ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
P07688 | MWRLLATLSCLLVLTSARSSLYFPPLSDELVNFVNKQNTTWKAGHNFYNVDLSYVKKLCGAILGGPKLPQRDAFAADVVLPESFDAREQWPNCPTIKEIRDQGSCGSCWAFGAVEAISDRICIHSNGRVNVEVSAEDMLTCCGGECGDGCNGGFPSGAWNFWTKKGLVSGGLYNSHVGCRPYSIPPCEHHVNGSRPPCTGEGDTPKCSKTCEPGYSPSYKEDKHFGCSSYSVANNEKEIMAEIYKNGPVEGAFSVYSDFLLYKSGVYQHVSGEIMGGHAIRILGWGVENGTPYWLVGNSWNTDWGDNGFFKILRGQDHCG... | 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... |
P43233 | MSWSRSILCLLGAFANARSIPYYPPLSSDLVNHINKLNTTGRAGHNFHNTDMSYVKKLCGTFLGGPKAPERVDFAEDMDLPDTFDTRKQWPNCPTISEIRDQGSCGSCWAFGAVEAISDRICVHTNAKVSVEVSAEDLLSCCGFECGMGCNGGYPSGAWRYWTERGLVSGGLYDSHVGCRAYTIPPCEHHVNGSRPPCTGEGGETPRCSRHCEPGYSPSYKEDKHYGITSYGVPRSEKEIMAEIYKNGPVEGAFIVYEDFLMYKSGVYQHVSGEQVGGHAIRILGWGVENGTPYWLAANSWNTDWGITGFFKILRGEDHC... | 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 s... |
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 s... |
Q55DH8 | MNKKLEQLEKFKTNDKNPVYSTTNTGVSLSDDANSLKAGPRGPTLLEDFVLREKITHFDHERIPERIVHARGTGAHGYFLSYKDHSKLTKADFLSKQDKKTPVFIRISTVQGPRGSADTVRDVHGFAVKFYTDEGNYDLVGNNMPVFFIQDASSFPDFVHAVKMEPQNEMPTGGSAHDTFYDFCGLKPESAHSVLWVMSDRGIPISLRHQQGFGVHSYRFINQEGKSTFVKLHWKPLSGTCSLLWDEAQKIAGKDCDYHRRRFWEDIESGDFPQWELGAQLLDEDLQKKFDFDILDPTKLIPEELTPVIPLGRMVIDRNP... | 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 ... |
P06115 | MNVFGKKEEKQEKVYSLQNGFPYSHHPYASQYSRPDGPILLQDFHLLENIASFDRERVPERVVHAKGGGCRLEFELTDSLSDITYAAPYQNVGYKCPGLVRFSTVGGESGTPDTARDPRGVSFKFYTEWGNHDWVFNNTPVFFLRDAIKFPVFIHSQKRDPQSHLNQFQDTTIYWDYLTLNPESIHQITYMFGDRGTPASWASMNAYSGHSFIMVNKEGKDTYVQFHVLSDTGFETLTGDKAAELSGSHPDYNQAKLFTQLQNGEKPKFNCYVQTMTPEQATKFRYSVNDLTKIWPHKEFPLRKFGTITLTENVDNYFQE... | 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 | MTKLLNFVILASVLTVTAHALTYDLNNSDELFKNFAIKYNKTYVSDEERAIKLENFKNNLKMINEKNMASKYAVFDINEYSDLNKNALLRRTTGFRLGLKKNPSAFTMTECSVVVIKDEPQALLPETLDWRDKHGVTPVKNQMECGSCWAFSTIANIESLYNIKYDKALNLSEQHLVNCDNINNGCAGGLMHWALESILQEGGVVSAENEPYYGFDGVCKKSPFELSISGSRRYVLQNENKLRELLVVNGPISVAIDVSDLINYKAGIADICENNEGLNHAVLLVGYGVKNDVPYWILKNSWGAEWGEEGYFRVQRDKNS... | 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 t... |
Q9PYY5 | MLFFNFYKHIMFLPWVFCVALLTLNVCAVSYIAYDMSNAQELFNEFVVKYNKVYKDDQEKEARFEIFKQNLADINARNALEDSAMFEINSRADISSNELLQKLTGLKLSLMRGEKKNSFCTPTVISGDSSGKVPDSFDWRDRNSVTSVKMQKECGSCWAFSAVANIESLYHIKHNVSLDLSEQQLVDCDKVNNGCNGGLMSWAFEGIIRAGGISYEAPYPYTGVDGVCKNTTRYVQLSGCYAYDLRSEKKLRQVLHEKGPVSVAIDVVDLTNYKSGVAKHCSVDHGLNHGVLLVGYGQENDVKYWTLKNSWGSDWGEQGF... | 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 t... |
P25783 | MNKILFYLFVYGVVNSAAYDLLKAPNYFEEFVHRFNKDYGSEVEKLRRFKIFQHNLNEIINKNQNDSAKYEINKFSDLSKDETIAKYTGLSLPIQTQNFCKVIVLDQPPGKGPLEFDWRRLNKVTSVKNQGMCGACWAFATLASLESQFAIKHNQLINLSEQQMIDCDFVDAGCNGGLLHTAFEAIIKMGGVQLESDYPYEADNNNCRMNSNKFLVQVKDCYRYITVYEEKLKDLLRLVGPIPMAIDAADIVNYKQGIIKYCFNSGLNHAVLLVGYGVENNIPYWTFKNTWGTDWGEDGFFRVQQNINACGMRNELASTA... | 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... |
Q8V5U0 | MRKYHSNIMHKIITFVSLLWTFVVCDEISLHTSSSPPPLSSPVPVLYYNLDQSEIYFKHFLQQYNKSYDDPKEYQYRYNVFKDNLNKINSQNRENLLNNKNNNDSLSTSAQFGVNKFSDKTPDEVLHSNTGFFLNLSQHYTLCENRIVKGAPDIRLPDYYDWRDTNKVTPIKDQGVCGSCWAFVAIGNIESQYAIRHNKLIDLSEQQLLDCDEVDLGCNGGLMHLAFQELLLMGGVETEADYPYQGSEQMCTLDNRKIAVKLNSCFKYDIRDENKLKELVYTTGPVAIAVDAMDIINYRRGILNQCHIYDLNHAVLLIGW... | 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 t... |
Q91BH1 | MYLIYYYTIIAVATASIANEKIFYDIDSASVYYENFIKQHNKEYTTPDQRDAAFVNFKRNLADMNAMNNVSNQAVYGINKFSDIDKITFVNEHAGLVSNLINSTDSNFDPYRLCEYVTVAGPSARTPESFDWRKLNKVTKVKEQGVCGSCWAFAAIGNIESQYAIMHDSLIDLSEQQLLDCDRVDQGCDGGLMHLAFQEIIRIGGVEHEIDYPYQGIEYACRLAPSKLAVRLSHCYQYDLRDERKLLELLYKNGPIAVAIDCVDIIDYRSGIATVCNDNGLNHAVLLVGYGIENDTPYWIFKNSWGSNWGENGYFRARRN... | 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 t... |
Q18879 | MTRQNTSESDNTQRPPIPQYDTVDDIDELTDAMDKEDHHHHHHHHEHHHQHQGIAQYDTVEEVETLETVHHRTSLNQEVPTPQRRSHPQYDNLDDIDDQEYITEVEVKSNRGSTLTTRPHVTIKQDEIEDIGERQVTVIEIASQKGSTKRVAPRKDYAPSIPLPEHPAQQSAPPTQQSRPQTTSHKPPNPEMEFDIGVKNIAPVLIHKMNMDDRDPKDSAQYLNTSFFEVFNEPSEQYHSIACVWTLSFKIFEIVRIYSYKILTLIFGLIIAFLGGILFALFAFLNIWIFRPILILTRMAFAQIVLIWPMFLIYIVRPFF... | 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. Af... |
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... |
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 phos... |
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 phos... |
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 phos... |
A4G3R1 | MVMSSPTNSARIILISGIASGQGKTTVTAALARKLIRQGLRVRVFKTGPDYLDPMILQRASGAEVYALDLWMVGLDDCRRLLARAASEVDVILIEGVMGLYDGDPSSADLARAFGVPVVVVLDAAKMAQTVGAVVLGLQQYGPVDLAGVIVNRLASPSHASMVTRGIRNVPILATLPKQQQALPERHLGLVQPDEIAQVDQVLDQLADQIEIDMVAWDAIAPVVLDGSLAAASTQQLLAGKTIAIARDAAFAFVYHANLECLRAAGAQLKFFSPLNDETIPAEADAVYIPGGYPELHCATLSSAQRWQDSMRAAHVRNMP... | 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
Seq... |
Q8EXQ4 | MNIKIPRIVIGGTGSGVGKTTIALALTQILRKKGLKVATFKCGPDYLDPTYHSRASQKICHNLDGWLMGKESVLNTFYQACHNVDIVIIEGMMGLFDGHSPNSEIGSTAEIAKWLASPVLVVLDTRGMARTVSAILKGLKIFDPDLNLAGAFANFTGSPSHIQLLKDASTEVPILGGLCKHSEQTFPERHLGLYSASEENVSEEKFNFWGEEGEKSLEVNSILEIANSAPEISIPVSNINTTLKRCKIGIAMDSAFHFYYEENLMRLRQAGAELVFFSPLSDSKLTDVDGLYFGGGYPEVFAPTLSKNKSLLNYIQDLSY... | 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
Seq... |
Q8Y7T0 | MNKILIAAASSGTGKTTVTLGIMHALKKRGLRVQPFKVGPDYIDTNYHQAITGVASINLDSFLIDDDAMLAALFEKHGQSADISVIEGVMGLFDGLGIDRDNSSTSFIAKCTKTPVILVVDGKAISTSAAAIVDGFNRFDPELTIAGVIINRVASENHFSLIKGAIERYTDVPVLGYLPKNAAVALPERHLGLVPKEEMTELETKWEVLGDLIAEHVDLDRLLAISKTGAKLTVHPPEIQVPDFSGMRVAYALDAAFHFYYQDNLDFIRSTGATLIPFSPLEEREVPDADFIYIGGGFPEVFAERLAKNKSMHESILAAH... | 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
Seq... |
A0L8B9 | MPYRIPRLFISATRKSSGKTFIAVGLTAALSARGLVVQPFKKGPDYIDPRWHSLAAGRECRNLDDFIMGRPKVLTSFVAHAQGADVAIIEGNLGLFDGQDLEGSDSSAALAKALGAPVLLVVDCKHLARSVAPLVCGHLHFPGGETIVGIILNNVATPRQEKRLREAIERFCPIPILGAIPRSAEIMIDERHLGLVPANEKQGAPHTVETMGRMMESHLDLDRLVALAATATPLALPDNPPALASKAPLVGGRPVRVGYAADQAFSFYYPDNLEALRQNGVELVPFSLLDEQPLPQVDGLYIGGGFPEMFMEHLQQNRAT... | 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
Seq... |
Q46FL0 | MLNDKQSVENIPRILISADRSSSGKTTISMGLMAALVSRGYKVQPFKVALDYIDPSYHTEITGRFCRNLDGYLMDENGILDVYTHACEAGEKADIAIIEGVRGLYEGFESLSDLGSTAQIAKILNCPVIFVINARSITRSSAALINGYRNFDPDVEIAGVILNNIGSRRHAKKAKEAIEYYTGVPVIGIVPRDPAMQISMRHLGLMPALEGRRRLGDGGFEARLRGIEEIINKGIDVDRFMEIAKSAKALKSPENSVFSSVSDPGAPRPKIGVALDEAFNFYYRDNIDLLNLAGAEIVYFSPVKDASLPEVDGLYIGGGY... | 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 red... |
Q58816 | MIMKRVVIAGTSSEVGKTVISTGIMKALSKKYNVQGYKVGPDYIDPTYHTIATGNKSRNLDSFFMNKEQIKYLFQKHSKDKDISVIEGVRGLYEGISAIDDIGSTASVAKALDSPIILLVNAKSLTRSAIAIIKGFMSFDNVKIKGVIFNFVRSENHIKKLKDAMSYYLPDIEIIGFIPRNEDFKVEGRHLGLVPTPENLKEIESKIVLWGELVEKYLDLDKIVEIADEDFEEVDDVFLWEVNENYKKIAVAYDKAFNFYYWDNFEALKENKAKIEFFSPLKDSEVPDADILYIGGGYPELFKEELSRNKEMIESIKEFD... | 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)... |
A1AT17 | MSINGFLIAAPQSGSGKTTISLAIMAALRRRGLVVAPFKCGPDFIDPGYHRMASGRASINLDGWMCPESFVAETFRLHAEAADVAVIEAVMGLFDGLGASPLQGSSAQIAAICGAPVVLVVNARGMAASAAALVKGFAEFDPDVRLAGVIFNNVGSAGHAELLARVMASALPEIALLGCIPRDEALAIPSRHLGLVTAEDNPLPPEYLDRLADLAEKHLDLAGLAGLRITPRSVGASLSRTNGGGMLPVRIAVARDAAFCFVYQDNLRLLREAGGELLFFSPLADGALPEGISGIYLPGGYPELYAERLAVNVPMLDAIR... | 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
Seq... |
Q6L2V8 | MKINSIIIGAPSSSSGKTTISIGIMRALSRRLRVQPFKVGPDYIDPGYHNIATGRFSSNLDTWMSSREKMKEIFIKRSTGSDISIIEGVMGLYDGKQPDKDTGSTAEVARTLKSPVIIVIDISAMARTAAAIILGLIKMDKRLRISGVILNNAGSDYHCSIVRTAIEKYTGIPVIGCVKRSDDLKIDDRYLGLKTAMEDDNSGKIDKIADIIERSVDLDLLIKISKESGDISFKSGLFSKKNVNRVRIAIAYDAAFNFYYYDNIEMLKMYGAEIVYFSPLNDYKLPEADGLYIGGGFPELFAERLSDNYSIKKDIMEFFN... | 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
Seq... |
Q7VEH6 | MRGFTLPVWVVAAAKAAVKVLIGESWQSHEVIELLNNEESIVVPIRSASILDNGEKALGITNCDPGECLDLTRGLEIWVCLRYIENQQIISSDGLELEPWLKIIPGYGVGKFDLTNDISISEFARQLLIVNLKPYRKEGYSLNLEIIFPSGQELAEKTSNHAFGVVDGLALIGTQADVQESASPKKLQSTIHALRSRCAESSFTGSLIFVIGENGLDLALQYGIDSSKIIKTGNWLGPLLVAAAQEKVQQLLIFGYHGKLIKLAGGVFHTHHHLADNRLETLIAFAVKERIPLSLIKEFEEAVSIEAALSILENKDISTA... | 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... |
Q48DG3 | MREETAEQPAPLRSGLTTGSCATATSLAAARLLLSGQISDAVEIVLPKGKQVQMRLEFCRLVDNFAEAGTLKDAGDDPDVTHGALVFARVRLEMAPGVRFVAGAGVGSVTRPGLVLAVGEPAINPVPRRMMTEHLLQLAEELGYSGGFEVTIGVEGGEALALKTMNPRLGILGGLSILGTSGIVRPFSCAAYIASIHQGIDVATTNGYRHIAACTGNASEDTMRRVYNIPDIALIEMGDFVGAVLKHLRKVPVDKLSLCGGFGKISKLAAGHMDLHSRHSSIDLPQLALWAADTGADADLQQRIRDANTSQQALAMCATA... | 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... |
Q8ZZB0 | MNPFLKYGITTGLAAAAAAKAAALYSKGIVPKSVTVPTPIGLRVEVFVERVFQRGEIYCAEVRKFSGDNPDVLNGVIIRACVRPLNNGVVIKGGEGVGIVTRPGLPVPPGEHAINPVPRRMIEEAVREVLEGAEVLVEVPDGKLLAEKTMNPRLGIVGGISILGTTGIEAPVSADEFLGHIEAELSALRERRDIAILAQGNTSYKAAQAVFGDVVVKIGDMVGYAVEKAAALGYKAAYLFTMPGKLAKLALGAYNTHSAQCDGRVEAVLYALVKLRAPYEVLLEVSNAASVGEALAKAGDYAGGVIAIMARRAKEYLERF... | 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... |
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 biosynt... |
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 biosynt... |
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 biosynt... |
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 biosynt... |
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 biosynt... |
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 biosynt... |
B9K7M6 | MKFGYFDDKNREYVIVTPRTPYPWINYLGTEDFFSIISHMAGGYCFYKDARLRRITRFRYNNVPTDAGGRYFYIREEDGDFWSPTWMPVRRDLSFFEARHGLGYTKIAGERNGLRATITFFVPRHFTGEVHHLVLQNRTERPRRIKLFSFIEFCLWNALDDMTNFQRNYSTGEVEIEGSVIYHKTEYRERRNHYAFYSVNHSIDGFDTDRESFMGLYNGFEAPQAVVEGNPRNSVASGWAPIASHYLELEIPPLGEKELIFILGYVENPEEEKWERPGVINKKRAKEMIERFKTGEDVERALKELKEYWDELLGRIQVET... | 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-... |
A0A1S4F020 | MIPRIVVVLLSVLAVVTARRSYEGYKVYGIVPESPDEAEILYQIRQSNPDLDFWHLTKQPGDEARVLVAPKDQRSFLIKLIRHGLHYQEVISDVEGTLAPYNEPRTRGMSLDRDVSTSYLRHNEINEYLQTLSQKYPSLVSVEEAGTSYEGRSIKTITINKKPGNAVVFLDAGIHAREWIAPATALYAIEQLVEHSSENQEVLSNLTWVIMPVVNPDGYEFSHETDRFWRKTRKPTGKTCKGTDGNRNFDYHWGEVGASTQACADTFRGETAFSEPETRAVRDAVMKLKGSCKFYLSLHSYGNYILYPWGWTSKLPETWE... | 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-te... |
P55261 | MAFLILVTLALASAHYSGEHFEGEKVFRVNVEDENHINLLHTLASTTQIDFWKPDSVTQIKPHSTADFRVKAEDILTVEDFLKQNELHYEVLINNLRLVLEGQFGRQVPATGHSYEKYNRWETIEAWTQQVTSENPDLISRRSIGTTFEGRTIYLLKVGKAGQNKPAIFMDCGFHAREWISPAFWQWFVREXIRTYGQEIHMTELLDKLDFYVLPVGNIDGYVYTWTKNRMWRKTRSTQVGTNCVGTDPTRNFDAGWCKIGASRNPCDETYCGPAAESEKETKALANFIRSNLSSIKAYLTIHSYSQMMLYPYSYDYKLT... | 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 | MLALLVLVTVALASAHHGGEHFEGEKVFRVNVEDENHINIIRELASTTQIDFWKPDSVTQIKPHSTVDFRVKAEDTVTVENVLKQNELQYKVLISNLRNVVEAQFDSRVRATGHSYEKYNKWETIEAWTQQVATENPALISRSVIGTTFEGRAIYLLKVGKAGQNKPAIFMDCGFHAREWISPAFCQWFVREAVRTYGREIQVTELLDKLDFYVLPVLNIDGYIYTWTKSRFWRKTRSTHTGSSCIGTDPNRNFDAGWCEIGASRNPCDETYCGPAAESEKETKALADFIRNKLSSIKAYLTIHSYSQMMIYPYSYAYKL... | 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... |
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... |
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... |
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... |
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... |
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- naphthoquino... |
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... |
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 ... |
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 homot... |
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 ... |
Q97PP9 | MRLTQMPSEFQKALPVLEKIKEAGFEAYFVGGSVRDALLHSPIHDVDIATSSYPEETKQIFPRTADIGIEHGTVLVLDGDEEYEVTTFRTEDVYVDYRRPSAVSFVRSLEEDLKRRDFTVNAFALDETGEIVDLFHGLEDLEKQVLRAVGVASERFNEDALRIMRGFRFQASLGFALEPETFKAMKTLTPLLEKISVERTFVEFDKLLLAPFWRRGLASMIESQAYDYLPDMASSQDKLNRLFDLETDFTFESSEQAWAALLWALEIENAQSFLKSWKTSRQFAKQVQDLLIILALRENGELSKRDCYRFDIDLLLQAEN... | 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 i... |
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-D... |
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... |
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 m... |
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... |
Q2RAR6 | MLCVAMAARPVSSTTSTCRPCLPAQVSASKPSTSSSPGTGVLVGVPRERGSSVSKAAIRGARLEAAARCSLVRQRPMLLATVAVGSLVAAGAANATEIGDSLLGSSGLALADLSVGDWFGNLLYSAGQQANEAVQDQLSALSFTSLAVIFGAGLVTSLSPCTLSVLPLTLGYIGAFGSGKDRSEVVGNSVAFSLGLATTLAILGVAASFAGKAYGQVGQGLPVAASGLAVIMGLNLLEVIELQLPSFFSDYDPRAAAANLPSSVQAYLAGLTFALAASPCSTPVLATLLGYVATSRDPIVGGSLLLTYTTGYVAPLLIAA... | 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 | MNLSVNRCITGGFVGGFSSCRLNHEKRWVRAGKHCELERERSLVSDAVSLERLESKSIKLAMLASGLGVANLVTLSSAKAADLKMIVLDQATSIYILAEGSLGDSVGNFLYSANQQANEAVQDQLSALSVTSLAVIFGAGLVTSLSPCTLSVLPLTLGYIGAFGSGKSRGQVIGDTVAFALGLATTLALLGIVASFAGKAYGQIGQGLPVAASGLAIVMGLNLLEIIELQLPSFFNNFDPRAAAANFPSSVQAYLAGLTFALAASPCSTPVLATLLGYVATSRDPVIGGSLLLTYTTGYVAPLIVAASFAGALQSLLSLR... | 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 pro... |
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
... |
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 ch... |
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 ... |
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)... |
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 eosinoph... |
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 Loc... |
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 Loc... |
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 Loc... |
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 Loc... |
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 Loc... |
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 Loc... |
P20248 | MLGNSAPGPATREAGSALLALQQTALQEDQENINPEKAAPVQQPRTRAALAVLKSGNPRGLAQQQRPKTRRVAPLKDLPVNDEHVTVPPWKANSKQPAFTIHVDEAEKEAQKKPAESQKIEREDALAFNSAISLPGPRKPLVPLDYPMDGSFESPHTMDMSIILEDEKPVSVNEVPDYHEDIHTYLREMEVKCKPKVGYMKKQPDITNSMRAILVDWLVEVGEEYKLQNETLHLAVNYIDRFLSSMSVLRGKLQLVGTAAMLLASKFEEIYPPEVAEFVYITDDTYTKKQVLRMEHLVLKVLTFDLAAPTVNQFLTQYFL... | 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... |
P51943 | MPGTSRHSGRDAGSALLSLHQEDQENVNPEKLAPAQQPRAQAVLKAGNVRGPAPQQKLKTRRVAPLKDLPINDEHVTAGPSWKAVSKQPAFTIHVDEAEETQKRPAELKETECEDALAFNAAVSLPGARKPLTPLDYPMDGSFESPHAMDMSIVLEDKPVNVNEVPDYQEDIHTYLREMEVKCKPKVGYMKRQPDITNSMRAILVDWLVEVGEEYKLQNETLHLAVNYIDRFLSSMSVLRGKLQLVGTAAMLLASKFEEIYPPEVAEFVYITDDTYSKKQVLRMEHLVLKVLAFDLAAPTVNQFLTQYFLHLQPANCKVE... | 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 di... |
Q1LZG6 | MALRITRNTKISAENKAKISMAGAKRVPVAAVATSKPGLRPRTALGDIGNKVSEQPQAKLPLKKEAKTLASGKVTAKKVPKPLEKAPVPVPEPQPEPEPEPEHVKEDKLSPEPILVDTPSPSPMETSGCAPAEEYLCQAFSDVILAVSDVDAEDGADPNLCSEYVKDIYAYLRQLEEEQAVKPKYLMGREVTGNMRAILIDWLVQVQIKFRLLQETMYMTVSIIDRFMQDTYVPKKMLQLVGVTAMFVASKYEEMYPPEIGDFAFVTDNTYTKFQIRQMEMKILRALNFSLGRPLPLHFLRRASKIGEVDVELHTLAKYL... | 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
|
Q10653 | MLRATNNRRTSNNVEKDSLQMAKHGNGPLKPVNAQGLQTKREAREILALKPSNPAPVETAQKSQRINLQDAETKCLAMADDIYKYLVHHEKKYLLEECFMEGGEPTPKMRRILVDWLVQVHVRFHLTPETLHLTVFILDRMLQKKVTSKADLQLLGISAMFVASKFEEVYLPDIHDYEFITENTYSKKQILAMEQTILNSLNFDLSCPSSLVFLRCLSRILSENDASPIDNQAFCYTYNISKCLGELALLDSVMASTPRSHIASASMIIALEVHPVDGIEAENAVSVICKQLGASKKVIEDAVALLAEVSYKNFKQGKLV... | 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
|
P14635 | MALRVTRNSKINAENKAKINMAGAKRVPTAPAATSKPGLRPRTALGDIGNKVSEQLQAKMPMKKEAKPSATGKVIDKKLPKPLEKVPMLVPVPVSEPVPEPEPEPEPEPVKEEKLSPEPILVDTASPSPMETSGCAPAEEDLCQAFSDVILAVNDVDAEDGADPNLCSEYVKDIYAYLRQLEEEQAVRPKYLLGREVTGNMRAILIDWLVQVQMKFRLLQETMYMTVSIIDRFMQNNCVPKKMLQLVGVTAMFIASKYEEMYPPEIGDFAFVTDNTYTKHQIRQMEMKILRALNFGLGRPLPLHFLRRASKIGEVDVEQH... | 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
|
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.-
|
Q6BIB1 | MTAIQKPVVAKREAPKAEVNPTVSRSTQTETIKPTKERTVSVFSPPVFNFAANSFAQSVSNEYKHASPKRIKLDNSRVQVPSIVKPKQDKPRPPAIVTKPRVINIEFPNKQKSGFKLLIRPKHEPSIKKQKQGIEVLSTSNTKRITKSISVDDVEYVEKVKHAIKQVLPKPDYDDGSLGPVILRLAWHCCATYNKFTGNGGSNGSTMRFVPEITDDGNSGLDIARSALEPIKQKFPDITYSDLWTLAGKISIQEMGGPKIPWRCGRVDCIDDRYVPPNGRLPFAYKNANHIRETFGRMGFNDRETVSLLGAHGLGRCHKR... | 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.-
|
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.-
|
Q4HWQ2 | MGIVDQPQSKGQESTPGDFAAVQKSIIDLLNQPDYDDGSAGPVLVRLAWHSSGTYDKVTDTGGSNGAGMRYEAEGGDPANAGLQNARVFLEPVKRLHPWITYSDLWTLAGVTAIHAMGGPEIDWLPGRTDFVDDSKLPPRGRLPDAAQGAEHIRHIFYRMGFNDREIVALSGAHNLGRCHTANSGFEGKWVNNPTRFSNQYFRLLLSETWTEKTIPESGLLQFSSVDQDTEEELMMLPTDIALTTDSEFSKYVQLYAKDKDVFFQDFKKAFAKLLELGIARNSEGKVINTDNQKGGYRSAPKKSDSTPATSGQPGASKTG... | 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.-
|
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.-
|
Q4PD66 | MSKLGDYAAVKKDILAVLKQPEYDDGSAGPVLVRLAWHASGTYCARTDTGGSNGAGMRYEAEGGDPANAGLQHARVFLEPIKEKHSWITYADLWTLAGVVAIEAMGGPSIQWKPGRTDFADDSRLPPRGRLPDGAQGADHLRFIFNRMGFNDQEIVALSGAHNLGRCHSDRSGFEGPWVNSPTRFSNQYYKLLLKLKWQPKKWDGPFQYVAKAPGADDDDEQLMMLPTDYALIQDEKMRPWVEKYAEDRDAFFNDFAKVFAKLIELGVYRDESGIARADKMKQFKGEYKSAPQKSPVPGAPGAGKDGEANPLARQNERAH... | 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.-
|
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 L... |
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.-
|
Q4WPF8 | MASAARSASRAFLRSTPTTSSFRPAVRAARFALPAQGFRAAGRRGYASEANSGKSSSNVFLWAGLAVAGGAGAYLYLNGSDSVTSKTFVPGKEDYQKVYDAIARRLADETDYDDGSYGPVLVRLAWHASGTYDKETGTGGSNGATMRFAPESDHGANAGLKIARDFLEPIKAQFPWISYSDLWTLAGACAIQELGGPTIPWRPGRQDKDVAACTPDGRLPDASKDQRHIRDIFYRMGFNDQEIVALIGAHALGRAHPDRSGYDGPWDFSPTVFTNEFFRLLVDEKWQNRKWNGPAQFTDKTTKTLMMLPADLALIKDKEF... | 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 L... |
Q5AEN1 | MATFAPHISKITKSSTKFNYGRIAKTFLGVAGSAAIATYFYNNGNPFNNNNNNNNNNGGSKNAAKALFGASAGANVKIAKVPEGKSASDYQKVYNDIATKISENLEFDENAGYYGQLLRLAWHTSGTYDKSDNSGGSYGGTMIFAPEEFDPENAGLQVGREFLMEFLVKYPWISRGDLWTLGGVAAVQESGGPKIEWRPGRVDDNTASKVPPNGRLPDASKDGKYVKDLFARMGFNERETVALLGAHVLGRCHKHNSGYDGPWGPSFNQFTNVFYTTLLGDWHVKKWDGKKQYEDDETGEFMMLPTDMALKEESYFLKYV... | 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 L... |
Q6FMG7 | MSATALRIAPIASRTFQRRLGYLLAGVATGAAATVAYKAQKNNNYYKYNNNNNNNSGFKAGALAAAAGVVHLAHEEDKKTADYQKVYNLIAERLRDDDEYDNYIGYGPVLVRLAWHSSGTWDKNDNTGGSYGGTYRYKKESQDPSNAGLENAAKFLEPVKKQFPWISYGDLYTLGGVVGIQELQGPKIPWRSGRTDLPEDMTPDNGRLPDGDKDANYVRNFYKRLDFNDREVVALLGAHALGKTHLKNSGFEGPWGAANNIFTNEFYLNLLNEDWKLEKNDAGNLQYNSPKGYMMLPTDYALIQDSNYLKIVKEYAADQD... | 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 L... |
Q6URB0 | MSFRAPNLIRSTVGRRAGQTLNLRSQVIRRRFATEGGPEITKPSAPRSSNTGYIFAGLGVAAVGAAYYFYGTGRTEHDSTNKADTVVREAVATVEAKTGLRRGKDEYQKVYNRIAETLDKEGYDDGSLAPVLLRLAWHASGTYSKADGTGGSNFATMRFKPEAEHSANNGLHVAREHMEKIKQEFPWISYGDLWTLGGVCAIQESGGPTIPWRPGRIDGYAAQVTPDGRLPDATQAQDHLRFIFNRMGFNDQEIVALSGAHAMGRCHPNRSGFDGPWTFSPVTFSNQYFALLRDEPWQWKKWTGPAQFEDKKTKTLMMLP... | 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 L... |
Q6BKY9 | MSTAAFKRQSVPLSKLFQSYGKNNSQSKYGGYFLATLIGSGILATSYFNNNKNGNTPSNNHKKLLAGSGIVNTAAIPKGKSIKDYQSLYNEIAEKVRDQDDADDGAGRYGLLTRLAWHTSGTYKKEDNTGGSYGGTMIYKPESTDGENSGLNHGRDFLQEFKDKYSWLSHGDLWTLGGVVAVQECGGPKIKWRPGRQDISDKTRVPENGRLPDASKDADYVKGVFGRMGFNERETVCLIGAHCLGKCHKENTNYDGPWGPSFNMFTNDFFVRLLQNWHVKKWDGKKQYEDDETNSFMMLPTDMALKEDSSFLKYVKMYAD... | 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 L... |
Q4ING3 | MASATRQFARAATRATRNGFAIAPRQVIRQQGRRYYSSEPAQKSSSAWIWLTGAAVAGGAGYYFYGNSASSATAKVFNPSKEDYQKVYNEIAARLEEKDDYDDGSYGPVLVRLAWHASGTYDKETGTGGSNGATMRFAPESDHGANAGLAAARDFLQPVKEKFPWITYSDLWILAGVCAIQEMLGPAIPYRPGRSDRDVSGCTPDGRLPDASKRQDHLRGIFGRMGFNDQEIVALSGAHALGRCHTDRSGYSGPWTFSPTVLTNDYFRLLVEEKWQWKKWNGPAQYEDKSTKSLMMLPSDIALIEDKKFKPWVEKYAKDN... | 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 L... |
P0CAW2 | MKFGPETIIHGDCIEQMNALPEKSVDLIFADPPYNLQLGGDLLRPDNSKVDAVDDHWDQFESFAAYDKFTREWLKAARRVLKDDGAIWVIGSYHNIFRVGVAVQDLGFWILNDIVWRKSNPMPNFKGTRFANAHETLIWASKSQNAKRYTFNYDALKMANDEVQMRSDWTIPLCTGEERIKGADGQKAHPTQKPEALLYRVILSTTKPGDVILDPFFGVGTTGAAAKRLGRKFIGIEREAEYLEHAKARIAKVVPIAPEDLDVMGSKRAEPRVPFGTIVEAGLLSPGDTLYCSKGTHVAKVRPDGSITVGDLSGSIHKIG... | 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 specific... |
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 m... |
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 met... |
Q82LU9 | MKEILDAIQSQTATSADFAALPLPDSYRAITVHKDETEMFAGLSTRDKDPRKSIHLDDVPVPELGPGEALVAVMASSVNYNSVWTSIFEPVSTFNFLERYGRLSDLSKRHDLPYHIIGSDLAGVVLRTGPGVNSWKPGDEVVAHCLSVELESSDGHNDTMLDPEQRIWGFETNFGGLAEIALVKSNQLMPKPDHLSWEEAAAPGLVNSTAYRQLVSRNGAGMKQGDNVLIWGASGGLGSYATQFALAGGANPICVVSSEQKADICRSMGAEAIIDRNAEGYKFWKDETTQDPKEWKRFGKRIREFTGGEDIDIVFEHPGR... | 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 ... |
Q9XIA4 | MIVTLNPKILHFSKIHPFSRPSSYLCRTRNVSLITNCKLQKPQDGNQRSSSNRNLTKTISLSDSAPPVTEETGDGIVKGGGNGGGGGGDGRGGLGFLKILPRKVLSVLSNLPLAITEMFTIAALMALGTVIEQGETPDFYFQKYPEDNPVLGFFTWRWISTLGLDHMYSAPIFLGMLVLLAASLMACTYTTQIPLVKVARRWSFMKSDEAIKKQEFADTLPRASIQDLGMILMGDGFEVFMKGPSLYAFKGLAGRFAPIGVHIAMLLIMVGGTLSATGSFRGSVTVPQGLNFVMGDVLAPIGFFSIPTDAFNTEVHVNRF... | 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
|
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
|
Q8GTZ9 | MQPYASVSGRCLSRPDALHVIPFGRPLQAIAGRRFVRCFAKGGQPGDKKKLNVTDKLRLGNTPPTLDVLKAPRPTDAPSAIDDAPSTSGLGLGGGVASPRTLVQSNAVQVAWRRLMKELSSLPRAIAIMALIAVLSGLGTFIPQNKSIEYYLVNYPDGAEKVLGFLTGDLILTLQLDHIYTADYFYLSMGLLAASLAACTYTRQWPAVKVAQRWRFLTQPKSLLKQGRTEVLPNARVSDLGAILLQRGYQVFVKDGSLYGFKGLAGKLGPIGVHAALLLCLFGTAWSGFGTLKGNVMCPEGQDFQVASFLQPSSPIASMP... | 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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