
Q7NEE9 | MSQDAPSCFTAIISPADRVQVLAEALPYIQRFAGKTIVVKYGGAAMVKENLRDLVIRDIVFLATVGIKPVVVHGGGPEINSWLERLNIPVQFVGGLRVTDKITMEVVEMVLAGKVNKSIVQMINQAGGSAVGLCGRDGSIIEARPHQSAQLQPDIGFVGDIQSVNPKLIQSLLKEGHIPVLSSVASDENGQAYNINADTAAGELAAALDAEKLILLTDTPGILLDKDHPRSLIRKLDIYQARKLIAEGVVDGGMIPKVQCCVRALAQGVRAAHIVDGRQMHALLLEVLTDQGIGSMLVASELV | Function: Catalyzes the ATP-dependent phosphorylation of N-acetyl-L-glutamate.
Catalytic Activity: ATP + N-acetyl-L-glutamate = ADP + N-acetyl-L-glutamyl 5-phosphate
Sequence Mass (Da): 32258
Sequence Length: 303
Pathway: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 2... |
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