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P28548 | MSSSEEVSWITWFCGLRGNEFFCEVDEEYIQDRFNLTGLNEQVPKYRQALDMILDLEPDDIEDNATNTDLVEQAAEMLYGLIHARYILTNRGISQMVEKWRDHDFGVCPRVYCENQPMLPIGLSDVPGEAMVKLYCPRCNDVFVPRSSRHQHTDGSYFGTGFPHMLFFVHPDLRPRRPVTQFVPKLYGFKIHPVAYGGQEGNSGGNTANNVAAAQNNTTPAGQQSGGQFNNYGL | Function: Participates in Wnt signaling. Plays a complex role in regulating the basal catalytic activity of the alpha subunit (By similarity). Modulates two aspects of male mating behavior; response to hermaphrodite contact and vulval location, acting in the same pathway as lov-1 and pkd-2.
PTM: Phosphorylated by alpha subunit.
Sequence Mass (Da): 26436
Sequence Length: 234
Subcellular Location: Cell projection
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Q91398 | MSSSEEVSWISWFCGLRGNEFFCEVDEDYIQDKFNLTGLNEQVPHYRQALDMILDLEPDEELEDNPNQSDLIEQAAEMLYGLIHARYILTNRGIAQMLEKYQQGDFGYCPRVYCENQPMLPIGLSDIPGEAMVKLYCPKCMDVYTPKSSRHHHTDGAYFGTGFPHMLFMVHPEYRPKRPANQFVPRLYGFKIHPMAYQLQLQAASSFKSPVKAIR | Function: Regulatory subunit of casein kinase II/CK2. As part of the kinase complex regulates the basal catalytic activity of the alpha subunit a constitutively active serine/threonine-protein kinase that phosphorylates a large number of substrates containing acidic residues C-terminal to the phosphorylated serine or threonine (By similarity). Participates in Wnt signaling (By similarity).
PTM: Phosphorylated by alpha subunit.
Sequence Mass (Da): 24885
Sequence Length: 215
Domain: The KSSR motif is part of a protein interaction pocket that mediates interaction with cellular and viral proteins.
Subcellular Location: Nucleus
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P67870 | MSSSEEVSWISWFCGLRGNEFFCEVDEDYIQDKFNLTGLNEQVPHYRQALDMILDLEPDEELEDNPNQSDLIEQAAEMLYGLIHARYILTNRGIAQMLEKYQQGDFGYCPRVYCENQPMLPIGLSDIPGEAMVKLYCPKCMDVYTPKSSRHHHTDGAYFGTGFPHMLFMVHPEYRPKRPANQFVPRLYGFKIHPMAYQLQLQAASNFKSPVKTIR | Function: Regulatory subunit of casein kinase II/CK2. As part of the kinase complex regulates the basal catalytic activity of the alpha subunit a constitutively active serine/threonine-protein kinase that phosphorylates a large number of substrates containing acidic residues C-terminal to the phosphorylated serine or threonine . Participates in Wnt signaling (By similarity).
PTM: Phosphorylated by alpha subunit.
Sequence Mass (Da): 24942
Sequence Length: 215
Domain: The KSSR motif is part of a protein interaction pocket that mediates interaction with cellular and viral proteins.
Subcellular Location: Nucleus
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P28021 | MSSSEEVSWISWFCGLRGNEFFCEVDEDYIQDKFNLTGLNEQVPHYRQALDMILDLEPDEELEDNPNQSDLIEQAAEMLYGLIHARYILTNRGIAQMLEKYQQGDFGYCPRVYCENQPMLPIGLSDIPGEAMVKLYCPKCMDVYTPKSSRHHHTDGAYFGTGFPHMLFMVHPEYRPKRPANQFVPRLYGFKIHPMAYQLQLQAASNFKSPVKTMR | Function: Regulatory subunit of casein kinase II/CK2. As part of the kinase complex regulates the basal catalytic activity of the alpha subunit a constitutively active serine/threonine-protein kinase that phosphorylates a large number of substrates containing acidic residues C-terminal to the phosphorylated serine or threonine (By similarity). Participates in Wnt signaling.
PTM: Phosphorylated by alpha subunit.
Sequence Mass (Da): 24960
Sequence Length: 215
Domain: The KSSR motif is part of a protein interaction pocket that mediates interaction with cellular and viral proteins.
Subcellular Location: Nucleus
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P40229 | MYRERGMVGSKSEVVDRKRINEIHDNRPSHSMSQPVNGKGKVTSTSVLMGKQQLHDKESSRSGSISKTNISDAVDISDTDSEESEVSGSDGEDTSWISWFCNLRGNEFFCEVDDDYIQDDFNLCGLSHQVPYYDYALDLILDVESSHGEMFTEEQNELIESAAEMLYGMIHARFILTSKGLASMLDKYKNYDFGRCPRVYCCGQPCLPVGQSDIPRASTVKIYCPKCEDVYYPRSKYQGNIDGAYFGTTFPHLFLMTYGHLKPQKASQSYTQRVFGFKLHKP | Function: Plays a complex role in regulating the basal catalytic activity of the alpha subunit. The tetrameric holoenzyme CK2, composed of two alpha and two beta subunits, phosphorylates the transcription factor PIF1 after an exposure to light, resulting in a proteasome-dependent degradation of PIF1 and promotion of photomorphogenesis . CK2 phosphorylates translation initiation factors. May participate in the regulation of the initiation of translation .
PTM: Phosphorylated by alpha subunit.
Sequence Mass (Da): 31978
Sequence Length: 282
Subcellular Location: Cytoplasm
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A0A0A7HIF0 | MTFAKIKFSAQIRLETGLHIGGSDAFAAIGAIDSPVIKDPITNIPIIPGSSLKGKMRTLLAKVYNEKVAEKPSDDSDILSRLFGNSKDKRFKMGRLIFRDAFLSNADELDSLGVRSYTEVKFENTIDRITAEANPRQIERAIRNSTFDFELIYEITDENENQVEEDFKVIRDGLKLLELDYLGGSGSRGYGKVAFEKLKATTVFGNYDVKTLNELLTAEV | Cofactor: Endonucleolytic cleavage of target ssRNA by the Csm complex requires a divalent metal ion; Mg(2+) has the best activity in vitro, but Mn(2+), Ca(2+), Zn(2+), Ni(2+), and Co(2+) also support cleavage.
Function: CRISPR (clustered regularly interspaced short palindromic repeat) is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain spacers, sequences complementary to antecedent mobile elements, and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA). The type III-A Csm effector complex binds crRNA and acts as a crRNA-guided RNase, DNase and cyclic oligoadenylate synthase; binding of target RNA cognate to the crRNA is required for all activities. In a heterologous host this Csm effector complex restricts ssRNA phage MS2, suggesting it may target RNA viruses in vivo.
Sequence Mass (Da): 24569
Sequence Length: 220
EC: 3.1.-.-
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Q92905 | MAASGSGMAQKTWELANNMQEAQSIDEIYKYDKKQQQEILAAKPWTKDHHYFKYCKISALALLKMVMHARSGGNLEVMGLMLGKVDGETMIIMDSFALPVEGTETRVNAQAAAYEYMAAYIENAKQVGRLENAIGWYHSHPGYGCWLSGIDVSTQMLNQQFQEPFVAVVIDPTRTISAGKVNLGAFRTYPKGYKPPDEGPSEYQTIPLNKIEDFGVHCKQYYALEVSYFKSSLDRKLLELLWNKYWVNTLSSSSLLTNADYTTGQVFDLSEKLEQSEAQLGRGSFMLGLETHDRKSEDKLAKATRDSCKTTIEAIHGLMSQVIKDKLFNQINIS | Function: Probable protease subunit of the COP9 signalosome complex (CSN), a complex involved in various cellular and developmental processes. The CSN complex is an essential regulator of the ubiquitin (Ubl) conjugation pathway by mediating the deneddylation of the cullin subunits of the SCF-type E3 ligase complexes, leading to decrease the Ubl ligase activity of SCF-type complexes such as SCF, CSA or DDB2. The complex is also involved in phosphorylation of p53/TP53, c-jun/JUN, IkappaBalpha/NFKBIA, ITPK1 and IRF8, possibly via its association with CK2 and PKD kinases. CSN-dependent phosphorylation of TP53 and JUN promotes and protects degradation by the Ubl system, respectively. In the complex, it probably acts as the catalytic center that mediates the cleavage of Nedd8 from cullins. It however has no metalloprotease activity by itself and requires the other subunits of the CSN complex. Interacts directly with a large number of proteins that are regulated by the CSN complex, confirming a key role in the complex. Promotes the proteasomal degradation of BRSK2.
Sequence Mass (Da): 37579
Sequence Length: 334
Domain: The JAMM motif is essential for the protease activity of the CSN complex resulting in deneddylation of cullins. It constitutes the catalytic center of the complex (By similarity).
Subcellular Location: Cytoplasm
EC: 3.4.-.-
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Q6CRJ8 | MSSIKFHEKSLKEVTRWIQANEDINTETSLSSSSDSSTTIPVIDHLPARIPYATDLKRNPCHFQKCLISRLATTKMLSHAVDGGDIEVMGMLVGYTSNDMIVVKDCYSLPVQGTETRVNAHMESYEYMVQYLDAFVTKEDKIVGWYHSHPGYGCWLSNIDIQTQSLNQNYQDPYLAIVVDPKKSLSGNTLDIGAFRTLPSKDNNEHVDYYPLNIQLYQNSLDVNISKLKLKFKVDPAIQNNPNEPELMKELHECVENWFHAKKVMKSTVGFNAIGSTVVNETEIGNEDFTHERSNSISSTSSLTTRHTTDVEMDDQESAQSSLDIPANVIPGMQFQEAEIKHEYELKKKKLLLLKVKQYQKLRTYRQLFNASE | Function: Catalytic Component of the COP9 signalosome (CSN) complex that acts as an regulator of the ubiquitin (Ubl) conjugation pathway by mediating the deneddylation of the cullin subunit of SCF-type E3 ubiquitin-protein ligase complexes. The CNS complex is involved in the regulation of the mating pheromone response.
Sequence Mass (Da): 42457
Sequence Length: 373
Domain: The JAMM motif is essential for the protease activity of the CSN complex resulting in deneddylation of cullins. It constitutes the catalytic center of the complex (By similarity).
Subcellular Location: Cytoplasm
EC: 3.4.-.-
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O35864 | MAASGSGMAQKTWELANNMQEAQSIDEIYKYDKKQQQEILAAKPWTKDHHYFKYCKISALALLKMVMHARSGGNLEVMGLMLGKVDGETMIIMDSFALPVEGTETRVNAQAAAYEYMAAYIENAKQVGRLENAIGWYHSHPGYGCWLSGIDVSTQMLNQQFQEPFVAVVIDPTRTISAGKVNLGAFRTYPKGYKPPDEGPSEYQTIPLNKIEDFGVHCKQYYALEVSYFKSSLDRKLLELLWNKYWVNTLSSSSLLTNADYTTGQVFDLSEKLEQSEAQLGRGSFMLGLETHDRKSEDKLAKATRDSCKTTIEAIHGLMSQVIKDKLFNQINVA | Function: Probable protease subunit of the COP9 signalosome complex (CSN), a complex involved in various cellular and developmental processes. The CSN complex is an essential regulator of the ubiquitin (Ubl) conjugation pathway by mediating the deneddylation of the cullin subunits of the SCF-type E3 ligase complexes, leading to decrease the Ubl ligase activity of SCF-type complexes such as SCF, CSA or DDB2. Promotes the proteasomal degradation of BRSK2. The complex is also involved in phosphorylation of p53/TP53, c-jun/JUN, IkappaBalpha/NFKBIA, ITPK1 and IRF8, possibly via its association with CK2 and PKD kinases. CSN-dependent phosphorylation of TP53 and JUN promotes and protects degradation by the Ubl system, respectively. In the complex, it probably acts as the catalytic center that mediates the cleavage of Nedd8 from cullins. It however has no metalloprotease activity by itself and requires the other subunits of the CSN complex. Interacts directly with a large number of proteins that are regulated by the CSN complex, confirming a key role in the complex.
Sequence Mass (Da): 37549
Sequence Length: 334
Domain: The JAMM motif is essential for the protease activity of the CSN complex resulting in deneddylation of cullins. It constitutes the catalytic center of the complex.
Subcellular Location: Cytoplasm
EC: 3.4.-.-
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Q7RXX8 | MELPPNPGLVDVQRDALYAYDSEAHKAVVNSRPWTNDHKYFKTVRISSVAMIKMVMHARSGGNLEVMGMMQGYIEGSTMVITDAYRLPVEGTETRVNAQDEANEYMVEYLRLCREENRLENVIGWYHSHPGYGCWLSGIDVGTQSLQQQFNEPFVAVVIDPDRTVSQNKVEIGAFRTIPEGIKPFAATNTTTGDGQSVPLNKVEDFGAHSHRYYALDVEHFKSTLDSKLLETLWNKYWVQTLAQNPLLTNRDYTSSQMVDLGSRISKASKSLEMLSTTGQRGPKSDAVDQNIEKLLSEVKQIAAKERSGLMAAEVKGKVFGCGCRGQAEGVQPEKS | Function: Catalytic component of the COP9 signalosome (CSN) complex that acts as an regulator of the ubiquitin (Ubl) conjugation pathway by mediating the deneddylation of the cullin subunit of SCF-type E3 ubiquitin-protein ligase complexes (By similarity). The CSN complex is involved in the regulation of the circadian clock through its control of the stability of the SCF(FWD-1) complex.
Sequence Mass (Da): 37462
Sequence Length: 336
Domain: The JAMM motif is essential for the protease activity of the CSN complex resulting in deneddylation of cullins. It constitutes the catalytic center of the complex (By similarity).
Subcellular Location: Cytoplasm
EC: 3.4.-.-
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O94454 | MNNQLENVFRFDEEKERAKIRESPWKHDPEFFRSVKISAVALLKMLRHVSQGMPLEVMGYVQGKVEGASLIILDSFALPVEGTETRVNAHEEAQEYSVQYHTLCKSVYRHENVIGWYHSHPNYGCWLSGVDVETQRQNQKYQDPFVAVVLDPKRSLESPYVNIGAFRTYPVGNDGSIRTKSRHHPSVLFKNLPSSKIEDAGAHAEAYYSLPITYFHSKAEKKVTEFLRNRNWSRSITECSILQNNEFLHDSEKLIDHLIHETGNNELPVASAYEQSKACCNELSTFLSQIDVQDKLFKE | Function: Catalytic Component of the COP9 signalosome (CSN) complex that acts as an regulator of the ubiquitin (Ubl) conjugation pathway by mediating the deneddylation of the cullin subunit of SCF-type E3 ubiquitin-protein ligase complexes.
Sequence Mass (Da): 34394
Sequence Length: 299
Domain: The JAMM motif is essential for the protease activity of the CSN complex resulting in deneddylation of cullins. It constitutes the catalytic center of the complex (By similarity).
Subcellular Location: Cytoplasm
EC: 3.4.-.-
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Q4P804 | MTAPSSSSSASMARANFELNNAIIPLSSTTLDSIFAYDNEAQRAILHAQPWKTDPHFFQKVRISAVALIKMVMHARSGGIYEIMGLMQGKIDVENRTLYVMDSFALPVEGTETRVNAQNEAYEYMVQYLDHSKEVGRLENVVGWYHSHPGYGCWLSGIDVNTQRTNQQFQDPFVAIVIDPNRTISSGKVDIGAFRTFPEGYTSSSSIGGGDSEYQSIPLSKIEDFGVHANEYYPLEVEHFKSSLDGKLLDLLWNKYWQNTLSQSPLVSNRAYTTSQIRDLADKLAQTNAAVLNRNSVSSAPFTTTAGAASVRIGAGKDVAAETEQNSGGSAKDTPAGTAQDAAGLVKEFEQRSKMSAISRASNDAAKLASEANHGLLASQLKHTLFHNHTATPTPASASAPTPIRL | Function: Catalytic Component of the COP9 signalosome (CSN) complex that acts as an regulator of the ubiquitin (Ubl) conjugation pathway by mediating the deneddylation of the cullin subunit of SCF-type E3 ubiquitin-protein ligase complexes.
Sequence Mass (Da): 44129
Sequence Length: 406
Domain: The JAMM motif is essential for the protease activity of the CSN complex resulting in deneddylation of cullins. It constitutes the catalytic center of the complex (By similarity).
Subcellular Location: Cytoplasm
EC: 3.4.-.-
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Q6C703 | MASLATFQVENDIVDVDSTPQQGFDRDDLYKYDDVEQKAILAAHPWRTDPSYFRNVLVSSIALVKMAMHARSGGAIEVMGMMTGKILPNTFVVMDCYPLPVEGTETRVNAQQEGIEFMVEYLQGLKDVGRRENIVGWYHSHPGYGCWLSGIDVDTQFQNQQFQEPFLAVVVDPNRTISAGKVEIGAFRTYPKDYKPPKKATKQNQDQSVPLSKAKDYGAHSERYYELDVSFFKSSLDENLLQLLWNKNWAATLSQSTIQLNHDYTSKLMLDLSEKNAQLAIGLGEKTPQSQGRGFREAMSKADNEPHTNLLNYSTKGQWEAVNRSVKDGVQIGSDELQGLMSLEIQRRLFGRAK | Function: Catalytic Component of the COP9 signalosome (CSN) complex that acts as an regulator of the ubiquitin (Ubl) conjugation pathway by mediating the deneddylation of the cullin subunit of SCF-type E3 ubiquitin-protein ligase complexes.
Sequence Mass (Da): 39933
Sequence Length: 354
Domain: The JAMM motif is essential for the protease activity of the CSN complex resulting in deneddylation of cullins. It constitutes the catalytic center of the complex (By similarity).
Subcellular Location: Cytoplasm
EC: 3.4.-.-
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Q12468 | MSLSNKTVKELRQLLKERYTVEDELTESIALSSMRFKPSQEPEFHALSQSSLLKTKLKQQSSTDIPSYTHVLISKLSCEKITHYAVRGGNIEIMGILMGFTLKDNIVVMDCFNLPVVGTETRVNAQLESYEYMVQYIDEMYNHNDGGDGRDYKGAKLNVVGWFHSHPGYDCWLSNIDIQTQDLNQRFQDPYVAIVVDPLKSLEDKILRMGAFRTIESKSDDNSATSYYELETIIFDSELNRALFETKLNLHCVIEDDESEQISLNRLIDSMKQYSYLMDSKNVRTRIKLATTSERVSNENKKNIDYQNRSTRSQFCLNTQRGDSTETSSFGSMFSGDNTSDVDMEDRNLTEFDSTDTSLCINGEPSIHVNRVERSSRSTDNFHNSKKRMNSNQERCHDEGNDMLQRNVLETDYARAKNRILASKIKQYERLRFYKDTFTL | Function: Catalytic component of the COP9 signalosome (CSN) complex that acts as an regulator of the ubiquitin (Ubl) conjugation pathway by mediating the deneddylation of the cullin subunit of SCF-type E3 ubiquitin-protein ligase complexes (By similarity). The CSN complex is involved in the regulation of the mating pheromone response.
Sequence Mass (Da): 50812
Sequence Length: 440
Domain: The JAMM motif is essential for the protease activity of the CSN complex resulting in deneddylation of cullins. It constitutes the catalytic center of the complex (By similarity).
Subcellular Location: Cytoplasm
EC: 3.4.-.-
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P33911 | MLVLSRKINEAIQIGADIEVKVIAVEGDQVKLGIDAPKHIDIHRKEIYLTIQEENNRAAALSSDVISALSSQKK | Function: A translational regulator that binds mRNA to regulate translation initiation and/or mRNA stability. Usually binds in the 5'-UTR at or near the Shine-Dalgarno sequence preventing ribosome-binding, thus repressing translation. Represses expression of flagellin (hag) in a post-transcriptional fashion. Specifically binds to 2 sites in the 5'-UTR of hag mRNA in a cooperative fashion; the second site overlaps the Shine-Dalgarno sequence and prevents 30S ribosomal subunit binding . Mutation of either binding site abolishes CsrA regulation of hag expression . Repression is greater in the 1A96 than 168 genetic background and higher in minimal than rich medium . Translation repression is antagonized by FliW . Partner switching by flagellin between FliW and CsrA provides a flagellar assembly checkpoint to tightly control the timing of flagellin synthesis. Flagellin binds to assembly factor FliW, freeing CsrA to repress translation of the flagellin mRNA. When the flagellar hook is assembled flagellin is secreted, depleting intracellular flagellin, which frees FliW to interact with CsrA and inhibits CsrA binding to mRNA. This derepresses flagellin translation and provides protein for flagellar assembly. Once the flagellar filament is completed cytoplasmic flagellin levels rise and CsrA translation repression of flagellin reinitiates . Overexpression leads to a dramatic reduction in motility, a significant reduction in flagellin synthesis and reduced flagella assembly .
Sequence Mass (Da): 8136
Sequence Length: 74
Domain: Contacts FliW via its C-terminus (residues 49-58).
Subcellular Location: Cytoplasm
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Q3ECR7 | MTMSRNGKTNKAAYSQRFTRCSVAVAATRSASVVAAAFDFYICIIISTLLSLIVSLASQLLF | Function: Involved in resistance to abiotic stress.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 6680
Sequence Length: 62
Subcellular Location: Cell membrane
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A0A178WF56 | MAQYHQQHEMKQTMAETQYVTAPPPMGYPVMMKDSPQTVQPPHEGQSKGSGGFLRGCLAAMCCCCVLDCVF | Function: Regulates negatively salt stress responses and Na(+) homeostasis . Prevents Na(+) efflux, disturbs reactive oxygen species (ROS) homeostasis, and represses the expression of nuclear salt stress-responsive genes . Involved in resistance to abiotic stress .
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 7812
Sequence Length: 71
Subcellular Location: Cell membrane
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Q1PEX8 | MSQYSQNQYAGAYPTPPVSTGPYVAPPPLGYPTNDTTHATVAPVETKSKGEAADGFLKGCLATMLACCVLDACIF | Function: Involved in resistance to abiotic stress.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 7800
Sequence Length: 75
Subcellular Location: Cell membrane
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Q9SKX9 | MSQYSQNQSSGAYPTPPVSTGPYVAPPPLGYPTNDTSHATVATVETKSKGDGFLKGCLAAMCCCCVLDACF | Function: Involved in resistance to abiotic stress.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 7337
Sequence Length: 71
Subcellular Location: Cell membrane
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O22802 | MASYHVSHDSYQSPGPSPLYQPIIEAPPPPYPPTRTRYQDYYGGYGQPHPPPLRPYRSDHEYYGDGEYVGCFPFLRSCLTTLCCCWFVEQCCFRSRY | Function: Involved in resistance to abiotic stress.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 11313
Sequence Length: 97
Subcellular Location: Cell membrane
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Q8W472 | MNQSAQNYFSVQKPSETSSGPYTSPPPIGYPTRDAVVGDPPAAAVETNSKGVNPEGCCAAICCCCVLDACF | Function: Involved in resistance to abiotic stress.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 7317
Sequence Length: 71
Subcellular Location: Membrane
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Q9LHJ3 | MNPSEQNHLSVEKPSQTSSGPYTSPPPIGYPTRDAMVGDPPAAAVETKSKGDGFWKGCCAAICCCCVLDACF | Function: Involved in resistance to abiotic stress.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 7525
Sequence Length: 72
Subcellular Location: Cell membrane
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Q9V498 | MTFHKTFGYGCIVLICFELLFAGVETSSENDDEYLTQKEIILEKSYHGLIRENETLVEITPLIKVNEEKICNFHILKKPYHEIPFKIELVNNLGILKARRTLNCENRKSYHFEICAIYCDGTPSNTANVHITVIDVNEYAPTFLEPSYVIEVDEGRLYNEILRVEASDKDCTPLFGDVCKYEILNNDEPFSIDNEGSIKNTEPLSHKASHNHILSVVAYDCAMKESAPIMVSIKVRRVCETKFVGMPERIDYTSGSTESLQLFPNARLDLCDISCKNEEDLRIHSSIALKTKHISFGCDRDISNCTSGQKVKDLLPHGAEWTKELSYDEGLEPIFHFDGSTGVVVPATVIDHYDFSSQPFSILTLFRHNSQVEINKHVKEHIVCSADDHKMNRHHMALFVRNCRLIFLLRKNFNEGDLNIFSPAEWRWKIPEVCDNEWHHYVLNVEDSSKVDLFIDGVRFENSIENRHSNPEVIDDWPLHAAHGVNTSLAIGACYQSLENRLKHGFNGDISEVKVSLNSVLTAEDIKCGTTCAEHLLAPKPLQSNNEKSYSDNSQIKENIEMNEIYISAKNKHDIEQFMRKVQYINTKQKPTVGRRNIEVLTTLNCKNESSLRLPPIETYIMVNEPIAPLGIDIDVVSASLETSDLTPPSYSPKIAISGTSNKLVSYQEIKLGVHILEKTCIDSVSKNNGKLEEKNHIDSCSVVVFPSLNPDHEDIKIDGDESLSSSMDIKTNINKDGVEMIGKDTISNYINVLRSLVYSNKKPAYYLNRVFKLSCAQQSSQYKSGEYTLTLTVLHPKQTLFKSTNVLPSSLSKVNFIGNTDNETSFHRNSGSVNGNDNNQPTESKVYSYSLLHTNNVQEPKSHIHSFIHKAEGSHVTMLIILVSVFLAVLLCGVSIARLKNNQKYIEHHQPCPKISDDGLIWDDSALTITINPMQADVTSDASSESENSESEDEEALKDGFTHINQLEWDNSNIFQQ | Function: Postsynaptic adhesion molecule that binds to presynaptic neurexins to mediate both excitatory and inhibitory synapse formation (By similarity). Promotes synapse development by acting as a cell adhesion molecule at the postsynaptic membrane, which associates with neurexin-alpha at the presynaptic membrane (By similarity).
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 110493
Sequence Length: 978
Domain: The cytoplasmic domain binds synaptic Ca(2+).
Subcellular Location: Postsynaptic cell membrane
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Q9EPL2 | MLRRPAPALAPAVRLLLAGLLCGGGVWAARVNKHKPWLEPTYHGIVTENDNTVLLDPPLIALDKDSPLRFAESFEVTVTKEGEICGFKIHGQNVPFDAVVVDKSTGEGIIRSKEKLDCELQKDYTFTIQAYDCGKGPDGTGVKKSHKATVHIQVNDVNEYAPVFKEKSYKAAVVEGKQHSSILRVEAVDADCSPQFSQICSYEILTPDVPFTVDKDGYIKNTEKLNYGKEHQYKLTVTAYDCGKKRATEDVLVKISVKPTCSPGWQGWSSRIEYEPGTGALAVFPSIHLETCDEPVASVQATVELETSHIGKGCDRDTYSEKSLHRLCGAAAGTSELLPSPSSSFNWTVGLPTDNGHDSDQVFEFNGTQAVRIPDGVVTLDPKEPFTISVWMRHGPFGRKKETILCSSDKTDMNRHHYSLYVHGCRLVFLLRQDPSEEKKYRPAEFHWKLNQVCDEDWHHFVLNVEVPSVTLYVDGIPHEPFSVTEDYPLHPTKIETQLVVGACWQEYSGVESGNETEPATMASAGGDLHMTQFFRGNLAGLTVRSGKLADKKVIDCLYTCKEGLDLQVPEDANRGVQIQASSSQAVLTLEGDNVGELDKAMQHISYLNSRQFPTPGIRRLKITSTVKCFNEAACIEVPPVEGYVMVLQPEEPKISLSGVHHFARAASEFESAEGISLFPELRIISTITREVEPEADGSEDPTVQESLVSEEIVHDLDTCEVTVEGDELNAEQESLEVDVTRLQQKGIEASHSDLGVVFTGVETMASYEEVLHLLRYRNWHTRSLLDRKFKLICSELNGRYLSNEFKVEVNVIHTANPVEHANHMAAQPQFVHPEHRSFVDLSGHNLANPHPFAVVPSTATVVIVVCVSFLVFMIILGVFRIRAAHQRTMRDQDTGKENEMDWDDSALTITVNPMETYEDQHSSEEEEEEEEEEESEDGEEEEDITSAESESSEEEEGGPGDGQNATRQLEWDDSTLSY | Function: Postsynaptic adhesion molecule that binds to presynaptic neurexins to mediate both excitatory and inhibitory synapse formation . Promotes synapse development by acting as a cell adhesion molecule at the postsynaptic membrane, which associates with neurexin-alpha at the presynaptic membrane (By similarity). Also functions as a cargo in axonal anterograde transport by acting as a molecular adapter that promotes KLC1 association with vesicles . Complex formation with APBA2 and APP, stabilizes APP metabolism and enhances APBA2-mediated suppression of beta-APP40 secretion, due to the retardation of intracellular APP maturation .
PTM: Proteolytically processed under normal cellular conditions . A primary zeta-cleavage generates a large extracellular (soluble) N-terminal domain (sAlc) and a short C-terminal transmembrane fragment (CTF1) . A secondary cleavage catalyzed by presenilin gamma-secretase within the transmembrane domain releases the beta-Alc-alpha chain in the extracellular milieu and produces an intracellular fragment (AlcICD) . Beta-Alc-alpha secretion is largely dependent upon PSEN1 and PSEN2 . This processing is strongly suppressed in the tripartite complex formed with APBA2 and APP, which seems to prevent the association with PSEN1 .
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 108900
Sequence Length: 979
Domain: The cytoplasmic domain binds synaptic Ca(2+).
Subcellular Location: Postsynaptic cell membrane
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Q9H4D0 | MLPGRLCWVPLLLALGVGSGSGGGGDSRQRRLLAAKVNKHKPWIETSYHGVITENNDTVILDPPLVALDKDAPVPFAGEICAFKIHGQELPFEAVVLNKTSGEGRLRAKSPIDCELQKEYTFIIQAYDCGAGPHETAWKKSHKAVVHIQVKDVNEFAPTFKEPAYKAVVTEGKIYDSILQVEAIDEDCSPQYSQICNYEIVTTDVPFAIDRNGNIRNTEKLSYDKQHQYEILVTAYDCGQKPAAQDTLVQVDVKPVCKPGWQDWTKRIEYQPGSGSMPLFPSIHLETCDGAVSSLQIVTELQTNYIGKGCDRETYSEKSLQKLCGASSGIIDLLPSPSAATNWTAGLLVDSSEMIFKFDGRQGAKVPDGIVPKNLTDQFTITMWMKHGPSPGVRAEKETILCNSDKTEMNRHHYALYVHNCRLVFLLRKDFDQADTFRPAEFHWKLDQICDKEWHYYVINVEFPVVTLYMDGATYEPYLVTNDWPIHPSHIAMQLTVGACWQGGEVTKPQFAQFFHGSLASLTIRPGKMESQKVISCLQACKEGLDINSLESLGQGIKYHFNPSQSILVMEGDDIGNINRALQKVSYINSRQFPTAGVRRLKVSSKVQCFGEDVCISIPEVDAYVMVLQAIEPRITLRGTDHFWRPAAQFESARGVTLFPDIKIVSTFAKTEAPGDVKTTDPKSEVLEEMLHNLDFCDILVIGGDLDPRQECLELNHSELHQRHLDATNSTAGYSIYGVGSMSRYEQVLHHIRYRNWRPASLEARRFRIKCSELNGRYTSNEFNLEVSILHEDQVSDKEHVNHLIVQPPFLQSVHHPESRSSIQHSSVVPSIATVVIIISVCMLVFVVAMGVYRVRIAHQHFIQETEAAKESEMDWDDSALTITVNPMEKHEGPGHGEDETEGEEEEEAEEEMSSSSGSDDSEEEEEEEGMGRGRHGQNGARQAQLEWDDSTLPY | Function: Postsynaptic adhesion molecule that binds to presynaptic neurexins to mediate synapse formation, and which is involved in learning and memory (By similarity). Promotes synapse development by acting as a cell adhesion molecule at the postsynaptic membrane, which associates with neurexin-alpha at the presynaptic membrane (By similarity).
PTM: Proteolytically processed under normal cellular conditions . A primary zeta-cleavage generates a large extracellular (soluble) N-terminal domain (sAlc) and a short C-terminal transmembrane fragment (CTF1) . A secondary cleavage catalyzed by gamma-secretase within the transmembrane domain releases the beta-Alc-gamma chain in the extracellular milieu and produces an intracellular fragment (AlcICD) . This processing is strongly suppressed in the tripartite complex formed with APBA2 and APP, which seems to prevent the association with PSEN1 .
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 107006
Sequence Length: 955
Domain: Binds synaptic Ca(2+) with its cytoplasmic domain.
Subcellular Location: Postsynaptic cell membrane
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Q9ER65 | MLPGRLCLVPLLLALGVGSGGGSGDGGDSRRRRLLVAKVNKHKPWIETSYHGVITENNDTVILDPPLVALDKDAPVPFAGEICAFKIHGQELPFEAVVLNKTSGEGRLRAKSPIDCELQKEYTFIIQAYDCGAGPREAAWKKSHKAVVHIQVKDVNEFAPTFKEPAYKAIVTEGKIYDSILQVEAIDEDCSPQYSQICNYEIVTTDVPFAIDRNGNIRNTEKLSYDKQHQYEILVTAYDCGQKPAAQDTLVQVDVKPVCKPGWQDWTKRIEYQPGSGSMPLFPSIHLETCDGAVSSLQVTAELQTNYIGKGCDRETYSEKSLQKLCGASSGIIDLLPSPSAATNWTAGLLVDSSEMIFKFDGRQGAKIPDGIVPKNLTDQFTITMWMKHGPSPGVRAEKETILCNSDKTEMNRHHYALYVHNCRLVFLLRKDFDQADTFRPAEFHWKLDQICDKEWHYYVINVEFPVVTLYMDGATYEPYLVTNDWPIHPSHIAMQLTVGACWQGGEVAKPRFAQFFHGSLASLTIRPGKMESQKVISCLQACKEGLDINSLESLGRGIKYHFNPSQSILVMEGDDIGNINRALQKVSYINSRQFPTAGVRRLRLSSKVQCFGEDVCISIPDVDAYIMVLQAIEPQITLQGTERFWRPAAQFESARGVTLFPDIKIVSTFAKTEASGDMRATGTAPKSAVLEEMLHNLDFCDILVLGGDLDPRQECLELNHSELHQRHLDATNSTAGYSIYGVGSMNRYEQVLHHLRYRNWHPTSLETRRFRIKCSELNGRYTSNEFNLEVSVLHEVRVSDKEHVNHLIVQPPFLQSVHHPETRSSIQRSSVVPSIATVVIIISVCMLVFVVAMGVYRVRIAHQHFIQETEAAKEAEMDWDDSALTITVNPMEKHEGPGNGEDETTEVEEEEEAEEGSSSSSSGSDDSEEEEEEGMGRVRHGQSGTSSQSPERSTWNTAGVINIWK | Function: Postsynaptic adhesion molecule that binds to presynaptic neurexins to mediate synapse formation, and which is involved in learning and memory . Promotes synapse development by acting as a cell adhesion molecule at the postsynaptic membrane, which associates with neurexin-alpha at the presynaptic membrane (By similarity).
PTM: Proteolytically processed under normal cellular conditions. A primary zeta-cleavage generates a large extracellular (soluble) N-terminal domain (sAlc) and a short C-terminal transmembrane fragment (CTF1). A secondary cleavage catalyzed by gamma-secretase within the transmembrane domain releases the beta-Alc-gamma chain in the extracellular milieu and produces an intracellular fragment (AlcICD). This processing is strongly suppressed in the tripartite complex formed with APBA2 and APP, which seems to prevent the association with PSEN1.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 107887
Sequence Length: 966
Domain: Binds synaptic Ca(2+) with its cytoplasmic domain.
Subcellular Location: Postsynaptic cell membrane
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A0A8M9PFP2 | MARMSFLSFLLFCLTSVAHGNKANKHKPWIETEYQGIVMENDNTVLLNPPLFALDKDAPLHYAGEICGFRVHNGPGGSGSAQFEAVVLDRSTGEGLVRSKEPLDCESQKEHSFTIQAYDCGEGPDGTNSKKSHKATVHVRVNDVNEFSPVFVERRYEASVPEGRLFDRIVRVEAVDADCSPQYSQICFYDIITPNVPFTIDNDGNIKNTEPLDSKRQRVHSFWVTAFDCGKNRAQADAQVIVTVKPSCKPGWIGWTKRIEYTPGSGSIPLFPNLHLETCEETVWNIQATVELQTSHIGKGCDRDSYSDRSVRRLCGAVRGEVDLLPPPSPATNWTAALPTLPSSDSSLVFSFNGSTHVAVVPDSVASAVSGDHFTLQLWMRRGGASTQPPANQARGTRKEEETIVCSTVKNDDSYSHYSLSVHGCRLSLFYWPDVSAARPVKFLWKLEQVCDSEWHHLSLSVQFPSVTLYVDGVTFDPALIHDNGAIPNPAPHQRLVIGACWEPEEKPKDIVNNTMPENKDTGKFVSGYKGLLSGVTVRPGNVEPHSVVECLYACREGLDFGDLETLGSGMKVHVNPSQSVLVLEGDDIESFNRAVQQVTYRNSLRFATPGVRPLKLTTSLRCFSEESCLSLRQLEGYLVVLQPDAPQISLSGVGPHLARPAAEFEGPQGVPLFPELRIVCSLSHAVNTAAQGMEGGALMSDAVAHTLDGCEVQPLGEELNTEREELLVDMESLRERGLDIINTTAYIAITGAESISVYEDVLRSIHYRLAKGSARFERRFRLSCSEMNGRYTSNELTLEVNFLHSLDSLYHPSHLLASQQQFLHPSHHTGELSGHTLPNPHRNSVVPGAATVIIMVCVGFLVVMVILGVFRIRSIHRRGEGARGGGKEGGNQWDDSALTIIVNPMETYENRMGITTDMEGECEDEEEVVDSPDDTSDDQRIIIKKEGRDSAPRRY | Function: Synaptic adhesion molecule . Promotes synapse development by acting as a cell adhesion molecule at the postsynaptic membrane, which associates with presynaptic neurexins (By similarity).
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 105444
Sequence Length: 956
Domain: The cytoplasmic domain binds synaptic Ca(2+).
Subcellular Location: Postsynaptic cell membrane
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A5VF68 | MSILARPAAPSPRPNALANWLLLVAVLVFAIVVVGGITRLTESGLSITEWKPVRGIVPPLNQAEWLAEFENYKRIPQYAAFNLHMTLEGFKAIYFWEYMHRLLARGIGAVLAGVMIVAWWKRAIPAGYGWRMIGIFALGGLQGAIGWWMVYSGLSVRTEVSHIRLATHLIAALLIFSALVWTVLDLRRLARDPDARPARPTALAIAAVLILAVQIMLGAFVAGLRAGYAFATWPKMGDEWFPAGGWNVAQGLANLHENPIVVQFVHRWWAWAAAIAALAVARAARKRGAVGPVHAVATLIVVQIALGIATLLTGVDIAVAVAHQAVAVLLLAALLWAGHGLDKPKVS | Function: Catalyzes the conversion of heme O to heme A by two successive hydroxylations of the methyl group at C8. The first hydroxylation forms heme I, the second hydroxylation results in an unstable dihydroxymethyl group, which spontaneously dehydrates, resulting in the formyl group of heme A.
Catalytic Activity: 2 A + Fe(II)-heme o + H2O = 2 AH2 + Fe(II)-heme a
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 37512
Sequence Length: 347
Pathway: Porphyrin-containing compound metabolism; heme A biosynthesis; heme A from heme O: step 1/1.
Subcellular Location: Cell membrane
EC: 1.17.99.9
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B6IUZ7 | MTSLSLSPAAGPQRSAAAPKAVAVWLLVCAGMVFAMAIIGAITRLTESGLSITEWKPVTGALPPLSEAQWLAEFEKYRQIPEYQLLKRGMSLEEFKGIYFWEWLHRLWGRLIGVVFLLPFVWFWVRGQVSRALAPTLAGLFLLGGLQGFIGWFMVQSGLTERTDVSHYRLALHLGMAFLIYAALLKVALGLLDPAPAPQPAAGRLRPHAWAALALLGVTIVWGAFVAGINAGFAYNTWPLMGGTLAPAEMWTQTPVWLNLLENTAAVQFVHRWLAVVTALVVLSLCWQAWRTGGGTRLRGVAAGLAAATVAQVGLGIATLLSVVWIPLATAHQGGALVLTGLLVWTLHLLRPPETPRQATPLTATPLTEMPAPR | Function: Catalyzes the conversion of heme O to heme A by two successive hydroxylations of the methyl group at C8. The first hydroxylation forms heme I, the second hydroxylation results in an unstable dihydroxymethyl group, which spontaneously dehydrates, resulting in the formyl group of heme A.
Catalytic Activity: 2 A + Fe(II)-heme o + H2O = 2 AH2 + Fe(II)-heme a
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 40440
Sequence Length: 374
Pathway: Porphyrin-containing compound metabolism; heme A biosynthesis; heme A from heme O: step 1/1.
Subcellular Location: Cell membrane
EC: 1.17.99.9
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A8F119 | MQKSLITKWLCISCIMVIATIVIGGITRLTGSGLSIVEWRPVTGILPPFSFESWQAEFAKYKAFPEYNSVNYGITLSQFKFIYLLEFIHRLLGRITALIYIVPLIYFYFKDVIKNRDMLPYIIALWLFCVQGFMGWYMVKSGLLNSPYVSHCRLAFHLIIAVIIYHILFYQLIKNRCDILLIPSQTDLKLPLIFSGIAITVVYVQIFLGALVAGLDAGLIYNSFPLMDYSFIPMEIKDNFFDLKNWYDPVFIQFIHRLGGYSVFLVVVVLIICLLKIEHPKLNKIAYFLMIALLMQVSTGIITLLYSVPIIIASIHQLFAVILLSIIIWCCFLIKSS | Function: Catalyzes the conversion of heme O to heme A by two successive hydroxylations of the methyl group at C8. The first hydroxylation forms heme I, the second hydroxylation results in an unstable dihydroxymethyl group, which spontaneously dehydrates, resulting in the formyl group of heme A.
Catalytic Activity: 2 A + Fe(II)-heme o + H2O = 2 AH2 + Fe(II)-heme a
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 38692
Sequence Length: 337
Pathway: Porphyrin-containing compound metabolism; heme A biosynthesis; heme A from heme O: step 1/1.
Subcellular Location: Cell membrane
EC: 1.17.99.9
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F6SNN2 | MNISASTCGSPSSSESLPAGDLFKELWSKLKECHDKELQELLLKINKLKKQRCLDAQRLEEFYTKNQHLREQQKTLHDTIKVLEDRLRAGLCDRCTVTEEHMRKKQQEFENIRQQNLKLITELMNDKNALQDENKRLSEQLHNMQKSRWKSDEENPADTGEGEDGVIPDSPLSTFSLSMVSRMRRKKDNKHIRYSEKAPEDTLTLERKITCIPSQGSAEKNASHSSHRRKGEDILVAETLELSPLPNGKSKRKKVYLCSKTSIAFASILLVLLHLFAEQLHSWMNNLSQVSKSLRWCLPLKGNNKQGYIEYLFRFTEGSMEESQGNDDDGWNTKEASPVFGGPARNIRRSAEMDCISPPLPVGLNSKLISKCSRNPSDFLFNSVQAKAEDGAQATRLCLGKETDSVISQCSSNGQGVLRCSPNKSVPGGAQMGKDILDSEHHKQMANRYGKRKNAEAEQEESCESSFDKENNIPIKDIGSERHSMLDKPLDLSDRFSVLRPQDRSHGSSRGRTKQTFALVPEKPDPKKPLHIDLREDLYHQTKQKKVFVSGLVERSAFNLHEDKEVTEEGNQLFDDLEIETVHEPKRNARSVHRGVQPTSVLQPNLHMVQACPESQQGKPPIDNMQWSIDPGADLSQYEMDMTMEDSKGGSPAKPELEDMDYTYVSESFLLKMKKGDPGDSEDESKGQDSFEKMFDKSEYGEYVLCIKDRSPSQSCKERNDLSSMVCKNIYTHSVRFDRVKKQKAFVEPYFQRPEQKKPAMDFPHIEVVRKKDERRKMLGHTCKECELYYADLPEEERAKKLASCSRHRFRYIPPSTPENFWEVGFPSTQTCQDRGYIKEELSPCQRPRRRQPYNAKFSSKIKEQKT | Function: Endonuclease that cooperates with the MRE11-RAD50-NBN (MRN) complex in DNA-end resection, the first step of double-strand break (DSB) repair through the homologous recombination (HR) pathway. Functions downstream of the MRN complex and ATM, promotes ATR activation and its recruitment to DSBs in the S/G2 phase facilitating the generation of ssDNA.
Sequence Mass (Da): 99332
Sequence Length: 867
Domain: The damage-recruitment motif is required for DNA binding and translocation to sites of DNA damage.
Subcellular Location: Nucleus
EC: 3.1.-.-
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Q8SQW2 | MEPAEEGEILAHRRFTATKMEYEKIRIIGEGTFGQVILARKGRARYALKKVSKEKEGLSVTTIREVQVLRAMGHPSIVRLIEVVVEPGGDIYMVFPYFPYDLNRFIRSNKMTCSEIKHIFYQIAQGVCYIHSKGIMHRDLKSANILLDQKLNASIADFGMARYTTKTGAYTPGMVTLWYRAPEILLGSSSYTYAVDIWSLGCILTEMYLGHMIFQGSTEMLQLEMVIHACGSINENSYPGVQDLPGFRNFRLPQSPRRIEGIIRKHDASAVELVSKMLCLDPSKRITVEQVVGSKYFEHEARRDASSAGLQGCSYREDRLSLSKRKNVD | Function: Catalytic subunit of the CTDK-I complex, which hyperphosphorylates the C-terminal heptapeptide repeat domain (CTD) of the largest RNA polymerase II subunit. Involved in RNA polymerase II transcriptional elongation and pre-mRNA 3'-end processing (By similarity).
Catalytic Activity: [DNA-directed RNA polymerase] + ATP = ADP + H(+) + phospho-[DNA-directed RNA polymerase]
Sequence Mass (Da): 37291
Sequence Length: 329
Subcellular Location: Nucleus
EC: 2.7.11.23
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O14098 | MSYSKSTIYRRQGTEPNSHFRRTVEEKSQLSGTNEESLGGHTLSSNAFKNNSSSISPSSSAKDPREQRKRTFPLNDTHSSRARQHERPFRSRKSRRRKGKKAFSPRPGSPPSPSFYRSGSQKRARNLTTKDYFAKRSESSSSASVSPISPSANRNDSKRQASSFRRSPPSSVHMKPSAFNGRKVSRRPSSSPPPIPSIPHETTSSDTQKKSSVSSGFPENKHGKFHFHIPNERRSRFDQPPSKRMALTSTARESVPAPLPSPPSGPIYTYTYPKPAYEKIDQIGEGTYGKVYKAINTVTGDLVALKRIRLEQEKDGFPITTVREVKILQRLRHKNIVRLLEIMVEKSSVYMVFEYMDHDLTGVLLNSQLHFTPGNIKHLSKQIFEALAYLHHRGVLHRDIKGSNILLNNNGDLKFADFGLARFNTSSKSANYTNRVITLWFRPPELLLGETAYDTAVDIWSAGCIVMELFTGKPFFQGRDEISQLEVIYDMMGTPDVHSWPEVKNLPWYELLKPVEEKKSRFVETFKEILSPAAIDLCQKLLALNPFCRPSAHETLMHEYFTSESPPPEPAVILKNMQGSWHEWESKKRKSKR | Function: Catalytic subunit of the CTDK-I complex, which hyperphosphorylates the C-terminal heptapeptide repeat domain (CTD) of the largest RNA polymerase II subunit. Involved in RNA polymerase II transcriptional elongation and pre-mRNA 3'-end processing (By similarity). Together with ctk2/lsc1, required for the regulation of cytokinesis by phosphorylating 'Ser-2' residues found in the heptad repeats of the CTD. Required for nuclear localization of ctk2/lsc1. Positively regulates the septation initiation network (SIN) and promotes successful completion of cytokinesis in response to perturbation of the actomyosin ring. Acts in parallel to clp1 to promote actomyosin ring stability upon cytokinesis checkpoint activation.
Catalytic Activity: [DNA-directed RNA polymerase] + ATP = ADP + H(+) + phospho-[DNA-directed RNA polymerase]
Sequence Mass (Da): 67366
Sequence Length: 593
Subcellular Location: Nucleus
EC: 2.7.11.23
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Q03957 | MSYNNGNTYSKSYSRNNKRPLFGKRSPNPQSLARPPPPKRIRTDSGYQSNMDNISSHRVNSNDQPGHTKSRGNNNLSRYNDTSFQTSSRYQGSRYNNNNTSYENRPKSIKRDETKAEFLSHLPKGPKSVEKSRYNNSSNTSNDIKNGYHASKYYNHKGQEGRSVIAKKVPVSVLTQQRSTSVYLRIMQVGEGTYGKVYKAKNTNTEKLVALKKLRLQGEREGFPITSIREIKLLQSFDHPNVSTIKEIMVESQKTVYMIFEYADNDLSGLLLNKEVQISHSQCKHLFKQLLLGMEYLHDNKILHRDVKGSNILIDNQGNLKITDFGLARKMNSRADYTNRVITLWYRPPELLLGTTNYGTEVDMWGCGCLLVELFNKTAIFQGSNELEQIESIFKIMGTPTINSWPTLYDMPWFFMIMPQQTTKYVNNFSEKFKSVLPSSKCLQLAINLLCYDQTKRFSATEALQSDYFKEEPKPEPLVLDGLVSCHEYEVKLARKQKRPNILSTNTNNKGNGNSNNNNNNNNDDDDK | Function: Catalytic subunit of the CTDK-I complex, which hyperphosphorylates the C-terminal heptapeptide repeat domain (CTD) of the largest RNA polymerase II subunit. CTDK-I phosphorylates 'Ser-5' if the CTD substrate is not phosphorylated at 'Ser-5', but will phosphorylate 'Ser-2' of a CTD substrate if 'Ser-5' is already phosphorylated. CTDK-I is also more reactive toward substrates that are prephosphorylated at 'Ser-2' or 'Ser-5' compared with an unphosphorylated CTD substrate, therefore efficiently creating doubly phosphorylated CTD repeats. Involved in RNA polymerase II transcriptional elongation, and through PTI1, pre-mRNA 3'-end processing. Participates in both positive and negative regulation of CTD phosphorylation. Required for DNA damage induced transcription, including the expression of the RNR genes, and reprogramming of gene expression upon amino acid starvation. Required for SET2 mediated H3K36 methylation. Also regulates H3K4 methylation. Controls the maintenance of suppressive chromatin in the coding regions of genes by both promoting H3K36 methylation, which leads to histone deacetylation, and catalyzing phosphorylation of the CTD required to localize H3K4 chromatin modification specifically to the 5' ends of genes, thereby creating a boundary for H3K4 methylation that prevents a mark associated with transcriptional initiation from spreading into the bodies of genes. Involved in RNA polymerase I transcription. Involved in telomere maintenance. Acts together with SNF1 to induce GSY2 transcription in response to glucose limitation. Involved in the adaptation to alternative carbon sources, including galactose, glycerol and ethanol, but not raffinose. Required for the integrity of the rDNA locus. Functions in translation elongation by enhancing decoding fidelity. Needed for translational accuracy by phosphorylating RPS2.
PTM: Phosphorylated on Thr-338 by CAK1. Phosphorylation is essential for the elevated CTD Ser-2 phosphorylation and required to activate transcription of stationary-phase genes during the diauxic shift.
Catalytic Activity: [DNA-directed RNA polymerase] + ATP = ADP + H(+) + phospho-[DNA-directed RNA polymerase]
Sequence Mass (Da): 60501
Sequence Length: 528
Subcellular Location: Nucleus
EC: 2.7.11.23
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P79955 | MDSTDKKVQVASRLPVPPKRKYVSNDENQEQMQRKRLRSSLESELPAVRVAASIATSKPRAAPVAALPKPQVIGRQSLAVMRPKNSGPGITSTSFSGKTKVSSSVTQPAAIGAEKKKRAAWDLKGQVNDMRDTVSNYKGKMQNLTGENARLLNSKEKLQREVEVLASENSKLSQERCTLESQLREVRQQVSTFEREVARLTELCQRQEKELSSHTNTIEELQGANAILTKQLLDKEVKLDCVSGENTSLKHTVNEQTDEIAALKVCLAEKDTEVHSLDTERRRLHNLVQELKGNIRVFCRVRPTLTPERELPAGHISFPSNDGKAIVLSKMEESHIGREKKDAVKYDFNFDCVFPPPCSQESVFEEISLLVQSALDGYPVCIFAYGQTGSGKTYTMEGPEDVTDDSMGMIPRAIHQIFSSAEELKAKGWQYTFTASFLEIYNETIRDLLINRPDKKLEYEIRKVNSANMLLYVTNLRYVKVSCVEEVHELLKIAKANRSVAKTAINDRSSRSHSVFQLKIEGENKQRDLKTSSMISLIDLAGSERLDRSLSTGDRLKETQCINTSLSTLGMVITSLCNKDSHIPYRNSKLTYLLQNSLGGNAKVLMFVNISPLEENFAESLNSLRFASKVNECVIGTARANRK | Function: Promotes mitotic spindle assembly.
Sequence Mass (Da): 71949
Sequence Length: 643
Domain: Composed of three structural domains; a small globular N-terminal, a central alpha-helical coiled coil and a large globular C-terminal which is responsible for the motor activity (it hydrolyzes ATP and binds microtubules).
Subcellular Location: Cytoplasm
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P46962 | MPSTFESQLFFSRPFLSKRQIQRAQKNTISDYRNYNQKKLAVFKFLSDLCVQLKFPRKTLETAVYFYQRYHLFNRFETEVCYTVATSCLTLGCKEVETIKKTNDICTLSLRLRNVVKINTDILENFKKRVFQIELRILESCSFDYRVNNYVHIDEYVIKIGRELSFDYKLCNLAWVIAYDALKLETILVIPQHSIALAILKIAYELLDNKNWSSKRYSLFETDEKSVNEAYFDIVNFYINSFDMCDLQRHLPADLLPIGVERFMELKKNAGPESGLPQIPDHLLNADPYITITRDNNVQERRYVLSLELINGESSINSSTRHA | Function: Cyclin subunit of the CTDK-I complex, which hyperphosphorylates the C-terminal heptapeptide repeat domain (CTD) of the largest RNA polymerase II subunit. CTDK-I phosphorylates 'Ser-5' if the CTD substrate is not phosphorylated at 'Ser-5', but will phosphorylate 'Ser-2' of a CTD substrate if 'Ser-5' is already phosphorylated. CTDK-I is also more reactive toward substrates that are prephosphorylated at 'Ser-2' or 'Ser-5' compared with an unphosphorylated CTD substrate, therefore efficiently creating doubly phosphorylated CTD repeats. Involved in RNA polymerase II transcriptional elongation, and as part of the CTDK-I complex, pre-mRNA 3'-end processing and SET2 mediated H3K36 methylation. Together with CTK3, required for CTK1 CTD kinase activation. Required for DNA damage induced transcription. Involved in the adaptation to alternative carbon sources, including galactose, glycerol and ethanol, but not raffinose. Required for the integrity of the rDNA locus.
PTM: Phosphorylated. Ubiquitinated. Phosphorylation and ubiquitination lead to degradation in growth-related way by the ubiquitin-proteasome pathway. Neither phosphorylation nor degradation requires association with CTK1.
Sequence Mass (Da): 37905
Sequence Length: 323
Subcellular Location: Nucleus
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P46963 | MDSLEARLQFIQVLKNLQKTLHKTRDSITSSSTTTPPSSQQKLNNDPIQFYLRNYRHHYEDFHQCLFDTTMKMDPLDRLDVVIYYVRIIRNLYPHSHSNTNVTKVLNEVLLMDIDLVFELCLPCQDWKSLTNQATCKELFLDLSKLIHYDATSVTHTPSDTTLIDATTWYSVKTERTTKDYKESLQRTESLLKDRDLKKLAFFQQFNSDTTAINPDLQTQPTNANILLHRMEADRELHKRSKETSWYIERPSNDILDESEFKSLWTHFETTDSGFDKDDYKNIKALNDIAKASYIY | Function: Gamma subunit of the CTDK-I complex, which hyperphosphorylates the C-terminal heptapeptide repeat domain (CTD) of the largest RNA polymerase II subunit. CTDK-I phosphorylates 'Ser-5' if the CTD substrate is not phosphorylated at 'Ser-5', but will phosphorylate 'Ser-2' of a CTD substrate if 'Ser-5' is already phosphorylated. CTDK-I is also more reactive toward substrates that are prephosphorylated at 'Ser-2' or 'Ser-5' compared with an unphosphorylated CTD substrate, therefore efficiently creating doubly phosphorylated CTD repeats. Involved in RNA polymerase I transcription and RNA polymerase II transcriptional elongation, and as part of the CTDK-I complex, pre-mRNA 3'-end processing and SET2 mediated H3K36 methylation. Together with CTK2, required for CTK1 CTD kinase activation. Required for DNA damage induced transcription. Involved in the adaptation to alternative carbon sources, including galactose, glycerol and ethanol, but not raffinose. Required for the integrity of the rDNA locus.
PTM: Ubiquitinated. Ubiquitination leads to degradation by the 26S proteasome pathway.
Sequence Mass (Da): 34809
Sequence Length: 296
Subcellular Location: Nucleus
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Q9ZKJ5 | MPTIDFTFCEINPKKGFGGANGNKISLFYNNELYMVKFPPKPSTHKEMSYTNGCFSEYVACHIVNSLGLKVQETLLGTYKNKIVVACKDFTTHQYELVDFLSLKNTMIELEKSGKDTNLNDVLYAIDNQHFIEPKVLKCFFWDMFVADTLLGNFDRHNGNWGFLRASNSKEYQIAPIFDCGSCLYPQADDVVCQKVLSNIDELNARIYNFPQSILKDDNDKKINYYDFLTQTNNKDCLDALLRIYPRIDMNKIHSIIDNTPFMSEIHKEFLHTMLDERKSKIIDVAHTRAIELSLQHKQAHSNPYDNADDLDNSNEYTPTPKRRR | Function: Virulence factor acting as a pro-inflammatory protein that induces the secretion of the pro-inflammatory cytokines TNF-alpha (tumor necrosis factor-alpha) and IL-8 (interleukin-8) from human macrophages, as well as enhanced translocation of the transcription factor NF-kappa-B complex in macrophages. Is a kinase capable of autophosphorylating itself at a threonine residue near the N-terminus. Also leads to enhanced phosphorylation of the NF-kappa-B p65 subunit (RELA) at 'Ser-276' in human epithelial cancer cells; its kinase activity is required for this enhanced phosphorylation that up-regulates NF-kappa-B activity, but it does not directly phosphorylate this protein. Thus, the kinase activity of CtkA may play an important role in the induction of host inflammatory responses during H.pylori infection.
PTM: Autophosphorylates on either Thr-3 or Thr-7.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 37606
Sequence Length: 325
Domain: The C-terminal tail (residues 301-325) is not required for the kinase activity and for translocation into human cells.
Subcellular Location: Secreted
EC: 2.7.11.1
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Q8WWI5 | MGCCSSASSAAQSSKREWKPLEDRSCTDIPWLLLFILFCIGMGFICGFSIATGAAARLVSGYDSYGNICGQKNTKLEAIPNSGMDHTQRKYVFFLDPCNLDLINRKIKSVALCVAACPRQELKTLSDVQKFAEINGSALCSYNLKPSEYTTSPKSSVLCPKLPVPASAPIPFFHRCAPVNISCYAKFAEALITFVSDNSVLHRLISGVMTSKEIILGLCLLSLVLSMILMVIIRYISRVLVWILTILVILGSLGGTGVLWWLYAKQRRSPKETVTPEQLQIAEDNLRALLIYAISATVFTVILFLIMLVMRKRVALTIALFHVAGKVFIHLPLLVFQPFWTFFALVLFWVYWIMTLLFLGTTGSPVQNEQGFVEFKISGPLQYMWWYHVVGLIWISEFILACQQMTVAGAVVTYYFTRDKRNLPFTPILASVNRLIRYHLGTVAKGSFIITLVKIPRMILMYIHSQLKGKENACARCVLKSCICCLWCLEKCLNYLNQNAYTATAINSTNFCTSAKDAFVILVENALRVATINTVGDFMLFLGKVLIVCSTGLAGIMLLNYQQDYTVWVLPLIIVCLFAFLVAHCFLSIYEMVVDVLFLCFAIDTKYNDGSPGREFYMDKVLMEFVENSRKAMKEAGKGGVADSRELKPMASGASSA | Function: Choline/H+ antiporter . Also acts as a high-affinity ethanolamine/H+ antiporter, regulating the supply of extracellular ethanolamine (Etn) for the CDP-Etn pathway, redistribute intracellular Etn and balance the CDP-Cho and CDP-Etn arms of the Kennedy pathway . Involved in membrane synthesis and myelin production .
Catalytic Activity: choline(out) + n H(+)(in) = choline(in) + n H(+)(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 73302
Sequence Length: 657
Subcellular Location: Cell membrane
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P63690 | MTTVVDAEVQLTVVSDAAGRMRVQATGFQFDAGRAVAIEDTVGKVAGVQAVHAYPRTASIVIWYSRAICDTAAILSAIIDAETVPAAAVPAYASRSASNRKAGVVQKIIDWSTRTLSGVRRDVAAQPSGETSDACCDGEDNEDREPEQLWQVAKLRRAAFSGVLLTASLVAAWAYPLWPVVLGLKALALAVGASTFVPSSLKRLAEGRVGVGTLMTIAALGAVALGELGEAATLAFLFSISEGLEEYATARTRRGLRALLSLVPDQATVLREGTETIVASTELHVGDQMIVKPGERLATDGIIRAGRTALDVSAITGESVPVEVGPGDEVFAGSINGLGVLQVGVTATAANNSLARIVHIVEAEQVRKGASQRLADCIARPLVPSIMIAAALIAGTGSVLGNPLVWIERALVVLVAAAPCALAIAVPVTVVASIGAASRLGVLIKGGAALETLGTIRAVALDKTGTLTANRPVVIDVATTNGATREEVLAVAAALEARSEHPLAVAVLAATQATTAASDVQAVPGAGLIGRLDGRVVRLGRPGWLDAAELADHVACMQQAGATAVLVERDQQLLGAIAVRDELRPEAAEVVAGLRTGGYQVTMLTGDNHATAAALAAQAGIEQVHAELRPEDKAHLVAQLRARQPTAMVGDGVNDAPALAAADLGIAMGAMGTDVAIETADVALMGQDLRHLPQALDHARRSRQIMVQNVGLSLSIITVLMPLALFGILGLAAVVLVHEFTEVIVIANGVRAGRIKPLAGPPKTPDRTIPG | Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 79309
Sequence Length: 771
Subcellular Location: Cell membrane
EC: 7.2.2.-
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G3XDA3 | MPASPGHRDVLGCLVAACVPVQPGNPSRRSMLQQSLRAQILVLLGGSLAALLLIALACFGSLTGDVRAYRELLGGPVRAAQLIDEANLQFRGQVQEWKNVLLRGRQTEAQTKYWSQFEAQERAVQDILGRLGSVAEGELKDRVERLREEHRRLGTAYRQGRQRFLEAGADPIAGDQAVTGIDRATTAQMQTLRDELHQASDLHSSSISAEARRTMLLGSLVLIGASLAVALLSLWLVNRNLVRPVQRLIEHIAQLSHGDFGERIEIRRKDELGKLALAANTLRDFLVDIFDRLRRSTRDLDSASGSLNAIASLMAAGTREQFSRTDQVATAMQEMSATAQEVARYAGDAARAADEADDSAQRGEDVMEETIRSIGEMRKEIDHTVEVIRQLESDSGRIGKVLDVIRGIAEQTNLLALNAAIEAARAGDAGRGFAVVADEVRTLAQRTAESIAEIHQIIDTVQNGAVNAARAIESGQSRSEAGAEQVANAGAMLRQITASVESIRDMNRQIATAAEEQTAVAEEISRNLTEIASIASSNQEQVEQTEAASRDLHGLSAQLGDALQRLRA | Function: Chemotactic-signal transducers respond to changes in the concentration of attractants and repellents in the environment, transduce a signal from the outside to the inside of the cell, and facilitate sensory adaptation through the variation of the level of methylation. Chemoreceptor for inorganic phosphate, which is required for taxis at high concentrations of phosphate . Recognizes inorganic phosphate directly. Can also bind to other components that have a pyrophosphate group, including ATP and ADP .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 61573
Sequence Length: 568
Domain: Binding to inorganic phosphate induces dimerization and stabilization of the ligand binding domain.
Subcellular Location: Cell inner membrane
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Q9HUW6 | MRLKQLTNLNTLLLLTVCLALGITLWWSQRAMERPFQLLDQYLELSQRFDEQVARNIRQYLGSGDAVRQQAALQALESLAEALPELPPDLARTLAPSLAELREFSAGDLLAAGKLAGDPQGLLLQAERDLTGNLEQWSAYLDAAAGQPQAGAYRTPLLLASLHLTRLSLARAKLVESANPALAGDVERELANLREQAGRIEALPLLGVLDEQRSASDDFAAMMGLAGDAEAGAGNAEDRGVALRRELASLLQRYPDELRRTRDLIERRQQLSADTGARLDAVRQALATLEPQVRGERQRLQGQVRLIQGGMIALILLIALAIDSLQRRLARVLGQLVPALSAWADGDFSRPISLRTRTEDLRNLEDSLNRLRSFLAELVGAIHRRAEQVAGSSQTLAEVSSGLHAGVERQAGDTGQIRDALGDMEAAIQQVAGDASQTADASRSAGQAVEHGQRVIGESLGGLRELVDEVQGNAQSIERLAEESATIGSVLTVIRSIAEQTNLLALNAAIEAARAGDQGRGFAVVAEEVRSLAQRTAGATEEIQQLIGRLQQAARQSVEAMRSQVEHAERTAEQAGAAEGALDEVVAAIHTIGVMAERIAEGSTQQSQAVGEIRSHSERIHALGGENLRLIGHSREQGEQLRQLGGDLRTTVQAFRL | Function: Chemotactic-signal transducers respond to changes in the concentration of attractants and repellents in the environment, transduce a signal from the outside to the inside of the cell, and facilitate sensory adaptation through the variation of the level of methylation. Chemoreceptor for inorganic phosphate, which is required for taxis at low concentrations of phosphate. Is also responsible for the positive chemotaxis toward 4-chloroaniline (4CA) and catechol . Does not recognize inorganic phosphate directly, but via a complex between the periplasmic protein PstS and inorganic phosphate .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 70783
Sequence Length: 657
Subcellular Location: Cell inner membrane
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Q9I0I6 | MMRLTLKSKVLLLAMVPVLLFALVLSGGAVLILKKQADAEVKDTRERLLGDRRAELEHYVQIAMGSIQAEYDRSANGDLNARAEAIARLSKIKYGKDGYIFGYDSQVVRLFRGDSPVDVGKSFRDRRDPSGVYLNRELVEAGRNGSHYVTYTSPLPGNESVMVPKLSYTLYLPKWDMVIGSAINLDGVEAQLVEIKQDIDERIGTLIASIVGIAGVLLVVLLVIGLAVANAMLRPLHQIRQNLDDIAAGEGDLTRRLPVTSYDELGELAGSFNRFVEKIHGLVRQIAGMTGDLKQLVEQMSAQAERSEQAMERQRHETDQVATAINEMSAAAHEVAQSAQRAAEAAQQTDHEGQAAKRVVDGSIERIHALVDEIRDSGTSLDSLQQDVQSIVSVLGVIRSIAEQTNLLALNAAIEAARAGEAGRGFAVVADEVRALASRTQQSTQEIQGMIDRLQQGTNAAVDAMRRSGEAGEGTSNQANQAGDSLDAIAQLIATINAMNAQIASAAEEQTAVAEEINRSVHQIAGAVDSVADEAQQGAQTARSLAQLGQGLGRLVGQFRI | Function: Chemotactic-signal transducers respond to changes in the concentration of attractants and repellents in the environment, transduce a signal from the outside to the inside of the cell, and facilitate sensory adaptation through the variation of the level of methylation (Probable). Directly recognizes five C4-dicarboxylic acids: L-malic, citramalic, citraconic, bromosuccinic and methylsuccinic acids . Three of the identified ligands act as chemoattractants (L-malic, D,L-bromosuccinic and L-citramalic acids) whereas two of them (L-methylsuccinic and citraconic acids) behave as antagonists by inhibiting the downstream chemotaxis signaling cascade . Antagonists compete with chemoattractants, thereby decreasing the affinity for chemoattractants and the subsequent chemotactic response . Acts through the che chemosensory pathway .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 60344
Sequence Length: 561
Subcellular Location: Cell inner membrane
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P9WPS2 | MRVCVTGFNVDAVRAVAIEETVSQVTGVHAVHAYPRTASVVIWYSPELGDTAAVLSAITKAQHVPAELVPARAPHSAGVRGVGVVRKITGGIRRMLSRPPGVDKPLKASRCGGRPRGPVRGSASWPGEQNRRERRTWLPRVWLALPLGLLALGSSMFFGAYPWAGWLAFAATLPVQFVAGWPILRGAVQQARALTSNMDTLIALGTLTAFVYSTYQLFAGGPLFFDTSALIIAFVVLGRHLEARATGKASEAISKLLELGAKEATLLVDGQELLVPVDQVQVGDLVRVRPGEKIPVDGEVTDGRAAVDESMLTGESVPVEKTAGDRVAGATVNLDGLLTVRATAVGADTALAQIVRLVEQAQGDKAPVQRLADRVSAVFVPAVIGVAVATFAGWTLIAANPVAGMTAAVAVLIIACPCALGLATPTAIMVGTGRGAELGILVKGGEVLEASKKIDTVVFDKTGTLTRARMRVTDVIAGQRRQPDQVLRLAAAVESGSEHPIGAAIVAAAHERGLAIPAANAFTAVAGHGVRAQVNGGPVVVGRRKLVDEQHLVLPDHLAAAAVEQEERGRTAVFVGQDGQVVGVLAVADTVKDDAADVVGRLHAMGLQVAMITGDNARTAAAIAKQVGIEKVLAEVLPQDKVAEVRRLQDQGRVVAMVGDGVNDAPALVQADLGIAIGTGTDVAIEASDITLMSGRLDGVVRAIELSRQTLRTIYQNLGWAFGYNTAAIPLAALGALNPVVAGAAMGFSSVSVVTNSLRLRRFGRDGRTA | Function: Necessary for copper homeostasis and likely functions as a copper exporter. Also required for full virulence (By similarity).
Catalytic Activity: ATP + Cu(+)(in) + H2O = ADP + Cu(+)(out) + H(+) + phosphate
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 80103
Sequence Length: 770
Subcellular Location: Cell membrane
EC: 7.2.2.8
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Q27289 | MLRKVFAVVSVLLVVSAAKVTKLVLDDNYVNRVVGGEVAKNGSAPYQVSLQVPGWGHNCGGSLLNDRWVLTAAHCLVGHAPGDLMVLVGTNSLKEGGELLKVDKLLYHSRYNLPRFHNDIGLVRLEQPVRFSELVQSVEYSEKAVPANATVRLTGWGHTSANGPSPTLLQSLNVVTLSNEDCNKKGGDPGYTDVGHLCTLTKTGEGACNGDSGGPLVYEGKLVGVVNFGVPCALGYPDGFARVSYYHDWVRTTMANNSK | Catalytic Activity: Preferential cleavage: Tyr-|-Xaa, Trp-|-Xaa, Phe-|-Xaa, Leu-|-Xaa.
Sequence Mass (Da): 27722
Sequence Length: 259
Subcellular Location: Secreted
EC: 3.4.21.1
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Q05609 | MEMPGRRSNYTLLSQFSDDQVSVSVTGAPPPHYDSLSSENRSNHNSGNTGKAKAERGGFDWDPSGGGGGDHRLNNQPNRVGNNMYASSLGLQRQSSGSSFGESSLSGDYYMPTLSAAANEIESVGFPQDDGFRLGFGGGGGDLRIQMAADSAGGSSSGKSWAQQTEESYQLQLALALRLSSEATCADDPNFLDPVPDESALRTSPSSAETVSHRFWVNGCLSYYDKVPDGFYMMNGLDPYIWTLCIDLHESGRIPSIESLRAVDSGVDSSLEAIIVDRRSDPAFKELHNRVHDISCSCITTKEVVDQLAKLICNRMGGPVIMGEDELVPMWKECIDGLKEIFKVVVPIGSLSVGLCRHRALLFKVLADIIDLPCRIAKGCKYCNRDDAASCLVRFGLDREYLVDLVGKPGHLWEPDSLLNGPSSISISSPLRFPRPKPVEPAVDFRLLAKQYFSDSQSLNLVFDPASDDMGFSMFHRQYDNPGGENDALAENGGGSLPPSANMPPQNMMRASNQIEAAPMNAPPISQPVPNRANRELGLDGDDMDIPWCDLNIKEKIGAGSFGTVHRAEWHGSDVAVKILMEQDFHAERVNEFLREVAIMKRLRHPNIVLFMGAVTQPPNLSIVTEYLSRGSLYRLLHKSGAREQLDERRRLSMAYDVAKGMNYLHNRNPPIVHRDLKSPNLLVDKKYTVKVCDFGLSRLKASTFLSSKSAAGTPEWMAPEVLRDEPSNEKSDVYSFGVILWELATLQQPWGNLNPAQVVAAVGFKCKRLEIPRNLNPQVAAIIEGCWTNEPWKRPSFATIMDLLRPLIKSAVPPPNRSDL | Function: Acts as a negative regulator in the ethylene response pathway . Phosphorylates the cytosolic C-terminal domain of EIN2, preventing the signaling in the absence of ethylene . Interacts with C24:1-ceramide upon hypoxic conditions (e.g. submergences) to in turn regulate EIN2 endoplasmic reticulum (ER)-to-nucleus translocation and EIN3 stabilization .
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 90306
Sequence Length: 821
EC: 2.7.11.1
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Q59NP1 | MEFLKRHEGHMHMSDSATSMVTSATSAVMDMASATMSMTMSSSTSSSSGMAMEGMDHGSSHMAMNMWLTASFKDYPVVFKDLRASTKAQAFGIFVLLFFVAFLARMLEFVRNYLEEIVWKNNNYAEVEQGISQHSANLQSPPVKSCCDDNAKEVVSDESIDKQNSPQHEETTKARGTGKSLSLASTISRDIIRLALCIIPDLFAYSLMLAAMTYTLTYFFAVVIGSGVGRFVAERLMEHYRIKRGPPRNCC | Function: Required for high affinity copper (probably reduced Cu I) transport into the cell.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 27859
Sequence Length: 251
Subcellular Location: Cell membrane
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J9VX37 | MDMSGMDGMDHMSSTSSNMSMSMKMYFHGTIGGDLLWFASWMPSSAGATVGVCIGLFILAIFERYLVAFRRACDAAWRRGQVGYVRPCSNGPLVFSSGKSTSLPPPVLFNRRSSTKKEKDVYNPLTPSDYALESNQDGSVEPVTPYTPSIHALRESQEGSSAPSYAHSQQGQAQAQGSGVGCDPCAEGRVAEIERCKEKAVERGLVHSHLPKAVRRSLDPGREGRWSRPFRLAVDVPRGLLQALQTLIHYLLMLVVMTFNIWWMISVVIGCGVGEMLFGRFGSSHVGH | Function: High affinity copper transporter involved in Cu(+) import into the cell upon copper-limitating conditions . Functions with BIM1 and probably also FRE4 and FRE7, where FRE4 and FRE7 metalloreductases liberate the Cu(2+) bound to the BIM1 copper-binding site for subsequent import of Cu(+) into the cell by CTR1, via the reduction of BIM1-bound Cu(2+) to Cu(+) to reduce binding affinity for BIM1 but increase affinity for CTR1 (Probable). The BIM1-CTR1 pathway for copper uptake plays a key role in colonization in the brain where copper amounts are low and thus in cryptococcal meningitis .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 31538
Sequence Length: 288
Subcellular Location: Cell membrane
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P30825 | MGCKVLLNIGQQMLRRKVVDCSREETRLSRCLNTFDLVALGVGSTLGAGVYVLAGAVARENAGPAIVISFLIAALASVLAGLCYGEFGARVPKTGSAYLYSYVTVGELWAFITGWNLILSYIIGTSSVARAWSATFDELIGRPIGEFSRTHMTLNAPGVLAENPDIFAVIIILILTGLLTLGVKESAMVNKIFTCINVLVLGFIMVSGFVKGSVKNWQLTEEDFGNTSGRLCLNNDTKEGKPGVGGFMPFGFSGVLSGAATCFYAFVGFDCIATTGEEVKNPQKAIPVGIVASLLICFIAYFGVSAALTLMMPYFCLDNNSPLPDAFKHVGWEGAKYAVAVGSLCALSASLLGSMFPMPRVIYAMAEDGLLFKFLANVNDRTKTPIIATLASGAVAAVMAFLFDLKDLVDLMSIGTLLAYSLVAACVLVLRYQPEQPNLVYQMASTSDELDPADQNELASTNDSQLGFLPEAEMFSLKTILSPKNMEPSKISGLIVNISTSLIAVLIITFCIVTVLGREALTKGALWAVFLLAGSALLCAVVTGVIWRQPESKTKLSFKVPFLPVLPILSIFVNVYLMMQLDQGTWVRFAVWMLIGFIIYFGYGLWHSEEASLDADQARTPDGNLDQCK | Function: High-affinity, low capacity permease involved in the transport of the cationic amino acids (arginine, lysine and ornithine) in non-hepatic tissues.
Catalytic Activity: L-arginine(in) = L-arginine(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 67638
Sequence Length: 629
Subcellular Location: Cell membrane
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P84310 | VIGGSDTTIGQYPHQLSLR | Catalytic Activity: Preferential cleavage: Tyr-|-Xaa, Trp-|-Xaa, Phe-|-Xaa, Leu-|-Xaa.
Sequence Mass (Da): 2042
Sequence Length: 19
Subcellular Location: Secreted
EC: 3.4.21.1
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Q7Q9I4 | MPVPCGSSCGRNAFMRRPKTGDTLCKECFFLAFETEIHNTIQQEQLFRPGEKVAIAASGGKDSTVLAHVMNLLNKRYNYGLDLVLLSIDEGITGYRDDSLKTVAQNRDDYGMPLRVLSYQELYGWTMDRIVAEIGRSNNCTFCGVFRRQALDRGARLMEVDCVATGHNADDIAETVIMNILRGDTARLRRCCDIKTGSKEADTIPRVKPLKYSYEKEIVMYAHFKKLVYFSTECVFAPNAYRGHARAFLKDLEKVRPSAIMDIIHAGEQLQIKGTVKKPVRGVCGRCGFVSSQQPCKACVLLEGLNRGLPKLGIGKKSKGERMVALQEQQLREKAHLVKNDF | Function: Plays a central role in 2-thiolation of mcm(5)S(2)U at tRNA wobble positions of tRNA(Lys), tRNA(Glu) and tRNA(Gln). Directly binds tRNAs and probably acts by catalyzing adenylation of tRNAs, an intermediate required for 2-thiolation. It is unclear whether it acts as a sulfurtransferase that transfers sulfur from thiocarboxylated URM1 onto the uridine of tRNAs at wobble position.
Sequence Mass (Da): 38355
Sequence Length: 342
Pathway: tRNA modification; 5-methoxycarbonylmethyl-2-thiouridine-tRNA biosynthesis.
Subcellular Location: Cytoplasm
EC: 2.7.7.-
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O64862 | MEAKNKKAVASRLCCLCNLRRPVLKRPKTLQQICRECFYEVFEEEIHQVIVQNRLFKSGERVAIGASGGKDSTVLAYVLSELNRRHNYGLDLFLLSIDEGITGYRDDSLETVKRNEVQYGLPLKIVSYKDLYGWTMDEIVKMIGLKNNCTFCGVFRRQALDRGAALLKVEKLVTGHNADDIAETVLLNILRGDIARLSRCTSITTGEDGPIPRCKPFKYTYEKEIVMYAYFKKLDYFSTECIYSPNAYRGFAREFIKDLERIRPRAILDIIKSGEDFRIATTTKMPEQGTCERCGYISSQKWCKACVLLEGLNRGLPKMGIGRPRGVNGDHNKETKKPGSVAKSIESKQCGSLDF | Function: Plays a central role in 2-thiolation of mcm(5)S(2)U at tRNA wobble positions of tRNA(Lys), tRNA(Glu) and tRNA(Gln). Directly binds tRNAs and probably acts by catalyzing adenylation of tRNAs, an intermediate required for 2-thiolation. It is unclear whether it acts as a sulfurtransferase that transfers sulfur from thiocarboxylated URM1 onto the uridine of tRNAs at wobble position.
Sequence Mass (Da): 40279
Sequence Length: 355
Pathway: tRNA modification; 5-methoxycarbonylmethyl-2-thiouridine-tRNA biosynthesis.
Subcellular Location: Cytoplasm
EC: 2.7.7.-
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Q0VC66 | MPAPQCASCHKARAALRRPRSGQALCGSCFCAAFEAEVLHTVVAGRLLPPGAVVAVGASGGKDSTVLAHVLRELAPRLGISLHLVAVDEGIGGYRDAALAAVRRQAARWELPLTVVAYADLFGGWTMDAVARSTAGSGRSRACCTFCGVLRRRALEEGARLVGATHVVTGHNADDMAETVLMNFLRGDAGRLARGGGLGSPGEGGALPRCRPLQLASQKEVVLYAHFRRLDYFSEECVYAPEAFRGHARDLLKMLEAARPSAVLDLVHSAERLALAPTARPPPPGACSRCGALASRALCQACALLDGLNRGRPRLAIGKGRRGLDEEGPPREPQPSRPLTSEPVPDF | Function: Plays a central role in 2-thiolation of mcm(5)S(2)U at tRNA wobble positions of tRNA(Lys), tRNA(Glu) and tRNA(Gln). Directly binds tRNAs and probably acts by catalyzing adenylation of tRNAs, an intermediate required for 2-thiolation. It is unclear whether it acts as a sulfurtransferase that transfers sulfur from thiocarboxylated URM1 onto the uridine of tRNAs at wobble position.
Sequence Mass (Da): 36599
Sequence Length: 347
Pathway: tRNA modification; 5-methoxycarbonylmethyl-2-thiouridine-tRNA biosynthesis.
Subcellular Location: Cytoplasm
EC: 2.7.7.-
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P0DQY6 | LFHYCQCQCPPGFKGKFCQFKLRPP | Function: Peptide with nanomolar affinity for human melanocortin receptors. The natural disulfide pairing being unknown, the activity of all three possible peptides (with the cysteine pairings 'bead (I-II, III-IV), 'globular' (I-III, II-IV), and 'ribbon' (I-IV, II-III)) have been tested. All three isomers show similar affinities on each human melanocortin subtype (MC1R (~500 nM), MC3R (~100 nM), MC4R (~50 nM), and MC5R (~50 nM)).
PTM: Contains 2 disulfide bonds (Probable). However, cysteine pairing is not critical for peptide binding to melanocortin receptors, since peptides with different pairings have similar potency at the receptors tested .
Sequence Mass (Da): 2974
Sequence Length: 25
Domain: The cysteine framework is XIV (C-C-C-C).
Subcellular Location: Secreted
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A5F2W6 | MNISQIAKLTSLTAKSIRLYEEKGLIIPPLRSESGYRTYTQQHVDDLLLIARCRRVGFSLDECKAMLTLANDPNRTSAAVRARAQEKWQEISRKLSELTMIKQQLEEWIASCPGDQGSDCPIIEQLKGHCCSNNKTKTP | Function: Regulates the transcription of the copA and cueO genes. It detects cytoplasmic copper stress and activates transcription in response to increasing copper concentrations (By similarity).
Sequence Mass (Da): 15693
Sequence Length: 139
Domain: It contains a N-terminal DNA binding region and a C-terminal metal binding region.
Subcellular Location: Cytoplasm
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Q8ZCA8 | MNISDVAKKTGLTSKAIRFYEEKKLVTPPVRTDNGYRSYTAKHIEELTLLRQARQVGFTLDECRELLALFHNPARHSADVKAATLLKVAEIEQHINDLNQMRMRLLALAEECPGDEGADCPIINSLAGCCHSSSSLPLK | Function: Regulates the transcription of the copA and cueO genes. It detects cytoplasmic copper stress and activates transcription in response to increasing copper concentrations (By similarity).
Sequence Mass (Da): 15463
Sequence Length: 139
Domain: It contains a N-terminal DNA binding region and a C-terminal metal binding region.
Subcellular Location: Cytoplasm
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Q16YE7 | MRNLGIAVTFAVLLVIGYVTALEWDAVVTTDSGILFFDKNWTQISSGGHQFHHISAFAYDEVKRKLYFSDLKDPSFRIFSLDTKPEEEYHKVAKLLPKSDQTGYITGLAFDHLERKLYWTEKGTHSVYSVEVDKLGAPANATDGLINLVAQVEENHDLAALTIDECRRHLYWTNSYLQTSSIVRAAMNGTVLDDHKEDVYEPRGISVDHYNNRIYWVEKKYGRAFTVESANLEVQDRQTFLRGEDKIPTHVSPNSQYLYWIDQEDGEVHETMKSDSKVTRVVYKGSRPSALIIRSGLLVEYQKNNPSCKAVVSEIIDNVRKESSEVKDVAQAVTSKPEMITCLNKGILNHNTNSCICLPEYQGTFCEIPICNNFCVHGECVVGADSRPMCKCHAEFEGERCDRNICDGYCLNNGRCALSATGQRSCTCSKNFSGARCETAICTSDYCYNGECFVENEVPECKCNVGYRGDRCEEYTCNNYCLHDGTCILNNDTMLVECRCGSEYTGKRCEIPKRFCSLDNGNPEMQQYCEGVAIAKNLVEPQVTYCKNSFNRTVVYVSLAFTASLVTLVTILCTVRRMYERNRPRITKRFKVTNNTQMTSRPATQCEITIENCCNMNVCETPCFDTKILQKSATKAEDKQFLLDDIESIAGSYRKLPSCVAEKN | Function: Has a role in spermatogenesis and oogenesis.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 75077
Sequence Length: 664
Subcellular Location: Cell membrane
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Q7QIQ6 | MKSPCRAAAGWLVLLLSSCCLGYVIATEWAAAVTTDNGILFFDSNWRKISSAAHQYSRISAFAYDEVLGKLYFADLDHPEYRLFALDYDDTDELHKVTKLLPKSAQTAYISGMAFDHLERRLYWTEKGTRSVYYVAIDELLSSTRSAAAAANGTAAAAATAVEATTSAPPPSSSSPVQLVATVQPDHELAGLAIDECRRHLYWTNCYPKTSNIVRAAMNGTVLNVHEEQVYLPKGITVDHYRNRLYWVEKKYGRRYTIESADLEVNDQRTLQTGLDRLPADIAVKNDYIYWTDQENNEIYEMSKEPNAPSRTVYRGEHPSAVILRANLLLEHQRNNPDCRSVVDRILENMQNSKPASVLQQETQQQGQLTVCLNNGTVNHHTNTCLCQPAFGGKLCEIDLCNNYCAQGSCRIGRDNRPRCDCDRRYEGDRCDRNRCDGFCLNGGRCQFSNGTAGRTEEEMGDRTCLCESTGYSGARCENPICGTDYCYNGECYVEEGKRPKCRCKAGYRGERCEEYSCNNYCLNGGHCTLGNETTVPECECGEEFAGQRCEIAVRLCSTYNEDPQWQQYCLGISKTLPLMEPKVTYCKESFNRTVVYTSLCFTVSFALLLAVVLVVSRMMKPPRPRITKKMVVTPMTSRPPTTQCEITIENCCNMNVCETPCFDTKLLKKSKKEDKQFLLEDIEDVGGSYRKLPNCGDGTAERK | Function: Has a role in spermatogenesis and oogenesis.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 79143
Sequence Length: 704
Subcellular Location: Cell membrane
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B4IXJ2 | MAYIDQKHNTFWDDFAIALRDKIVFLNSTWGEIHASAHRFEDLSALAFDEAEEMIYFSDQTHQNGSIFALRRDDSTPIVVQRTGNDSVEGLAYDPLNRNLFWADMRQQKIFFSSVDTLATELPKVLVDLSGEGGQPDGIAVDICRRQLYWTNGNIKSASVERIGLDGKGRQTIISADIDMPRGIVVDQLSDRIFWVDNKVGIFFAIESARLDGSDRQVVVKGKHQDPKHLAINEDAIYWTDRMDKAVWSYPKPTYSQEVTNVTQAEPELAKPFSKEKAYGIVTRTGFYQRLQKDAHCASIVKKVKQQLNTRLNNRTHIRSAEGDRISQLEREHCLNGASFMSRGEFCICPVGFKGARCEISECHNYCVHGTCEISDAGFPKCYCQAEFYGERCEYHKCNGHCLNSGHCSMDKESDAMRCECRPNFGGERCEHNLTEQCAIYCQHPETQLPVSCLDFCEEWSNSNDTATITEYQTAGQCGPAPPVQGPLIIVIVLGLVTTSGLVALTVHGVRLIYKPKRPRIKKTFVVRKQARLNSSSDTPLTNRPLTTEQCEITIENCCNMNICETPCFDPKLVEQTFSSRDRKAPCVKEDKKILIHSMEDNLLS | Function: Has a role in spermatogenesis and oogenesis.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 68309
Sequence Length: 605
Subcellular Location: Cell membrane
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Q95RU0 | MIRIRFGMDVLLVLLLATCLLTPAHGTPLEWDFAVTLRTKIQFMDSSWQTIATAAHEFDELSALTFDESEELIYFNDLKHRNGSIFSLKRDLIAANHVAEQTIARTGNESVGGLAYDPLNMNLFWSDTEQRKIFFAPIHGSATPQVLVDLSAEGGRPDGVAVDVCRRKLYWTNSNVTHPTVERINLDGSNRTVIISSNIDMPRGIVVDQLSDRLFWIDDLKGVFFSVESSKLDGSDRQVVLKDKHHEPLNLAVTNDAIYWTDRTTRAVWSHPKVPVIKVTTTSKPDEEDSTDSTDFKDPEPVAEDCPLVRVANLSEEARGIVARTGFYQRLQKDHHCASIVRKVKERVDEQSRKFEIRSLLDQKIKVLEDERCMNDGEYRAATDLCICPTGFKGSRCEIRECHNYCVHGTCQMSELAYPKCYCQPGFKGERCELSVCSGLCLNGGHCRVSKDENEAPSCECPAKFGGARCEQNSTEICSLFCRLLKHEPEMYVPFGCHSICEELAQDNSTNIAIPQYQHLEVCLTPRVWTSSVIIILVVGIVSSLLLVAVIVQGIRRLYKPKRPRIRKTFVVRKQARTNSAGDTPLTNRPLATEQCEITIENCCNMNICETPCFDPKLVEQTLSKSSCKEDKKILIHNMEDDLY | Function: Has a role in spermatogenesis and oogenesis . Might have a role in triglyceride homeostasis . Probably by regulating lipid storage and catabolism, plays a role in neuronal function .
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 72623
Sequence Length: 644
Subcellular Location: Cell membrane
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B4MLE8 | MILRLFILLSIITVYLQLSVGIQQQFEFAITLKSKILFVDEHWNVVNTAAHEFDELSALTFDESEERIYFNDGQHQNSSIFSLRKVGKSNHLAEQTIQRYGNESVGGIAYDPLNRTIYWSDLLQKKIFYASIDTVATEMPKILVDLSEENGTPYGVAIDICGRKLYWTNSNINHPTVERIDLNGTGRLAIIDKNIDSPRGIVVDQGAKRIFWIDDLKGIFFAVMSAQLDGSDVKLVLKDKNHEPQNLAVTRNAIYWTDRTTKSVWSHLKEPEIATTTTTTTTSTTQIPTVEGEEGTGAMDDNDIWPVGDFETTPKKSPLERKINLTEEARGIVARTGFYQLQKDSQCSKVIQLVKQRLDESQQNNRVLNVVDEQLDELQREHCLGGGTYYPQQKFCVCVPGYKGTRCETNECHNFCVHGTCQISEMGYPKCYCQPGYSGERCEVKKCLNFCQNGGDCQLDELTGEASCQCPSNFGGLRCEHNSTEICGLFCRLLKHDSNTSVPFGCHDICEQLAKDSSDLIAIPEYKHLDVCLAPNAWTGSVLMPLMISLILILLLLTIFIHGLRRLYKPKRPHIKKTFVVRKQARTNSSSDTPLTNRPLATEQCEITIENCCNMNICETPCFDPKLVEFAKSNCKDDKKILIHNMEDDLY | Function: Has a role in spermatogenesis and oogenesis.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 73571
Sequence Length: 651
Subcellular Location: Cell membrane
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Q2RSU5 | MSDSNDDRPFRPFQSQYRWPGVDLLAYKEEGSAPFRSVTRQVLFSGNGLTGELRYFEVGPGGHSTLERHQHAHGVMILKGRGHAMVGRAVSAVAPYDLVTIPGWSWHQFRAPADEALGFLCMVNAERDKPQLPTEADLAMLRADDAVAAFLDGLAG | Function: Catalyzes the formation of S-(methylsulfanyl)glutathione and 1-deoxy-D-xylulose 5-phosphate (DXP) from 1-methylthioxylulose 5-phosphate (MTXu-5P) . The S-(methylsulfanyl)glutathione is reductively cleaved to relase methanethiol in a second reaction. Involved in the MTA-isoprenoid shunt of the methionine salvage pathway .
Catalytic Activity: glutathione + S-methyl-1-thio-D-xylulose 5-phosphate = 1-deoxy-D-xylulose 5-phosphate + S-(methylsulfanyl)glutathione
Sequence Mass (Da): 17124
Sequence Length: 156
Pathway: Amino-acid biosynthesis; L-methionine biosynthesis via salvage pathway.
EC: 2.8.4.6
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P0DN32 | MVNMNILTTVALAGLAAAKTVEVVVAENGGLTFTPNQIKADVNDIVHFKLAKSGHDISSGPFDMPCKPSDNSLYSGKLNEGDEFSVNITNTDPIWLYCSVSKHCSKGMVAVINPPSSGNTIEAYKQAAAGAGNGQAPSRVNNGSSGSGTPTSGGAPAATSPNAASSLTFSGAAALVAMGGAWIGLL | Cofactor: Binds 1 copper ion per subunit.
Function: Probable electron transfer copper protein that serves as a direct electron donor (By similarity).
Location Topology: Lipid-anchor
Sequence Mass (Da): 18699
Sequence Length: 186
Subcellular Location: Cell membrane
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P76113 | MGQQKQRNRRWVLASRPHGAPVPENFRLEEDDVATPGEGQVLLRTVYLSLDPYMRGRMSDEPSYSPPVDIGGVMVGGTVSRVVESNHPDYQSGDWVLGYSGWQDYDISSGDDLVKLGDHPQNPSWSLGVLGMPGFTAYMGLLDIGQPKEGETLVVAAATGPVGATVGQIGKLKGCRVVGVAGGAEKCRHATEVLGFDVCLDHHADDFAEQLAKACPKGIDIYYENVGGKVFDAVLPLLNTSARIPVCGLVSSYNATELPPGPDRLPLLMATVLKKRIRLQGFIIAQDYGHRIHEFQREMGQWVKEDKIHYREEITDGLENAPQTFIGLLKGKNFGKVVIRVAGDD | Function: Catalyzes the metal-independent reduction of curcumin to dihydrocurcumin (DHC) as an intermediate product, followed by further reduction to tetrahydrocurcumin (THC) as an end product. It also acts on 3-octene-2-one, 3-hepten-2-one, resveratrol, and trans-2-octenal.
Catalytic Activity: 2 NADP(+) + tetrahydrocurcumin = curcumin + 2 H(+) + 2 NADPH
Sequence Mass (Da): 37610
Sequence Length: 345
EC: 1.3.1.n3
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Q30W70 | MDLQDFSHKLAEATKNLTPAERASLKKIFEGVSAEVFSQPAPVSAVATGAESGIPDGPTPRHVKLKENFLKQVPSITVQRAVAITKIAKENPGLPKPLLRAKTFRYCCETAPLVIQDHELIVGSPNGAPRAGAFSPEVAWRWLQDELDTIGSRPQDPFYISEEDKKVLREEVFPFWQNKSVDEFCEGQYREADLWEMSGESFVSDCSYHAVNGGGDSNPGYDVILMKKGMLDIQREAREKLEQLDYANPEDIDKIYFYKSVIETAEGVMIYARRLSAYAAELAARETDPRRKAELQKISEVNARVPAHAPSNFWEAIQAVWTVESLLVVEENQTGMSIGRVDQYMYPFYRADIDSGRLTEYEAFDLAGCMLVKMSEMMWITSEGASKFFAGYQPFVNMCVGGVTREGHDATNDLTYMLMDAVRHVRIYQPTLATRVHNKSPQKYLKKIVDVIRSGMGFPAVHFDDAHIKMMLAKGVSIEDARDYCLMGCVEPQKSGRLYQWTSTGYTQWPICIELVLNHGVPLWYGKKVTPDMGDLSQYDTYEKFEAAVKEQIRWITKNTSVATVISQRAHRELAPKPLMSLMYEGCMESGRDVSAGGAMYNFGPGVVWSGLATYVDSMAAIKKLVYDDRKYTLAQLNEALKADFAGYDQILADCLAAPKYGNDDDYADMIAADLVHFTETEHRKYKTLYSVLSHGTLSISNNTPFGQLLGASANGRRAWMPLSDGISPTQGADYKGPTAIIKSVSKMANDNMNIGMVHNFKLMSGLLDTPEGENGLITLIRTACMLGNGEMQFNYLDNELLLDAQKHPEKYRDLVVRVAGYSAFFVELCKDVQDEIISRTMLHGF | Function: Glycine radical enzyme that catalyzes the cleavage of a C-N bond in choline, producing trimethylamine (TMA) and acetaldehyde . Is involved in the anaerobic choline utilization pathway that allows D.alaskensis to grow on choline as a source of carbon and energy . Is strictly specific for choline as substrate .
PTM: Requires the activating protein CutD to generate the key active site glycyl radical on Gly-821 that is involved in catalysis.
Catalytic Activity: choline = acetaldehyde + trimethylamine
Sequence Mass (Da): 94640
Sequence Length: 846
Pathway: Amine and polyamine metabolism; choline degradation.
EC: 4.3.99.4
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B3FIA6 | MMPVILPLLLSLAIRGGDGQAIQGDRDLIAKLFKRYQEHGLSVKRACHTCDDGTECCDSRCSCPWNTCTCIPWGK | PTM: Contains 4 disulfide bonds.
Sequence Mass (Da): 8298
Sequence Length: 75
Domain: The cysteine framework is XV (C-C-CC-C-C-C-C).
Subcellular Location: Secreted
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B3FIA5 | MMPVILLLLLSLAIRCADGKAVQGDSDPSASLLTGDKNHDLPVKRDCTTCAGEECCGRCTCPWGDNCSCIEWGK | PTM: Contains four disulfide bonds.
Sequence Mass (Da): 7887
Sequence Length: 74
Domain: The cysteine framework is XV (C-C-CC-C-C-C-C).
Subcellular Location: Secreted
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P43497 | MQFSTVASVAFVALANFVAAESAAAISQITDGQIQATTTATTEATTTAAPSSTVETVSPSSTETISQQTENGAAKAAVGMGAGALAAAAMLL | Function: Component of the cell wall.
PTM: Extensively O-glycosylated.
Location Topology: Lipid-anchor
Sequence Mass (Da): 8911
Sequence Length: 92
Subcellular Location: Secreted
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P48165 | MGDWSFLGNILEEVNEHSTVIGRVWLTVLFIFRILILGTAAEFVWGDEQSDFVCNTQQPGCENVCYDEAFPISHIRLWVLQIIFVSTPSLMYVGHAVHYVRMEEKRKSREAEELGQQAGTNGGPDQGSVKKSSGSKGTKKFRLEGTLLRTYICHIIFKTLFEVGFIVGHYFLYGFRILPLYRCSRWPCPNVVDCFVSRPTEKTIFILFMLSVASVSLFLNVMELGHLGLKGIRSALKRPVEQPLGEIPEKSLHSIAVSSIQKAKGYQLLEEEKIVSHYFPLTEVGMVETSPLPAKPFNQFEEKISTGPLGDLSRGYQETLPSYAQVGAQEVEGEGPPAEEGAEPEVGEKKEEAERLTTEEQEKVAVPEGEKVETPGVDKEGEKEEPQSEKVSKQGLPAEKTPSLCPELTTDDARPLSRLSKASSRARSDDLTV | Function: Structural component of eye lens gap junctions . Gap junctions are dodecameric channels that connect the cytoplasm of adjoining cells. They are formed by the docking of two hexameric hemichannels, one from each cell membrane (By similarity). Small molecules and ions diffuse from one cell to a neighboring cell via the central pore .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 48229
Sequence Length: 433
Subcellular Location: Cell membrane
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P28236 | MGDWSFLGNILEEVNEHSTVIGRVWLTVLFIFRILILGTAAEFVWGDEQSDFVCNTQQPGCENVCYDEAFPISHIRLWVLQIIFVSTPSLMYVGHAVHHVRMEEKRKDREAEELCQQSRSNGGERVPIAPDQASIRKSSSSSKGTKKFRLEGTLLRTYVCHIIFKTLFEVGFIVGHYFLYGFRILPLYRCSRWPCPNVVDCFVSRPTEKTIFILFMLSVAFVSLFLNIMEMSHLGMKGIRSAFKRPVEQPLGEIAEKSLHSIAVSSIQKAKGYQLLEEEKIVSHYFPLTEVGMVETSPLSAKPFSQFEEKIGTGPLADMSRSYQETLPSYAQVGVQEVEREEPPIEEAVEPEVGEKKQEAEKVAPEGQETVAVPDRERVETPGVGKEDEKEELQAEKVTKQGLSAEKAPSLCPELTTDDNRPLSRLSKASSRARSDDLTI | Function: Structural component of eye lens gap junctions . Gap junctions are dodecameric channels that connect the cytoplasm of adjoining cells. They are formed by the docking of two hexameric hemichannels, one from each cell membrane (By similarity). Small molecules and ions diffuse from one cell to a neighboring cell via the central pore .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 49598
Sequence Length: 440
Subcellular Location: Cell membrane
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P55917 | MGDWSFLGNILEEVNEHSTVIGRVWLTVLFIFRILILGTAAEFVWGDEQSDFVCNTQQPGCENVCYDEAFPISHIRLWVLQIIFVSTPSLVYVGHAVHHVRMEEKRKEREAEELSQQSPGNGGERAPLAADQGSVKKSSSSSKGTKKFRLEGTLLRTYVCHIIFKTLFEVGFIVGHYFLYGFRILPLYRCSRWPCPNVVDCFVSRPTEKTIFILFMLSVASVSLFLNILEMSHLGLKKIRSAFKRPVEQPLGEIPEKSLHSIAVSSIQKAKGYQLLEEEKIVSHYFPLTEVGMVEASPLSAKPFSQFEEKVGPGPLGDLSRAYQETLPSYAQVGAQEGVEEEQPIEAAAEPEVGDKSQEAERVSTEGEETLAVLEEEKVEPPEVEKEAEKEETPPEKVSKQELTPEKAPSLCAELPGEDTRPLSRLSKASSRARSDDLTV | Function: Structural component of eye lens gap junctions. Gap junctions are dodecameric channels that connect the cytoplasm of adjoining cells. They are formed by the docking of two hexameric hemichannels, one from each cell membrane. Small molecules and ions diffuse from one cell to a neighboring cell via the central pore.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 49160
Sequence Length: 440
Subcellular Location: Cell membrane
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P57773 | MGDWNLLGDTLEEVHIHSTMIGKIWLTILFIFRMLVLGVAAEDVWNDEQSGFICNTEQPGCRNVCYDQAFPISLIRYWVLQVIFVSSPSLVYMGHALYRLRVLEEERQRMKAQLRVELEEVEFEMPRDRRRLEQELCQLEKRKLNKAPLRGTLLCTYVIHIFTRSVVEVGFMIGQYLLYGFHLEPLFKCHGHPCPNIIDCFVSRPTEKTIFLLFMQSIATISLFLNILEIFHLGFKKIKRGLWGKYKLKKEHNEFHANKAKQNVAKYQSTSANSLKRLPSAPDYNLLVEKQTHTAVYPSLNSSSVFQPNPDNHSVNDEKCILDEQETVLSNEISTLSTSCSHFQHISSNNNKDTHKIFGKELNGNQLMEKRETEGKDSKRNYYSRGHRSIPGVAIDGENNMRQSPQTVFSLPANCDWKPRWLRATWGSSTEHENRGSPPKGNLKGQFRKGTVRTLPPSQGDSQSLDIPNTADSLGGLSFEPGLVRTCNNPVCPPNHVVSLTNNLIGRRVPTDLQI | Function: One gap junction consists of a cluster of closely packed pairs of transmembrane channels, the connexons, through which materials of low MW diffuse from one cell to a neighboring cell.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 58842
Sequence Length: 515
Subcellular Location: Cell membrane
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Q8WMV3 | MELLLRFLLLCGVADFTRGLSITTPEQMIEKAKGETAYLPCKFTLGPEDQGPLDIEWLLSPADNQKVDQVIILYSGDKIYDDYYQDLKGRVHFTSNDLKSGDASINVTNLQLSDIGTYQCKVKKAPGVGNKKIQLTVLVKPSGIRCYVDGSEEIGNDFKLKCEPKEGSLPLRYEWQKLSDSQKLPTSWLPEMTSPVISVKNASAEYSGTYTCTVRNRVGSDQCLLRLDVVPPSNRAGTIAGAVIGTLLALVLIALIVFCCHKKRREEKYEKEVHHDIREDVPPPKSRTSTARSYIGSNHSSLGSMSPSNMEGYSKTQYNQVPSEDLERAPQSPTLPPAKVAAPNLSRMGAVPVMIPAQSKDGSIV | Function: Component of the epithelial apical junction complex that may function as a homophilic cell adhesion molecule and is essential for tight junction integrity. Also involved in transepithelial migration of leukocytes through adhesive interactions with JAML a transmembrane protein of the plasma membrane of leukocytes. The interaction between both receptors also mediates the activation of gamma-delta T-cells, a subpopulation of T-cells residing in epithelia and involved in tissue homeostasis and repair. Upon epithelial CXADR-binding, JAML induces downstream cell signaling events in gamma-delta T-cells through PI3-kinase and MAP kinases. It results in proliferation and production of cytokines and growth factors by T-cells that in turn stimulate epithelial tissues repair (By similarity).
PTM: N-glycosylated.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 40153
Sequence Length: 365
Domain: The Ig-like C2-type 1 domain mediates homodimerization and interaction with JAML.
Subcellular Location: Cell membrane
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P78310 | MALLLCFVLLCGVVDFARSLSITTPEEMIEKAKGETAYLPCKFTLSPEDQGPLDIEWLISPADNQKVDQVIILYSGDKIYDDYYPDLKGRVHFTSNDLKSGDASINVTNLQLSDIGTYQCKVKKAPGVANKKIHLVVLVKPSGARCYVDGSEEIGSDFKIKCEPKEGSLPLQYEWQKLSDSQKMPTSWLAEMTSSVISVKNASSEYSGTYSCTVRNRVGSDQCLLRLNVVPPSNKAGLIAGAIIGTLLALALIGLIIFCCRKKRREEKYEKEVHHDIREDVPPPKSRTSTARSYIGSNHSSLGSMSPSNMEGYSKTQYNQVPSEDFERTPQSPTLPPAKVAAPNLSRMGAIPVMIPAQSKDGSIV | Function: Component of the epithelial apical junction complex that may function as a homophilic cell adhesion molecule and is essential for tight junction integrity. Also involved in transepithelial migration of leukocytes through adhesive interactions with JAML a transmembrane protein of the plasma membrane of leukocytes. The interaction between both receptors also mediates the activation of gamma-delta T-cells, a subpopulation of T-cells residing in epithelia and involved in tissue homeostasis and repair. Upon epithelial CXADR-binding, JAML induces downstream cell signaling events in gamma-delta T-cells through PI3-kinase and MAP kinases. It results in proliferation and production of cytokines and growth factors by T-cells that in turn stimulate epithelial tissues repair.
PTM: N-glycosylated.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 40030
Sequence Length: 365
Domain: The Ig-like C2-type 1 domain mediates homodimerization and interaction with JAML.
Subcellular Location: Cell membrane
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Q8BSU2 | MRRGFGPLSLAFFLFLLALLTLPGDGNQGSVAGSCSCDRTISSGTQIPQGTLDHIRKYLKAFHRCPFFIRFQLQSKSVCGGSQDQWVRELVDCFERKECGTGHGKSFHHQKHLPQASTQTPEAAEGTPSDTSTPAHSQSTQHSTLPSGALSLNKEHTQPWEMTTLPSGYGLEARPEAEANEKQQDDRQQEAPGAGASTPAWVPVLSLLAIVFFLTAAMAYVLCNRRATQQNSAGLQLWYTPVEPRP | Function: Induces a strong chemotactic response. Induces calcium mobilization. Binds to CXCR6/Bonzo. Also acts as a scavenger receptor on macrophages, which specifically binds to OxLDL (oxidized low density lipoprotein), suggesting that it may be involved in pathophysiology such as atherogenesis.
PTM: Glycosylated.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 26896
Sequence Length: 246
Subcellular Location: Membrane
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Q9GKE2 | MPLWELWFFLLALFLAWLTPPGNGNEGSMAGSCPCNRRISSHSPPTDHDMRHLRKYLNHYQHCTSYVRFQLPRGSVCGGSSDQWVLKLMGCFDRGECGRAHARTVAHQQHLAPQNTRVPELPERAPPDSSTPAQTNLPSTLQPTQKPTLPEGMPSLAKKLIPTSETDTSTVGHSLGAKSEARENQEQLGKNVGATAGTSALVPVLSLLVIIFLLTGVLLYVMCKKRQEQSRQYPPDPQLHYVPVASNINT | Function: Induces a strong chemotactic response. Induces calcium mobilization. Binds to CXCR6/Bonzo. Also acts as a scavenger receptor on macrophages, which specifically binds to OxLDL (oxidized low density lipoprotein), suggesting that it may be involved in pathophysiology such as atherogenesis (By similarity).
PTM: Glycosylated.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 27570
Sequence Length: 250
Subcellular Location: Membrane
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Q6UXB2 | MKVLISSLLLLLPLMLMSMVSSSLNPGVARGHRDRGQASRRWLQEGGQECECKDWFLRAPRRKFMTVSGLPKKQCPCDHFKGNVKKTRHQRHHRKPNKHSRACQQFLKQCQLRSFALPL | Function: Chemokine that acts as chemoattractant for monocytes, macrophages and dendritic cells . Plays a role in angiogenesis and possibly in the development of tumors . Acts as an anti-inflammatory in the stomach . May play a role in the innate defense against infections . Activates the C-X-C chemokine receptor GPR35 to induce a rapid and transient rise in the level of intracellular calcium ions .
PTM: Likely to undergo an endoproteolytic process to form a four-cysteine-containing mature peptide with a canonical CXC chemokine scaffold after secretion.
Sequence Mass (Da): 13819
Sequence Length: 119
Subcellular Location: Secreted
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Q5UW37 | MKLLASPFLLLLPVMLMSMVFSSPNPGVARSHGDQHLAPRRWLLEGGQECECKDWFLQAPKRKATAVLGPPRKQCPCDHVKGREKKNRHQKHHRKSQRPSRACQQFLKRCHLASFALPL | Function: Chemokine that acts as chemoattractant for monocytes, macrophages and dendritic cells . Plays a role in angiogenesis and possibly in the development of tumors . Acts as an anti-inflammatory in the stomach. May play a role in the innate defense against infections. Activates the C-X-C chemokine receptor GPR35 to induce a rapid and transient rise in the level of intracellular calcium ions.
PTM: Likely to undergo an endoproteolytic process to form a four-cysteine-containing mature peptide with a canonical CXC chemokine scaffold after secretion.
Sequence Mass (Da): 13627
Sequence Length: 119
Subcellular Location: Secreted
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A0A125S9G2 | MKFFTCLLLLLVVLTVVFDNVDACDRSCTGVMGHPSCATCCACFTSAGKRHADGQHSRMKVRTGAKNLLKRMPLH | Function: Probable neurotoxin.
Sequence Mass (Da): 8214
Sequence Length: 75
Domain: The cysteine framework is XXIII (C-C-C-CC-C).
Subcellular Location: Secreted
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P0DM45 | CKCPSCNFNDVTENCKCCIFRQP | Function: Upon intracranial injection in mice, as25a (the toxin without the two 4-hydroxyprolines) provokes paralysis of the hind limbs and death with a dose of 240 pmol.
PTM: The name as25b given in PubMed:23474143 corresponds to the hydroxylated peptide . The amidation of the C-terminus of this hydroxylated peptide is not directly confirmed .
Sequence Mass (Da): 2653
Sequence Length: 23
Domain: The cysteine framework is XXV (C-C-C-C-CC).
Subcellular Location: Secreted
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P51199 | MLKRSSWLATLLGLLTVASVSTIVYAIELDEATRTVPLESSGRTVVLTPEQVKRGKRLFNNSCAICHNGGITKTNPNVGLDPESLGLATPQRDNIEALVDYMKDPTSYDGAESIAELHPSIKSAEIFPKMRNLTDEDLFTIAGHILLQPKIVSEKWGGGKIYY | Cofactor: Binds 1 heme c group covalently per subunit.
Function: Low-potential cytochrome c that plays a role in the oxygen-evolving complex of photosystem II.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 17844
Sequence Length: 163
Subcellular Location: Plastid
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Q9I2C5 | MNKNNVLRGLLVLAGLSLSSLALAHGDVTPQAVDTKGLEPLGKEWRDTNPYRKPYAKHDLAVEIGASAYNQNCARCHGLEAKSGGIAPDLRLLETGAEGDEWFKERVINGAVRDGAVYMPKMADFISQEGLWAIRSYLESVHVDE | Function: Is an essential component of the ethanol oxidation system that allows P.aeruginosa to grow on ethanol as the sole carbon and energy source. Is the direct electron acceptor of the quinoprotein ethanol dehydrogenase (QEDH).
PTM: Binds 1 heme group per subunit.
Sequence Mass (Da): 15850
Sequence Length: 145
Pathway: Alcohol metabolism; ethanol degradation; acetate from ethanol.
Subcellular Location: Periplasm
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Q2JTY6 | MFSKFFSLQKAFAAARRRLLILILVLGMAGYAWGPALAARQIPPVALSPTESITFTEAQLARGKQLFNRACAQCHVGGQTYPNPDVTLKLSDLEGATPPRDNVLAIVDYIKNPVTYDGVESLVEYHPNTQLLSEYPRLRNLTDEDLKLIAGYILVQAKTVPGWGGTKSESHSDLSAYL | Cofactor: Binds 1 heme c group covalently per subunit.
Function: Low-potential cytochrome c that plays a role in the oxygen-evolving complex of photosystem II.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 19535
Sequence Length: 178
Subcellular Location: Cellular thylakoid membrane
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Q55210 | MNKILGIDPLKKFIFGISAFVLLFWQLNVGAANATALREVDRTVNLNETETVVLSDQQVAKGERIFINTCSTCHNSGRTKSNPNVTLSLVDLEGAEPRRDNILAMVDYLKNPTSYDGELDLSQLHPNTVRADIWSSMRNLNEEDLQNVSGYVLVQAQVRGVAWGGGKTVN | Cofactor: Binds 1 heme c group covalently per subunit.
Function: Low-potential cytochrome c that plays a role in the oxygen-evolving complex of photosystem II.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 18777
Sequence Length: 170
Subcellular Location: Cellular thylakoid membrane
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Q3AZH8 | MVSVFSSLRQSFKGLLVLVPVLIGLAFISPAEAVQWDAETLTVPVNPDGAEVTFTDREINAGRKVFNTSCGTCHAGGITKTNQNVGLDPETLALATPARDNVDALVDYMKDPTSYDGEYSISDVHPSMRSAELYPAMRDLDDEDLRLMAGYILVSPKVQGSSWGGGKIYF | Cofactor: Binds 1 heme c group covalently per subunit.
Function: Low-potential cytochrome c that plays a role in the oxygen-evolving complex of photosystem II.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 18378
Sequence Length: 170
Subcellular Location: Cellular thylakoid membrane
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Q55013 | MKRFFLVAIASVLFFFNTMVGSANAVELTESTRTIPLDEAGGTTTLTARQFTNGQKIFVDTCTQCHLQGKTKTNNNVSLGLADLAGAEPRRDNVLALVEFLKNPKSYDGEDDYSELHPNISRPDIYPEMRNYTEDDIFDVAGYTLIAPKLDERWGGTIYF | Cofactor: Binds 1 heme c group covalently per subunit.
Function: Low-potential cytochrome c that plays a role in the oxygen-evolving complex of photosystem II (PSII). Required for normal function or stabilization of PSII. Extrinsic protein associated with PSII that enhances oxygen evolution.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 17884
Sequence Length: 160
Subcellular Location: Cellular thylakoid membrane
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A0T0N2 | MFKTYSKSFACILFCIFNIFVVSASAIDLDEATRTVVTDSSGNTTVLTPEQVKRGKRLFNATCGACHTGGITKTNPNVGLDPEALSLATPRRDNISALVDYLKNPTTYDGLESIAEIHPSIKSADIYPRMRSLTDEDLYSIAGHIMLQPKIVAEKWGGGKIYF | Cofactor: Binds 1 heme c group covalently per subunit.
Function: Low-potential cytochrome c that plays a role in the oxygen-evolving complex of photosystem II.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 17840
Sequence Length: 163
Subcellular Location: Plastid
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P0A386 | MLKKCVWLAVALCLCLWQFTMGTALAAELTPEVLTVPLNSEGKTITLTEKQYLEGKRLFQYACASCHVGGITKTNPSLDLRTETLALATPPRDNIEGLVDYMKNPTTYDGEQEIAEVHPSLRSADIFPKMRNLTEKDLVAIAGHILVEPKILGDKWGGGKVYY | Cofactor: Binds 1 heme c group covalently per subunit. PSII binds multiple chlorophylls, carotenoids and specific lipids.
Function: Low-potential cytochrome c that plays a role in the oxygen-evolving complex of photosystem II. It is not essential for growth under normal conditions but is required under low CO(2) concentrations. PSII is a light-driven water plastoquinone oxidoreductase, using light energy to abstract electrons from H(2)O, generating a proton gradient subsequently used for ATP formation.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 18027
Sequence Length: 163
Subcellular Location: Cellular thylakoid membrane
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B0TBL5 | MNWLEERMPGIGRIAKDIAEHPVPSHTLNIFYCLGGLTLLCFIIQCLTGVFLAFYYKPTPEAAFASVQMITNEVRFGSVIRSMHHWSCQLMILLVFLHMLRVYYTGAFKKPRELNWVAGCFLLVLSLGLAFTGYLLPYEQLSYWASVIGAETANTLPVIGPTLKIMMQGGIKVTAEMLSRFYVLHVMILPAITIGFLVAHFIMIRVQGISDPM | Cofactor: Binds 2 heme b groups non-covalently with two histidine residues as axial ligands.
Function: Component of the cytochrome bc complex which donates electrons to the photosynthetic reaction center.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 23981
Sequence Length: 213
Subcellular Location: Cell membrane
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P92845 | YINYKNMSHQHMLTLFNLLPVGSNISIWWNFGSMLLTCLMIQIATGFFLAIHYTANINLAFSSIIHISRDVPYGWIMQNTHAIGASLFFICIYIHIARGIYYGSYLNKEVWLSGTTLLIILMATAFFGYVLPWGQMSFWAATVITNLLTAIPYLGTTLTTWLWGGYAINDPTLTRFFALHFILPFAIISMSSIHILLLHNEGSNNPLGTNSDID | Cofactor: Binds 2 heme b groups non-covalently.
Function: Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex) that is part of the mitochondrial respiratory chain. The b-c1 complex mediates electron transfer from ubiquinol to cytochrome c. Contributes to the generation of a proton gradient across the mitochondrial membrane that is then used for ATP synthesis.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 24168
Sequence Length: 214
Subcellular Location: Mitochondrion inner membrane
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P87421 | SINYXNMSNHHMLSTFNLLPVGSNISTWWNFGSMLMTCLALQTITGFFLAIHYTANINLAFSSIMHITRDIPYGWIMQNLHAIGASMFFVCIYIHIARGIYYGSYLNKEVWLSGVILLTALMATAFFGYVLPWGQMSFWAATVITNLLTAIPYLGTMLTTWLWGGFSINDPTLTRFFALHFVLPFIIISMSSIHIILLHNEGSSNPLGTNSDID | Cofactor: Binds 2 heme b groups non-covalently.
Function: Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex) that is part of the mitochondrial respiratory chain. The b-c1 complex mediates electron transfer from ubiquinol to cytochrome c. Contributes to the generation of a proton gradient across the mitochondrial membrane that is then used for ATP synthesis.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 24060
Sequence Length: 214
Subcellular Location: Mitochondrion inner membrane
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P23662 | MRMHNKIQLLSVLNTHLVAYPTPMNLNYSWNGGSLAGMMLASQMLTGILLAMHYVGHVDYAFASVQHLMTDVPSGMILRYAHANGASLFFIVVYLHVLRGMYYGSGAQPREIVWISGVVILLVMIITAFIGYVLPWGQMSFWGATVITSLATAIPVVGKHIMYWLWGGFSVDNPTLNRFYSFHYTLPFILAGLSVFHIAALHQYGSTNPLGVNSQSSLISFGSYFGAKDLVGALFLALVFSILVFFYPDLLGHPDNLIPANPYSTPQHIVPEWYFLWVYAILRSIPNKAMGVLAIGLVFASLFAMPFIGLGGGKFRIITEWLYWTFLADVLLLTWLGGNEITPITSFVGQCCTAYLFFYLLVCQPLVGYLETQFAHGTQTN | Cofactor: Binds 2 heme b groups non-covalently.
Function: Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex) that is part of the mitochondrial respiratory chain. The b-c1 complex mediates electron transfer from ubiquinol to cytochrome c. Contributes to the generation of a proton gradient across the mitochondrial membrane that is then used for ATP synthesis.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 42331
Sequence Length: 381
Subcellular Location: Mitochondrion inner membrane
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P48875 | MRFIKRPLISIVNDHLIDYPTPINIHYAWNFGFLSSICLIVQILTGIFLAMHYTPHVDLAFASVEHIMRDVNYGWLLRYIHTNGASMFFIVVYIHIFRGLYFGSYIKPRHWVWVIGVLILLLMILTAFIGYVLPWGQMSLWGATVITNLVSAVPFIGDSIVTWLWGGFSVDNATLNRFFSLHYLMPFVIAAVSLVHLAILHQDGSGNPLGIDSNVDKVSMFPYFIVKDFLGMVIFIIFFSIFVYFSPNVLGHPDNYIEANPMVTPAHIVPEWYFLPFYAILRSIPHKLGGVTAMISAIAILAFLPWIHSTEIRSSRFRPLYRLFYWVMISCCLILGWIGGMPVENPYVIIGQIASIYYFIYFIILLPVLGRIEKFLLEFKI | Cofactor: Binds 2 heme b groups non-covalently.
Function: Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex) that is part of the mitochondrial respiratory chain. The b-c1 complex mediates electron transfer from ubiquinol to cytochrome c. Contributes to the generation of a proton gradient across the mitochondrial membrane that is then used for ATP synthesis.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 43765
Sequence Length: 381
Subcellular Location: Mitochondrion inner membrane
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P00161 | MRILKSHPLLKIVNSYIIDSPQPANLSYLWNFGSLLALCLGIQIVTGVTLAMHYTPSVSEAFNSVEHIMRDVNNGWLVRYLHSNTASAFFFLVYLHIGRGLYYGSYKTPRTLTWAIGTVILIVMMATAFLGYVLPYGQMSLWGATVITNLMSAIPWIGQDIVEFIWGGFSVNNATLNRFFALHFLLPFVLAALALMHLIAMHDTVGSGNPLGISANYDRLPFAPYFIFKDLITIFIFFIVLSIFVFFMPNALGDSENYVMANPMQTPPAIVPEWYLLPFYAILRSIPNKLLGVIAMFAAILALMVMPITDLSKLRGVQFRPLSKVVFYIFVANFLILMQIGAKHVETPFIEFGQISTIIYFAYFFVIVPVVSLIENTLVELGTKKNF | Cofactor: Binds 2 heme b groups non-covalently.
Function: Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex) that is part of the mitochondrial respiratory chain. The b-c1 complex mediates electron transfer from ubiquinol to cytochrome c. Contributes to the generation of a proton gradient across the mitochondrial membrane that is then used for ATP synthesis.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 43522
Sequence Length: 387
Subcellular Location: Mitochondrion inner membrane
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Q5DNB7 | MFFNIFKSSIKGFLLNLPTPINLNYWYGFGSMLGLIYSIQIISGLILSWFYFIDLSGGFKSLILIMQDVWGGWFIRFIHSSGVSLFMFIMYLHILRGLIYGSFCKVDVWYSGILLLFICMGSAFLGYVLPWGSMSYWGMTVVTNMLSAIPMVGVYLVETIWGGSSAGVSTLVRFFSFHYLLSLFIMVFILIHLILLHECGSSNPLGVYYSCEKFTFHPLFSLKDTLVFVLVVFLYWFCIFVCPYLLLDAINFEEINFMMTPSHIKPEWYFLFIYCILRSTPSKLGGVILMVMAILMLVFLGIGKNLGSVLMVKTLYWKLMLSSFLLVFIILTIMGGYTVEYPYDILGNVNSVLYFFIYVIMLLYSFMFNFVY | Cofactor: Binds 2 heme b groups non-covalently.
Function: Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex) that is part of the mitochondrial respiratory chain. The b-c1 complex mediates electron transfer from ubiquinol to cytochrome c. Contributes to the generation of a proton gradient across the mitochondrial membrane that is then used for ATP synthesis.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 42894
Sequence Length: 372
Subcellular Location: Mitochondrion inner membrane
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O20672 | MVSRTLSLSMSLFRAHLVFYRCALNLNSSYNFGFLVAMTFVLQIITGITLAFRYTSEASCAFASVQHLVREVAAGWEFRMLHATTASFVFLCILIHMTRGLYNWSYSYLTTAWMSGLVLYLLTIATAFLGYVLPWGQMSFWGATVITNLLSPIPYLVPWLLGGYYVSDVTLKRFFVLHFILPFIGCIIIVLHIFYLHLNGSSNPAGIDTALKVAFYPHMLMTDAKCLSYLIGLIFLQAAFGLMELSHPDNSIPVNRFVTPLHIVPEWYFLAYYAVLKVIPSKTGGLLVFMSSLINLGLLSEIRALNTRMLIRQQFMTRNVVSGWVIIWVYSMIFLIIIGSAIPQATYILYGRLATILYLTTGLVLCLY | Cofactor: Binds 2 heme b groups non-covalently.
Function: Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex) that is part of the mitochondrial respiratory chain. The b-c1 complex mediates electron transfer from ubiquinol to cytochrome c. Contributes to the generation of a proton gradient across the mitochondrial membrane that is then used for ATP synthesis.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 41595
Sequence Length: 368
Subcellular Location: Mitochondrion inner membrane
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P84029 | MGVPAGDVEKGKKLFVQRCAQCHTVEAGGKHKVGPNLHGLIGRKTGQAAGFAYTDANKAKGITWNEDTLFEYLENPKKYIPGTKMIFAGLKKPNERGDLIAYLKSATK | Function: Electron carrier protein. The oxidized form of the cytochrome c heme group can accept an electron from the heme group of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c then transfers this electron to the cytochrome oxidase complex, the final protein carrier in the mitochondrial electron-transport chain.
PTM: Binds 1 heme c group covalently per subunit.
Sequence Mass (Da): 11735
Sequence Length: 108
Subcellular Location: Mitochondrion intermembrane space
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Q9AJE3 | MPDAIEFEHEGRRNPNSAEAESAYSSIIAALDLQESDYAVISGHSRIVGAAALVYPDADAETLLAASLWTACLIVNDDRWDYVQEDGGRLAPGEWFDGVTEVVDTWRTAGPRLPDPFFELVRTTMSRLDAALGAEAADEIGHEIKRAITAMKWEGVWNEYTKKTSLATYLSFRRGYCTMDVQVVLDKWINGGRSFAALRDDPVRRAIDDVVVRFGCLSNDYYSWGREKKAVDKSNAVRILMDHAGYDESTALAHVRDDCVQAITDLDCIEESIKRSGHLGSHAQELLDYLACHRPLIYAAATWPTETNRYR | Function: Involved in the production of the isoprenoid antibiotic terpentecin. Converts terpentedienol diphosphate (TDP) into terpentetriene (TTE). Can also accept geranylgeranyl diphosphate (GGDP) and farnesyl diphosphate (FDP) as substrates.
Catalytic Activity: terpentedienyl diphosphate = diphosphate + terpentetriene
Sequence Mass (Da): 34773
Sequence Length: 311
Pathway: Antibiotic biosynthesis.
EC: 4.2.3.36
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P00015 | MGDAEAGKKIFVQKCAQCHTVEKGGKHKTGPNLWGLFGRKTGQAPGFSYTDANKNKGVIWSEETLMEYLENPKKYIPGTKMIFAGIKKKSEREDLIKYLKQATSS | Function: Electron carrier protein. The oxidized form of the cytochrome c heme group can accept an electron from the heme group of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c then transfers this electron to the cytochrome oxidase complex, the final protein carrier in the mitochondrial electron-transport chain.
PTM: Binds 1 heme c group covalently per subunit.
Sequence Mass (Da): 11714
Sequence Length: 105
Subcellular Location: Mitochondrion intermembrane space
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P86320 | VDVSGDAAAGEKAFRQCITCHVVVDDSGETLAGRNAKVGPNLYKVPGRHAGQIEGFRYSDSMSQAGQNGLVWVEEEFVKYVQDPTGYLREYLGDSKARGAMTHKVRKEDEAVDIYAYLASLGVHEE | Function: Cytochrome c2 is found mainly in purple, non-sulfur, photosynthetic bacteria where it functions as the electron donor to the oxidized bacteriochlorophyll in the photophosphorylation pathway. However, it may also have a role in the respiratory chain and is found in some non-photosynthetic bacteria.
PTM: Binds 1 heme c group covalently per subunit.
Sequence Mass (Da): 13782
Sequence Length: 126
Subcellular Location: Periplasm
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Subsets and Splits