ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
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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... |
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 t... |
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 t... |
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 t... |
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 ph... |
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 ... |
Q92905 | MAASGSGMAQKTWELANNMQEAQSIDEIYKYDKKQQQEILAAKPWTKDHHYFKYCKISALALLKMVMHARSGGNLEVMGLMLGKVDGETMIIMDSFALPVEGTETRVNAQAAAYEYMAAYIENAKQVGRLENAIGWYHSHPGYGCWLSGIDVSTQMLNQQFQEPFVAVVIDPTRTISAGKVNLGAFRTYPKGYKPPDEGPSEYQTIPLNKIEDFGVHCKQYYALEVSYFKSSLDRKLLELLWNKYWVNTLSSSSLLTNADYTTGQVFDLSEKLEQSEAQLGRGSFMLGLETHDRKSEDKLAKATRDSCKTTIEAIHGLMS... | 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, l... |
Q6CRJ8 | MSSIKFHEKSLKEVTRWIQANEDINTETSLSSSSDSSTTIPVIDHLPARIPYATDLKRNPCHFQKCLISRLATTKMLSHAVDGGDIEVMGMLVGYTSNDMIVVKDCYSLPVQGTETRVNAHMESYEYMVQYLDAFVTKEDKIVGWYHSHPGYGCWLSNIDIQTQSLNQNYQDPYLAIVVDPKKSLSGNTLDIGAFRTLPSKDNNEHVDYYPLNIQLYQNSLDVNISKLKLKFKVDPAIQNNPNEPELMKELHECVENWFHAKKVMKSTVGFNAIGSTVVNETEIGNEDFTHERSNSISSTSSLTTRHTTDVEMDDQESAQ... | 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.... |
O35864 | MAASGSGMAQKTWELANNMQEAQSIDEIYKYDKKQQQEILAAKPWTKDHHYFKYCKISALALLKMVMHARSGGNLEVMGLMLGKVDGETMIIMDSFALPVEGTETRVNAQAAAYEYMAAYIENAKQVGRLENAIGWYHSHPGYGCWLSGIDVSTQMLNQQFQEPFVAVVIDPTRTISAGKVNLGAFRTYPKGYKPPDEGPSEYQTIPLNKIEDFGVHCKQYYALEVSYFKSSLDRKLLELLWNKYWVNTLSSSSLLTNADYTTGQVFDLSEKLEQSEAQLGRGSFMLGLETHDRKSEDKLAKATRDSCKTTIEAIHGLMS... | 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, l... |
Q7RXX8 | MELPPNPGLVDVQRDALYAYDSEAHKAVVNSRPWTNDHKYFKTVRISSVAMIKMVMHARSGGNLEVMGMMQGYIEGSTMVITDAYRLPVEGTETRVNAQDEANEYMVEYLRLCREENRLENVIGWYHSHPGYGCWLSGIDVGTQSLQQQFNEPFVAVVIDPDRTVSQNKVEIGAFRTIPEGIKPFAATNTTTGDGQSVPLNKVEDFGAHSHRYYALDVEHFKSTLDSKLLETLWNKYWVQTLAQNPLLTNRDYTSSQMVDLGSRISKASKSLEMLSTTGQRGPKSDAVDQNIEKLLSEVKQIAAKERSGLMAAEVKGKVF... | 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 ... |
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 essent... |
Q4P804 | MTAPSSSSSASMARANFELNNAIIPLSSTTLDSIFAYDNEAQRAILHAQPWKTDPHFFQKVRISAVALIKMVMHARSGGIYEIMGLMQGKIDVENRTLYVMDSFALPVEGTETRVNAQNEAYEYMVQYLDHSKEVGRLENVVGWYHSHPGYGCWLSGIDVNTQRTNQQFQDPFVAIVIDPNRTISSGKVDIGAFRTFPEGYTSSSSIGGGDSEYQSIPLSKIEDFGVHANEYYPLEVEHFKSSLDGKLLDLLWNKYWQNTLSQSPLVSNRAYTTSQIRDLADKLAQTNAAVLNRNSVSSAPFTTTAGAASVRIGAGKDVA... | 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 essent... |
Q6C703 | MASLATFQVENDIVDVDSTPQQGFDRDDLYKYDDVEQKAILAAHPWRTDPSYFRNVLVSSIALVKMAMHARSGGAIEVMGMMTGKILPNTFVVMDCYPLPVEGTETRVNAQQEGIEFMVEYLQGLKDVGRRENIVGWYHSHPGYGCWLSGIDVDTQFQNQQFQEPFLAVVVDPNRTISAGKVEIGAFRTYPKDYKPPKKATKQNQDQSVPLSKAKDYGAHSERYYELDVSFFKSSLDENLLQLLWNKNWAATLSQSTIQLNHDYTSKLMLDLSEKNAQLAIGLGEKTPQSQGRGFREAMSKADNEPHTNLLNYSTKGQWE... | 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 essent... |
Q12468 | MSLSNKTVKELRQLLKERYTVEDELTESIALSSMRFKPSQEPEFHALSQSSLLKTKLKQQSSTDIPSYTHVLISKLSCEKITHYAVRGGNIEIMGILMGFTLKDNIVVMDCFNLPVVGTETRVNAQLESYEYMVQYIDEMYNHNDGGDGRDYKGAKLNVVGWFHSHPGYDCWLSNIDIQTQDLNQRFQDPYVAIVVDPLKSLEDKILRMGAFRTIESKSDDNSATSYYELETIIFDSELNRALFETKLNLHCVIEDDESEQISLNRLIDSMKQYSYLMDSKNVRTRIKLATTSERVSNENKKNIDYQNRSTRSQFCLNTQ... | 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 phe... |
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. Specifical... |
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
Sequen... |
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 | MTFHKTFGYGCIVLICFELLFAGVETSSENDDEYLTQKEIILEKSYHGLIRENETLVEITPLIKVNEEKICNFHILKKPYHEIPFKIELVNNLGILKARRTLNCENRKSYHFEICAIYCDGTPSNTANVHITVIDVNEYAPTFLEPSYVIEVDEGRLYNEILRVEASDKDCTPLFGDVCKYEILNNDEPFSIDNEGSIKNTEPLSHKASHNHILSVVAYDCAMKESAPIMVSIKVRRVCETKFVGMPERIDYTSGSTESLQLFPNARLDLCDISCKNEEDLRIHSSIALKTKHISFGCDRDISNCTSGQKVKDLLPHGAE... | 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 ... |
Q9EPL2 | MLRRPAPALAPAVRLLLAGLLCGGGVWAARVNKHKPWLEPTYHGIVTENDNTVLLDPPLIALDKDSPLRFAESFEVTVTKEGEICGFKIHGQNVPFDAVVVDKSTGEGIIRSKEKLDCELQKDYTFTIQAYDCGKGPDGTGVKKSHKATVHIQVNDVNEYAPVFKEKSYKAAVVEGKQHSSILRVEAVDADCSPQFSQICSYEILTPDVPFTVDKDGYIKNTEKLNYGKEHQYKLTVTAYDCGKKRATEDVLVKISVKPTCSPGWQGWSSRIEYEPGTGALAVFPSIHLETCDEPVASVQATVELETSHIGKGCDRDTYS... | 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). Al... |
Q9H4D0 | MLPGRLCWVPLLLALGVGSGSGGGGDSRQRRLLAAKVNKHKPWIETSYHGVITENNDTVILDPPLVALDKDAPVPFAGEICAFKIHGQELPFEAVVLNKTSGEGRLRAKSPIDCELQKEYTFIIQAYDCGAGPHETAWKKSHKAVVHIQVKDVNEFAPTFKEPAYKAVVTEGKIYDSILQVEAIDEDCSPQYSQICNYEIVTTDVPFAIDRNGNIRNTEKLSYDKQHQYEILVTAYDCGQKPAAQDTLVQVDVKPVCKPGWQDWTKRIEYQPGSGSMPLFPSIHLETCDGAVSSLQIVTELQTNYIGKGCDRETYSEKSL... | 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 presynapti... |
Q9ER65 | MLPGRLCLVPLLLALGVGSGGGSGDGGDSRRRRLLVAKVNKHKPWIETSYHGVITENNDTVILDPPLVALDKDAPVPFAGEICAFKIHGQELPFEAVVLNKTSGEGRLRAKSPIDCELQKEYTFIIQAYDCGAGPREAAWKKSHKAVVHIQVKDVNEFAPTFKEPAYKAIVTEGKIYDSILQVEAIDEDCSPQYSQICNYEIVTTDVPFAIDRNGNIRNTEKLSYDKQHQYEILVTAYDCGQKPAAQDTLVQVDVKPVCKPGWQDWTKRIEYQPGSGSMPLFPSIHLETCDGAVSSLQVTAELQTNYIGKGCDRETYSEK... | 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 ... |
A0A8M9PFP2 | MARMSFLSFLLFCLTSVAHGNKANKHKPWIETEYQGIVMENDNTVLLNPPLFALDKDAPLHYAGEICGFRVHNGPGGSGSAQFEAVVLDRSTGEGLVRSKEPLDCESQKEHSFTIQAYDCGEGPDGTNSKKSHKATVHVRVNDVNEFSPVFVERRYEASVPEGRLFDRIVRVEAVDADCSPQYSQICFYDIITPNVPFTIDNDGNIKNTEPLDSKRQRVHSFWVTAFDCGKNRAQADAQVIVTVKPSCKPGWIGWTKRIEYTPGSGSIPLFPNLHLETCEETVWNIQATVELQTSHIGKGCDRDSYSDRSVRRLCGAVRG... | 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 cytoplas... |
A5VF68 | MSILARPAAPSPRPNALANWLLLVAVLVFAIVVVGGITRLTESGLSITEWKPVRGIVPPLNQAEWLAEFENYKRIPQYAAFNLHMTLEGFKAIYFWEYMHRLLARGIGAVLAGVMIVAWWKRAIPAGYGWRMIGIFALGGLQGAIGWWMVYSGLSVRTEVSHIRLATHLIAALLIFSALVWTVLDLRRLARDPDARPARPTALAIAAVLILAVQIMLGAFVAGLRAGYAFATWPKMGDEWFPAGGWNVAQGLANLHENPIVVQFVHRWWAWAAAIAALAVARAARKRGAVGPVHAVATLIVVQIALGIATLLTGVDIAVA... | 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... |
B6IUZ7 | MTSLSLSPAAGPQRSAAAPKAVAVWLLVCAGMVFAMAIIGAITRLTESGLSITEWKPVTGALPPLSEAQWLAEFEKYRQIPEYQLLKRGMSLEEFKGIYFWEWLHRLWGRLIGVVFLLPFVWFWVRGQVSRALAPTLAGLFLLGGLQGFIGWFMVQSGLTERTDVSHYRLALHLGMAFLIYAALLKVALGLLDPAPAPQPAAGRLRPHAWAALALLGVTIVWGAFVAGINAGFAYNTWPLMGGTLAPAEMWTQTPVWLNLLENTAAVQFVHRWLAVVTALVVLSLCWQAWRTGGGTRLRGVAAGLAAATVAQVGLGIATL... | 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... |
A8F119 | MQKSLITKWLCISCIMVIATIVIGGITRLTGSGLSIVEWRPVTGILPPFSFESWQAEFAKYKAFPEYNSVNYGITLSQFKFIYLLEFIHRLLGRITALIYIVPLIYFYFKDVIKNRDMLPYIIALWLFCVQGFMGWYMVKSGLLNSPYVSHCRLAFHLIIAVIIYHILFYQLIKNRCDILLIPSQTDLKLPLIFSGIAITVVYVQIFLGALVAGLDAGLIYNSFPLMDYSFIPMEIKDNFFDLKNWYDPVFIQFIHRLGGYSVFLVVVVLIICLLKIEHPKLNKIAYFLMIALLMQVSTGIITLLYSVPIIIASIHQLFA... | 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... |
F6SNN2 | MNISASTCGSPSSSESLPAGDLFKELWSKLKECHDKELQELLLKINKLKKQRCLDAQRLEEFYTKNQHLREQQKTLHDTIKVLEDRLRAGLCDRCTVTEEHMRKKQQEFENIRQQNLKLITELMNDKNALQDENKRLSEQLHNMQKSRWKSDEENPADTGEGEDGVIPDSPLSTFSLSMVSRMRRKKDNKHIRYSEKAPEDTLTLERKITCIPSQGSAEKNASHSSHRRKGEDILVAETLELSPLPNGKSKRKKVYLCSKTSIAFASILLVLLHLFAEQLHSWMNNLSQVSKSLRWCLPLKGNNKQGYIEYLFRFTEGSM... | 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... |
Q8SQW2 | MEPAEEGEILAHRRFTATKMEYEKIRIIGEGTFGQVILARKGRARYALKKVSKEKEGLSVTTIREVQVLRAMGHPSIVRLIEVVVEPGGDIYMVFPYFPYDLNRFIRSNKMTCSEIKHIFYQIAQGVCYIHSKGIMHRDLKSANILLDQKLNASIADFGMARYTTKTGAYTPGMVTLWYRAPEILLGSSSYTYAVDIWSLGCILTEMYLGHMIFQGSTEMLQLEMVIHACGSINENSYPGVQDLPGFRNFRLPQSPRRIEGIIRKHDASAVELVSKMLCLDPSKRITVEQVVGSKYFEHEARRDASSAGLQGCSYREDRL... | 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... |
O14098 | MSYSKSTIYRRQGTEPNSHFRRTVEEKSQLSGTNEESLGGHTLSSNAFKNNSSSISPSSSAKDPREQRKRTFPLNDTHSSRARQHERPFRSRKSRRRKGKKAFSPRPGSPPSPSFYRSGSQKRARNLTTKDYFAKRSESSSSASVSPISPSANRNDSKRQASSFRRSPPSSVHMKPSAFNGRKVSRRPSSSPPPIPSIPHETTSSDTQKKSSVSSGFPENKHGKFHFHIPNERRSRFDQPPSKRMALTSTARESVPAPLPSPPSGPIYTYTYPKPAYEKIDQIGEGTYGKVYKAINTVTGDLVALKRIRLEQEKDGFPIT... | 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 regula... |
Q03957 | MSYNNGNTYSKSYSRNNKRPLFGKRSPNPQSLARPPPPKRIRTDSGYQSNMDNISSHRVNSNDQPGHTKSRGNNNLSRYNDTSFQTSSRYQGSRYNNNNTSYENRPKSIKRDETKAEFLSHLPKGPKSVEKSRYNNSSNTSNDIKNGYHASKYYNHKGQEGRSVIAKKVPVSVLTQQRSTSVYLRIMQVGEGTYGKVYKAKNTNTEKLVALKKLRLQGEREGFPITSIREIKLLQSFDHPNVSTIKEIMVESQKTVYMIFEYADNDLSGLLLNKEVQISHSQCKHLFKQLLLGMEYLHDNKILHRDVKGSNILIDNQGNL... | 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 alre... |
P79955 | MDSTDKKVQVASRLPVPPKRKYVSNDENQEQMQRKRLRSSLESELPAVRVAASIATSKPRAAPVAALPKPQVIGRQSLAVMRPKNSGPGITSTSFSGKTKVSSSVTQPAAIGAEKKKRAAWDLKGQVNDMRDTVSNYKGKMQNLTGENARLLNSKEKLQREVEVLASENSKLSQERCTLESQLREVRQQVSTFEREVARLTELCQRQEKELSSHTNTIEELQGANAILTKQLLDKEVKLDCVSGENTSLKHTVNEQTDEIAALKVCLAEKDTEVHSLDTERRRLHNLVQELKGNIRVFCRVRPTLTPERELPAGHISFPS... | 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... |
P46962 | MPSTFESQLFFSRPFLSKRQIQRAQKNTISDYRNYNQKKLAVFKFLSDLCVQLKFPRKTLETAVYFYQRYHLFNRFETEVCYTVATSCLTLGCKEVETIKKTNDICTLSLRLRNVVKINTDILENFKKRVFQIELRILESCSFDYRVNNYVHIDEYVIKIGRELSFDYKLCNLAWVIAYDALKLETILVIPQHSIALAILKIAYELLDNKNWSSKRYSLFETDEKSVNEAYFDIVNFYINSFDMCDLQRHLPADLLPIGVERFMELKKNAGPESGLPQIPDHLLNADPYITITRDNNVQERRYVLSLELINGESSINSST... | 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... |
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 ... |
Q9ZKJ5 | MPTIDFTFCEINPKKGFGGANGNKISLFYNNELYMVKFPPKPSTHKEMSYTNGCFSEYVACHIVNSLGLKVQETLLGTYKNKIVVACKDFTTHQYELVDFLSLKNTMIELEKSGKDTNLNDVLYAIDNQHFIEPKVLKCFFWDMFVADTLLGNFDRHNGNWGFLRASNSKEYQIAPIFDCGSCLYPQADDVVCQKVLSNIDELNARIYNFPQSILKDDNDKKINYYDFLTQTNNKDCLDALLRIYPRIDMNKIHSIIDNTPFMSEIHKEFLHTMLDERKSKIIDVAHTRAIELSLQHKQAHSNPYDNADDLDNSNEYTPT... | 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 kina... |
Q8WWI5 | MGCCSSASSAAQSSKREWKPLEDRSCTDIPWLLLFILFCIGMGFICGFSIATGAAARLVSGYDSYGNICGQKNTKLEAIPNSGMDHTQRKYVFFLDPCNLDLINRKIKSVALCVAACPRQELKTLSDVQKFAEINGSALCSYNLKPSEYTTSPKSSVLCPKLPVPASAPIPFFHRCAPVNISCYAKFAEALITFVSDNSVLHRLISGVMTSKEIILGLCLLSLVLSMILMVIIRYISRVLVWILTILVILGSLGGTGVLWWLYAKQRRSPKETVTPEQLQIAEDNLRALLIYAISATVFTVILFLIMLVMRKRVALTIAL... | 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 product... |
P63690 | MTTVVDAEVQLTVVSDAAGRMRVQATGFQFDAGRAVAIEDTVGKVAGVQAVHAYPRTASIVIWYSRAICDTAAILSAIIDAETVPAAAVPAYASRSASNRKAGVVQKIIDWSTRTLSGVRRDVAAQPSGETSDACCDGEDNEDREPEQLWQVAKLRRAAFSGVLLTASLVAAWAYPLWPVVLGLKALALAVGASTFVPSSLKRLAEGRVGVGTLMTIAALGAVALGELGEAATLAFLFSISEGLEEYATARTRRGLRALLSLVPDQATVLREGTETIVASTELHVGDQMIVKPGERLATDGIIRAGRTALDVSAITGESV... | 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 | MPASPGHRDVLGCLVAACVPVQPGNPSRRSMLQQSLRAQILVLLGGSLAALLLIALACFGSLTGDVRAYRELLGGPVRAAQLIDEANLQFRGQVQEWKNVLLRGRQTEAQTKYWSQFEAQERAVQDILGRLGSVAEGELKDRVERLREEHRRLGTAYRQGRQRFLEAGADPIAGDQAVTGIDRATTAQMQTLRDELHQASDLHSSSISAEARRTMLLGSLVLIGASLAVALLSLWLVNRNLVRPVQRLIEHIAQLSHGDFGERIEIRRKDELGKLALAANTLRDFLVDIFDRLRRSTRDLDSASGSLNAIASLMAAGTRE... | 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, wh... |
Q9HUW6 | MRLKQLTNLNTLLLLTVCLALGITLWWSQRAMERPFQLLDQYLELSQRFDEQVARNIRQYLGSGDAVRQQAALQALESLAEALPELPPDLARTLAPSLAELREFSAGDLLAAGKLAGDPQGLLLQAERDLTGNLEQWSAYLDAAAGQPQAGAYRTPLLLASLHLTRLSLARAKLVESANPALAGDVERELANLREQAGRIEALPLLGVLDEQRSASDDFAAMMGLAGDAEAGAGNAEDRGVALRRELASLLQRYPDELRRTRDLIERRQQLSADTGARLDAVRQALATLEPQVRGERQRLQGQVRLIQGGMIALILLIAL... | 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, wh... |
Q9I0I6 | MMRLTLKSKVLLLAMVPVLLFALVLSGGAVLILKKQADAEVKDTRERLLGDRRAELEHYVQIAMGSIQAEYDRSANGDLNARAEAIARLSKIKYGKDGYIFGYDSQVVRLFRGDSPVDVGKSFRDRRDPSGVYLNRELVEAGRNGSHYVTYTSPLPGNESVMVPKLSYTLYLPKWDMVIGSAINLDGVEAQLVEIKQDIDERIGTLIASIVGIAGVLLVVLLVIGLAVANAMLRPLHQIRQNLDDIAAGEGDLTRRLPVTSYDELGELAGSFNRFVEKIHGLVRQIAGMTGDLKQLVEQMSAQAERSEQAMERQRHETDQ... | 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-di... |
P9WPS2 | MRVCVTGFNVDAVRAVAIEETVSQVTGVHAVHAYPRTASVVIWYSPELGDTAAVLSAITKAQHVPAELVPARAPHSAGVRGVGVVRKITGGIRRMLSRPPGVDKPLKASRCGGRPRGPVRGSASWPGEQNRRERRTWLPRVWLALPLGLLALGSSMFFGAYPWAGWLAFAATLPVQFVAGWPILRGAVQQARALTSNMDTLIALGTLTAFVYSTYQLFAGGPLFFDTSALIIAFVVLGRHLEARATGKASEAISKLLELGAKEATLLVDGQELLVPVDQVQVGDLVRVRPGEKIPVDGEVTDGRAAVDESMLTGESVPVE... | 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
Subcellula... |
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 | MEMPGRRSNYTLLSQFSDDQVSVSVTGAPPPHYDSLSSENRSNHNSGNTGKAKAERGGFDWDPSGGGGGDHRLNNQPNRVGNNMYASSLGLQRQSSGSSFGESSLSGDYYMPTLSAAANEIESVGFPQDDGFRLGFGGGGGDLRIQMAADSAGGSSSGKSWAQQTEESYQLQLALALRLSSEATCADDPNFLDPVPDESALRTSPSSAETVSHRFWVNGCLSYYDKVPDGFYMMNGLDPYIWTLCIDLHESGRIPSIESLRAVDSGVDSSLEAIIVDRRSDPAFKELHNRVHDISCSCITTKEVVDQLAKLICNRMGGPV... | 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... |
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,... |
P30825 | MGCKVLLNIGQQMLRRKVVDCSREETRLSRCLNTFDLVALGVGSTLGAGVYVLAGAVARENAGPAIVISFLIAALASVLAGLCYGEFGARVPKTGSAYLYSYVTVGELWAFITGWNLILSYIIGTSSVARAWSATFDELIGRPIGEFSRTHMTLNAPGVLAENPDIFAVIIILILTGLLTLGVKESAMVNKIFTCINVLVLGFIMVSGFVKGSVKNWQLTEEDFGNTSGRLCLNNDTKEGKPGVGGFMPFGFSGVLSGAATCFYAFVGFDCIATTGEEVKNPQKAIPVGIVASLLICFIAYFGVSAALTLMMPYFCLDNN... | 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 Loc... |
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 | MPVPCGSSCGRNAFMRRPKTGDTLCKECFFLAFETEIHNTIQQEQLFRPGEKVAIAASGGKDSTVLAHVMNLLNKRYNYGLDLVLLSIDEGITGYRDDSLKTVAQNRDDYGMPLRVLSYQELYGWTMDRIVAEIGRSNNCTFCGVFRRQALDRGARLMEVDCVATGHNADDIAETVIMNILRGDTARLRRCCDIKTGSKEADTIPRVKPLKYSYEKEIVMYAHFKKLVYFSTECVFAPNAYRGHARAFLKDLEKVRPSAIMDIIHAGEQLQIKGTVKKPVRGVCGRCGFVSSQQPCKACVLLEGLNRGLPKLGIGKKSKG... | 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 f... |
O64862 | MEAKNKKAVASRLCCLCNLRRPVLKRPKTLQQICRECFYEVFEEEIHQVIVQNRLFKSGERVAIGASGGKDSTVLAYVLSELNRRHNYGLDLFLLSIDEGITGYRDDSLETVKRNEVQYGLPLKIVSYKDLYGWTMDEIVKMIGLKNNCTFCGVFRRQALDRGAALLKVEKLVTGHNADDIAETVLLNILRGDIARLSRCTSITTGEDGPIPRCKPFKYTYEKEIVMYAYFKKLDYFSTECIYSPNAYRGFAREFIKDLERIRPRAILDIIKSGEDFRIATTTKMPEQGTCERCGYISSQKWCKACVLLEGLNRGLPKMG... | 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 f... |
Q0VC66 | MPAPQCASCHKARAALRRPRSGQALCGSCFCAAFEAEVLHTVVAGRLLPPGAVVAVGASGGKDSTVLAHVLRELAPRLGISLHLVAVDEGIGGYRDAALAAVRRQAARWELPLTVVAYADLFGGWTMDAVARSTAGSGRSRACCTFCGVLRRRALEEGARLVGATHVVTGHNADDMAETVLMNFLRGDAGRLARGGGLGSPGEGGALPRCRPLQLASQKEVVLYAHFRRLDYFSEECVYAPEAFRGHARDLLKMLEAARPSAVLDLVHSAERLALAPTARPPPPGACSRCGALASRALCQACALLDGLNRGRPRLAIGKG... | 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 f... |
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 ... |
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 bi... |
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 bi... |
Q16YE7 | MRNLGIAVTFAVLLVIGYVTALEWDAVVTTDSGILFFDKNWTQISSGGHQFHHISAFAYDEVKRKLYFSDLKDPSFRIFSLDTKPEEEYHKVAKLLPKSDQTGYITGLAFDHLERKLYWTEKGTHSVYSVEVDKLGAPANATDGLINLVAQVEENHDLAALTIDECRRHLYWTNSYLQTSSIVRAAMNGTVLDDHKEDVYEPRGISVDHYNNRIYWVEKKYGRAFTVESANLEVQDRQTFLRGEDKIPTHVSPNSQYLYWIDQEDGEVHETMKSDSKVTRVVYKGSRPSALIIRSGLLVEYQKNNPSCKAVVSEIIDNVR... | 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 | MKSPCRAAAGWLVLLLSSCCLGYVIATEWAAAVTTDNGILFFDSNWRKISSAAHQYSRISAFAYDEVLGKLYFADLDHPEYRLFALDYDDTDELHKVTKLLPKSAQTAYISGMAFDHLERRLYWTEKGTRSVYYVAIDELLSSTRSAAAAANGTAAAAATAVEATTSAPPPSSSSPVQLVATVQPDHELAGLAIDECRRHLYWTNCYPKTSNIVRAAMNGTVLNVHEEQVYLPKGITVDHYRNRLYWVEKKYGRRYTIESADLEVNDQRTLQTGLDRLPADIAVKNDYIYWTDQENNEIYEMSKEPNAPSRTVYRGEHPS... | 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 | MAYIDQKHNTFWDDFAIALRDKIVFLNSTWGEIHASAHRFEDLSALAFDEAEEMIYFSDQTHQNGSIFALRRDDSTPIVVQRTGNDSVEGLAYDPLNRNLFWADMRQQKIFFSSVDTLATELPKVLVDLSGEGGQPDGIAVDICRRQLYWTNGNIKSASVERIGLDGKGRQTIISADIDMPRGIVVDQLSDRIFWVDNKVGIFFAIESARLDGSDRQVVVKGKHQDPKHLAINEDAIYWTDRMDKAVWSYPKPTYSQEVTNVTQAEPELAKPFSKEKAYGIVTRTGFYQRLQKDAHCASIVKKVKQQLNTRLNNRTHIRS... | 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 | MIRIRFGMDVLLVLLLATCLLTPAHGTPLEWDFAVTLRTKIQFMDSSWQTIATAAHEFDELSALTFDESEELIYFNDLKHRNGSIFSLKRDLIAANHVAEQTIARTGNESVGGLAYDPLNMNLFWSDTEQRKIFFAPIHGSATPQVLVDLSAEGGRPDGVAVDVCRRKLYWTNSNVTHPTVERINLDGSNRTVIISSNIDMPRGIVVDQLSDRLFWIDDLKGVFFSVESSKLDGSDRQVVLKDKHHEPLNLAVTNDAIYWTDRTTRAVWSHPKVPVIKVTTTSKPDEEDSTDSTDFKDPEPVAEDCPLVRVANLSEEARG... | 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: Cel... |
B4MLE8 | MILRLFILLSIITVYLQLSVGIQQQFEFAITLKSKILFVDEHWNVVNTAAHEFDELSALTFDESEERIYFNDGQHQNSSIFSLRKVGKSNHLAEQTIQRYGNESVGGIAYDPLNRTIYWSDLLQKKIFYASIDTVATEMPKILVDLSEENGTPYGVAIDICGRKLYWTNSNINHPTVERIDLNGTGRLAIIDKNIDSPRGIVVDQGAKRIFWIDDLKGIFFAVMSAQLDGSDVKLVLKDKNHEPQNLAVTRNAIYWTDRTTKSVWSHLKEPEIATTTTTTTTSTTQIPTVEGEEGTGAMDDNDIWPVGDFETTPKKSPLE... | 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 salva... |
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 | MGQQKQRNRRWVLASRPHGAPVPENFRLEEDDVATPGEGQVLLRTVYLSLDPYMRGRMSDEPSYSPPVDIGGVMVGGTVSRVVESNHPDYQSGDWVLGYSGWQDYDISSGDDLVKLGDHPQNPSWSLGVLGMPGFTAYMGLLDIGQPKEGETLVVAAATGPVGATVGQIGKLKGCRVVGVAGGAEKCRHATEVLGFDVCLDHHADDFAEQLAKACPKGIDIYYENVGGKVFDAVLPLLNTSARIPVCGLVSSYNATELPPGPDRLPLLMATVLKKRIRLQGFIIAQDYGHRIHEFQREMGQWVKEDKIHYREEITDGLEN... | 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(+) + tetrahydrocu... |
Q30W70 | MDLQDFSHKLAEATKNLTPAERASLKKIFEGVSAEVFSQPAPVSAVATGAESGIPDGPTPRHVKLKENFLKQVPSITVQRAVAITKIAKENPGLPKPLLRAKTFRYCCETAPLVIQDHELIVGSPNGAPRAGAFSPEVAWRWLQDELDTIGSRPQDPFYISEEDKKVLREEVFPFWQNKSVDEFCEGQYREADLWEMSGESFVSDCSYHAVNGGGDSNPGYDVILMKKGMLDIQREAREKLEQLDYANPEDIDKIYFYKSVIETAEGVMIYARRLSAYAAELAARETDPRRKAELQKISEVNARVPAHAPSNFWEAIQAV... | 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 .... |
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 | MGDWSFLGNILEEVNEHSTVIGRVWLTVLFIFRILILGTAAEFVWGDEQSDFVCNTQQPGCENVCYDEAFPISHIRLWVLQIIFVSTPSLMYVGHAVHYVRMEEKRKSREAEELGQQAGTNGGPDQGSVKKSSGSKGTKKFRLEGTLLRTYICHIIFKTLFEVGFIVGHYFLYGFRILPLYRCSRWPCPNVVDCFVSRPTEKTIFILFMLSVASVSLFLNVMELGHLGLKGIRSALKRPVEQPLGEIPEKSLHSIAVSSIQKAKGYQLLEEEKIVSHYFPLTEVGMVETSPLPAKPFNQFEEKISTGPLGDLSRGYQETL... | 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... |
P28236 | MGDWSFLGNILEEVNEHSTVIGRVWLTVLFIFRILILGTAAEFVWGDEQSDFVCNTQQPGCENVCYDEAFPISHIRLWVLQIIFVSTPSLMYVGHAVHHVRMEEKRKDREAEELCQQSRSNGGERVPIAPDQASIRKSSSSSKGTKKFRLEGTLLRTYVCHIIFKTLFEVGFIVGHYFLYGFRILPLYRCSRWPCPNVVDCFVSRPTEKTIFILFMLSVAFVSLFLNIMEMSHLGMKGIRSAFKRPVEQPLGEIAEKSLHSIAVSSIQKAKGYQLLEEEKIVSHYFPLTEVGMVETSPLSAKPFSQFEEKIGTGPLADMS... | 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... |
P55917 | MGDWSFLGNILEEVNEHSTVIGRVWLTVLFIFRILILGTAAEFVWGDEQSDFVCNTQQPGCENVCYDEAFPISHIRLWVLQIIFVSTPSLVYVGHAVHHVRMEEKRKEREAEELSQQSPGNGGERAPLAADQGSVKKSSSSSKGTKKFRLEGTLLRTYVCHIIFKTLFEVGFIVGHYFLYGFRILPLYRCSRWPCPNVVDCFVSRPTEKTIFILFMLSVASVSLFLNILEMSHLGLKKIRSAFKRPVEQPLGEIPEKSLHSIAVSSIQKAKGYQLLEEEKIVSHYFPLTEVGMVEASPLSAKPFSQFEEKVGPGPLGDLS... | 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 ... |
P57773 | MGDWNLLGDTLEEVHIHSTMIGKIWLTILFIFRMLVLGVAAEDVWNDEQSGFICNTEQPGCRNVCYDQAFPISLIRYWVLQVIFVSSPSLVYMGHALYRLRVLEEERQRMKAQLRVELEEVEFEMPRDRRRLEQELCQLEKRKLNKAPLRGTLLCTYVIHIFTRSVVEVGFMIGQYLLYGFHLEPLFKCHGHPCPNIIDCFVSRPTEKTIFLLFMQSIATISLFLNILEIFHLGFKKIKRGLWGKYKLKKEHNEFHANKAKQNVAKYQSTSANSLKRLPSAPDYNLLVEKQTHTAVYPSLNSSSVFQPNPDNHSVNDEKC... | 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 membr... |
Q8WMV3 | MELLLRFLLLCGVADFTRGLSITTPEQMIEKAKGETAYLPCKFTLGPEDQGPLDIEWLLSPADNQKVDQVIILYSGDKIYDDYYQDLKGRVHFTSNDLKSGDASINVTNLQLSDIGTYQCKVKKAPGVGNKKIQLTVLVKPSGIRCYVDGSEEIGNDFKLKCEPKEGSLPLRYEWQKLSDSQKLPTSWLPEMTSPVISVKNASAEYSGTYTCTVRNRVGSDQCLLRLDVVPPSNRAGTIAGAVIGTLLALVLIALIVFCCHKKRREEKYEKEVHHDIREDVPPPKSRTSTARSYIGSNHSSLGSMSPSNMEGYSKTQYNQ... | 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 leukocy... |
P78310 | MALLLCFVLLCGVVDFARSLSITTPEEMIEKAKGETAYLPCKFTLSPEDQGPLDIEWLISPADNQKVDQVIILYSGDKIYDDYYPDLKGRVHFTSNDLKSGDASINVTNLQLSDIGTYQCKVKKAPGVANKKIHLVVLVKPSGARCYVDGSEEIGSDFKIKCEPKEGSLPLQYEWQKLSDSQKMPTSWLAEMTSSVISVKNASSEYSGTYSCTVRNRVGSDQCLLRLNVVPPSNKAGLIAGAIIGTLLALALIGLIIFCCRKKRREEKYEKEVHHDIREDVPPPKSRTSTARSYIGSNHSSLGSMSPSNMEGYSKTQYNQ... | 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 leukocy... |
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.
Loc... |
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: G... |
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... |
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 t... |
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
|
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 i... |
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
|
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
Path... |
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
|
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
|
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
|
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: Peripher... |
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
|
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) concen... |
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:... |
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... |
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... |
P23662 | MRMHNKIQLLSVLNTHLVAYPTPMNLNYSWNGGSLAGMMLASQMLTGILLAMHYVGHVDYAFASVQHLMTDVPSGMILRYAHANGASLFFIVVYLHVLRGMYYGSGAQPREIVWISGVVILLVMIITAFIGYVLPWGQMSFWGATVITSLATAIPVVGKHIMYWLWGGFSVDNPTLNRFYSFHYTLPFILAGLSVFHIAALHQYGSTNPLGVNSQSSLISFGSYFGAKDLVGALFLALVFSILVFFYPDLLGHPDNLIPANPYSTPQHIVPEWYFLWVYAILRSIPNKAMGVLAIGLVFASLFAMPFIGLGGGKFRIITE... | 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... |
P48875 | MRFIKRPLISIVNDHLIDYPTPINIHYAWNFGFLSSICLIVQILTGIFLAMHYTPHVDLAFASVEHIMRDVNYGWLLRYIHTNGASMFFIVVYIHIFRGLYFGSYIKPRHWVWVIGVLILLLMILTAFIGYVLPWGQMSLWGATVITNLVSAVPFIGDSIVTWLWGGFSVDNATLNRFFSLHYLMPFVIAAVSLVHLAILHQDGSGNPLGIDSNVDKVSMFPYFIVKDFLGMVIFIIFFSIFVYFSPNVLGHPDNYIEANPMVTPAHIVPEWYFLPFYAILRSIPHKLGGVTAMISAIAILAFLPWIHSTEIRSSRFRPL... | 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... |
P00161 | MRILKSHPLLKIVNSYIIDSPQPANLSYLWNFGSLLALCLGIQIVTGVTLAMHYTPSVSEAFNSVEHIMRDVNNGWLVRYLHSNTASAFFFLVYLHIGRGLYYGSYKTPRTLTWAIGTVILIVMMATAFLGYVLPYGQMSLWGATVITNLMSAIPWIGQDIVEFIWGGFSVNNATLNRFFALHFLLPFVLAALALMHLIAMHDTVGSGNPLGISANYDRLPFAPYFIFKDLITIFIFFIVLSIFVFFMPNALGDSENYVMANPMQTPPAIVPEWYLLPFYAILRSIPNKLLGVIAMFAAILALMVMPITDLSKLRGVQFR... | 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... |
Q5DNB7 | MFFNIFKSSIKGFLLNLPTPINLNYWYGFGSMLGLIYSIQIISGLILSWFYFIDLSGGFKSLILIMQDVWGGWFIRFIHSSGVSLFMFIMYLHILRGLIYGSFCKVDVWYSGILLLFICMGSAFLGYVLPWGSMSYWGMTVVTNMLSAIPMVGVYLVETIWGGSSAGVSTLVRFFSFHYLLSLFIMVFILIHLILLHECGSSNPLGVYYSCEKFTFHPLFSLKDTLVFVLVVFLYWFCIFVCPYLLLDAINFEEINFMMTPSHIKPEWYFLFIYCILRSTPSKLGGVILMVMAILMLVFLGIGKNLGSVLMVKTLYWKLM... | 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... |
O20672 | MVSRTLSLSMSLFRAHLVFYRCALNLNSSYNFGFLVAMTFVLQIITGITLAFRYTSEASCAFASVQHLVREVAAGWEFRMLHATTASFVFLCILIHMTRGLYNWSYSYLTTAWMSGLVLYLLTIATAFLGYVLPWGQMSFWGATVITNLLSPIPYLVPWLLGGYYVSDVTLKRFFVLHFILPFIGCIIIVLHIFYLHLNGSSNPAGIDTALKVAFYPHMLMTDAKCLSYLIGLIFLQAAFGLMELSHPDNSIPVNRFVTPLHIVPEWYFLAYYAVLKVIPSKTGGLLVFMSSLINLGLLSEIRALNTRMLIRQQFMTRNV... | 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... |
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-trans... |
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 + terpentetrien... |
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-trans... |
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 ... |
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