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P07688 | MWRLLATLSCLLVLTSARSSLYFPPLSDELVNFVNKQNTTWKAGHNFYNVDLSYVKKLCGAILGGPKLPQRDAFAADVVLPESFDAREQWPNCPTIKEIRDQGSCGSCWAFGAVEAISDRICIHSNGRVNVEVSAEDMLTCCGGECGDGCNGGFPSGAWNFWTKKGLVSGGLYNSHVGCRPYSIPPCEHHVNGSRPPCTGEGDTPKCSKTCEPGYSPSYKEDKHFGCSSYSVANNEKEIMAEIYKNGPVEGAFSVYSDFLLYKSGVYQHVSGEIMGGHAIRILGWGVENGTPYWLVGNSWNTDWGDNGFFKILRGQDHCGIESEIVAGMPCTHQY | Function: Thiol protease which is believed to participate in intracellular degradation and turnover of proteins . Cleaves matrix extracellular phosphoglycoprotein MEPE (By similarity). Involved in the solubilization of cross-linked TG/thyroglobulin in the thyroid follicle lumen (By similarity). Has also been implicated in tumor invasion and metastasis (By similarity).
Catalytic Activity: Hydrolysis of proteins with broad specificity for peptide bonds. Preferentially cleaves -Arg-Arg-|-Xaa bonds in small molecule substrates (thus differing from cathepsin L). In addition to being an endopeptidase, shows peptidyl-dipeptidase activity, liberating C-terminal dipeptides.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 36661
Sequence Length: 335
Subcellular Location: Lysosome
EC: 3.4.22.1
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P43233 | MSWSRSILCLLGAFANARSIPYYPPLSSDLVNHINKLNTTGRAGHNFHNTDMSYVKKLCGTFLGGPKAPERVDFAEDMDLPDTFDTRKQWPNCPTISEIRDQGSCGSCWAFGAVEAISDRICVHTNAKVSVEVSAEDLLSCCGFECGMGCNGGYPSGAWRYWTERGLVSGGLYDSHVGCRAYTIPPCEHHVNGSRPPCTGEGGETPRCSRHCEPGYSPSYKEDKHYGITSYGVPRSEKEIMAEIYKNGPVEGAFIVYEDFLMYKSGVYQHVSGEQVGGHAIRILGWGVENGTPYWLAANSWNTDWGITGFFKILRGEDHCGIESEIVAGVPRMEQYWTRV | Function: Thiol protease which is believed to participate in intracellular degradation and turnover of proteins. Has also been implicated in tumor invasion and metastasis.
Catalytic Activity: Hydrolysis of proteins with broad specificity for peptide bonds. Preferentially cleaves -Arg-Arg-|-Xaa bonds in small molecule substrates (thus differing from cathepsin L). In addition to being an endopeptidase, shows peptidyl-dipeptidase activity, liberating C-terminal dipeptides.
Sequence Mass (Da): 37587
Sequence Length: 340
Subcellular Location: Lysosome
EC: 3.4.22.1
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P81494 | LPDTFDSRKQWPNCPTISEIRDQGSVSVEVSAEDLLSCCGFECGMGCN | Function: Thiol protease which is believed to participate in intracellular degradation and turnover of proteins. Has also been implicated in tumor invasion and metastasis.
Catalytic Activity: Hydrolysis of proteins with broad specificity for peptide bonds. Preferentially cleaves -Arg-Arg-|-Xaa bonds in small molecule substrates (thus differing from cathepsin L). In addition to being an endopeptidase, shows peptidyl-dipeptidase activity, liberating C-terminal dipeptides.
Sequence Mass (Da): 5226
Sequence Length: 48
Subcellular Location: Lysosome
EC: 3.4.22.1
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Q55DH8 | MNKKLEQLEKFKTNDKNPVYSTTNTGVSLSDDANSLKAGPRGPTLLEDFVLREKITHFDHERIPERIVHARGTGAHGYFLSYKDHSKLTKADFLSKQDKKTPVFIRISTVQGPRGSADTVRDVHGFAVKFYTDEGNYDLVGNNMPVFFIQDASSFPDFVHAVKMEPQNEMPTGGSAHDTFYDFCGLKPESAHSVLWVMSDRGIPISLRHQQGFGVHSYRFINQEGKSTFVKLHWKPLSGTCSLLWDEAQKIAGKDCDYHRRRFWEDIESGDFPQWELGAQLLDEDLQKKFDFDILDPTKLIPEELTPVIPLGRMVIDRNPDNFFAETEQVAFCVSHVVPGIDFSNDPLLQGRIFSYLDTQLSRLGGPNFNEIPINRPVCPFANNQRDGIHRMTINKGGASYFPNSIDKGYPLLKEPSANKGGFRPYPENISGTKSYDRSETFEDHFSQATMFWNSMSQHEKNHIIAAYTFEISKCSRPEVRTRYVNNILVNIDSVLAEKVAKNLGVKIEPTSTKPIKKIMVKPSPALSQPNLLSGDIVSRRISVIIEKGVDYDDVINFKDDMEKRGAMVMLVSSTLAQVECSGGEMLSPKGTIIGNPSIFFDAVYVPKSTEEATKILSDDGNFLHYILEAFKHLKTIAFGGSVSVIKELLRLPQDHGLLLGNGYKDITEQFFYSLAHHRVWERESKVSKIPA | Function: Occurs in almost all aerobically respiring organisms and serves to protect cells from the toxic effects of hydrogen peroxide. Its accumulation in prespore cells affords the spores protection from oxidation during prolonged dormancy. Required for normal developmental timing, possibly through a regulatory role in differentiation and morphogenesis.
Catalytic Activity: 2 H2O2 = 2 H2O + O2
Sequence Mass (Da): 78033
Sequence Length: 692
Subcellular Location: Cytoplasm
EC: 1.11.1.6
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P06115 |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| Function: Occurs in almost all aerobically respiring organisms and serves to protect cells from the toxic effects of hydrogen peroxide.
Catalytic Activity: 2 H2O2 = 2 H2O + O2
Sequence Mass (Da): 64583
Sequence Length: 562
Subcellular Location: Cytoplasm
EC: 1.11.1.6
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O91466 | MTKLLNFVILASVLTVTAHALTYDLNNSDELFKNFAIKYNKTYVSDEERAIKLENFKNNLKMINEKNMASKYAVFDINEYSDLNKNALLRRTTGFRLGLKKNPSAFTMTECSVVVIKDEPQALLPETLDWRDKHGVTPVKNQMECGSCWAFSTIANIESLYNIKYDKALNLSEQHLVNCDNINNGCAGGLMHWALESILQEGGVVSAENEPYYGFDGVCKKSPFELSISGSRRYVLQNENKLRELLVVNGPISVAIDVSDLINYKAGIADICENNEGLNHAVLLVGYGVKNDVPYWILKNSWGAEWGEEGYFRVQRDKNSCGMMNEYASSAIL | Function: Cysteine protease that plays an essential role in host liquefaction to facilitate horizontal transmission of the virus. May participate in the degradation of foreign protein expressed by the baculovirus system (By similarity).
PTM: Synthesized as an inactive proenzyme and activated by proteolytic removal of the inhibitory propeptide.
Catalytic Activity: Endopeptidase of broad specificity, hydrolyzing substrates of both cathepsin L and cathepsin B.
Sequence Mass (Da): 37434
Sequence Length: 333
EC: 3.4.22.50
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Q9PYY5 | MLFFNFYKHIMFLPWVFCVALLTLNVCAVSYIAYDMSNAQELFNEFVVKYNKVYKDDQEKEARFEIFKQNLADINARNALEDSAMFEINSRADISSNELLQKLTGLKLSLMRGEKKNSFCTPTVISGDSSGKVPDSFDWRDRNSVTSVKMQKECGSCWAFSAVANIESLYHIKHNVSLDLSEQQLVDCDKVNNGCNGGLMSWAFEGIIRAGGISYEAPYPYTGVDGVCKNTTRYVQLSGCYAYDLRSEKKLRQVLHEKGPVSVAIDVVDLTNYKSGVAKHCSVDHGLNHGVLLVGYGQENDVKYWTLKNSWGSDWGEQGFFRIKRDVNSCGILNQFAASAILSSSS | Function: Cysteine protease that plays an essential role in host liquefaction to facilitate horizontal transmission of the virus. May participate in the degradation of foreign protein expressed by the baculovirus system (By similarity).
PTM: Synthesized as an inactive proenzyme and activated by proteolytic removal of the inhibitory propeptide.
Catalytic Activity: Endopeptidase of broad specificity, hydrolyzing substrates of both cathepsin L and cathepsin B.
Sequence Mass (Da): 38819
Sequence Length: 346
EC: 3.4.22.50
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P25783 | MNKILFYLFVYGVVNSAAYDLLKAPNYFEEFVHRFNKDYGSEVEKLRRFKIFQHNLNEIINKNQNDSAKYEINKFSDLSKDETIAKYTGLSLPIQTQNFCKVIVLDQPPGKGPLEFDWRRLNKVTSVKNQGMCGACWAFATLASLESQFAIKHNQLINLSEQQMIDCDFVDAGCNGGLLHTAFEAIIKMGGVQLESDYPYEADNNNCRMNSNKFLVQVKDCYRYITVYEEKLKDLLRLVGPIPMAIDAADIVNYKQGIIKYCFNSGLNHAVLLVGYGVENNIPYWTFKNTWGTDWGEDGFFRVQQNINACGMRNELASTAVIY | Function: Cysteine protease that plays an essential role in host liquefaction to facilitate horizontal transmission of the virus. Accumulates within infected cells as an inactive proenzyme (proV-CATH), which is activated by proteolytic cleavage upon cell death.
PTM: Synthesized as an inactive proenzyme and activated by proteolytic removal of the inhibitory propeptide.
Catalytic Activity: Endopeptidase of broad specificity, hydrolyzing substrates of both cathepsin L and cathepsin B.
Sequence Mass (Da): 36938
Sequence Length: 323
Subcellular Location: Host endoplasmic reticulum
EC: 3.4.22.50
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Q8V5U0 | MRKYHSNIMHKIITFVSLLWTFVVCDEISLHTSSSPPPLSSPVPVLYYNLDQSEIYFKHFLQQYNKSYDDPKEYQYRYNVFKDNLNKINSQNRENLLNNKNNNDSLSTSAQFGVNKFSDKTPDEVLHSNTGFFLNLSQHYTLCENRIVKGAPDIRLPDYYDWRDTNKVTPIKDQGVCGSCWAFVAIGNIESQYAIRHNKLIDLSEQQLLDCDEVDLGCNGGLMHLAFQELLLMGGVETEADYPYQGSEQMCTLDNRKIAVKLNSCFKYDIRDENKLKELVYTTGPVAIAVDAMDIINYRRGILNQCHIYDLNHAVLLIGWGIENNVPYWIIKNSWGEDWGENGFLRVRRNVNACGLLNEFGASSVIQ | Function: Cysteine protease that plays an essential role in host liquefaction to facilitate horizontal transmission of the virus. May participate in the degradation of foreign protein expressed by the baculovirus system (By similarity).
PTM: Synthesized as an inactive proenzyme and activated by proteolytic removal of the inhibitory propeptide.
Catalytic Activity: Endopeptidase of broad specificity, hydrolyzing substrates of both cathepsin L and cathepsin B.
Sequence Mass (Da): 42203
Sequence Length: 367
EC: 3.4.22.50
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Q91BH1 | MYLIYYYTIIAVATASIANEKIFYDIDSASVYYENFIKQHNKEYTTPDQRDAAFVNFKRNLADMNAMNNVSNQAVYGINKFSDIDKITFVNEHAGLVSNLINSTDSNFDPYRLCEYVTVAGPSARTPESFDWRKLNKVTKVKEQGVCGSCWAFAAIGNIESQYAIMHDSLIDLSEQQLLDCDRVDQGCDGGLMHLAFQEIIRIGGVEHEIDYPYQGIEYACRLAPSKLAVRLSHCYQYDLRDERKLLELLYKNGPIAVAIDCVDIIDYRSGIATVCNDNGLNHAVLLVGYGIENDTPYWIFKNSWGSNWGENGYFRARRNINACGMLNEFAASAVLL | Function: Cysteine protease that plays an essential role in host liquefaction to facilitate horizontal transmission of the virus. May participate in the degradation of foreign protein expressed by the baculovirus system (By similarity).
PTM: Synthesized as an inactive proenzyme and activated by proteolytic removal of the inhibitory propeptide.
Catalytic Activity: Endopeptidase of broad specificity, hydrolyzing substrates of both cathepsin L and cathepsin B.
Sequence Mass (Da): 38098
Sequence Length: 337
EC: 3.4.22.50
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Q18879 | MTRQNTSESDNTQRPPIPQYDTVDDIDELTDAMDKEDHHHHHHHHEHHHQHQGIAQYDTVEEVETLETVHHRTSLNQEVPTPQRRSHPQYDNLDDIDDQEYITEVEVKSNRGSTLTTRPHVTIKQDEIEDIGERQVTVIEIASQKGSTKRVAPRKDYAPSIPLPEHPAQQSAPPTQQSRPQTTSHKPPNPEMEFDIGVKNIAPVLIHKMNMDDRDPKDSAQYLNTSFFEVFNEPSEQYHSIACVWTLSFKIFEIVRIYSYKILTLIFGLIIAFLGGILFALFAFLNIWIFRPILILTRMAFAQIVLIWPMFLIYIVRPFFYSVGAIFSTARLHTSRGEQVVEVWEKHIHHV | Function: May act as a scaffolding protein within caveolar membranes. Interacts directly with G-protein alpha subunits and can regulate their activity. Thought to have a role in the uptake of lipids and proteins in the intestinal cells; operates in the apical uptake of lipid markers and trafficking of yolk proteins. Affects fecundity and egg laying.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 40771
Sequence Length: 351
Subcellular Location: Golgi apparatus membrane
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A0M8S6 | MGLETEKADVQLFMDDDSYSRHSGVDYADPDKFADSGSDRDPHRLNSNLKVGFEDVIAEPVSTHSFDKVWICSHALFEISKYVIYKFLTLFLAIPLAFAAGILFATLSCLHIWIIMPFVKTCLMVLPSVQTIWKSITDVVIAPLCTSVGRSFSSVSLQLSHD | Function: May act as a scaffolding protein within caveolar membranes. Interacts directly with G-protein alpha subunits and can functionally regulate their activity. Acts as an accessory protein in conjunction with CAV1 in targeting to lipid rafts and driving caveolae formation. The Ser-36 phosphorylated form has a role in modulating mitosis in endothelial cells. Positive regulator of cellular mitogenesis of the MAPK signaling pathway. Required for the insulin-stimulated nuclear translocation and activation of MAPK1 and STAT3, and the subsequent regulation of cell cycle progression (By similarity).
PTM: Phosphorylated on serine and tyrosine residues. CAV1 promotes phosphorylation on Ser-23 which then targets the complex to the plasma membrane, lipid rafts and caveolae. Phosphorylation on Ser-36 appears to modulate mitosis in endothelial cells (By similarity). Phosphorylation on both Tyr-19 and Tyr-27 is required for insulin-induced 'Ser-727' phosphorylation of STAT3 and its activation. Phosphorylation on Tyr-19 is required for insulin-induced phosphorylation of MAPK1 and DNA binding of STAT3. Tyrosine phosphorylation is induced by both EGF and insulin (By. similarity).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 18065
Sequence Length: 162
Subcellular Location: Nucleus
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P84991 | TTKPVPSGSPWYGPDRVKNRELEVIHSR | Cofactor: Binds at least 14 chlorophylls (8 Chl-a and 6 Chl-b) and carotenoids such as lutein and neoxanthin.
Function: The light-harvesting complex (LHC) functions as a light receptor, it captures and delivers excitation energy to photosystems with which it is closely associated.
PTM: Photoregulated by reversible phosphorylation of its threonine residues.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 3207
Sequence Length: 28
Domain: The N-terminus of the protein extends into the stroma where it is involved with adhesion of granal membranes and post-translational modifications; both are believed to mediate the distribution of excitation energy between photosystems I and II.
Subcellular Location: Plastid
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P27489 | MASMAATASSTTVVKATPFLGQTKNANPLRDVVAMGSARFTMSNDLWYGPDRVKYLGPFSAQTPSYLNGEFPGDYGWDTAGLSADPEAFAKNRALEVIHGRWAMLGALGCIFPEVLEKWVKVDFKEPVWFKAGSQIFSDGGLDYLGNPNLVHAQSILAVLGFQVVLMGLVEGFRINGLPGVGEGNDLYPGGQYFDPLGLADDPTTFAELKVKEIKNGRLAMFSMFGFFVQAIVTGKGPLENLLDHLDNPVANNAWVYATKFVPGA | Cofactor: Binds at least 14 chlorophylls (8 Chl-a and 6 Chl-b) and carotenoids such as lutein and neoxanthin.
Function: The light-harvesting complex (LHC) functions as a light receptor, it captures and delivers excitation energy to photosystems with which it is closely associated.
PTM: Photoregulated by reversible phosphorylation of its threonine residues.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 28623
Sequence Length: 265
Domain: The N-terminus of the protein extends into the stroma where it is involved with adhesion of granal membranes and post-translational modifications; both are believed to mediate the distribution of excitation energy between photosystems I and II.
Subcellular Location: Plastid
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P14278 | MATCAIQQSAFVGQAVGKSQNEFIRKVGNFGEGRITMRRTVKSAPQSIWYGEDRPKYLGPFSEQTPSYLTGEFPGDYGWDTAGLSADPETFARNRELEVIHCRWAMLGALGCVFPEILSKNGVKFGEAVWFKAGSQIFSEGGLDYLGNPNLVHAQSILAIWACQVVLMGFVEGYRVGGGPLGEGLDKIYPGGAFDPLGLADDPEAFAELKVKEIKNGRLAMFSMFGFFVQAIVTGKGPIENLSDHINDPVANNAWAYATNFVPGK | Cofactor: Binds at least 14 chlorophylls (8 Chl-a and 6 Chl-b) and carotenoids such as lutein and neoxanthin.
Function: The light-harvesting complex (LHC) functions as a light receptor, it captures and delivers excitation energy to photosystems with which it is closely associated.
PTM: Photoregulated by reversible phosphorylation of its threonine residues.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 28775
Sequence Length: 265
Domain: The N-terminus of the protein extends into the stroma where it is involved with adhesion of granal membranes and post-translational modifications; both are believed to mediate the distribution of excitation energy between photosystems I and II.
Subcellular Location: Plastid
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A4G3R1 | MVMSSPTNSARIILISGIASGQGKTTVTAALARKLIRQGLRVRVFKTGPDYLDPMILQRASGAEVYALDLWMVGLDDCRRLLARAASEVDVILIEGVMGLYDGDPSSADLARAFGVPVVVVLDAAKMAQTVGAVVLGLQQYGPVDLAGVIVNRLASPSHASMVTRGIRNVPILATLPKQQQALPERHLGLVQPDEIAQVDQVLDQLADQIEIDMVAWDAIAPVVLDGSLAAASTQQLLAGKTIAIARDAAFAFVYHANLECLRAAGAQLKFFSPLNDETIPAEADAVYIPGGYPELHCATLSSAQRWQDSMRAAHVRNMPILAECGGMMVIADSLIDAQGKKWPMVGLIPGEVAMQGKLAGLGMQSLATEDGELRGHAFHYSTLSTPVEPQAQTVKRSNGAHGEAVYKQGALTATYFHAYFSSCPAATARIFSPEIKA | Function: Catalyzes the ATP-dependent amidation of the two carboxylate groups at positions a and c of cobyrinate, using either L-glutamine or ammonia as the nitrogen source.
Catalytic Activity: 2 ATP + cob(II)yrinate + 2 H2O + 2 L-glutamine = 2 ADP + cob(II)yrinate a,c diamide + 2 H(+) + 2 L-glutamate + 2 phosphate
Sequence Mass (Da): 46549
Sequence Length: 438
Domain: Comprises of two domains. The C-terminal domain contains the binding site for glutamine and catalyzes the hydrolysis of this substrate to glutamate and ammonia. The N-terminal domain is anticipated to bind ATP and cobyrinate and catalyzes the ultimate synthesis of the diamide product. The ammonia produced via the glutaminase domain is probably translocated to the adjacent domain via a molecular tunnel, where it reacts with an activated intermediate.
Pathway: Cofactor biosynthesis; adenosylcobalamin biosynthesis; cob(II)yrinate a,c-diamide from sirohydrochlorin (anaerobic route): step 10/10.
EC: 6.3.5.11
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Q8EXQ4 | MNIKIPRIVIGGTGSGVGKTTIALALTQILRKKGLKVATFKCGPDYLDPTYHSRASQKICHNLDGWLMGKESVLNTFYQACHNVDIVIIEGMMGLFDGHSPNSEIGSTAEIAKWLASPVLVVLDTRGMARTVSAILKGLKIFDPDLNLAGAFANFTGSPSHIQLLKDASTEVPILGGLCKHSEQTFPERHLGLYSASEENVSEEKFNFWGEEGEKSLEVNSILEIANSAPEISIPVSNINTTLKRCKIGIAMDSAFHFYYEENLMRLRQAGAELVFFSPLSDSKLTDVDGLYFGGGYPEVFAPTLSKNKSLLNYIQDLSYKNIPIYAECGGLMYLSKGIKLVEGEFFPMLGLISATSIMEKKLKALGYVEVTTKKETIFGEVGLRFRGHQFRYSDLELDESNPIELVYNLRKRKSDQVSEEGYSKNSILASYIHAHWASNPNLAEGFVQSCLRK | Function: Catalyzes the ATP-dependent amidation of the two carboxylate groups at positions a and c of cobyrinate, using either L-glutamine or ammonia as the nitrogen source.
Catalytic Activity: 2 ATP + cob(II)yrinate + 2 H2O + 2 L-glutamine = 2 ADP + cob(II)yrinate a,c diamide + 2 H(+) + 2 L-glutamate + 2 phosphate
Sequence Mass (Da): 50165
Sequence Length: 454
Domain: Comprises of two domains. The C-terminal domain contains the binding site for glutamine and catalyzes the hydrolysis of this substrate to glutamate and ammonia. The N-terminal domain is anticipated to bind ATP and cobyrinate and catalyzes the ultimate synthesis of the diamide product. The ammonia produced via the glutaminase domain is probably translocated to the adjacent domain via a molecular tunnel, where it reacts with an activated intermediate.
Pathway: Cofactor biosynthesis; adenosylcobalamin biosynthesis; cob(II)yrinate a,c-diamide from sirohydrochlorin (anaerobic route): step 10/10.
EC: 6.3.5.11
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Q8Y7T0 | MNKILIAAASSGTGKTTVTLGIMHALKKRGLRVQPFKVGPDYIDTNYHQAITGVASINLDSFLIDDDAMLAALFEKHGQSADISVIEGVMGLFDGLGIDRDNSSTSFIAKCTKTPVILVVDGKAISTSAAAIVDGFNRFDPELTIAGVIINRVASENHFSLIKGAIERYTDVPVLGYLPKNAAVALPERHLGLVPKEEMTELETKWEVLGDLIAEHVDLDRLLAISKTGAKLTVHPPEIQVPDFSGMRVAYALDAAFHFYYQDNLDFIRSTGATLIPFSPLEEREVPDADFIYIGGGFPEVFAERLAKNKSMHESILAAHEQGKPIYAECGGLMYLGSSLEMEAESYEMVGVFDGVSKMTTRLRKFGYCIAEPLEDTLLGKKGTAIRGHEFHHSVFETTEPTRMKLTKKRDGETVKEWHGGYQKGNTFASYLHIHFYQNLAMITHMFGAIER | Function: Catalyzes the ATP-dependent amidation of the two carboxylate groups at positions a and c of cobyrinate, using either L-glutamine or ammonia as the nitrogen source.
Catalytic Activity: 2 ATP + cob(II)yrinate + 2 H2O + 2 L-glutamine = 2 ADP + cob(II)yrinate a,c diamide + 2 H(+) + 2 L-glutamate + 2 phosphate
Sequence Mass (Da): 49766
Sequence Length: 452
Domain: Comprises of two domains. The C-terminal domain contains the binding site for glutamine and catalyzes the hydrolysis of this substrate to glutamate and ammonia. The N-terminal domain is anticipated to bind ATP and cobyrinate and catalyzes the ultimate synthesis of the diamide product. The ammonia produced via the glutaminase domain is probably translocated to the adjacent domain via a molecular tunnel, where it reacts with an activated intermediate.
Pathway: Cofactor biosynthesis; adenosylcobalamin biosynthesis; cob(II)yrinate a,c-diamide from sirohydrochlorin (anaerobic route): step 10/10.
EC: 6.3.5.11
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A0L8B9 | MPYRIPRLFISATRKSSGKTFIAVGLTAALSARGLVVQPFKKGPDYIDPRWHSLAAGRECRNLDDFIMGRPKVLTSFVAHAQGADVAIIEGNLGLFDGQDLEGSDSSAALAKALGAPVLLVVDCKHLARSVAPLVCGHLHFPGGETIVGIILNNVATPRQEKRLREAIERFCPIPILGAIPRSAEIMIDERHLGLVPANEKQGAPHTVETMGRMMESHLDLDRLVALAATATPLALPDNPPALASKAPLVGGRPVRVGYAADQAFSFYYPDNLEALRQNGVELVPFSLLDEQPLPQVDGLYIGGGFPEMFMEHLQQNRATLETIRTRSELGMPIYAECGGLMVLSQRLIWAGKRVELAGALPIEITMHPKPQGYGYMKIHGTGALPWPPVDQEICCHEFHYSKVSKLGEGVRFAYQVTRGSGVDGWHDGILYHNIFASYAHIHVEGAPEWAPFLARFWRERGSFSQP | Function: Catalyzes the ATP-dependent amidation of the two carboxylate groups at positions a and c of cobyrinate, using either L-glutamine or ammonia as the nitrogen source.
Catalytic Activity: 2 ATP + cob(II)yrinate + 2 H2O + 2 L-glutamine = 2 ADP + cob(II)yrinate a,c diamide + 2 H(+) + 2 L-glutamate + 2 phosphate
Sequence Mass (Da): 51067
Sequence Length: 467
Domain: Comprises of two domains. The C-terminal domain contains the binding site for glutamine and catalyzes the hydrolysis of this substrate to glutamate and ammonia. The N-terminal domain is anticipated to bind ATP and cobyrinate and catalyzes the ultimate synthesis of the diamide product. The ammonia produced via the glutaminase domain is probably translocated to the adjacent domain via a molecular tunnel, where it reacts with an activated intermediate.
Pathway: Cofactor biosynthesis; adenosylcobalamin biosynthesis; cob(II)yrinate a,c-diamide from sirohydrochlorin (anaerobic route): step 10/10.
EC: 6.3.5.11
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Q46FL0 | MLNDKQSVENIPRILISADRSSSGKTTISMGLMAALVSRGYKVQPFKVALDYIDPSYHTEITGRFCRNLDGYLMDENGILDVYTHACEAGEKADIAIIEGVRGLYEGFESLSDLGSTAQIAKILNCPVIFVINARSITRSSAALINGYRNFDPDVEIAGVILNNIGSRRHAKKAKEAIEYYTGVPVIGIVPRDPAMQISMRHLGLMPALEGRRRLGDGGFEARLRGIEEIINKGIDVDRFMEIAKSAKALKSPENSVFSSVSDPGAPRPKIGVALDEAFNFYYRDNIDLLNLAGAEIVYFSPVKDASLPEVDGLYIGGGYPELFAAELEANESMRQDIKKASAAGMPIYAECGGLMYLTEKISTGVPGKGTYHDASMPESTYSMVGALPGHTIMGQTRVVSYNIGTLNKDCLLGKKYNSFKGHEFHHSEIREIPEDAEFAITLSRGTGIKNGMDGLISGNTLGSYAHLHGVAYREFASSLVEAARNFRDSRVLP | Function: Catalyzes the ATP-dependent amidation of the two carboxylate groups at positions a and c of cobyrinate, using either L-glutamine or ammonia as the nitrogen source (Potential). Involved in the biosynthesis of the unique nickel-containing tetrapyrrole coenzyme F430, the prosthetic group of methyl-coenzyme M reductase (MCR), which plays a key role in methanogenesis and anaerobic methane oxidation . Catalyzes the ATP-dependent amidation of the two carboxylate groups at positions a and c of Ni-sirohydrochlorin, using L-glutamine or ammonia as the nitrogen source . Also able to use sirohydrochlorin as substrate, but only produces a monoamide species in a much slower reaction . Unable to use other metallosirohydrochlorins such as sirohaem and Co-sirohydrochlorin .
Catalytic Activity: 2 ATP + cob(II)yrinate + 2 H2O + 2 L-glutamine = 2 ADP + cob(II)yrinate a,c diamide + 2 H(+) + 2 L-glutamate + 2 phosphate
Sequence Mass (Da): 53786
Sequence Length: 494
Domain: Comprises of two domains. The C-terminal domain contains the binding site for glutamine and catalyzes the hydrolysis of this substrate to glutamate and ammonia. The N-terminal domain is anticipated to bind ATP, and cobyrinate or Ni-sirohydrochlorin, and catalyzes the ultimate synthesis of the diamide product. The ammonia produced via the glutaminase domain is probably translocated to the adjacent domain via a molecular tunnel, where it reacts with an activated intermediate.
Pathway: Cofactor biosynthesis; adenosylcobalamin biosynthesis; cob(II)yrinate a,c-diamide from sirohydrochlorin (anaerobic route): step 10/10.
EC: 6.3.5.11
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Q58816 | MIMKRVVIAGTSSEVGKTVISTGIMKALSKKYNVQGYKVGPDYIDPTYHTIATGNKSRNLDSFFMNKEQIKYLFQKHSKDKDISVIEGVRGLYEGISAIDDIGSTASVAKALDSPIILLVNAKSLTRSAIAIIKGFMSFDNVKIKGVIFNFVRSENHIKKLKDAMSYYLPDIEIIGFIPRNEDFKVEGRHLGLVPTPENLKEIESKIVLWGELVEKYLDLDKIVEIADEDFEEVDDVFLWEVNENYKKIAVAYDKAFNFYYWDNFEALKENKAKIEFFSPLKDSEVPDADILYIGGGYPELFKEELSRNKEMIESIKEFDGYIYGECGGLMYITKSIDNVPMVGLLNCSAVMTKHVQGLSYVKAEFLEDCLIGRKGLKFKGHEFHYSKLVNIKEERFAYKIERGRGIINNLDGIFNGKVLAGYLHNHAVANPYFASSMVNFGE | Function: Catalyzes the ATP-dependent amidation of the two carboxylate groups at positions a and c of cobyrinate, using either L-glutamine or ammonia as the nitrogen source. Involved in the biosynthesis of the unique nickel-containing tetrapyrrole coenzyme F430, the prosthetic group of methyl-coenzyme M reductase (MCR), which plays a key role in methanogenesis and anaerobic methane oxidation. Catalyzes the ATP-dependent amidation of the two carboxylate groups at positions a and c of Ni-sirohydrochlorin, using L-glutamine or ammonia as the nitrogen source.
Catalytic Activity: 2 ATP + cob(II)yrinate + 2 H2O + 2 L-glutamine = 2 ADP + cob(II)yrinate a,c diamide + 2 H(+) + 2 L-glutamate + 2 phosphate
Sequence Mass (Da): 50206
Sequence Length: 443
Domain: Comprises of two domains. The C-terminal domain contains the binding site for glutamine and catalyzes the hydrolysis of this substrate to glutamate and ammonia. The N-terminal domain is anticipated to bind ATP, and cobyrinate or Ni-sirohydrochlorin, and catalyzes the ultimate synthesis of the diamide product. The ammonia produced via the glutaminase domain is probably translocated to the adjacent domain via a molecular tunnel, where it reacts with an activated intermediate.
Pathway: Cofactor biosynthesis; adenosylcobalamin biosynthesis; cob(II)yrinate a,c-diamide from sirohydrochlorin (anaerobic route): step 10/10.
EC: 6.3.5.11
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A1AT17 | MSINGFLIAAPQSGSGKTTISLAIMAALRRRGLVVAPFKCGPDFIDPGYHRMASGRASINLDGWMCPESFVAETFRLHAEAADVAVIEAVMGLFDGLGASPLQGSSAQIAAICGAPVVLVVNARGMAASAAALVKGFAEFDPDVRLAGVIFNNVGSAGHAELLARVMASALPEIALLGCIPRDEALAIPSRHLGLVTAEDNPLPPEYLDRLADLAEKHLDLAGLAGLRITPRSVGASLSRTNGGGMLPVRIAVARDAAFCFVYQDNLRLLREAGGELLFFSPLADGALPEGISGIYLPGGYPELYAERLAVNVPMLDAIRGAARDGMPLYAECGGFIYLTRGMEDSQGAPLADFAGIFPVRARMLPKRKALGYRQVECLSVSILGPAGETARGHEFHYSEICEMPVDVTRTYSVTRQGAFLGQEGYCLSNCLASYVHLHFGSNPCLAPSLVAACRKFAATRRS | Function: Catalyzes the ATP-dependent amidation of the two carboxylate groups at positions a and c of cobyrinate, using either L-glutamine or ammonia as the nitrogen source.
Catalytic Activity: 2 ATP + cob(II)yrinate + 2 H2O + 2 L-glutamine = 2 ADP + cob(II)yrinate a,c diamide + 2 H(+) + 2 L-glutamate + 2 phosphate
Sequence Mass (Da): 48879
Sequence Length: 463
Domain: Comprises of two domains. The C-terminal domain contains the binding site for glutamine and catalyzes the hydrolysis of this substrate to glutamate and ammonia. The N-terminal domain is anticipated to bind ATP and cobyrinate and catalyzes the ultimate synthesis of the diamide product. The ammonia produced via the glutaminase domain is probably translocated to the adjacent domain via a molecular tunnel, where it reacts with an activated intermediate.
Pathway: Cofactor biosynthesis; adenosylcobalamin biosynthesis; cob(II)yrinate a,c-diamide from sirohydrochlorin (anaerobic route): step 10/10.
EC: 6.3.5.11
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Q6L2V8 | MKINSIIIGAPSSSSGKTTISIGIMRALSRRLRVQPFKVGPDYIDPGYHNIATGRFSSNLDTWMSSREKMKEIFIKRSTGSDISIIEGVMGLYDGKQPDKDTGSTAEVARTLKSPVIIVIDISAMARTAAAIILGLIKMDKRLRISGVILNNAGSDYHCSIVRTAIEKYTGIPVIGCVKRSDDLKIDDRYLGLKTAMEDDNSGKIDKIADIIERSVDLDLLIKISKESGDISFKSGLFSKKNVNRVRIAIAYDAAFNFYYYDNIEMLKMYGAEIVYFSPLNDYKLPEADGLYIGGGFPELFAERLSDNYSIKKDIMEFFNSGRPVFAECGGYMYLSRGIKINGKYYEMASIINGESYMDSLILGYRNIRAESNNILMMGGWHVKGHEFHYSRLNVNANAYKTERGPDGISTKNLLAGYMHLYFPSNPRIPERFVRSCYNV | Function: Catalyzes the ATP-dependent amidation of the two carboxylate groups at positions a and c of cobyrinate, using either L-glutamine or ammonia as the nitrogen source.
Catalytic Activity: 2 ATP + cob(II)yrinate + 2 H2O + 2 L-glutamine = 2 ADP + cob(II)yrinate a,c diamide + 2 H(+) + 2 L-glutamate + 2 phosphate
Sequence Mass (Da): 49267
Sequence Length: 440
Domain: Comprises of two domains. The C-terminal domain contains the binding site for glutamine and catalyzes the hydrolysis of this substrate to glutamate and ammonia. The N-terminal domain is anticipated to bind ATP and cobyrinate and catalyzes the ultimate synthesis of the diamide product. The ammonia produced via the glutaminase domain is probably translocated to the adjacent domain via a molecular tunnel, where it reacts with an activated intermediate.
Pathway: Cofactor biosynthesis; adenosylcobalamin biosynthesis; cob(II)yrinate a,c-diamide from sirohydrochlorin (anaerobic route): step 10/10.
EC: 6.3.5.11
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Q7VEH6 | MRGFTLPVWVVAAAKAAVKVLIGESWQSHEVIELLNNEESIVVPIRSASILDNGEKALGITNCDPGECLDLTRGLEIWVCLRYIENQQIISSDGLELEPWLKIIPGYGVGKFDLTNDISISEFARQLLIVNLKPYRKEGYSLNLEIIFPSGQELAEKTSNHAFGVVDGLALIGTQADVQESASPKKLQSTIHALRSRCAESSFTGSLIFVIGENGLDLALQYGIDSSKIIKTGNWLGPLLVAAAQEKVQQLLIFGYHGKLIKLAGGVFHTHHHLADNRLETLIAFAVKERIPLSLIKEFEEAVSIEAALSILENKDISTAKKLWKRLAVEIEKRSIDYVKRYETSSIEIGAVMFDRARKIRWAGNYALKQINSFGLKLEDY | Function: Catalyzes the methylation of C-1 in cobalt-precorrin-5B to form cobalt-precorrin-6A.
Catalytic Activity: Co-precorrin-5B + S-adenosyl-L-methionine = Co-precorrin-6A + S-adenosyl-L-homocysteine
Sequence Mass (Da): 42287
Sequence Length: 381
Pathway: Cofactor biosynthesis; adenosylcobalamin biosynthesis; cob(II)yrinate a,c-diamide from sirohydrochlorin (anaerobic route): step 6/10.
EC: 2.1.1.195
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Q48DG3 | MREETAEQPAPLRSGLTTGSCATATSLAAARLLLSGQISDAVEIVLPKGKQVQMRLEFCRLVDNFAEAGTLKDAGDDPDVTHGALVFARVRLEMAPGVRFVAGAGVGSVTRPGLVLAVGEPAINPVPRRMMTEHLLQLAEELGYSGGFEVTIGVEGGEALALKTMNPRLGILGGLSILGTSGIVRPFSCAAYIASIHQGIDVATTNGYRHIAACTGNASEDTMRRVYNIPDIALIEMGDFVGAVLKHLRKVPVDKLSLCGGFGKISKLAAGHMDLHSRHSSIDLPQLALWAADTGADADLQQRIRDANTSQQALAMCATAGVPLGDEVCRHALAFARSVVPAQVQVEVFAIDRQGGIVGQAGVALSKEHT | Function: Catalyzes the methylation of C-1 in cobalt-precorrin-5B to form cobalt-precorrin-6A.
Catalytic Activity: Co-precorrin-5B + S-adenosyl-L-methionine = Co-precorrin-6A + S-adenosyl-L-homocysteine
Sequence Mass (Da): 38787
Sequence Length: 370
Pathway: Cofactor biosynthesis; adenosylcobalamin biosynthesis; cob(II)yrinate a,c-diamide from sirohydrochlorin (anaerobic route): step 6/10.
EC: 2.1.1.195
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Q8ZZB0 | MNPFLKYGITTGLAAAAAAKAAALYSKGIVPKSVTVPTPIGLRVEVFVERVFQRGEIYCAEVRKFSGDNPDVLNGVIIRACVRPLNNGVVIKGGEGVGIVTRPGLPVPPGEHAINPVPRRMIEEAVREVLEGAEVLVEVPDGKLLAEKTMNPRLGIVGGISILGTTGIEAPVSADEFLGHIEAELSALRERRDIAILAQGNTSYKAAQAVFGDVVVKIGDMVGYAVEKAAALGYKAAYLFTMPGKLAKLALGAYNTHSAQCDGRVEAVLYALVKLRAPYEVLLEVSNAASVGEALAKAGDYAGGVIAIMARRAKEYLERFKIPVEIYVVNDKGEVLFSTT | Function: Catalyzes the methylation of C-1 in cobalt-precorrin-5B to form cobalt-precorrin-6A.
Catalytic Activity: Co-precorrin-5B + S-adenosyl-L-methionine = Co-precorrin-6A + S-adenosyl-L-homocysteine
Sequence Mass (Da): 36015
Sequence Length: 340
Pathway: Cofactor biosynthesis; adenosylcobalamin biosynthesis; cob(II)yrinate a,c-diamide from sirohydrochlorin (anaerobic route): step 6/10.
EC: 2.1.1.195
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A5UJR5 | MLNDMDFIKTCDVPGPTKEAIRAIILYKSAVTPNDEVVDVGCGTGGITCEFAQRAKKVTSIDTNPDAISVTKQNLEKFNLGDNVELINDSGSNALKNIDNMDIAVVGGSGRELEDILEIIDSKLNPKGRIIVTAILVDTKIEAINKLKKLNYNPKIMEVNISNGRVLDRGVMMISENPIAIISANKR | Function: Catalyzes the methylation of C-15 in cobalt-precorrin-6B followed by the decarboxylation of C-12 to form cobalt-precorrin-7.
Catalytic Activity: Co-precorrin-6B + S-adenosyl-L-methionine = Co-precorrin-7 + CO2 + S-adenosyl-L-homocysteine
Sequence Mass (Da): 20313
Sequence Length: 187
Pathway: Cofactor biosynthesis; adenosylcobalamin biosynthesis; cob(II)yrinate a,c-diamide from sirohydrochlorin (anaerobic route): step 8/10.
EC: 2.1.1.196
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O26249 | MIPDDEFIKNPSVPGPTAMEVRCLIMCLAEPGKNDVAVDVGCGTGGVTLELAGRVRRVYAIDRNPEAISTTEMNLQRHGLGDNVTLMEGDAPEALCKIPDIDIAVVGGSGGELQEILRIIKDKLKPGGRIIVTAILLETKFEAMECLRDLGFDVNITELNIARGRALDRGTMMVSRNPVALIYTGVSHENKD | Function: Catalyzes the methylation of C-15 in cobalt-precorrin-6B followed by the decarboxylation of C-12 to form cobalt-precorrin-7.
Catalytic Activity: Co-precorrin-6B + S-adenosyl-L-methionine = Co-precorrin-7 + CO2 + S-adenosyl-L-homocysteine
Sequence Mass (Da): 20714
Sequence Length: 192
Pathway: Cofactor biosynthesis; adenosylcobalamin biosynthesis; cob(II)yrinate a,c-diamide from sirohydrochlorin (anaerobic route): step 8/10.
EC: 2.1.1.196
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Q8ZZA9 | MSWPYATPGIPDEEFIRAEGVPMTKAEIRALALSKLRLIKGGTLVDVGCGTGTISVEAALIMGEGSKVYAIDKDPLAVEITKKNAAKFGVGDRLIVAEGDALELLPKLPRSNRYFLGGGGRELPMLFQTALELAGTGGVIVADVITLESLRLALDFLENAGVKYEIAQVYIARGRRLGGYTILSPLNPVYIITAYA | Function: Catalyzes the methylation of C-15 in cobalt-precorrin-6B followed by the decarboxylation of C-12 to form cobalt-precorrin-7.
Catalytic Activity: Co-precorrin-6B + S-adenosyl-L-methionine = Co-precorrin-7 + CO2 + S-adenosyl-L-homocysteine
Sequence Mass (Da): 20910
Sequence Length: 196
Pathway: Cofactor biosynthesis; adenosylcobalamin biosynthesis; cob(II)yrinate a,c-diamide from sirohydrochlorin (anaerobic route): step 8/10.
EC: 2.1.1.196
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Q97WC7 | MEWNYVIPGIPDNLFERDEEIPMTKEEIRALALSKLRIKKGDKVLDIGCGTGSITVEASLLVGNSGRVYGIDKEEKAINLTRRNAEKFGVLNNIVLIKGEAPAILSTINEKFDRIFIGGGSEKIKEIISASWEIINKGGRIVIDAILLETVNNALSAMEKIGFVNLEITEVIIAKGMKTKVGTAMMARNPIFIISGEKP | Function: Catalyzes the methylation of C-15 in cobalt-precorrin-6B followed by the decarboxylation of C-12 to form cobalt-precorrin-7.
Catalytic Activity: Co-precorrin-6B + S-adenosyl-L-methionine = Co-precorrin-7 + CO2 + S-adenosyl-L-homocysteine
Sequence Mass (Da): 21799
Sequence Length: 199
Pathway: Cofactor biosynthesis; adenosylcobalamin biosynthesis; cob(II)yrinate a,c-diamide from sirohydrochlorin (anaerobic route): step 8/10.
EC: 2.1.1.196
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Q05632 | MKDELFLRGENVPMTKEAVRALALSKLELHRASHLIDVGAGTGSVSIEAALQFPSLQVTAIERNPAALRLLDENRQRFACGNIDILPGEAPMTITGKADAVFMGGSGGHLTALIDWAMGHLHPGGRLVMTFILQENLHSALAHLAHIGACRMDCVQLQLSSLTPLGAGHYFKPNNPVFVIACQKEENHVRDI | Function: Catalyzes the methylation of C-15 in cobalt-precorrin-6B followed by the decarboxylation of C-12 to form cobalt-precorrin-7.
Catalytic Activity: Co-precorrin-6B + S-adenosyl-L-methionine = Co-precorrin-7 + CO2 + S-adenosyl-L-homocysteine
Sequence Mass (Da): 20746
Sequence Length: 192
Pathway: Cofactor biosynthesis; adenosylcobalamin biosynthesis; cob(II)yrinate a,c-diamide from sirohydrochlorin (anaerobic route): step 8/10.
EC: 2.1.1.196
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Q4JBL7 | MRVPGIPDEEFIREEKIPMTKEEIRVLALSKARLFYGAKFLDVGSGTGSVSVEAGLIVGEKGKVYAVERDPQAVELTRKNVEKFSLRNVEIIEGEAPEVLNKINDELDSAFIGGTERLEEIIPVVSEKIRRGGMIVLDAILIESAVKALHTLSELGYKAEVIEVIVAKGMKTSKGYAMISRNPIFIIYGEKK | Function: Catalyzes the methylation of C-15 in cobalt-precorrin-6B followed by the decarboxylation of C-12 to form cobalt-precorrin-7.
Catalytic Activity: Co-precorrin-6B + S-adenosyl-L-methionine = Co-precorrin-7 + CO2 + S-adenosyl-L-homocysteine
Sequence Mass (Da): 21191
Sequence Length: 192
Pathway: Cofactor biosynthesis; adenosylcobalamin biosynthesis; cob(II)yrinate a,c-diamide from sirohydrochlorin (anaerobic route): step 8/10.
EC: 2.1.1.196
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B9K7M6 | MKFGYFDDKNREYVIVTPRTPYPWINYLGTEDFFSIISHMAGGYCFYKDARLRRITRFRYNNVPTDAGGRYFYIREEDGDFWSPTWMPVRRDLSFFEARHGLGYTKIAGERNGLRATITFFVPRHFTGEVHHLVLQNRTERPRRIKLFSFIEFCLWNALDDMTNFQRNYSTGEVEIEGSVIYHKTEYRERRNHYAFYSVNHSIDGFDTDRESFMGLYNGFEAPQAVVEGNPRNSVASGWAPIASHYLELEIPPLGEKELIFILGYVENPEEEKWERPGVINKKRAKEMIERFKTGEDVERALKELKEYWDELLGRIQVETHDEKLNRMVNIWNQYQCMVTFNIARSASYFESGISRGIGFRDSNQDILGFVHMIPEKARQRILDLASIQFEDGSTYHQFQPLTKKGNNEIGGGFNDDPLWLILSTSAYIKETGDWSILNEEVPFDNDPDKKATLFEHLKRSFYFTVNNLGPHGLPLIGRADWNDCLNLNCFSKNPDESFQTTVNALDGRVAESVFIAGLFVLAGKEFVEICRRLGLEDEAKEAEKHVKKMIETTLEYGWDGEWFLRAYDAFGRKVGSKECEEGKIFIEPQGMCVMAGIGVENGYAKKALDSVKEHLDTPYGLVLQQPAYSRYYIELGEISSYPPGYKENAGIFCHNNPWVAIAETVIGRGDRAFEIYRKITPAYLEDISEIHRTEPYVYAQMVAGKDAPRHGEAKNSWLTGTAAWSFVAITQYILGVRPTYDGLMVDPCIPEDWDGFKITRRFRGATYEITVKNPHHVSKGVKEIIVDGKKIEGQVLPVFNDGKVHRVEVLMG | Function: Catalyzes the phosphorolysis of cellobiose, yielding glucose 1-phosphate and glucose. Is inactive against cellotriose and the disaccharides lactose, chitobiose and xylobiose. May be the primary enzyme for processing cellobiose in T.neapolitana.
Catalytic Activity: D-cellobiose + phosphate = alpha-D-glucose 1-phosphate + D-glucose
Sequence Mass (Da): 93679
Sequence Length: 813
Pathway: Glycan metabolism; cellulose degradation.
EC: 2.4.1.20
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A0A1S4F020 | MIPRIVVVLLSVLAVVTARRSYEGYKVYGIVPESPDEAEILYQIRQSNPDLDFWHLTKQPGDEARVLVAPKDQRSFLIKLIRHGLHYQEVISDVEGTLAPYNEPRTRGMSLDRDVSTSYLRHNEINEYLQTLSQKYPSLVSVEEAGTSYEGRSIKTITINKKPGNAVVFLDAGIHAREWIAPATALYAIEQLVEHSSENQEVLSNLTWVIMPVVNPDGYEFSHETDRFWRKTRKPTGKTCKGTDGNRNFDYHWGEVGASTQACADTFRGETAFSEPETRAVRDAVMKLKGSCKFYLSLHSYGNYILYPWGWTSKLPETWEAIDEVAQAGAEAIKQSTGSRYTVGSSTNVLYAAAGGSDDWAFAVAEVPISITMELPGGGNGGFNPPPSSIEKIVNESWVGIKAMALKVAQMF | Cofactor: Binds 1 zinc ion per subunit.
Function: Carboxypeptidase that preferentially hydrolyzes arginine and lysine residues at the C-terminus . During infection by dengue virus, may play a role in preventing viral packaging, maturation, and release from the midgut .
Catalytic Activity: Preferential release of a C-terminal lysine or arginine amino acid.
Sequence Mass (Da): 45840
Sequence Length: 412
Subcellular Location: Endoplasmic reticulum
EC: 3.4.17.2
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P55261 | MAFLILVTLALASAHYSGEHFEGEKVFRVNVEDENHINLLHTLASTTQIDFWKPDSVTQIKPHSTADFRVKAEDILTVEDFLKQNELHYEVLINNLRLVLEGQFGRQVPATGHSYEKYNRWETIEAWTQQVTSENPDLISRRSIGTTFEGRTIYLLKVGKAGQNKPAIFMDCGFHAREWISPAFWQWFVREXIRTYGQEIHMTELLDKLDFYVLPVGNIDGYVYTWTKNRMWRKTRSTQVGTNCVGTDPTRNFDAGWCKIGASRNPCDETYCGPAAESEKETKALANFIRSNLSSIKAYLTIHSYSQMMLYPYSYDYKLTENNAELNALAKATVKELATLHGTKYTYGPGATTIYPAAGGSDDWAYDQGIKYSFTFELRDKGRYGFALPESQISPTCEETLLAIKHLARYVLQHLY | Cofactor: Binds 1 zinc ion per subunit.
Catalytic Activity: Preferential release of a C-terminal lysine or arginine amino acid.
Sequence Mass (Da): 47597
Sequence Length: 416
Subcellular Location: Secreted
EC: 3.4.17.2
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P15086 | MLALLVLVTVALASAHHGGEHFEGEKVFRVNVEDENHINIIRELASTTQIDFWKPDSVTQIKPHSTVDFRVKAEDTVTVENVLKQNELQYKVLISNLRNVVEAQFDSRVRATGHSYEKYNKWETIEAWTQQVATENPALISRSVIGTTFEGRAIYLLKVGKAGQNKPAIFMDCGFHAREWISPAFCQWFVREAVRTYGREIQVTELLDKLDFYVLPVLNIDGYIYTWTKSRFWRKTRSTHTGSSCIGTDPNRNFDAGWCEIGASRNPCDETYCGPAAESEKETKALADFIRNKLSSIKAYLTIHSYSQMMIYPYSYAYKLGENNAELNALAKATVKELASLHGTKYTYGPGATTIYPAAGGSDDWAYDQGIRYSFTFELRDTGRYGFLLPESQIRATCEETFLAIKYVASYVLEHLY | Cofactor: Binds 1 zinc ion per subunit.
Catalytic Activity: Preferential release of a C-terminal lysine or arginine amino acid.
Sequence Mass (Da): 47368
Sequence Length: 417
Subcellular Location: Secreted
EC: 3.4.17.2
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P16152 | MSSGIHVALVTGGNKGIGLAIVRDLCRLFSGDVVLTARDVTRGQAAVQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGGLDVLVNNAGIAFKVADPTPFHIQAEVTMKTNFFGTRDVCTELLPLIKPQGRVVNVSSIMSVRALKSCSPELQQKFRSETITEEELVGLMNKFVEDTKKGVHQKEGWPSSAYGVTKIGVTVLSRIHARKLSEQRKGDKILLNACCPGWVRTDMAGPKATKSPEEGAETPVYLALLPPDAEGPHGQFVSEKRVEQW | Function: NADPH-dependent reductase with broad substrate specificity. Catalyzes the reduction of a wide variety of carbonyl compounds including quinones, prostaglandins, menadione, plus various xenobiotics. Catalyzes the reduction of the antitumor anthracyclines doxorubicin and daunorubicin to the cardiotoxic compounds doxorubicinol and daunorubicinol . Can convert prostaglandin E to prostaglandin F2-alpha (By similarity). Can bind glutathione, which explains its higher affinity for glutathione-conjugated substrates. Catalyzes the reduction of S-nitrosoglutathione . In addition, participates in the glucocorticoid metabolism by catalyzing the NADPH-dependent cortisol/corticosterone into 20beta-dihydrocortisol (20b-DHF) or 20beta-corticosterone (20b-DHB), which are weak agonists of NR3C1 and NR3C2 in adipose tissue .
Catalytic Activity: a secondary alcohol + NADP(+) = a ketone + H(+) + NADPH
Sequence Mass (Da): 30375
Sequence Length: 277
Subcellular Location: Cytoplasm
EC: 1.1.1.184
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Q28960 | MSSNTRVALVTGANKGIGFAIVRDLCRQFAGDVVLTARDVARGQAAVKQLQAEGLSPRFHQLDIIDLQSIRALCDFLRKEYGGLDVLVNNAAIAFQLDNPTPFHIQAELTMKTNFMGTRNVCTELLPLIKPQGRVVNVSSTEGVRALNECSPELQQKFKSETITEEELVGLMNKFVEDTKNGVHRKEGWSDSTYGVTKIGVSVLSRIYARKLREQRAGDKILLNACCPGWVRTDMGGPKAPKSPEVGAETPVYLALLPSDAEGPHGQFVTDKKVVEWGVPPESYPWVNA | Function: NADPH-dependent reductase with broad substrate specificity. Catalyzes the reduction of a wide variety of carbonyl compounds including quinones, prostaglandins, menadione, plus various xenobiotics. Catalyzes the reduction of the antitumor anthracyclines doxorubicin and daunorubicin to the cardiotoxic compounds doxorubicinol and daunorubicinol. Can convert prostaglandin E2 to prostaglandin F2-alpha . Can bind glutathione, which explains its higher affinity for glutathione-conjugated substrates. Catalyzes the reduction of S-nitrosoglutathione. In addition, participates in the glucocorticoid metabolism by catalyzing the NADPH-dependent cortisol/corticosterone into 20beta-dihydrocortisol (20b-DHF) or 20beta-corticosterone (20b-DHB), which are weak agonists of NR3C1 and NR3C2 in adipose tissue (By similarity).
Catalytic Activity: a secondary alcohol + NADP(+) = a ketone + H(+) + NADPH
Sequence Mass (Da): 31693
Sequence Length: 289
Subcellular Location: Cytoplasm
EC: 1.1.1.184
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P47844 | MPSDRRVALVTGANKGVGFAITRALCRLFSGDVLLTAQDEAQGQAAVQQLQAEGLSPRFHQLDITDLQSIRALRDFLRRAYGGLNVLVNNAVIAFKMEDTTPFHIQAEVTMKTNFDGTRDVCTELLPLMRPGGRVVNVSSMTCLRALKSCSPELQQKFRSETITEEELVGLMKKFVEDTKKGVHQTEGWPDTAYGVTKMGVTVLSRIQARHLSEHRGGDKILVNACCPGWVRTDMGGPNATKSPEEGAETPVYLALLPPDAEGPHGQFVMDKKVEQW | Function: NADPH-dependent reductase with broad substrate specificity. Catalyzes the reduction of a wide variety of carbonyl compounds including quinones, prostaglandins, menadione, plus various xenobiotics. Catalyzes the reduction of the antitumor anthracyclines doxorubicin and daunorubicin to the cardiotoxic compounds doxorubicinol and daunorubicinol (By similarity). Can convert prostaglandin E to prostaglandin F2-alpha (By similarity). Can bind glutathione, which explains its higher affinity for glutathione-conjugated substrates. Catalyzes the reduction of S-nitrosoglutathione. In addition, participates in the glucocorticoid metabolism by catalyzing the NADPH-dependent cortisol/corticosterone into 20beta-dihydrocortisol (20b-DHF) or 20beta-corticosterone (20b-DHB), which are weak agonists of NR3C1 and NR3C2 in adipose tissue (By similarity).
Catalytic Activity: a secondary alcohol + NADP(+) = a ketone + H(+) + NADPH
Sequence Mass (Da): 30452
Sequence Length: 277
Subcellular Location: Cytoplasm
EC: 1.1.1.184
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P08074 | MKLNFSGLRALVTGAGKGIGRDTVKALHASGAKVVAVTRTNSDLVSLAKECPGIEPVCVDLGDWDATEKALGGIGPVDLLVNNAALVIMQPFLEVTKEAFDRSFSVNLRSVFQVSQMVARDMINRGVPGSIVNVSSMVAHVTFPNLITYSSTKGAMTMLTKAMAMELGPHKIRVNSVNPTVVLTDMGKKVSADPEFARKLKERHPLRKFAEVEDVVNSILFLLSDRSASTSGGGILVDAGYLAS | Function: May function in the pulmonary metabolism of endogenous carbonyl compounds, such as aliphatic aldehydes and ketones derived from lipid peroxidation, 3-ketosteroids and fatty aldehydes, as well as in xenobiotic metabolism.
Catalytic Activity: a secondary alcohol + NADP(+) = a ketone + H(+) + NADPH
Sequence Mass (Da): 25958
Sequence Length: 244
Subcellular Location: Mitochondrion matrix
EC: 1.1.1.184
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Q29529 | MQMNFSGLRALVTGAGKGIGRDTVKALHVSGARVVAVTRTNGDLVSLSQECPGIEPVCVDLGDWEATERALGGVGPVDLLVNNAAVALMQPFLDTTKEVFDRSFNVNLRSVFQVSQIVARSMIERGVPGSIVNVSSMVSHVTYPGLAAYSSTKGAMTMLTKSMAMELGPHKIRVNSVNPTVVLTAMGRSVTSDPELARKLKERHPMRKFAEVEDVVNSILFLLSDRSASTSGSSIFVDAGYLAS | Function: May function in the pulmonary metabolism of endogenous carbonyl compounds, such as aliphatic aldehydes and ketones derived from lipid peroxidation, 3-ketosteroids and fatty aldehydes, as well as in xenobiotic metabolism.
Catalytic Activity: a secondary alcohol + NADP(+) = a ketone + H(+) + NADPH
Sequence Mass (Da): 25986
Sequence Length: 244
Subcellular Location: Mitochondrion matrix
EC: 1.1.1.184
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O75828 | MSSCSRVALVTGANRGIGLAIARELCRQFSGDVVLTARDVARGQAAVQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGGLNVLVNNAAVAFKSDDPMPFDIKAEMTLKTNFFATRNMCNELLPIMKPHGRVVNISSLQCLRAFENCSEDLQERFHSETLTEGDLVDLMKKFVEDTKNEVHEREGWPNSPYGVSKLGVTVLSRILARRLDEKRKADRILVNACCPGPVKTDMDGKDSIRTVEEGAETPVYLALLPPDATEPQGQLVHDKVVQNW | Function: Catalyzes the NADPH-dependent reduction of carbonyl compounds to their corresponding alcohols . Has low NADPH-dependent oxidoreductase activity. Acts on several orthoquinones, acts as well on non-quinone compounds, such as isatin or on the anticancer drug oracin . Best substrates for CBR3 is 1,2- naphthoquinone, hence could play a role in protection against cytotoxicity of exogenous quinones . Exerts activity toward ortho-quinones but not paraquinones. No endogenous substrate for CBR3 except isatin has been identified .
Catalytic Activity: a secondary alcohol + NADP(+) = a ketone + H(+) + NADPH
Sequence Mass (Da): 30850
Sequence Length: 277
Subcellular Location: Cytoplasm
EC: 1.1.1.184
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Q8K354 | MSSCSRVALVTGANKGIGFAITRDLCRKFSGDVVLTARDEARGRAAVQQLQAEGLSPRFHQLDIDDPQSIRALRDFLRKEYGGLNVLVNNAGIAFRMDDPTPFDIQAEVTLKTNFFATRNVCTELLPIMKPHGRVVNISSLQGLKALENCREDLQEKFRCDTLTEVDLVDLMKKFVEDTKNEVHEREGWPDSAYGVSKLGVTVLTRILARQLDEKRKADRILLNACCPGWVKTDMARDQGSRTVEEGAETPVYLALLPPDATEPHGQLVRDKVVQTW | Function: Catalyzes the NADPH-dependent reduction of carbonyl compounds to their corresponding alcohols. Has low NADPH-dependent oxidoreductase activity. Acts on several orthoquinones, acts as well on non-quinone compounds, such as isatin or on the anticancer drug oracin. Best substrates for CBR3 is 1,2- naphthoquinone, hence could play a role in protection against cytotoxicity of exogenous quinones. Exerts activity toward ortho-quinones but not paraquinones. No endogenous substrate for CBR3 except isatin has been identified.
Catalytic Activity: a secondary alcohol + NADP(+) = a ketone + H(+) + NADPH
Sequence Mass (Da): 30953
Sequence Length: 277
Subcellular Location: Cytoplasm
EC: 1.1.1.184
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A4IFA7 | MDKVCAVFGGSRGIGRAVARLMAQRGYRLAIVARNLEGARAAAGDLGGDHLALSCDVAKEHDVQNTFEEIEKNLGRVNFLVNAAGINRDNLLVRTNTEDMLSQLHTNLLGSMLTCRAALKTMIKQQRGSIVNVGSVVGLKGNSGQSVYSASKGGLVGFSRALAKEVAKKKIRVNVVAPGFIHTDMTKDLNEELLKKNIPLGRFGDALDVAQAAVFLLESPYVTGHVLVVDGGLQLTM | Function: Component of the heterotetramer complex KAR (3-ketoacyl-[acyl carrier protein] reductase or 3-ketoacyl-[ACP] reductase) that forms part of the mitochondrial fatty acid synthase (mtFAS). Beta-subunit of the KAR heterotetramer complex, responsible for the 3-ketoacyl-ACP reductase activity of the mtFAS, reduces 3-oxoacyl-[ACP] to (3R)-hydroxyacyl-[ACP] in a NADPH-dependent manner with no chain length preference, thereby participating in mitochondrial fatty acid biosynthesis. The homotetramer has NADPH-dependent quinone reductase activity (in vitro), hence could play a role in protection against cytotoxicity of exogenous quinones. As a heterotetramer, it can also reduce 9,10-phenanthrenequinone, 1,4-benzoquinone and various other o-quinones and p-quinones (in vitro).
Catalytic Activity: a (3R)-hydroxyacyl-[ACP] + NADP(+) = a 3-oxoacyl-[ACP] + H(+) + NADPH
Sequence Mass (Da): 25269
Sequence Length: 237
Pathway: Lipid metabolism; fatty acid biosynthesis.
Subcellular Location: Mitochondrion matrix
EC: 1.1.1.100
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Q6P0H7 | MSRLAVVFGGSRGIGRAASKLLAQRGHRIVLLSRNKEAAQSTAQSLPGENHLGLSCDVSKEEEVQKAFETINKTCGTVGFLVNAAGINRDALLLRSKSEDMLSVLHTNLLGSMLTCKAAVRNMLSHGGAIVNIGSVVGVKGNAGQCVYSASKAGLEGFTRSLAKEVASRNIRVNLVAPGLIHTDMTAGLAEEAAVRTIPLGRFGEPAEVAQAMLFLLESPYITGQILLVDGGLQLLM | Function: The heterotetramer with HSD17B8 has NADH-dependent 3-ketoacyl-acyl carrier protein reductase activity, and thereby plays a role in mitochondrial fatty acid biosynthesis. Within the heterotetramer, HSD17B8 binds NADH; CBR4 binds NADPD. The homotetramer has NADPH-dependent quinone reductase activity. Both homotetramer and the heterotetramer have broad in vitro substrate specificity and can reduce 9,10-phenanthrenequinone, 1,4-benzoquinone and various other o-quinones and p-quinones.
Sequence Mass (Da): 24879
Sequence Length: 237
Pathway: Lipid metabolism; fatty acid biosynthesis.
Subcellular Location: Mitochondrion matrix
EC: 1.-.-.-
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Q8N4T8 | MDKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDLGGDHLAFSCDVAKEHDVQNTFEELEKHLGRVNFLVNAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGSIVGLKGNSGQSVYSASKGGLVGFSRALAKEVARKKIRVNVVAPGFVHTDMTKDLKEEHLKKNIPLGRFGETIEVAHAVVFLLESPYITGHVLVVDGGLQLIL | Function: Component of the heterotetramer complex KAR (3-ketoacyl-[acyl carrier protein] reductase or 3-ketoacyl-[ACP] reductase) that forms part of the mitochondrial fatty acid synthase (mtFAS). Beta-subunit of the KAR heterotetramer complex, responsible for the 3-ketoacyl-ACP reductase activity of the mtFAS, reduces 3-oxoacyl-[ACP] to (3R)-hydroxyacyl-[ACP] in a NADPH-dependent manner with no chain length preference, thereby participating in mitochondrial fatty acid biosynthesis . The homotetramer has NADPH-dependent quinone reductase activity (in vitro), hence could play a role in protection against cytotoxicity of exogenous quinones . As a heterotetramer, it can also reduce 9,10-phenanthrenequinone, 1,4-benzoquinone and various other o-quinones and p-quinones (in vitro) .
Catalytic Activity: a (3R)-hydroxyacyl-[ACP] + NADP(+) = a 3-oxoacyl-[ACP] + H(+) + NADPH
Sequence Mass (Da): 25301
Sequence Length: 237
Pathway: Lipid metabolism; fatty acid biosynthesis.
Subcellular Location: Mitochondrion matrix
EC: 1.1.1.100
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Q97PP9 | MRLTQMPSEFQKALPVLEKIKEAGFEAYFVGGSVRDALLHSPIHDVDIATSSYPEETKQIFPRTADIGIEHGTVLVLDGDEEYEVTTFRTEDVYVDYRRPSAVSFVRSLEEDLKRRDFTVNAFALDETGEIVDLFHGLEDLEKQVLRAVGVASERFNEDALRIMRGFRFQASLGFALEPETFKAMKTLTPLLEKISVERTFVEFDKLLLAPFWRRGLASMIESQAYDYLPDMASSQDKLNRLFDLETDFTFESSEQAWAALLWALEIENAQSFLKSWKTSRQFAKQVQDLLIILALRENGELSKRDCYRFDIDLLLQAENLRQAQGKEVNPQAITEKYQSLTIHDKKEIQINGGILIKEYGYQPGPDLGEILTEIEFAIVDGELENNREAIHAYLREKK | Function: Catalyzes the addition and repair of the essential 3'-terminal CCA sequence in tRNAs without using a nucleic acid template. Adds these three nucleotides in the order of C, C, and A to the tRNA nucleotide-73, using CTP and ATP as substrates and producing inorganic pyrophosphate. tRNA 3'-terminal CCA addition is required both for tRNA processing and repair. Also involved in tRNA surveillance by mediating tandem CCA addition to generate a CCACCA at the 3' terminus of unstable tRNAs. While stable tRNAs receive only 3'-terminal CCA, unstable tRNAs are marked with CCACCA and rapidly degraded.
Catalytic Activity: a tRNA precursor + ATP + 2 CTP = a tRNA with a 3' CCA end + 3 diphosphate
Sequence Mass (Da): 45787
Sequence Length: 399
EC: 2.7.7.72
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Q3SZX8 | MVFYFTSSSVNSSAYTIYMGKDKYENEDLIKYGWPEDIWFHVDKLSSAHVYLRLHKGEKIEDIPKEVLMDCAHLVKANSIQGCKMNNVNVVYTPWSNLKKTADMDVGQIGFHRQKDVKIVTVEKKVNEILNRLEKTKMERFPDLEAEKECRDHEERNEKKAQIQEMKRREKEEMKKKREMDELRSYSSLMKVENMSSNQDGNDSDEFM | Function: Transmembrane receptor that senses neutrophil extracellular traps (NETs) and triggers the ILK-PARVB pathway to enhance cell motility. NETs are mainly composed of DNA fibers and are released by neutrophils to bind pathogens during inflammation. Formation of NETs is also associated with cancer metastasis, NET-DNA acting as a chemotactic factor to attract cancer cells. Specifically binds NETs on its extracellular region, in particular the 8-OHdG-enriched DNA present in NETs, and recruits ILK, initiating the ILK-PARVB cascade to induce cytoskeleton rearrangement and directional migration of cells.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 24618
Sequence Length: 208
Subcellular Location: Cell membrane
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Q86WR0 | MVFYFTSSSVNSSAYTIYMGKDKYENEDLIKHGWPEDIWFHVDKLSSAHVYLRLHKGENIEDIPKEVLMDCAHLVKANSIQGCKMNNVNVVYTPWSNLKKTADMDVGQIGFHRQKDVKIVTVEKKVNEILNRLEKTKVERFPDLAAEKECRDREERNEKKAQIQEMKKREKEEMKKKREMDELRSYSSLMKVENMSSNQDGNDSDEFM | Function: Transmembrane receptor that senses neutrophil extracellular traps (NETs) and triggers the ILK-PARVB pathway to enhance cell motility . NETs are mainly composed of DNA fibers and are released by neutrophils to bind pathogens during inflammation . Formation of NETs is also associated with cancer metastasis, NET-DNA acting as a chemotactic factor to attract cancer cells . Specifically binds NETs on its extracellular region, in particular the 8-OHdG-enriched DNA present in NETs, and recruits ILK, initiating the ILK-PARVB cascade to induce cytoskeleton rearrangement and directional migration of cells . In the context of cancer, promotes cancer metastasis by sensing NETs and promoting migration of tumor cells .
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 24479
Sequence Length: 208
Subcellular Location: Cell membrane
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Q78PG9 | MVFYFTSSSVNSSTYTIYMGKDKYENEDLIKYGWPEDIWFHVDKLSSAHVYLRLQKGEKIEDIPKEVLMDCAHLVKANSIQGCKMNNVNVVYTPWSNLKKTADMDVGQIGFHRQKDVKIVTVEKKVNEILNRLEKTKLEKFPDLAAEKEGRDREERNEKKAQIQEMKRKEKEEMKKKREMDELRSYSSLMKVENMSSNQDGNDSDEFM | Function: Transmembrane receptor that senses neutrophil extracellular traps (NETs) and triggers the ILK-PARVB pathway to enhance cell motility. NETs are mainly composed of DNA fibers and are released by neutrophils to bind pathogens during inflammation (By similarity). Formation of NETs is also associated with cancer metastasis, NET-DNA acting as a chemotactic factor to attract cancer cells (By similarity). Specifically binds NETs on its extracellular region, in particular the 8-OHdG-enriched DNA present in NETs, and recruits ILK, initiating the ILK-PARVB cascade to induce cytoskeleton rearrangement and directional migration of cells (By similarity). In the context of cancer, promotes cancer metastasis by sensing NETs and promoting migration of tumor cells (By similarity).
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 24480
Sequence Length: 208
Subcellular Location: Cell membrane
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Q6GLE1 | MVFYFTSNVISPPYTMYMGKDKYENEDLIKYGWPEDIWFHVDKLSSAHVYLRLQKDQTIEDIPKEVLLDCAQLVKANSIQGCKMNNINVVYTPWANLKKTADMDIGQIGFHRQKDVKTMTVEKVSKIVNRLEKTKDERFPDLAAEKEARDREERNEKKAQIQEIKRKEKEEMKKKKEMDELRSYSSLMKSENMSSNQDGNDSDDFM | Function: Transmembrane receptor that senses neutrophil extracellular traps (NETs) and triggers the ILK-PARVB pathway to enhance cell motility. NETs are mainly composed of DNA fibers and are released by neutrophils to bind pathogens during inflammation. Specifically binds NETs on its extracellular region, in particular the 8-OHdG-enriched DNA present in NETs, and recruits ILK, initiating the ILK-PARVB cascade to induce cytoskeleton rearrangement and directional migration of cells.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 24280
Sequence Length: 206
Subcellular Location: Cell membrane
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Q2RAR6 | MLCVAMAARPVSSTTSTCRPCLPAQVSASKPSTSSSPGTGVLVGVPRERGSSVSKAAIRGARLEAAARCSLVRQRPMLLATVAVGSLVAAGAANATEIGDSLLGSSGLALADLSVGDWFGNLLYSAGQQANEAVQDQLSALSFTSLAVIFGAGLVTSLSPCTLSVLPLTLGYIGAFGSGKDRSEVVGNSVAFSLGLATTLAILGVAASFAGKAYGQVGQGLPVAASGLAVIMGLNLLEVIELQLPSFFSDYDPRAAAANLPSSVQAYLAGLTFALAASPCSTPVLATLLGYVATSRDPIVGGSLLLTYTTGYVAPLLIAASFAGALQSLLSFRRYSAWINPISGAFLLGGGVYTLLDRLFPATSMVM | Function: Probably involved in the transfer of reducing equivalents from stroma to thylakoid lumen and required for the biogenesis of the plastid cytochrome b6f complex.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 37023
Sequence Length: 367
Subcellular Location: Plastid
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Q9M5P3 | MNLSVNRCITGGFVGGFSSCRLNHEKRWVRAGKHCELERERSLVSDAVSLERLESKSIKLAMLASGLGVANLVTLSSAKAADLKMIVLDQATSIYILAEGSLGDSVGNFLYSANQQANEAVQDQLSALSVTSLAVIFGAGLVTSLSPCTLSVLPLTLGYIGAFGSGKSRGQVIGDTVAFALGLATTLALLGIVASFAGKAYGQIGQGLPVAASGLAIVMGLNLLEIIELQLPSFFNNFDPRAAAANFPSSVQAYLAGLTFALAASPCSTPVLATLLGYVATSRDPVIGGSLLLTYTTGYVAPLIVAASFAGALQSLLSLRKVSAWINPISGALLLGGGLYTFLDRLFPAATMVM | Function: Required for the transfer of reducing equivalents from stroma to thylakoid lumen. Involved in the biogenesis of the plastid cytochrome b6f complex by probably transferring reducing equivalents from stromal m-type thioredoxin (Trx-m) to the lumenal thioredoxin HCF164.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 36530
Sequence Length: 354
Subcellular Location: Plastid
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P45706 | MGDVNYFLTFGAGFLSFISPCCLPLYPAFLSYITGVSMDDVKTEKLLLQKRSLFHTLCFLLGFSVIFIALGYGTSFIGSLFRDYHDAIRQIGALLIILFGFITLGVFRPEAMMKERRIHFKHKPSGFLGSVLIGMAFAAGWTPCTGPILAAVITLAGTNPGSAVPYMMLYVLGFAVPFLLLSFFITKLKWIRKNQLFIMKAGGVLMIVIGVLLFFNWMSLIIILLSDLFGGFTGF | Function: Required for cytochrome c synthesis and stage V of sporulation. Might transfer reducing equivalents across the cytoplasmic membrane, promoting efficient disulfide bond isomerization of proteins localized on the outer surface of the membrane or in the spore coat.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 26007
Sequence Length: 235
Subcellular Location: Cell membrane
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O00626 | MDRLQTALLVVLVLLAVALQATEAGPYGANMEDSVCCRDYVRYRLPLRVVKHFYWTSDSCPRPGVVLLTFRDKEICADPRVPWVKMILNKLSQ | Function: May play a role in the trafficking of activated/effector T-lymphocytes to inflammatory sites and other aspects of activated T-lymphocyte physiology. Chemotactic for monocytes, dendritic cells and natural killer cells. Mild chemoattractant for primary activated T-lymphocytes and a potent chemoattractant for chronically activated T-lymphocytes but has no chemoattractant activity for neutrophils, eosinophils, and resting T-lymphocytes. Binds to CCR4. Processed forms MDC(3-69), MDC(5-69) and MDC(7-69) seem not be active.
PTM: The N-terminal processed forms MDC(3-69), MDC(5-69) and MDC(7-69) are produced by proteolytic cleavage after secretion from monocyte derived dendrocytes.
Sequence Mass (Da): 10625
Sequence Length: 93
Subcellular Location: Secreted
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P55773 | MKVSVAALSCLMLVTALGSQARVTKDAETEFMMSKLPLENPVLLDRFHATSADCCISYTPRSIPCSLLESYFETNSECSKPGVIFLTKKGRRFCANPSDKQVQVCMRMLKLDTRIKTRKN | Function: Shows chemotactic activity for monocytes, resting T-lymphocytes, and neutrophils, but not for activated lymphocytes. Inhibits proliferation of myeloid progenitor cells in colony formation assays. This protein can bind heparin. Binds CCR1. CCL23(19-99), CCL23(22-99), CCL23(27-99), CCL23(30-99) are more potent chemoattractants than CCL23.
PTM: The N-terminal is proteolytically cleaved by proteases associated with inflammatory responses. The processed forms, CCL23(19-99), CCL23(22-99), CCL23(27-99) and CCL23(30-99) exhibit increase in CCR1-mediated signaling and chemotaxis assays in vitro.
Sequence Mass (Da): 13443
Sequence Length: 120
Subcellular Location: Secreted
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O00175 | MAGLMTIVTSLLFLGVCAHHIIPTGSVVIPSPCCMFFVSKRIPENRVVSYQLSSRSTCLKAGVIFTTKKGQQFCGDPKQEWVQRYMKNLDAKQKKASPRARAVAVKGPVQRYPGNQTTC | Function: Chemotactic for resting T-lymphocytes, and eosinophils . Has lower chemotactic activity for neutrophils but none for monocytes and activated lymphocytes . Is a strong suppressor of colony formation by a multipotential hematopoietic progenitor cell line . Binds to CCR3 .
PTM: N-glycosylated.
Sequence Mass (Da): 13134
Sequence Length: 119
Subcellular Location: Secreted
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P28291 | MKVSAALLCLLLTVAAFSTEVLAQPDAINSQVACCYTFNSKKISMQRLMNYRRVTSSKCPKEAVIFKTILGKELCADPKQKWVQDSINYLNKKNQTPKP | Function: Acts as a ligand for C-C chemokine receptor CCR2 (By similarity). Signals through binding and activation of CCR2 and induces a strong chemotactic response and mobilization of intracellular calcium ions (By similarity). Exhibits a chemotactic activity for monocytes and basophils but not neutrophils or eosinophils (By similarity). Plays an important role in mediating peripheral nerve injury-induced neuropathic pain (By similarity). Increases NMDA-mediated synaptic transmission in both dopamine D1 and D2 receptor-containing neurons, which may be caused by MAPK/ERK-dependent phosphorylation of GRIN2B/NMDAR2B (By similarity).
PTM: Processing at the N-terminus can regulate receptor and target cell selectivity (By similarity). Deletion of the N-terminal residue converts it from an activator of basophil to an eosinophil chemoattractant (By similarity).
Sequence Mass (Da): 11114
Sequence Length: 99
Subcellular Location: Secreted
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P38454 | MKRVREENETLHLENARRSPPLASTHFLGFPCISLFYSQHKSTKKNIYLDLKTKKKELLPMVFALRAFKIFLKLFYQHILLNLSTLITTFSLFLLYIVVTPLMIGFSKDFLCHFHLGLIWICLLFSFLPERFFQNDFEDGTLELYYLSGYCLQKILLSKLYGHWVLQISGVFCSFPVLQLLYQFDQSKMNWFTIIIGSQIFTLMCGIHSCLALGITSNGWNSLQNLTTLPTLLPLIVFCTSIETEWFHVILLMGYLLLFLFFYPILVSITLQTLLAK | Function: May be involved in the export of heme to the mitochondrion for the biogenesis of c-type cytochromes.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 32290
Sequence Length: 277
Subcellular Location: Mitochondrion membrane
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Q9I3N6 | MSNVFSLLLAREARLLFRRPAELANPLVFFAIVIALFPLAVGPESQLLQTLSPGLVWVAALLAVLLSLEGLFRSDFEDGSMEQWVLSPHPLALLVLAKVLAHWLFSGLALVLMSPLFALMLGLPARCIPVLLLSLLLGTPVLSLLGAVGAALTVGLKRGGLLLALLILPLYIPVLILGSGALQASLQGLPSSGHLLWLASLTALALTLTPFAIAAGLKISVGE | Function: Required for the export of heme to the periplasm for the biogenesis of c-type cytochromes.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 23398
Sequence Length: 223
Subcellular Location: Cell inner membrane
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P29960 | MRALLSRDLRLAIRAGGGFGLGLAFFLIVVTLVPFGVGPQGEILARIASGILWLGALLACLLSLDRIFALDFEDGSLDLLATAPIPMEAVVTIKALAHWITTGLPLVLAAPLFAVLLHLPAPAYLWLEVSLLLGTPALSVLGTFGAALTVGLKRGGLLLPLLALPLYVPTLIFGAELVRRGAEGLAIEVPLAMLAGITAATVALVPFASAAAIRVNLR | Function: Required for the export of heme to the periplasm for the biogenesis of c-type cytochromes.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 22593
Sequence Length: 218
Subcellular Location: Cell inner membrane
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P92527 | MSVSLLQPSFLMSKTRSYAQILIGSWLFLTAMAIYLSLGVAPLDFQQGGNSRILYVHVPVAWMSIIVYIATAINTFLFLLTKHPLYLRSSGTGIEMGAFFTLFTLVTGGFWGRPMWGTFWVWDARLTSVFILFFIYLGALCFQKLSVELASILICVGLIDIPIIKFSVNWWNTLHQPGSISRFGTSIHVSMLIPILSNFANFLFLTCILFVLETRLLILSFLESSITEEIEAREGIPKPSSLALFASMAEWLKRPT | Function: May be involved in the export of heme to the mitochondrion for the biogenesis of c-type cytochromes.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 28798
Sequence Length: 256
Subcellular Location: Mitochondrion membrane
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P30962 | MTLIDLANPTRFLALTARVLPWLAAATVILLAIGLYQSALAPDDYQQGATVKIMFIHVPNAWLSMFVWGVMSIASLGTLVWRHPLADVAAKAAAPIGAAFTFLALLTGSLWGRPMWGTYWEWDARLTSVLILFLMYLGLMALWRAVDDPSRAARAAAVLTLVGAINLPIIKFSVDWWNTLHQPASVMRMGGSSLDKSFLIPLLVMAIAFTLLFVTLHLAAMRNEILRRRVRSLQMMQASRMAFSSEMGAGSRQNNASNEVGAA | Function: Required for the export of heme to the periplasm for the biogenesis of c-type cytochromes.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 28831
Sequence Length: 263
Subcellular Location: Cell inner membrane
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P0ABM3 | MWKTLHQLAIPPRLYQICGWFIPWLAIASVVVLTVGWIWGFGFAPADYQQGNSYRIIYLHVPAAIWSMGIYASMAVAAFIGLVWQMKMANLAVAAMAPIGAVFTFIALVTGSAWGKPMWGTWWVWDARLTSELVLLFLYVGVIALWHAFDDRRLAGRAAGILVLIGVVNLPIIHYSVEWWNTLHQGSTRMQQSIDPAMRSPLRWSIFGFLLLSATLTLMRMRNLILLMEKRRPWVSELILKRGRK | Function: Required for the export of heme to the periplasm for the biogenesis of c-type cytochromes.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 27885
Sequence Length: 245
Subcellular Location: Cell inner membrane
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P38453 | MYVPLLRPFFFMCCSFRYAQILIGFCWFLTAMAIYLSIWVAPSDFQQGENYRIIYVHVPAAWMSLLIYIAMAISSVLFLLTKHPLFQLFSKTAAKIGALFTLFTLVTGGFWGKPMWGTFWVWDARLTSVLILFFIYLGALRFQEFSADVASIFICIGLINIPIIKFSVNWWNTLHQPSSISQFGTSIHISMLIPIFLIFASFFFLTGIFFILETRQIILSFYFQRKSQ | Function: May be involved in the export of heme to the mitochondrion for the biogenesis of c-type cytochromes.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 26462
Sequence Length: 228
Subcellular Location: Mitochondrion membrane
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Q9I3N5 | MMNWTWFHKLGSPKWFYEISGRWLPWFAVAAALLIVTGCVWGLAFAPPDYQQGNSFRIIYIHVPAAFLAQSCYVMLAVAGAVGLIWKMKIADVAVQCAAPIGAWMTFVALLTGAVWGKPTWGAWWVWDARLTAMLILLFLYFGIIALGQAISNRDSAAKACAVLAIVGVVNIPIIKYSVEWWNTLHQPATFTITEKPAMPVEMWLPLLIMVLGFYCFFAAMLLVRMRLEVLKRESRTAWAKAEVKALVEKAR | Function: Required for the export of heme to the periplasm for the biogenesis of c-type cytochromes.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 28289
Sequence Length: 252
Subcellular Location: Cell inner membrane
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P45407 | EFLRPLFIMAIAFTLLFFTLHIMAMRNEIWRRRIAAQRRLAARMASREE | Function: Required for the export of heme to the periplasm for the biogenesis of c-type cytochromes.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 5966
Sequence Length: 49
Subcellular Location: Cell inner membrane
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P29961 | MSIWEYANPVKFMQTSGRLLPWVVAATVLTLLPGLVWGFFFTPVAAEFGATVKVIYVHVPAATLAINIWVMMLVASLIWLIRRHHVSALAAKAAAPIGMVMTLIALITGAFWGQPMWGTWWEWDPRLTSFLILFLFYLGYMALWEAIENPDTAADLTGVLCLVGSVFAVLSRYAAIFWNQGLHQGSTLSLDKEEHIADVYWQPLVLSIAGFGMLFVALLLLRTRTEIRARRLKALEQRERMA | Function: Required for the export of heme to the periplasm for the biogenesis of c-type cytochromes.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 27196
Sequence Length: 242
Subcellular Location: Cell inner membrane
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Q1QND7 | MTRKQRRLTMIGGSLVVLAIAAALVLNALRDSIVFFSTPVMVSEHHIQPGQRFRLGGLVQNGSLVRGDNLVVTFKVSDGSATLPVTYKGILPDLFREGQGVVAEGALDSSGVFRADTVLAKHDETYMPKEVADALKKQGHWKDDYGPQAGAVEASGKQGVSQ | Function: Heme chaperone required for the biogenesis of c-type cytochromes. Transiently binds heme delivered by CcmC and transfers the heme to apo-cytochromes in a process facilitated by CcmF and CcmH.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 17333
Sequence Length: 162
Subcellular Location: Cell inner membrane
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Q2G8J0 | MNATKAPGGIKPKHQRLVLLVIALVALIGAGLLAAYALSNQASYFYVPNDLVKNPPEQGRAIRLGGMVQKGSLKTRADGITIDFVVGDGKARVPVRYTGITPDLFVEGSGVVAEGRMEGQTFVADNLLAKHDENYVPRQMGDMTKAQAEAVVAETK | Function: Heme chaperone required for the biogenesis of c-type cytochromes. Transiently binds heme delivered by CcmC and transfers the heme to apo-cytochromes in a process facilitated by CcmF and CcmH.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 16606
Sequence Length: 156
Subcellular Location: Cell inner membrane
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Q9CPM8 | MTPRRKSRMTVILFVLLGISIASALVLYALRQNIDLFYTPTEVVYGKNEDATQKPSVGQRIRVGGMVVAGTVERDPKSLKVKFDLNDIGPSISVEYEGILPDLFREGQGIVAQGVLKTPTLLEATEVLAKHDENYVPPELDAQMQKVHKPMGVADLKGESERDRQEKAYQKTSMQEGQK | Function: Heme chaperone required for the biogenesis of c-type cytochromes. Transiently binds heme delivered by CcmC and transfers the heme to apo-cytochromes in a process facilitated by CcmF and CcmH.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 19901
Sequence Length: 179
Subcellular Location: Cell inner membrane
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Q4FNY3 | MYGKKVKLRFIFLALILASVILTVFLVLQSLKENVVYFQSPSEIKSLIELNKKKIRVGGMVKEQSIFIDSDKVNFVITDFKNEINIVYTGAVPNLFAEGKGVVAEGFLKDKNYFTATKILAKHDENYMPPEVKEALGDK | Function: Heme chaperone required for the biogenesis of c-type cytochromes. Transiently binds heme delivered by CcmC and transfers the heme to apo-cytochromes in a process facilitated by CcmF and CcmH.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 15693
Sequence Length: 139
Subcellular Location: Cell inner membrane
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B4RHR0 | MSWLPKSPKARRRLMLVAAIAPVLAVAAGLTLWGLSDSISFFYTPSQAEAARPAPGRSIQLGGLVAAGSVVKHPDGRVEFTVADQDAEDRVLFQGDLPDLFREGQGVVAIGAFREDGVFEAKRVLAKHDERYMPREVSKALKEQGEWYGDGQRPEHQGDAL | Function: Heme chaperone required for the biogenesis of c-type cytochromes. Transiently binds heme delivered by CcmC and transfers the heme to apo-cytochromes in a process facilitated by CcmF and CcmH.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 17542
Sequence Length: 161
Subcellular Location: Cell inner membrane
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Q48GL4 | MNPLRKKRLLIIAALLAGVGLAMTLALGALKENINLFYTPSQIANGEAPLDTRIRAGGMVEKGSLQRSADSLDVRFVVTDFNKSVTITYRGILPDLFREGQGIVALGKLNAQGVVVADEVLAKHDEKYMPPEVTKALRDSGQAAPGGSSTPAKQG | Function: Heme chaperone required for the biogenesis of c-type cytochromes. Transiently binds heme delivered by CcmC and transfers the heme to apo-cytochromes in a process facilitated by CcmF and CcmH.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 16443
Sequence Length: 155
Subcellular Location: Cell inner membrane
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P20248 | MLGNSAPGPATREAGSALLALQQTALQEDQENINPEKAAPVQQPRTRAALAVLKSGNPRGLAQQQRPKTRRVAPLKDLPVNDEHVTVPPWKANSKQPAFTIHVDEAEKEAQKKPAESQKIEREDALAFNSAISLPGPRKPLVPLDYPMDGSFESPHTMDMSIILEDEKPVSVNEVPDYHEDIHTYLREMEVKCKPKVGYMKKQPDITNSMRAILVDWLVEVGEEYKLQNETLHLAVNYIDRFLSSMSVLRGKLQLVGTAAMLLASKFEEIYPPEVAEFVYITDDTYTKKQVLRMEHLVLKVLTFDLAAPTVNQFLTQYFLHQQPANCKVESLAMFLGELSLIDADPYLKYLPSVIAGAAFHLALYTVTGQSWPESLIRKTGYTLESLKPCLMDLHQTYLKAPQHAQQSIREKYKNSKYHGVSLLNPPETLNL | Function: Cyclin which controls both the G1/S and the G2/M transition phases of the cell cycle. Functions through the formation of specific serine/threonine protein kinase holoenzyme complexes with the cyclin-dependent protein kinases CDK1 or CDK2. The cyclin subunit confers the substrate specificity of these complexes and differentially interacts with and activates CDK1 and CDK2 throughout the cell cycle.
PTM: Polyubiquitinated via 'Lys-11'-linked ubiquitin by the anaphase-promoting complex (APC/C), leading to its degradation by the proteasome. Deubiquitinated and stabilized by USP37 enables entry into S phase.
Sequence Mass (Da): 48551
Sequence Length: 432
Subcellular Location: Nucleus
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P51943 | MPGTSRHSGRDAGSALLSLHQEDQENVNPEKLAPAQQPRAQAVLKAGNVRGPAPQQKLKTRRVAPLKDLPINDEHVTAGPSWKAVSKQPAFTIHVDEAEETQKRPAELKETECEDALAFNAAVSLPGARKPLTPLDYPMDGSFESPHAMDMSIVLEDKPVNVNEVPDYQEDIHTYLREMEVKCKPKVGYMKRQPDITNSMRAILVDWLVEVGEEYKLQNETLHLAVNYIDRFLSSMSVLRGKLQLVGTAAMLLASKFEEIYPPEVAEFVYITDDTYSKKQVLRMEHLVLKVLAFDLAAPTVNQFLTQYFLHLQPANCKVESLAMFLGELSLIDADPYLKYLPSLIAGAAFHLALYTVTGQSWPESLAQQTGYTLESLKPCLVDLHQTYLKAPQHAQQSIREKYKHSKYHSVSLLNPPETLSV | Function: Cyclin which controls both the G1/S and the G2/M transition phases of the cell cycle. Functions through the formation of specific serine/threonine kinase holoenzyme complexes with the cyclin-dependent protein kinases CDK1 and CDK2. The cyclin subunit confers the substrate specificity of these complexes and differentially interacts with and activates CDK1 and CDK2 throughout the cell cycle.
PTM: Polyubiquitinated via 'Lys-11'-linked ubiquitin by the anaphase-promoting complex (APC/C), leading to its degradation by the proteasome. Deubiquitinated and stabilized by USP37 enables entry into S phase.
Sequence Mass (Da): 47269
Sequence Length: 422
Subcellular Location: Nucleus
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Q1LZG6 | MALRITRNTKISAENKAKISMAGAKRVPVAAVATSKPGLRPRTALGDIGNKVSEQPQAKLPLKKEAKTLASGKVTAKKVPKPLEKAPVPVPEPQPEPEPEPEHVKEDKLSPEPILVDTPSPSPMETSGCAPAEEYLCQAFSDVILAVSDVDAEDGADPNLCSEYVKDIYAYLRQLEEEQAVKPKYLMGREVTGNMRAILIDWLVQVQIKFRLLQETMYMTVSIIDRFMQDTYVPKKMLQLVGVTAMFVASKYEEMYPPEIGDFAFVTDNTYTKFQIRQMEMKILRALNFSLGRPLPLHFLRRASKIGEVDVELHTLAKYLMELTMLDYDMVHFPPSQIAAGAFCLALKVLDNGEWTPTLQHYLSYTEESLLVVMQHLAKNVVMVNRGLTKHMTIKNKYATSKHAKISTLAQLNSALVQDLAKAVAKV | Function: Essential for the control of the cell cycle at the G2/M (mitosis) transition.
PTM: Ubiquitinated by the SCF(NIPA) complex during interphase, leading to its destruction. Not ubiquitinated during G2/M phases (By similarity).
Sequence Mass (Da): 47658
Sequence Length: 427
Subcellular Location: Cytoplasm
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Q10653 | MLRATNNRRTSNNVEKDSLQMAKHGNGPLKPVNAQGLQTKREAREILALKPSNPAPVETAQKSQRINLQDAETKCLAMADDIYKYLVHHEKKYLLEECFMEGGEPTPKMRRILVDWLVQVHVRFHLTPETLHLTVFILDRMLQKKVTSKADLQLLGISAMFVASKFEEVYLPDIHDYEFITENTYSKKQILAMEQTILNSLNFDLSCPSSLVFLRCLSRILSENDASPIDNQAFCYTYNISKCLGELALLDSVMASTPRSHIASASMIIALEVHPVDGIEAENAVSVICKQLGASKKVIEDAVALLAEVSYKNFKQGKLVAIKNKYQSSKLAQVSNLMTDDVLEKINRMGQNAKVDASEME | Function: Essential for the control of the cell cycle at the G2/M (mitosis) transition.
PTM: Ubiquitinated by etc-1 likely during meiosis, resulting in its degradation.
Sequence Mass (Da): 40519
Sequence Length: 361
Subcellular Location: Cytoplasm
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P14635 | MALRVTRNSKINAENKAKINMAGAKRVPTAPAATSKPGLRPRTALGDIGNKVSEQLQAKMPMKKEAKPSATGKVIDKKLPKPLEKVPMLVPVPVSEPVPEPEPEPEPEPVKEEKLSPEPILVDTASPSPMETSGCAPAEEDLCQAFSDVILAVNDVDAEDGADPNLCSEYVKDIYAYLRQLEEEQAVRPKYLLGREVTGNMRAILIDWLVQVQMKFRLLQETMYMTVSIIDRFMQNNCVPKKMLQLVGVTAMFIASKYEEMYPPEIGDFAFVTDNTYTKHQIRQMEMKILRALNFGLGRPLPLHFLRRASKIGEVDVEQHTLAKYLMELTMLDYDMVHFPPSQIAAGAFCLALKILDNGEWTPTLQHYLSYTEESLLPVMQHLAKNVVMVNQGLTKHMTVKNKYATSKHAKISTLPQLNSALVQDLAKAVAKV | Function: Essential for the control of the cell cycle at the G2/M (mitosis) transition.
PTM: Ubiquitinated by the SCF(NIPA) complex during interphase, leading to its destruction. Not ubiquitinated during G2/M phases.
Sequence Mass (Da): 48337
Sequence Length: 433
Subcellular Location: Cytoplasm
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Q59X94 | MIRSYIRNIILAILSPLLTTPPPLILPPPYEKIIQEITTVLSINNYDDGSLAPIILRLAWHCCATYDMTTNTGGSNGATMRFVPEITDEGNYGLDIARAALEPIKQRYPAISYADLWTLAGKVAIEYMGGPTIIWKSGRVDYTNDRCTPSNGLLPFADKDANHIRKTFTRLGYNDQQTVALIGAHGVGRCHKRFSGWEGKWTRTPKTFSNQFYVVLLNETWSQGEVPETGKTQYFNADKSLIMLNTDMELIRDKSYLHWVEIYAKDEPKFFHDFSSAFAKLLELGIKRETL | Cofactor: Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit.
Function: Destroys radicals which are normally produced within the cells and which are toxic to biological systems.
Sequence Mass (Da): 32950
Sequence Length: 291
EC: 1.11.1.-
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Q6BIB1 | MTAIQKPVVAKREAPKAEVNPTVSRSTQTETIKPTKERTVSVFSPPVFNFAANSFAQSVSNEYKHASPKRIKLDNSRVQVPSIVKPKQDKPRPPAIVTKPRVINIEFPNKQKSGFKLLIRPKHEPSIKKQKQGIEVLSTSNTKRITKSISVDDVEYVEKVKHAIKQVLPKPDYDDGSLGPVILRLAWHCCATYNKFTGNGGSNGSTMRFVPEITDDGNSGLDIARSALEPIKQKFPDITYSDLWTLAGKISIQEMGGPKIPWRCGRVDCIDDRYVPPNGRLPFAYKNANHIRETFGRMGFNDRETVSLLGAHGLGRCHKRFSGWEGKWTENPTSFSNDFYKVLLDEEWSLGTVPETGKEQYYNKDKSLIMLNTDIELIRDPHFLHFVKLYSQHQATFFQDFANAFGKLLELGIERDSNGNVLPKNEFY | Cofactor: Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit.
Function: Destroys radicals which are normally produced within the cells and which are toxic to biological systems.
Sequence Mass (Da): 48399
Sequence Length: 428
EC: 1.11.1.-
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Q5B1Z0 | MSKPGDYNAVRRDIAAQLKKPGYDDGSAGPVFVRLAWHSSGTYDAASDTGGSNGAGMRYEAEGGDPANAGLQHGRAFLEPVKEKHPWITYSDLWTLAGVVAIEEMGGPKIPWLPGRTDFVDDSKVPPRGRLPDGAQGADHLRFIFYRMGFNDQEIVALAGGHNLGRCHADRSGFQGPWVNNPTRFSNQFFKLLLNMEWKPKTLENGVSQFVYIDPEAEDHEEPLMMLPTDVALRDDPAFRPWVERYAKDKDLFFDHFSKAFAKLIELGIQRDASGKVTNTDNVKGGYHSAPKKSDEPTGPPRPHTAQRAAKL | Cofactor: Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit.
Function: Destroys radicals which are normally produced within the cells and which are toxic to biological systems.
Sequence Mass (Da): 34521
Sequence Length: 312
EC: 1.11.1.-
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Q4HWQ2 | MGIVDQPQSKGQESTPGDFAAVQKSIIDLLNQPDYDDGSAGPVLVRLAWHSSGTYDKVTDTGGSNGAGMRYEAEGGDPANAGLQNARVFLEPVKRLHPWITYSDLWTLAGVTAIHAMGGPEIDWLPGRTDFVDDSKLPPRGRLPDAAQGAEHIRHIFYRMGFNDREIVALSGAHNLGRCHTANSGFEGKWVNNPTRFSNQYFRLLLSETWTEKTIPESGLLQFSSVDQDTEEELMMLPTDIALTTDSEFSKYVQLYAKDKDVFFQDFKKAFAKLLELGIARNSEGKVINTDNQKGGYRSAPKKSDSTPATSGQPGASKTGGCPVMHHKAKL | Cofactor: Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit.
Function: Destroys radicals which are normally produced within the cells and which are toxic to biological systems.
Sequence Mass (Da): 36252
Sequence Length: 331
EC: 1.11.1.-
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A4R606 | MASKPGDFDAVRKDIVSLLDQPEYDDGSAGPVLVRLAWHSAGTYDKSTDTGGSNGAGMRYEAEGGDPANAGLQNARQFLEPVKARHPWITYADLRTLAGVVAVRAMGGPEIPWRAGRTDFADDSRVPPRGRLPDATQGAAHVRDIFYRMGFDDREIVALSGAHSLGRCHPANSGFEGKWVNNPTRFSNQYFRLLLSEDWREKTVAGTGLKQFVAVDEVTGDELMMLPTDLSLTSDPVFARWVKVYRDDQDLFFADFAKVFDKLMELGIKRDAEGKVINKENVEGGYVSAPKKQGKIASKL | Cofactor: Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit.
Function: Destroys radicals which are normally produced within the cells and which are toxic to biological systems.
Sequence Mass (Da): 32999
Sequence Length: 300
EC: 1.11.1.-
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Q4PD66 | MSKLGDYAAVKKDILAVLKQPEYDDGSAGPVLVRLAWHASGTYCARTDTGGSNGAGMRYEAEGGDPANAGLQHARVFLEPIKEKHSWITYADLWTLAGVVAIEAMGGPSIQWKPGRTDFADDSRLPPRGRLPDGAQGADHLRFIFNRMGFNDQEIVALSGAHNLGRCHSDRSGFEGPWVNSPTRFSNQYYKLLLKLKWQPKKWDGPFQYVAKAPGADDDDEQLMMLPTDYALIQDEKMRPWVEKYAEDRDAFFNDFAKVFAKLIELGVYRDESGIARADKMKQFKGEYKSAPQKSPVPGAPGAGKDGEANPLARQNERAHGQAQHALAKL | Cofactor: Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit.
Function: Destroys radicals which are normally produced within the cells and which are toxic to biological systems.
Sequence Mass (Da): 36483
Sequence Length: 330
EC: 1.11.1.-
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Q6CAB5 | MAEGDYNAVREAIADILDNDDYDDGSIGPVLVRLAWHASGTYDKATGTGGSNGATMRYMKEAKDEANNGLENARQFLEPIKAKFPWITYADLWTLAGVVAIEEMDGPKVPWKPGRQDYVDETNVPPNGRLPDGAQGQDHLRDIFYRMGFNDQEIVALCGAHNMGRCHMDRSGFEGAWVPNPIRFANTYFKLLMNEEWKLTTLKNGVKQYFNEDEELMMLPADYSLMQDPEFHKWVEIYAADKEKFFEDFSKVFAKLIELGVRRGPDGKAKTNFIDRNNNDPNPRL | Cofactor: Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit.
Function: Destroys radicals which are normally produced within the cells and which are toxic to biological systems.
Catalytic Activity: 2 Fe(II)-[cytochrome c] + 2 H(+) + H2O2 = 2 Fe(III)-[cytochrome c] + 2 H2O
Sequence Mass (Da): 32388
Sequence Length: 285
Subcellular Location: Mitochondrion matrix
EC: 1.11.1.5
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Q6C7U1 | MNYPSVSEQKHRVFIIYSAYLRVQFRESARLAVSVRNKNYNLVRADLHNILPQKNTTVFKDGTLAPLLIRLAWHSCATYDKYTRTGGSNGATMRYHLEASDEGNVGLEVARLSLEPIKRKHPWITYADLWILAGVVSIEACKGPSIKWRDGRVDYEDDLLVPPNGRLPLGGGDASHVRTIFSRMGFNDQETVALIGAHSLGRLHHHRSGFDGPWTSNPAKCDNEFYKLLLGNVWTLVDSPTGRKQYVNSTGQVMMPSDMSLIEDANFRFWVDQYAVSEELWRDHFALAFEKLTELGR | Cofactor: Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit.
Function: Destroys radicals which are normally produced within the cells and which are toxic to biological systems.
Sequence Mass (Da): 33712
Sequence Length: 297
EC: 1.11.1.-
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Q4WPF8 | MASAARSASRAFLRSTPTTSSFRPAVRAARFALPAQGFRAAGRRGYASEANSGKSSSNVFLWAGLAVAGGAGAYLYLNGSDSVTSKTFVPGKEDYQKVYDAIARRLADETDYDDGSYGPVLVRLAWHASGTYDKETGTGGSNGATMRFAPESDHGANAGLKIARDFLEPIKAQFPWISYSDLWTLAGACAIQELGGPTIPWRPGRQDKDVAACTPDGRLPDASKDQRHIRDIFYRMGFNDQEIVALIGAHALGRAHPDRSGYDGPWDFSPTVFTNEFFRLLVDEKWQNRKWNGPAQFTDKTTKTLMMLPADLALIKDKEFKKHVERYARDSDAFFKDFSDAFVKLLELGVPFTSKAEDRYVFKTSE | Cofactor: Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit.
Function: Destroys radicals which are normally produced within the cells and which are toxic to biological systems.
Catalytic Activity: 2 Fe(II)-[cytochrome c] + 2 H(+) + H2O2 = 2 Fe(III)-[cytochrome c] + 2 H2O
Sequence Mass (Da): 40379
Sequence Length: 366
Subcellular Location: Mitochondrion matrix
EC: 1.11.1.5
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Q5AEN1 | MATFAPHISKITKSSTKFNYGRIAKTFLGVAGSAAIATYFYNNGNPFNNNNNNNNNNGGSKNAAKALFGASAGANVKIAKVPEGKSASDYQKVYNDIATKISENLEFDENAGYYGQLLRLAWHTSGTYDKSDNSGGSYGGTMIFAPEEFDPENAGLQVGREFLMEFLVKYPWISRGDLWTLGGVAAVQESGGPKIEWRPGRVDDNTASKVPPNGRLPDASKDGKYVKDLFARMGFNERETVALLGAHVLGRCHKHNSGYDGPWGPSFNQFTNVFYTTLLGDWHVKKWDGKKQYEDDETGEFMMLPTDMALKEESYFLKYVKMYADDQDLFFKDFAKAFSKLISNGIKYPADSKPILFKTLDEQDEE | Cofactor: Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit.
Function: Destroys radicals which are normally produced within the cells and which are toxic to biological systems.
Catalytic Activity: 2 Fe(II)-[cytochrome c] + 2 H(+) + H2O2 = 2 Fe(III)-[cytochrome c] + 2 H2O
Sequence Mass (Da): 40682
Sequence Length: 366
Subcellular Location: Mitochondrion matrix
EC: 1.11.1.5
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Q6FMG7 | MSATALRIAPIASRTFQRRLGYLLAGVATGAAATVAYKAQKNNNYYKYNNNNNNNSGFKAGALAAAAGVVHLAHEEDKKTADYQKVYNLIAERLRDDDEYDNYIGYGPVLVRLAWHSSGTWDKNDNTGGSYGGTYRYKKESQDPSNAGLENAAKFLEPVKKQFPWISYGDLYTLGGVVGIQELQGPKIPWRSGRTDLPEDMTPDNGRLPDGDKDANYVRNFYKRLDFNDREVVALLGAHALGKTHLKNSGFEGPWGAANNIFTNEFYLNLLNEDWKLEKNDAGNLQYNSPKGYMMLPTDYALIQDSNYLKIVKEYAADQDAFFRDFSKAFAALLERGIDFPKNQPVHIFKTLDEQGL | Cofactor: Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit.
Function: Destroys radicals which are normally produced within the cells and which are toxic to biological systems.
Catalytic Activity: 2 Fe(II)-[cytochrome c] + 2 H(+) + H2O2 = 2 Fe(III)-[cytochrome c] + 2 H2O
Sequence Mass (Da): 40007
Sequence Length: 357
Subcellular Location: Mitochondrion matrix
EC: 1.11.1.5
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Q6URB0 | MSFRAPNLIRSTVGRRAGQTLNLRSQVIRRRFATEGGPEITKPSAPRSSNTGYIFAGLGVAAVGAAYYFYGTGRTEHDSTNKADTVVREAVATVEAKTGLRRGKDEYQKVYNRIAETLDKEGYDDGSLAPVLLRLAWHASGTYSKADGTGGSNFATMRFKPEAEHSANNGLHVAREHMEKIKQEFPWISYGDLWTLGGVCAIQESGGPTIPWRPGRIDGYAAQVTPDGRLPDATQAQDHLRFIFNRMGFNDQEIVALSGAHAMGRCHPNRSGFDGPWTFSPVTFSNQYFALLRDEPWQWKKWTGPAQFEDKKTKTLMMLPTDMALVKDKSFKKYVDIYADNEEKFFSDFAKAFSKLIELGVPERQWAGEPWTMATSD | Cofactor: Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit.
Function: Destroys radicals which are normally produced within the cells and which are toxic to biological systems.
Catalytic Activity: 2 Fe(II)-[cytochrome c] + 2 H(+) + H2O2 = 2 Fe(III)-[cytochrome c] + 2 H2O
Sequence Mass (Da): 42088
Sequence Length: 377
Subcellular Location: Mitochondrion matrix
EC: 1.11.1.5
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Q6BKY9 | MSTAAFKRQSVPLSKLFQSYGKNNSQSKYGGYFLATLIGSGILATSYFNNNKNGNTPSNNHKKLLAGSGIVNTAAIPKGKSIKDYQSLYNEIAEKVRDQDDADDGAGRYGLLTRLAWHTSGTYKKEDNTGGSYGGTMIYKPESTDGENSGLNHGRDFLQEFKDKYSWLSHGDLWTLGGVVAVQECGGPKIKWRPGRQDISDKTRVPENGRLPDASKDADYVKGVFGRMGFNERETVCLIGAHCLGKCHKENTNYDGPWGPSFNMFTNDFFVRLLQNWHVKKWDGKKQYEDDETNSFMMLPTDMALKEDSSFLKYVKMYADDEKLFFSDFAKNFSTLLELGVTFPDSIKPTEFKTLDEQDK | Cofactor: Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit.
Function: Destroys radicals which are normally produced within the cells and which are toxic to biological systems.
Catalytic Activity: 2 Fe(II)-[cytochrome c] + 2 H(+) + H2O2 = 2 Fe(III)-[cytochrome c] + 2 H2O
Sequence Mass (Da): 40439
Sequence Length: 360
Subcellular Location: Mitochondrion
EC: 1.11.1.5
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Q4ING3 | MASATRQFARAATRATRNGFAIAPRQVIRQQGRRYYSSEPAQKSSSAWIWLTGAAVAGGAGYYFYGNSASSATAKVFNPSKEDYQKVYNEIAARLEEKDDYDDGSYGPVLVRLAWHASGTYDKETGTGGSNGATMRFAPESDHGANAGLAAARDFLQPVKEKFPWITYSDLWILAGVCAIQEMLGPAIPYRPGRSDRDVSGCTPDGRLPDASKRQDHLRGIFGRMGFNDQEIVALSGAHALGRCHTDRSGYSGPWTFSPTVLTNDYFRLLVEEKWQWKKWNGPAQYEDKSTKSLMMLPSDIALIEDKKFKPWVEKYAKDNDAFFKDFSNVVLRLFELGVPFAQGTENQRWTFKPTHQE | Cofactor: Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit.
Function: Destroys radicals which are normally produced within the cells and which are toxic to biological systems.
Catalytic Activity: 2 Fe(II)-[cytochrome c] + 2 H(+) + H2O2 = 2 Fe(III)-[cytochrome c] + 2 H2O
Sequence Mass (Da): 40024
Sequence Length: 358
Subcellular Location: Mitochondrion matrix
EC: 1.11.1.5
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P0CAW2 | MKFGPETIIHGDCIEQMNALPEKSVDLIFADPPYNLQLGGDLLRPDNSKVDAVDDHWDQFESFAAYDKFTREWLKAARRVLKDDGAIWVIGSYHNIFRVGVAVQDLGFWILNDIVWRKSNPMPNFKGTRFANAHETLIWASKSQNAKRYTFNYDALKMANDEVQMRSDWTIPLCTGEERIKGADGQKAHPTQKPEALLYRVILSTTKPGDVILDPFFGVGTTGAAAKRLGRKFIGIEREAEYLEHAKARIAKVVPIAPEDLDVMGSKRAEPRVPFGTIVEAGLLSPGDTLYCSKGTHVAKVRPDGSITVGDLSGSIHKIGALVQSAPACNGWTYWHFKTDAGLAPIDVLRAQVRAGMN | Function: A beta subtype methylase that recognizes the double-stranded sequence 5'-GANTC-3' and methylates non-modifed A-2 on the hemimethylated, post-replicative DNA (Probable) (By similarity). Opens a bubble in the DNA at the recognition site, allowing precise recognition of the sequence and ensuring enzyme specificity . Functions only in the predivisional cell. Responsible for 5'-GANTC-3' methylation in the cell; methylation of hemimethylated sites generated after replication fork passage occurs late in the predivisional cell, near completion of chromosome replication but prior to cell division. Contributes to the accurate cell-cycle control of DNA replication and cellular morphology (By similarity).
PTM: Rapidly degraded by Lon protease prior to cell division.
Catalytic Activity: a 2'-deoxyadenosine in DNA + S-adenosyl-L-methionine = an N(6)-methyl-2'-deoxyadenosine in DNA + H(+) + S-adenosyl-L-homocysteine
Sequence Mass (Da): 39665
Sequence Length: 358
Domain: Has an N-terminal methyltransferase (MTase) domain linked to a C-terminal DNA-binding domain by a 10 residue linker. The MTase of one monomer recognizes, binds and modifies the target strand while C-terminal domain of the other monomer binds the non-target strand.
EC: 2.1.1.72
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C0SPC1 | MNIDMNWLGQLLGSDWEIFPAGGATGDAYYAKHNGQQLFLKRNSSPFLAVLSAEGIVPKLVWTKRMENGDVITAQHWMTGRELKPKDMSGRPVAELLRKIHTSKALLDMLKRLGKEPLNPGALLSQLKQAVFAVQQSSPLIQEGIKYLEEHLHEVHFGEKVVCHCDVNHNNWLLSEDNQLYLIDWDGAMIADPAMDLGPLLYHYVEKPAWESWLSMYGIELTESLRLRMAWYVLSETITFIAWHKAKGNDKEFHDAMEELHILMKRIVD | Function: Plays a role in cell cycle regulation and chromosome integrity. Activates DnaA-dependent chromosomal DNA replication initiation ensuring that the chromosome is replicated at the right time during the cell cycle (By similarity). May regulate replication initiation through phosphorylation of a possible second messenger or metabolite, and by interacting with replication initiation proteins. Has ATPase activity with D-ribose and 2-deoxy-D-ribose in vitro, but not with choline. Involved in DNA damage response .
Catalytic Activity: ATP + D-ribose = ADP + D-ribose 5-phosphate + H(+)
Sequence Mass (Da): 30791
Sequence Length: 269
Subcellular Location: Cytoplasm
EC: 2.7.1.15
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A0A0H2ZQL5 | MDLGDNELTLTPIPGKSGKAYMGSYPDGKRIFVKMNTSPILPGLAREQIAPQLLWSRRLADGRDMCAQEWLTGKILTPYDMNRKQIVNILTRLHRSRPLMTQLSRLGYAMETPVDLLQSWQETAPDALRKNHFISEVMADLRQTIPGFREDHATIVHGDVRHSNWIETDSGLIYLVDWDSVRLTDRMFDVAHMLCHYISEHQWKEWLTYYGYKYNQTVLSKLYWYGQLSYLSQISKYYMNQDLENVNREIHGLRHFRDKYGKRR | Function: Plays a role in cell cycle regulation and chromosome integrity. Activates DnaA-dependent chromosomal DNA replication initiation ensuring that the chromosome is replicated at the right time during the cell cycle . May regulate replication initiation through phosphorylation of a possible second messenger or metabolite, and by interacting with replication initiation proteins. Has ATPase activity with D-ribose and 2-deoxy-D-ribose in vitro, but not with choline. Involved in DNA damage response (By similarity).
Catalytic Activity: ATP + D-ribose = ADP + D-ribose 5-phosphate + H(+)
Sequence Mass (Da): 31105
Sequence Length: 264
Subcellular Location: Cytoplasm
EC: 2.7.1.15
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Q82LU9 | MKEILDAIQSQTATSADFAALPLPDSYRAITVHKDETEMFAGLSTRDKDPRKSIHLDDVPVPELGPGEALVAVMASSVNYNSVWTSIFEPVSTFNFLERYGRLSDLSKRHDLPYHIIGSDLAGVVLRTGPGVNSWKPGDEVVAHCLSVELESSDGHNDTMLDPEQRIWGFETNFGGLAEIALVKSNQLMPKPDHLSWEEAAAPGLVNSTAYRQLVSRNGAGMKQGDNVLIWGASGGLGSYATQFALAGGANPICVVSSEQKADICRSMGAEAIIDRNAEGYKFWKDETTQDPKEWKRFGKRIREFTGGEDIDIVFEHPGRETFGASVYVTRKGGTITTCASTSGYMHEYDNRYLWMSLKRIIGSHFANYREAWEANRLVAKGKIHPTLSKVYSLEDTGQAAYDVHRNLHQGKVGVLALAPREGLGVRDEEKRAQHIDAINRFRNI | Function: Catalyzes the conversion of crotonyl-CoA to butyryl-CoA. It uses only NADP as electron donor. May have a role in providing butyryl-CoA as a starter unit for straight-chain fatty acid biosynthesis.
Catalytic Activity: butanoyl-CoA + NADP(+) = (2E)-butenoyl-CoA + H(+) + NADPH
Sequence Mass (Da): 49160
Sequence Length: 445
EC: 1.3.1.86
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Q9XIA4 | MIVTLNPKILHFSKIHPFSRPSSYLCRTRNVSLITNCKLQKPQDGNQRSSSNRNLTKTISLSDSAPPVTEETGDGIVKGGGNGGGGGGDGRGGLGFLKILPRKVLSVLSNLPLAITEMFTIAALMALGTVIEQGETPDFYFQKYPEDNPVLGFFTWRWISTLGLDHMYSAPIFLGMLVLLAASLMACTYTTQIPLVKVARRWSFMKSDEAIKKQEFADTLPRASIQDLGMILMGDGFEVFMKGPSLYAFKGLAGRFAPIGVHIAMLLIMVGGTLSATGSFRGSVTVPQGLNFVMGDVLAPIGFFSIPTDAFNTEVHVNRFTMDYYDSGEVSQFHSDLSLRDLNGKEVLRKTISVNDPLRYGGVTVYQTDWSFSALQVTKDGEGPFNLAMAPIKINGDKKLYGTFLPVGDTNAPNVKGISMLARDLQSIVVYDLDGKFAGIRRPSSKLPIEINGMKIVIEDAIGSTGLELKTDPGVPVVYAGFGALMLTTCISYLSHSQIWALQNGTALVVGGKTNRAKNQFPDDMNRLLDQVPELIKKNTSVVSEQS | Function: Required during biogenesis of c-type cytochromes (cytochrome c6 and cytochrome f) at the step of heme attachment.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 59393
Sequence Length: 547
Subcellular Location: Plastid
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Q75DD6 | MIDPSESFEATYAVPMHCGDCTGEISRALRAVPGVQEVTPDLERQLVAVRGIAPPSSIVQALAATGRDAILRGSGEPDSAAVAILESASAGGPPVRGLVRAVQVAPNKTLFDITLNGLPGPAQYYASIRASGDVSRGAASTGPAWHVFEDAVACERASPLGADLCAGSALFVAPLAVQALIGRGFLVGADRGHALAGAAAVGVLARSAGAWQNDKVVCACSGDTLWQERGSARSANIA | Cofactor: Binds 2 copper ions per subunit.
Function: Copper chaperone for superoxide dismutase 1 (SOD1). Binds copper ions and delivers them specifically to SOD1 (By similarity).
Sequence Mass (Da): 24068
Sequence Length: 238
Subcellular Location: Cytoplasm
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Q8GTZ9 | MQPYASVSGRCLSRPDALHVIPFGRPLQAIAGRRFVRCFAKGGQPGDKKKLNVTDKLRLGNTPPTLDVLKAPRPTDAPSAIDDAPSTSGLGLGGGVASPRTLVQSNAVQVAWRRLMKELSSLPRAIAIMALIAVLSGLGTFIPQNKSIEYYLVNYPDGAEKVLGFLTGDLILTLQLDHIYTADYFYLSMGLLAASLAACTYTRQWPAVKVAQRWRFLTQPKSLLKQGRTEVLPNARVSDLGAILLQRGYQVFVKDGSLYGFKGLAGKLGPIGVHAALLLCLFGTAWSGFGTLKGNVMCPEGQDFQVASFLQPSSPIASMPASASNVIHVNKFTIDYRPDGSVAQFYSDLSLLDPAQGGKEMMRKTISVNDPFRFNGVTMYQTDWSLSAVTLRVLGQDAPLARAAQAAEAQAAASTSGPTSSASSTSDALPQQRTAFNLPMASLEGKPGVAGRLWATFLPLAEPGQDGSAPKGISILARDPQSVVFYDAKGQFVGVRRPGSGKPIEVEGLALVVEDVTGATGLELKSDPGVPAVYAGFGGLMVTTLISYLSHSQVWALQQGSSLFVSGRTNRAKLAFDRELDDILNAVPELPPTAATTVASSASTAAPAPTAKQ | Function: Required during biogenesis of c-type cytochromes (cytochrome c6 and cytochrome f) at the step of heme attachment.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 64897
Sequence Length: 613
Subcellular Location: Plastid
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Subsets and Splits