ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
P45593 | MASGVMVSDDVVKVFNDMKVRHQLSPEEAKKRKKAVIFCLSDDKKTIILEPGKEILQGDVGCNVEDPYKTFVKMLPRNDCRYALYDALYETKETKKEDLVFVFWAPEEASLKSKMIYASSKDAIRKRFTGIKHEWQTNTYDDINDPCNLADKLGGNTVVSLEGKSLRS | Function: May play a role in the regulation of cell morphology and cytoskeletal organization (By similarity). Binds to F-actin and exhibits pH-sensitive F-actin depolymerizing activity. Required for formation of the cleavage furrow during cytokinesis.
PTM: Inactive when phosphorylated. Phosphorylation levels vary durin... |
P23528 | MASGVAVSDGVIKVFNDMKVRKSSTPEEVKKRKKAVLFCLSEDKKNIILEEGKEILVGDVGQTVDDPYATFVKMLPDKDCRYALYDATYETKESKKEDLVFIFWAPESAPLKSKMIYASSKDAIKKKLTGIKHELQANCYEEVKDRCTLAEKLGGSAVISLEGKPL | Function: Binds to F-actin and exhibits pH-sensitive F-actin depolymerizing activity . In conjunction with the subcortical maternal complex (SCMC), plays an essential role for zygotes to progress beyond the first embryonic cell divisions via regulation of actin dynamics . Required for the centralization of the mitotic ... |
P45592 | MASGVAVSDGVIKVFNDMKVRKSSTPEEVKKRKKAVLFCLSEDKKNIILEEGKEILVGDVGQTVDDPYTTFVKMLPDKDCRYALYDATYETKESKKEDLVFIFWAPESAPLKSKMIYASSKDAIKKKLTGIKHELQANCYEEVKDRCTLAEKLGGSAVISLEGKPL | Function: Binds to F-actin and exhibits pH-sensitive F-actin depolymerizing activity (By similarity). Important for normal progress through mitosis and normal cytokinesis (By similarity). In conjunction with the subcortical maternal complex (SCMC), plays an essential role for zygotes to progress beyond the first embryo... |
Q9Y281 | MASGVTVNDEVIKVFNDMKVRKSSTQEEIKKRKKAVLFCLSDDKRQIIVEEAKQILVGDIGDTVEDPYTSFVKLLPLNDCRYALYDATYETKESKKEDLVFIFWAPESAPLKSKMIYASSKDAIKKKFTGIKHEWQVNGLDDIKDRSTLGEKLGGNVVVSLEGKPL | Function: Controls reversibly actin polymerization and depolymerization in a pH-sensitive manner. Its F-actin depolymerization activity is regulated by association with CSPR3 . It has the ability to bind G- and F-actin in a 1:1 ratio of cofilin to actin. It is the major component of intranuclear and cytoplasmic actin r... |
P45591 | MASGVTVNDEVIKVFNDMKVRKSSTQEEIKKRKKAVLFCLSDDKRQIIVEEAKQILVGDIGDTVEDPYTSFVKLLPLNDCRYALYDATYETKESKKEDLVFIFWAPESAPLKSKMIYASSKDAIKKKFTGIKHEWQVNGLDDIKDRSTLGEKLGGSVVVSLEGKPL | Function: Controls reversibly actin polymerization and depolymerization in a pH-sensitive manner. It has the ability to bind G- and F-actin in a 1:1 ratio of cofilin to actin. It is the major component of intranuclear and cytoplasmic actin rods. Required for muscle maintenance. May play a role during the exchange of al... |
O94677 | MDVKSKHGHIKSNPEESLLFRNSVSKNIAQLSSINYADRNVQAALEQLSERKFKNEREARKQLPFEVFSDLIWTNGSIIKELSELSSQTLSVQSQLLKVKNSIDSYKNEWSKKTNDAQILLNSYETFCEEEALIEEKLKNIEIFEKNFVIMDDDLIHLTSSTDVDDRFYLILDKAQEIHDSSDSLFASLSGFVEYSSFEEIVKKMSRYIEAAFEKLFRCVQTELSDPQTAQTLEANSHLKKAFTKLFSEPTMVNKSINLIVQARQQILSTAYLTALTRGDFLSSSRPIELSAPDTVRFIGDLLAWIHQTIVNEKELVEAL... | Function: Acts as component of the peripheral membrane COG complex that is involved in intra-Golgi protein trafficking. COG is located at the cis-Golgi, and regulates tethering of retrograde intra-Golgi vesicles and possibly a number of other membrane trafficking events (By similarity).
Location Topology: Peripheral me... |
P53959 | MDFVVDYQTYAMADTATPELPEPEPRLNLTSDAQSQPTGKLDLQFKLPDLQRYSNNNATLPVDNDGAGSKDLHKKMTHYAMSSIDKIQLSNPSKQLGQNSQDEKLSQQESQNFTNYEPKNLDLSKLVSPSSGSNKNTTNLVLSNKLSKILNNYTLINYQATVQLRKSLKVLEENKERLSLDEQKLMNPEYVGTLARRALRTDLESQLLKEHITVLEEFKPIIRRIKRLSSSVEKIQRTSEKLLSNETNEVPTNNVVLQEIDQYRLKAEQLKLKKKILLSIRDRFTLNQVEDDVITNGTIDNIFFEVVKKVINIKDESSFL... | Function: Acts as component of the peripheral membrane COG complex that is involved in intra-Golgi protein trafficking. COG is located at the cis-Golgi, and regulates tethering of retrograde intra-Golgi vesicles and possibly a number of other membrane trafficking events.
Location Topology: Peripheral membrane protein
S... |
Q9FGN0 | MMLDLGPFSDEKFDAKRWVNSSCQARHPQDSLEKHLVDLEMKLQIASEEIGASLEEQSGGALLRVPRATRDVLRLRDDAVSLRGSVAGILQKLKKAEGSSADCIAALARVDNVKQRMEAAYKTLQDAAGLTQLSSTVEDVFASGDLPRAAETLASMRNCLSAVGEVAEFANVRKQLEVLEDRLEAMVQPRLTDALTYHKVDVAQDLRVILIRIGRFKSLELQYSKVRLKPIKQLWEDFDTKQRANKLANERSESQRLSSGDEFQSTSSQTSFASWLTSFYDELLLYLEQEWKWCMVAFPDDYMTLVPKLLVETMGVLGAS... | Function: Required for normal Golgi function . Necessary for embryo development and pigmentation, especially for the expansion of cells and organs, and for the formation of the organized shoot apical meristem (SAM) . Probably involved in the generation of the extra-cellular matrix .
Location Topology: Peripheral membra... |
Q54LC8 | MINNELKDIFSSNDFNSKTWINNLLSDCGGSGSSSGNAKSNQQSILTDQNNIKAELEIENICSNYLSKLQLYQIELNISLESITSESLLIVPKSIREVDRIRKESLHLKNRIKSISSKIGEMNNDSPQSMETVSVIEKLDQVKSRMEISIRSLKEAEKLLSFSKTVDQLFSSNDYLMISDKLEEVKQSLSVLSDVPEFREQSKKFNVYQDRLESQLKQPLQQSLQQKDLESCKNYLKIFTNIQRQDKFFIYYYQVRIDPLKLLWNSYSSSSSSSSSSSNFHNWLSKFYDEVLVMINSEFNWLSGLCPIDYIQVLENLIIH... | Function: Required for normal Golgi function.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 113321
Sequence Length: 996
Subcellular Location: Golgi apparatus membrane
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Q9VAD6 | MDVSALSETTFSPAEWINANYKKFVEENGRDDSEAASAFIRSYVAKLQLYIFNVNNAVEESSRQVVASMPRIAKESAALQADVHRLQEKMSAMRLEVAAVQSETGECMATLERLNTKSQKLQVAKESLQESDGWGNLLAELEDGFERNDLKGVCDKLIALQKSLHAQEQLPGHAERQTQVEDFKNRLEALASPSVVQCFAEGNTEQAQHFVQIFTSIQRLPQLQQYYRAVQKNFWQQQWKQTLELQGTESQPQQQQFLTLYYDQLLEHCQRQVKWCSNLFGENSPQPFLVIAELLPALQPTRDAHILQLLKTSNERLEML... | Function: Required for normal Golgi function.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 84076
Sequence Length: 742
Subcellular Location: Golgi apparatus membrane
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P83436 | MDFSKFLADDFDVKEWINAAFRAGSKEAASGKADGHAATLVMKLQLFIQEVNHAVEETSHQALQNMPKVLRDVEALKQEASFLKEQMILVKEDIKKFEQDTSQSMQVLVEIDQVKSRMQLAAESLQEADKWSTLSADIEETFKTQDIAVISAKLTGMQNSLMMLVDTPDYSEKCVHLEALKNRLEALASPQIVAAFTSQAVDQSKVFVKVFTEIDRMPQLLAYYYKCHKVQLLAAWQELCQSDLSLDRQLTGLYDALLGAWHTQIQWATQVFQKPHEVVMVLLIQTLGALMPSLPSCLSNGVERAGPEQELTRLLEFYDA... | Function: Required for normal Golgi function.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 86344
Sequence Length: 770
Subcellular Location: Golgi apparatus membrane
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P53195 | MVELTITGDDDDILSMFFDEEFVPHAFVDILLSNALNEDQIQTQSVSSLLLTRLDFYTKNLTKELESTIWNLDKLSQTLPRTWASSRYHKEAEQNDSSLYSTESLKSSKLEYYLDTLASAVRALETGMHNVTEKLSDLDNENNRNTNVRQQLQSLMLIKERIEKVVYYLEQVRTVTNISTVRENNTTSTGTDLSITDFRTSLKALEDTIDESLSSAIDNEAKDETNKDLIGRIDSLSELKCLFKGLDKFFAEYSNFSESIKSKAQSYLSTKNIDDGMIS | Function: Acts as component of the peripheral membrane COG complex that is involved in intra-Golgi protein trafficking. COG is located at the cis-Golgi, and regulates tethering of retrograde intra-Golgi vesicles and possibly a number of other membrane trafficking events.
Location Topology: Peripheral membrane protein
S... |
Q84K25 | MAMEVGEMSQPEATASLLSLASATQQPYVSELLSFTLDRLHKEPELLRVDAERIQRQMQEVAVGNYRAFITAADALLAIRQEVSSIDKHLESLIGEVPKLTSGCTEFIDSAENILEKRKMNQALLANHSTLLDLLEIPQLMDTCVRNGNFDEALDLEAFVSKLATLHPKLPVIQALAAEVRQTTQSLLSQLLQKLRSNIQLPECLRIIGYLRRIGVFGEYEMRLQFLRCREAWLTGILEDLDQKNAYEYLKGMINCHRMHLFDVVNQYRAIFSDDTSGSEENYDGGLLFSWAMHQITSHLKTLKIMLPKITEGGSLSNIL... | Function: Acts as component of the peripheral membrane COG complex that is involved in intra-Golgi protein trafficking . Involved in pollen tube growth by modulating Golgi morphology and vesicle trafficking homeostasis leading to the deposition of cell wall components and proteins at the pollen tube tip . Required for ... |
O44502 | MDSDYIFHNGDDIRNMGLEEMRRQKVLLASELKAIDAQISDLAFNNYGTYADAGRATHDCSKTFGEMRDKTVNLSDQAEELTSAFVEFRAKAKQLSEEQDLVRKALDKSNPIWELLTLPSRMDICIRAGYYDLAYTLTNYGLQLQQQTQLYRNPLIKKVADHLVEARAYLLEELFNKFAGPLDLAESIKVVNNVRKMPSLTANQLRIAVLQHRDIYLEKQILDISGNVDMIVQAIEIYRTSMYDTLVLYLAVFPENEVVRKNPNADPRWESWPVLPPNSILSQWVISNVKKMLDLITKADVKSAVDLSAVWTKLMAMASS... | Function: Required for normal Golgi function.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 83844
Sequence Length: 743
Subcellular Location: Golgi apparatus membrane
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Q55BB8 | MSKVNTDENNFINNNNSNNNINNNDNNDNNNNNIQNVSNQIENGLLSNLPTISSSCESFSSKSHSLTERRSSIKNLLDNFSTLLDILEIPQLMDTCIKNNSFDEALQLESFAKKIYKQYSNNTVIIEIIKEIKVCTRSLISTLQQQLRQDITLTNCIKTIGYLRRLSIYKENELKIIFLHSRDQWLINSLKFDITNSNHVTYLTKLTDSCRTNIFDIVTQYNAIFSNESNDEDQLDDLILYNWIQQKIKVYINIVDSTLNHIKSGSSISYVLENSMYFSMSISRVGIDFRNLLEPIFEKHILNNFLSQITTANHHFLETL... | Function: Required for normal Golgi function.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 87207
Sequence Length: 779
Subcellular Location: Golgi apparatus membrane
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Q9VKH0 | MDFPDKMDLENERVLKLIFPDGVPDNLRGNPELDNYLAKLGTCKVEQLKKEQTRLAEEARTILEQTQDLAISNYRTFITTAENSRSIFSEFLRSEQQLDTLVSKLPDLSVQCERFLQDSAELNEQRRLNSITLQKNAQLLEVLELPQLMERCIREGRYEEALELAAYATRLGQHQGHIPVVTSIVRSVEALWHNMLVQLVAQLRTDLQLPKCLQIVGYLRRMQAFGDNELRLKFLQARDAWLTSCLEAIPTADAQQHLSKTIEITRINLFNIITQYRAIFPEDEGTLKTQSSLRPLQGVSCNGDRLFQAWLHNKISDFLQ... | Function: Required for normal Golgi function.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 64910
Sequence Length: 570
Subcellular Location: Golgi apparatus membrane
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B9J3S4 | MNKKSKINKVMLSISTMALSLGALQAPASAEEKVPYNVLKTKPVGIEKPVDEIGHVSKAEETLSFQERLKVGDFSQRPASIPNKAAVKQVKESYSMADLNKMNDQELVETLGCIKWHQITDLFQFNEDAKAFYKDKGKMQVIIDELAHRGSTFTRDDSKGIQTFTEVLRSAFYLAFYNNELSELNERSFQDKCLPALKAIAKNPNFKLGTAEQDTVVSAYGKLISNASSDVETVQYASNILKQYNDNFNTYVNDRMKGQAIYDIMQGIDYDIQSYLIEARKEANETMWYGKVDGFINEINRIALLNEVTPENKWLVNNGI... | Function: Acts as a true collagenase, which is highly active and cleaves natively folded collagen . In vitro, can also cleave gelatin and the synthetic peptide FALGPA (furylacryloyl-Leu-Gly-Pro-Ala) . Causes damage on dermal collagen (COL), resulting in gaps in the tissue, which might lead to an accelerated bacterial i... |
Q9Y215 | MVVLNPMTLGIYLQLFFLSIVSQPTFINSVLPISAALPSLDQKKRGGHKACCLLTPPPPPLFPPPFFRGGRSPLLSPDMKNLMLELETSQSPCMQGSLGSPGPPGPQGPPGLPGKTGPKGEKGELGRPGRKGRPGPPGVPGMPGPIGWPGPEGPRGEKGDLGMMGLPGSRGPMGSKGYPGSRGEKGSRGEKGDLGPKGEKGFPGFPGMLGQKGEMGPKGEPGIAGHRGPTGRPGKRGKQGQKGDSGVMGPPGKPGPSGQPGRPGPPGPPPAGQLIMGPKGERGFPGPPGRCLCGPTMNVNNPSYGESVYGPSSPRVPVIF... | Function: Anchors the catalytic subunits of asymmetric AChE to the synaptic basal lamina.
PTM: The triple-helical tail is stabilized by disulfide bonds at each end.
Sequence Mass (Da): 47766
Sequence Length: 455
Domain: The proline-rich attachment domain (PRAD) binds the AChE catalytic subunits.
Subcellular Location: S... |
Q899Y1 | MKKKFIKMLCSIAIGCMISTSYSIKVSAFSNGNTKTNPNGEFKSLSLNSTNPYKTKYSFNDLNKLSNKEILDLTSKIKWSDISDLFQYNKDSYTFYSNKERVQALIDGLYEKGCNYTSTDDKGIDTLVEILRSGFYLGYYNDSLKYLNDKSFKDKCIPAMIAIENNKNFKLGENGQDTVVHALGKLIGNTSCNDEVVNKTIPILEQYYNEIDKYSKDRLKSNAVYNFMKEINYDISQYEYAHNIRDYKNTPWSGKIDSFIDTISKFASISNVTKDNGWIINNSIYYTAKLSKYHSNPSIPHSVIDNCIEIFPDYSEQYFT... | Cofactor: Binds about 5 Ca(2+) per subunit (Probable). The metallopeptidase domain binds 1 Ca(2+), while each CDB binds 2 (Probable).
Function: Clostridial collagenases are among the most efficient degraders of eukaryotic collagen known; saprophytes use collagen as a carbon source while pathogens additionally digest co... |
P17811 | MKKSSIVATIITILSGSANAASSQLIPNISPDSFTVAASTGMLSGKSHEMLYDAETGRKISQLDWKIKNVAILKGDISWDPYSFLTLNARGWTSLASGSGNMDDYDWMNENQSEWTDHSSHPATNVNHANEYDLNVKGWLLQDENYKAGITAGYQETRFSWTATGGSYSYNNGAYTGNFPKGVRVIGYNQRFSMPYIGLAGQYRINDFELNALFKFSDWVRAHDNDEHYMRDLTFREKTSGSRYYGTVINAGYYVTPNAKVFAEFTYSKYDEGKGGTQTIDKNSGDSVSIGGDAAGISNKNYTVTAGLQYRF | Function: Seems to play an essential role in plague transmission by mediating flea blockage in a temperature-dependent fashion. Fibrinolytic activity prevails at 37 degrees Celsius whereas coagulase expression predominates at lower temperatures (<30 degrees Celsius). Activates plasminogen by cleaving it.
Catalytic Acti... |
F4ZGF2 | MLWVVLAVVVVLASVLVLLRQSSGLLALLWHDVVHQRLLNFFTGLSRPQRILKAVQKNATKGNPESVIAAIDHYCRHSEWAMNVGDEKGLILDSVVTEVNPSTALELGTYCGYSTVRIARLLSPGTKLITLEFNPDYAAIARQIIAYAGLQDKVILVEGPSGDLIPKMKQQHGIKSFDFVFLDHWKDRYVPDTKLLEECGLLRKGSVLLADNVICPGTPEYLKYVRNDPRYESRYFKSNLEYTKVEDGLEKSVFLG | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Catalyzes the O-methylation, and thereby the inactivation, of catecholamine neurotransmitters and catechol hormones. Shows highest activity towards catecholestrogens and dobutamine. Also has lower activity towards L-DOPA, dopamine and epinephrine. Active towards the x... |
A4IG53 | MLGVLLCWCLGASVLLYVLYSWLIPAAVQFNGSLALLWHDVIVERALDSLTRSTRPQRLLKAVKQHATRGDPQSVISAIDHFCRHREWAMNVGDEKGCILDSVVSELNPEKVLELGTYCGYSTVRIARLLPPGARLITLEFNPDYAVIARQVIAWAGIEDKVQLVEGASEDWIPRMKEHFGIETFDLVFLDHWKDHYLPDTKLMEGCGLLRKGTVLLADNVICPGVPDYLEYVRNSRSYKSCYFKSHLEYTRAEDGLEKSVFLG | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Catalyzes the O-methylation, and thereby the inactivation, of catecholamine neurotransmitters and catechol hormones.
Catalytic Activity: a catechol + S-adenosyl-L-methionine = a guaiacol + H(+) + S-adenosyl-L-homocysteine
Sequence Mass (Da): 29872
Sequence Length: 264... |
A7MBI7 | MLEAPPLLLVAGGVGLALLALRWLATTDLQFFGRAFIVWNEFIMKPIRNLLMGSSKEQRILQHVLQHAVAGDPQSVVAAIDSYSLEKEWAMHVGEKKGQIVDRVLREQQPSVLLELGAYCGYSAVRMARLLLPGARLLTIEFNPDYAAITQRMVEFAGLQDKVTVVLGASQDIIPQLKKKYDVDTLDMVFLDHWKDRYLPDMLLLEECGLLREGTVLLADNVIYPGAPDFLEYVRGNSRFECSHFSSYLEYSKVVDGLEKVVYKGLSGPARP | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Catalyzes the O-methylation, and thereby the inactivation, of catecholamine neurotransmitters and catechol hormones. Also shortens the biological half-lives of certain neuroactive drugs, like L-DOPA, alpha-methyl DOPA and isoproterenol.
Catalytic Activity: a catechol ... |
Q5H879 | MLEPTPMLLAAFSLGLALLPLLFFLRRWGWLLIGWNECILQPIHNLLMGDSKEQRILRHVLQHAVAGDPQSVLETIDAYCSQKEWAMNVGDKKGQFLDAVVQEQQPSVLLELGAYCGYSAVRMARLLPPGARLLTIEINPDYAAITQRMLDFAGLQDRVTVVLGASQDIIPQLKKKYDVDTLDVVFLDHWKDRYLPDTLLLEECGLLRKGTVLLADNVIVPGAPDFLAHVRGSGRFECTHFSSYLEYSLWVVDGVEKAVYLGPGSPAQP | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Catalyzes the O-methylation, and thereby the inactivation, of catecholamine neurotransmitters and catechol hormones. Also shortens the biological half-lives of certain neuroactive drugs, like L-DOPA, alpha-methyl DOPA and isoproterenol.
Catalytic Activity: a catechol ... |
P21964 | MPEAPPLLLAAVLLGLVLLVVLLLLLRHWGWGLCLIGWNEFILQPIHNLLMGDTKEQRILNHVLQHAEPGNAQSVLEAIDTYCEQKEWAMNVGDKKGKIVDAVIQEHQPSVLLELGAYCGYSAVRMARLLSPGARLITIEINPDCAAITQRMVDFAGVKDKVTLVVGASQDIIPQLKKKYDVDTLDMVFLDHWKDRYLPDTLLLEECGLLRKGTVLLADNVICPGAPDFLAHVRGSSCFECTHYQSFLEYREVVDGLEKAIYKGPGSEAGP | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Catalyzes the O-methylation, and thereby the inactivation, of catecholamine neurotransmitters and catechol hormones. Also shortens the biological half-lives of certain neuroactive drugs, like L-DOPA, alpha-methyl DOPA and isoproterenol.
Catalytic Activity: a catechol ... |
Q99028 | KERAMHVGRKKGQIVDTVVQEQRPSVLLELGAYCGYSAVRMARLLLPSARLLTIELNPDNAAIAQQVVDFAGLQDRVTVVVGASQDIIPQLKKKYDVDTLDMVFLDHWKDRYLPDTLLLEECGLLRKGTVLLADNVICPGAPDFLAHVRGCGRFECTHFSSYLEYSQMVDGLEKAVYKGPGSPAQP | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Catalyzes the O-methylation, and thereby the inactivation, of catecholamine neurotransmitters and catechol hormones. Also shortens the biological half-lives of certain neuroactive drugs, like L-DOPA, alpha-methyl DOPA and isoproterenol.
Catalytic Activity: a catechol ... |
Q9K5K3 | MMQDLINYFLSYPEVLKKLKNREACLIGFSSNETETIIKAYNDYHLSSPTTREWDG | Function: Part of a major quorum-sensing system that regulates the development of genetic competence . Acts through the activation of the two-component regulatory system ComP/ComA composed of a sensor histidine kinase, ComP, and a response regulator, ComA (By similarity).
PTM: Trp-54 is modified by farnesylation, which... |
Q9K5K8 | MQEMVGYLIKYPNVLREVMEGNACLLGVDKDQSECIINGFKGLEIYSMLDWKY | Function: Part of a major quorum-sensing system that regulates the development of genetic competence . Acts through the activation of the two-component regulatory system ComP/ComA composed of a sensor histidine kinase, ComP, and a response regulator, ComA (By similarity).
PTM: Trp-51 is modified by geranylation, which ... |
P0CY50 | MKQDMIDYLMKNPQVLTKLENGEASLIGIPDKLIPSIVDIFNKKMTLSKKCKGIFWEQ | Function: Part of a major quorum-sensing system that regulates the development of genetic competence (By similarity). Acts through the activation of the two-component regulatory system ComP/ComA composed of a sensor histidine kinase, ComP, and a response regulator, ComA (By similarity).
PTM: Trp-56 is modified by isopr... |
D4G0R3 | MKHIDKIISHLVNNPEAFDQFKNGNLTLLNINEKEKKAILYAFEQGEVPRTSKWPPIEAISNFFEDDKRKSLI | Function: Part of a major quorum-sensing system that regulates the development of genetic competence . Acts through the activation of the two-component regulatory system ComP/ComA composed of a sensor histidine kinase, ComP, and a response regulator, ComA (By similarity). Activates the expression of the genes for biosy... |
P45453 | MQDLINYFLNYPEALKKLKNKEACLIGFDVQETETIIKAYNDYYLADPITRQWGD | Function: Part of a major quorum-sensing system that regulates the development of genetic competence . Acts through the activation of the two-component regulatory system ComP/ComA composed of a sensor histidine kinase, ComP, and a response regulator, ComA . Activation of ComA leads to the direct regulation of over 20 g... |
Q38200 | MKSIRCKNCNKLLFKADSFDHIEIRCPRCKRHIIMLNACEHPTEKHCGKREKITHSDETVRY | Cofactor: One Zn(2+) per molecule.
Function: Trans-acting positive regulator required for mom mRNA translation. Binds the com-mom mRNA 5' and destabilizes a translation inhibition stem to expose mom translation start signals (By similarity).
Sequence Mass (Da): 7414
Sequence Length: 62
Subcellular Location: Host cytopl... |
Q7PVF6 | MWRTKRGRTRRRDAGGNPWQNLEKTSVLQETRMFNETPVNARKCTHILTKILYLLNQGEVLGTREATECFFAMTKLFQSKDVVMRRMVYLGIKELSPIADDVIIVTSSLTKDMTGKEDLYRAPAIRALCSITDSTMLQAVERYMKQCIVDRNAPVSSGALVSSLHLASTAGEVVKRWANEAQEALNSDNIMVQYHGLGLLYHIRKADRLAVTKLVNKLTRQHLRSPYATCFLIRIACKIMEEEDASGNATEDSPLFNFVECCLRNKSEMVVYEAAHAVVNLKRTNPRELSTAVSILQLFCGSSKATLRFAAVRTMNKVAM... | Function: The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. Coatomer complex is required for budding from Golgi membra... |
Q0WW26 | MAQPLVKKDDDHDDELEYSPFMGIEKGAVLQEARVFNDPQVDPRRCSQVITKLLYLLNQGESFTKVEATEVFFSVTKLFQSKDTGLRRMVYLIIKELSPSSDEVIIVTSSLMKDMNSKIDMYRANAIRVLCRIIDGTLLTQIERYLKQAIVDKNPVVSSAALVSGLHLLKTNPEIVKRWSNEVQEGIQSRSALVQFHALALLHQIRQNDRLAVSKLVGSLTRGSVRSPLAQCLLIRYTSQVIRDMANHGQSGERPFYEFLESCLRHKAEMVILEAARAITELDGVTSRELTPAITVLQLFLSSPRPVLRFAAVRTLNKVA... | Function: The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. Coatomer complex is required for budding from Golgi membra... |
Q54HL0 | MASRVQKKDDDESDFLFENLDKGQVIQEKRAFNESPIHPRKCSLVISQFLYLLSRGDSFTKTEATDIFFAATKLFQSKDIPLRRLMYLLLKELSTISQDAIIVISSLTKDMSHKIELYRANAIRILCKITDSSILPQIERYFKQSIVEKDPHVSSAALVSSIHLLKVCPEIVKRWANEVQEAISNKSNMVQYHALALLHRIKQHDRLAVSKLVSNLIKNSLRSPYAQSYLIRCCVEVIEETNTEDRIFREYIESCLRSKNEMVAYEAARSICTFKNVSNKEINSAVGVLQNFLNSTKPTLRFAAVRTLNKLAQTNPTAVI... | Function: The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. Coatomer complex is required for budding from Golgi membra... |
Q8I0G5 | MNYFSLTSHKKHRGHPSAGPSNAYQNLEKTSVLQETRTFNETPVNPRKCIHILTKILYLINQGEQLVAREATDCFFAMTKLFQSKDVVLRRMVYLGIKELSSIAEDVIIVTSSLTKDMTGKEDLYRAAAIRALCSITDNTMLQAVERYMKQCIVDKNAAVSCAALVSSLRLANTAGDVVKRWANEAQEALNSDNIMVQYHALGLLYHIRKSDRLAVSKLVNKLTRGSLKSPYAVCMLIRIACKLIEEEDIPSEELSDSPLFTFIESCLRHKSEMVIYEAAHAIVNLKNTNPRMLSPAFSILQLFCSSPKATLRFAAVRTL... | Function: The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. Coatomer complex is required for budding from Golgi membra... |
P87140 | MSYSKKDDDGDESIFANVNQVTVTQDARAFNSSSISPRKSRRLLSKIAYLIYTGEHFQEKQATELFFGITKLFQHKDPSLRQFVYIIIKELSVVAEDVIMITSSIMKDTATGRETIYRPNAIRSLIRVIDANTVPAIERILTTGIVDPISAVASAALVSAYHLYPVAKDIVSRWNNEVQDAVTSHNVGRKVASSPFFTSTLGYTPNASGISQYHALGLLYRIRRHDSIAMNKLLQLLVSNLGTVSNSHAFVMLIRYISSLMDQNTQFRDQMVPFLHGWLKSKGDMVNLEVARNMVRLKNISDDDLQPVVSVLKIFLSSHR... | Function: The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. Coatomer complex is required for budding from Golgi membra... |
P32074 | MSAHTYKKFENSTSGDLPDKMTIYQDCMNTFNESPVNSKRCRLLISRLLRLLAQGETFPQNEATALFFSISKLFQHQNDPLRQAVYLAIKELSGISEDVLMATSSIMKDVQNGSDLIKPDAIRSLTYVLDESTAFSAERLLKSAVVSRHPSISSAALCTSYHLLPISEVTIRRFTNETQEAVLDLKQFPNQHGNSEYYPNSTYISQYHALGLLYQLKKTDKMALLKLVRHFSENNSMKNQLAKVELVKIVNDLIYRDPQLFSQFRPLLSDWLSNKFESVQLETAKLITSFATRNSRLVAPELYAAAISALQSLLTVPRVS... | Function: The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. Coatomer complex is required for budding from Golgi membra... |
W8FLH9 | MKNRILRPALLCVAALFATTAQADAGHDHGSAHAGAHAHDADTPYGRPGDAAKAQRTVRVVMSDTMRFDPATITVRRGETVRFVAANGGRIEHEFVLGTTASLKAHAQEMRAMPDMQHADPGAVRVAAGASGEIVWQFTKAGSFEFACLIPGHFEAGMVGKVVVR | Function: Involved in copper tolerance . Required for copper resistance under both aerobic and anaerobic photosynthetic growth conditions . Binds copper . Could be an important defense against copper in the periplasm and may protect not only c type cytochromes but also other proteins with cysteine residues from copper ... |
O01884 | MKLPGGTIICARNASSYYDTVIVGGGMVGNAMACSLGANKSFQSKSVLLLDAGRSPSLASFKPGAPFNNRVVATSPTSIDTFKKLGVWDQINSHRTKKVNRLFVFDSCSTSEIEFERGQQEEVAFIIENDLIVGSLYEKLAEYKNVDVKTGAKVEDCSIPNALENMATIKLENGDVIETSLLIGADGVNSKVRHASNLDYTTFNYNQHGLVAIVNIETANGKNETAWQRFTTLGPVALLPLSDTVSGLTWSTSPEEAQRLKQLPSDQFVDELNSALFSQNNQIPLVNQTIFALNRMNPFRTETFGRKAEGTTPPHVITVQ... | Function: FAD-dependent monooxygenase required for the C5-ring hydroxylation during ubiquinone biosynthesis. Catalyzes the hydroxylation of 3-polyprenyl-4-hydroxybenzoic acid to 3-polyprenyl-4,5-dihydroxybenzoic acid. The electrons required for the hydroxylation reaction may be funneled indirectly from NADPH via a ferr... |
F1RAX8 | MLSLAKAKLAVVGIGRQCVAVRTLNGARAVHRSFSSSEHDQDSSTSENELFDIIISGGGMVGTAMACSLGLDPNLTGKKILLLEAGHEKKMDKIPETYSTRVSSISPGSATLLSGLGAWDHIVNMRCKPYNKMQVWDACSDALITFDKENLQDEMAYIVENDVIVAALTKQLQTLSDHVKVQYRTKVVKYTWPHPYHVSESIPWVQVALANGKTLHTKLLIGADGPNSMVRREAGIPTVKWNYDQSAVVAVLHLSEPTENNVAWQRFLPTGPIAMLPLSDTESSLVWSTSHQHAEELLQMDEESFVDAINSAFWSNENHS... | Function: FAD-dependent monooxygenase required for the C5-ring hydroxylation during ubiquinone biosynthesis. Catalyzes the hydroxylation of 3-polyprenyl-4-hydroxybenzoic acid to 3-polyprenyl-4,5-dihydroxybenzoic acid. The electrons required for the hydroxylation reaction may be funneled indirectly from NADPH via a ferr... |
Q54EN1 | MLRLINKTINKNDLIKINNSKRFCSTTTNSTINKDNIYDIIIIGGGLVGSTMACSIGNNNTTKHLKVALIESSKIQTVEQSISNAIPEIRTISFNNQTIELFKSINVWDTIKSTKRVNPFNQVRVWDTSGFEGIHFQDNDIIDDGNNTTAMGYIIENNIVTSSLLSKVKQFENIELFEQLSVKSMNDYNEETIRTTSILPSVTLSNDQQLHAKLIIGADGGNSILKKQLQVPSIGRVYNQKAVVCTLKLGIKQDNNNNSSNNNNNNNNTLFQRFLPTGPIALLPLANGYANIIWSTNLMHAQYLLELDDESFLEQVKDSF... | Function: FAD-dependent monooxygenase required for the C5-ring hydroxylation during ubiquinone biosynthesis. Catalyzes the hydroxylation of 3-polyprenyl-4-hydroxybenzoic acid to 3-polyprenyl-4,5-dihydroxybenzoic acid. The electrons required for the hydroxylation reaction may be funneled indirectly from NADPH via a ferr... |
Q9VMQ5 | MLGVLRIQGALASAGQARLLSVRLLASKSTTDMTTNRGESTQSTSTEHFDIIIGGGGLVGTTLAAALAKNSTLADKKVLLLEGAPEFRGFNPTGPYQNRVSAINHNSIELFKSIDAWKHIESARYKPVKQMQVWESNTDALIQFQHDNFASDVACIIENDLILDAVYALAKESPNVEILNKARIQCVRLPRDSNSNHSELQLEDGRNFSCDLLIGADGANSVVRKEMNVDVFSLNYDRMGLVATLELGEDACDNSVAWQRFLPNGPVALLPLTDRLSSLVWSTTNEQAKMLQALPPTEFVDALNEAFCRQYPRVELADKA... | Function: FAD-dependent monooxygenase required for the C5-ring hydroxylation during ubiquinone biosynthesis. Catalyzes the hydroxylation of 3-polyprenyl-4-hydroxybenzoic acid to 3-polyprenyl-4,5-dihydroxybenzoic acid. The electrons required for the hydroxylation reaction may be funneled indirectly from NADPH via a ferr... |
Q9Y2Z9 | MAARLVSRCGAVRAAPHSGPLVSWRRWSGASTDTVYDVVVSGGGLVGAAMACALGYDIHFHDKKILLLEAGPKKVLEKLSETYSNRVSSISPGSATLLSSFGAWDHICNMRYRAFRRMQVWDACSEALIMFDKDNLDDMGYIVENDVIMHALTKQLEAVSDRVTVLYRSKAIRYTWPCPFPMADSSPWVHITLGDGSTFQTKLLIGADGHNSGVRQAVGIQNVSWNYDQSAVVATLHLSEATENNVAWQRFLPSGPIALLPLSDTLSSLVWSTSHEHAAELVSMDEEKFVDAVNSAFWSDADHTDFIDTAGAMLQYAVSL... | Function: FAD-dependent monooxygenase required for the C5-ring hydroxylation during ubiquinone biosynthesis. Catalyzes the hydroxylation of 3-hexaprenyl-4-hydroxybenzoic acid (HHB) to 3-hexaprenyl-4,5-dihydroxybenzoic acid (DHHB). The electrons required for the hydroxylation reaction may be funneled indirectly from NAD... |
Q9Y7Z9 | MSSLVLRGVSRVEMPTISPTLGIYTRKFASQKILQRQFDVVIVGSGPVGLALAAGLQSNPVTQSLKVGLLDIQDTMKLKDWKFETYSNRCSSLTNHTRMFFDKIGAWDFARKDRIQPFQHILASDGLTNSSIHLDQKPGSEPMAFMSENVNLQYALLNSIIDKMNNNIKKPNLEFLMPCTITKLSKGENIYRTHIHTTTHGELTTKLLIGADGRNSIVRKYANISMPGWNYLTHAVVGTLKIDPLKGPAVAFQRFLPTGPLAYLPLPDNNATFVWSTRPHIASKLLRLPEETFVKFLNASFRLDYPDLSYLYQMDFSEPS... | Function: FAD-dependent monooxygenase required for the C5-ring hydroxylation during ubiquinone biosynthesis. Catalyzes the hydroxylation of 3-polyprenyl-4-hydroxybenzoic acid to 3-polyprenyl-4,5-dihydroxybenzoic acid. The electrons required for the hydroxylation reaction may be funneled indirectly from NADPH via a ferr... |
Q6DF46 | MRCLGGSSLSRLLRMLSQSQGRALSSTGPAVYDVVISGGGMVGTAMACALGSDPHLQHKKVLLLEAGNRKPFDHLPENFSNRVSSITPGSATLLASFGAWDHILAMRLKPYKRMQVWDACSDALITFDKDALEDMGYIVENDIIIEALTKQLELMSDHVEVMYRSRALSYSWPPPYNNGKATPWVEIELADGQRLHTKLLIGADGHNSMVRSAAGMQSVQWNYNHAAVVATLHLSEATDNNVAWQRFLPTGPIALLPLSDTCSSLVWSTSPEHASELVSMDEESFVDTVNSAFWSNENHSEFITSAGSLLHSALSFFMPT... | Function: FAD-dependent monooxygenase required for the C5-ring hydroxylation during ubiquinone biosynthesis. Catalyzes the hydroxylation of 3-polyprenyl-4-hydroxybenzoic acid to 3-polyprenyl-4,5-dihydroxybenzoic acid. The electrons required for the hydroxylation reaction may be funneled indirectly from NADPH via a ferr... |
P53318 | MFFSKVMLTRRILVRGLATAKSSAPKLTDVLIVGGGPAGLTLAASIKNSPQLKDLKTTLVDMVDLKDKLSDFYNSPPDYFTNRIVSVTPRSIHFLENNAGATLMHDRIQSYDGLYVTDGCSKATLDLARDSMLCMIEIINIQASLYNRISQYDSKKDSIDIIDNTKVVNIKHSDPNDPLSWPLVTLSNGEVYKTRLLVGADGFNSPTRRFSQIPSRGWMYNAYGVVASMKLEYPPFKLRGWQRFLPTGPIAHLPMPENNATLVWSSSERLSRLLLSLPPESFTALINAAFVLEDADMNYYYRTLEDGSMDTDKLIEDIKF... | Function: FAD-dependent monooxygenase required for the C5-ring hydroxylation during ubiquinone biosynthesis. Catalyzes the hydroxylation of 3-hexaprenyl-4-hydroxybenzoic acid (HHB) to 3-hexaprenyl-4,5-dihydroxybenzoic acid (DHHB). The electrons required for the hydroxylation reaction may be funneled indirectly from NAD... |
Q220S2 | MPNTLQDRFFTTCDAALRTLFVTPHAERACPTLPGEATALTDAEKVQSGALMRVNHVGEVCAQALYTAQAFATKNEALRAHFTKASADETNHLAWTQQRLDELGARPSLLNPLWYGAAFGLGLLAGRLGDPISLGFVVETENQVEAHLESHLSLLPANDHASRAIVAQMKDDEVRHALDAQKAGAVPLPPPVKSLMTAAAKVMTTVAHRI | Cofactor: Binds 2 iron ions per subunit.
Function: Catalyzes the hydroxylation of 2-nonaprenyl-3-methyl-6-methoxy-1,4-benzoquinol during ubiquinone biosynthesis.
Catalytic Activity: a 6-methoxy-3-methyl-2-all-trans-polyprenyl-1,4-benzoquinol + AH2 + O2 = A + a 3-demethylubiquinol + H2O
Location Topology: Peripheral mem... |
Q2NKS2 | MFGYAVRRALRKSKTLRYGVPMLLLIVGGSFGLREFSQIRYDAVKIKIDPELEKKLKMNKVSLESEYEKIKDSTFDDWKNIRGPRPWEDPDLLQGRNPEILKTNKTT | Function: Required for the assembly of the mitochondrial respiratory chain complex IV (CIV), also known as cytochrome c oxidase. Promotes the insertion of copper into the active site of cytochrome c oxidase subunit II (MT-CO2/COX2). Interacts specifically with newly synthesized MT-CO2/COX and its copper center-forming ... |
A0A1N7SYS3 | MSRLKFVRVGLPFFAIVLGSAYGLHFFQQVRFDFRKIKQEDDNLELLRSDLTRSGLRLREGVTVESVYKEVAELDTDNWENIRGPRDTEDLTDYNLIKKQQQEASRKVRELKSNV | Function: Required for the assembly of the mitochondrial respiratory chain complex IV (CIV), also known as cytochrome c oxidase.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 13522
Sequence Length: 115
Subcellular Location: Mitochondrion inner membrane
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Q5ACH7 | MSYSGNRVFRGKKEQEAYDKTLAGRYVKLVKKNHFLFFGLPFLVSIVAGSIYLQKFTSVKWEKYDEKYQQLGEEEMLNLIENKRTVDKKNDYYRLQGLLNDHTNQVADDYEIVRVQRRKEDEPVWDRQ | Function: Required for the assembly of the mitochondrial respiratory chain complex IV (CIV), also known as cytochrome c oxidase. May participate in merging the COX1 and COX2 assembly lines.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 15377
Sequence Length: 128
Subcellular Location: Mitochondrion... |
Q6FW43 | MALGGRSFRSKKQQLAYDRSFAGRYQKLLSKNPFIFFGLPFCGMMVLGSYWLAGISQVKFDRDDQKVQEMNEEEILKMKHGKREFDIKEEYYRLQGLAEEDWEPKRVERFKGESDNVF | Function: Required for the assembly of the mitochondrial respiratory chain complex IV (CIV), also known as cytochrome c oxidase. May participate in merging the COX1 and COX2 assembly lines.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 14019
Sequence Length: 118
Subcellular Location: Mitochondrion... |
P0CM85 | MPPFATRPLNSTKSHPIFAQIRRHPFILFGIPFIGIIVGSSFALQAFTQTRYDYQETKVKSVGKEEELGMKSGRRKIDLKEEYYFSMASVSQDDYEPVRVPRPVGVPEWGGGRSGEEAPMKGYRKEDRWV | Function: Required for the assembly of the mitochondrial respiratory chain complex IV (CIV), also known as cytochrome c oxidase. May participate in merging the COX1 and COX2 assembly lines.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 14887
Sequence Length: 130
Subcellular Location: Mitochondrion... |
Q5AXJ9 | MPAFPSKTYRRATTASSTLGEKLGEAYRARLPRHPFLLFGLPFIMVIVAGSFVLTPATALRYERYDRKVKQLSQEEAMDLGLKGPDGEEGIKRNPRRRIIGDDREEYYRLMAKDLDSWEQKRVQRFKGEPDGRL | Function: Required for the assembly of the mitochondrial respiratory chain complex IV (CIV), also known as cytochrome c oxidase. May participate in merging the COX1 and COX2 assembly lines.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 15492
Sequence Length: 134
Subcellular Location: Mitochondrion... |
Q4I8P5 | MPAFQSKKFRSAADMNSIGMRYRNLMNKHPFLMFGLPFLTVIVAGSFVLTPATAVRYERYDRKVRQMTKDEELNVRRSARKVDMKEEYYRLAGKDLDDWEQKRVKRLPGENDGLL | Function: Required for the assembly of the mitochondrial respiratory chain complex IV (CIV), also known as cytochrome c oxidase. May participate in merging the COX1 and COX2 assembly lines.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 13551
Sequence Length: 115
Subcellular Location: Mitochondrion... |
Q9P0S2 | MFAPAVMRAFRKNKTLGYGVPMLLLIVGGSFGLREFSQIRYDAVKSKMDPELEKKLKENKISLESEYEKIKDSKFDDWKNIRGPRPWEDPDLLQGRNPESLKTKTT | Function: Required for the assembly of the mitochondrial respiratory chain complex IV (CIV), also known as cytochrome c oxidase . Promotes the insertion of copper into the active site of cytochrome c oxidase subunit II (MT-CO2/COX2) . Interacts specifically with newly synthesized MT-CO2/COX and its copper center-formin... |
Q6CK73 | MSFGGKKFRSKRQQLAYEASLAGRYQKHMNKNPFLWFGLPFCSVIVLGSFWLSEFTAVRYQQKDQKVQEMKEDDLVKMKANQRQFDIKEEYYRLQGLGEQDWEPKRIPRFKGESENVW | Function: Required for the assembly of the mitochondrial respiratory chain complex IV (CIV), also known as cytochrome c oxidase. May participate in merging the COX1 and COX2 assembly lines.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 14180
Sequence Length: 118
Subcellular Location: Mitochondrion... |
Q9CR63 | MIAPAVLRALRKNKTLRYGVPMLLLVVGGSFGLREFSQIRYDAVTIKIDPELEKKLKVNKITLESEYEKIKDSTFENWKNIRGPRPWEDPQLLQGRNPETLKPKTT | Function: Required for the assembly of the mitochondrial respiratory chain complex IV (CIV), also known as cytochrome c oxidase. Promotes the insertion of copper into the active site of cytochrome c oxidase subunit II (MT-CO2/COX2). Interacts specifically with newly synthesized MT-CO2/COX and its copper center-forming ... |
Q7SI11 | MTFQSKKFPSTANTNTFAAKYRAMMKKHPFLLFGLPFMSVIVAGSFILTPAAAIRYEKYDRKVRQVSREEELGLGQRKRRVDIREEYYRLAAKDLDNWEQKRVERLKGESDGLL | Function: Required for the assembly of the mitochondrial respiratory chain complex IV (CIV), also known as cytochrome c oxidase. May participate in merging the COX1 and COX2 assembly lines.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 13350
Sequence Length: 114
Subcellular Location: Mitochondrion... |
Q0UIR3 | MPGPFSSRSFAATLPNSIAARYRKQLQKHPFLLFGLPFMATIVAGSFMLTPATALRYERYDRKNQQITQEEAMGLRQERRKVNMKDEYYRLQAKDLEDWEQRRVKRLPGEPDGTLV | Function: Required for the assembly of the mitochondrial respiratory chain complex IV (CIV), also known as cytochrome c oxidase. May participate in merging the COX1 and COX2 assembly lines.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 13566
Sequence Length: 116
Subcellular Location: Mitochondrion... |
Q9UTK1 | MLFYRFKSWYRLQAKKSPFIYVGLPFLSSVLLVWSCLIPISQVKFNRRDEQVKSLSRDAELDIIKRRRKVDVNEEYYRILLDQLNLQNEEYENKRVKRLKGEPTWEGNSSDKE | Function: Required for the assembly of the mitochondrial respiratory chain complex IV (CIV), also known as cytochrome c oxidase. May participate in merging the COX1 and COX2 assembly lines.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 13691
Sequence Length: 113
Subcellular Location: Mitochondrion... |
Q6CCF6 | MLEQNKFKTKKQQQAWNKTLAGRYYNAMVKRPFLFFGLPFLTTIYAASVYFAEFTAYRYEIQDGKVKALSEEEALKLDKGRRKVDMKEEFYRLQQLGKQDDWEQVRVPRMKGESDNVF | Function: Required for the assembly of the mitochondrial respiratory chain complex IV (CIV), also known as cytochrome c oxidase. May participate in merging the COX1 and COX2 assembly lines.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 14109
Sequence Length: 118
Subcellular Location: Mitochondrion... |
P47081 | MSFSGKKFRSRRQQLVYEASLAGRYKKALSKHPFLFFGLPFCATIVLGSFWLSSFTAIKYEQGDRKVQEINEEDILKIRKNQREFDIKEEYYRLQGLSEEDWEPVRVARLKDESENVW | Function: Required for the assembly of the mitochondrial respiratory chain complex IV (CIV), also known as cytochrome c oxidase . May participate in merging the COX1 and COX2 assembly lines .
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 14077
Sequence Length: 118
Subcellular Location: Mitochondri... |
Q35101 | MDNKFLTRWVFSTNHKDIGTLYLVFGIGSGMIGTALSMLIRLELSAPGTMLGDDHLYNVIVTAHAFIMIFFLVMPVMIGGFGNWLVPLYIGAPDMAFPRLNNISFWLLPPALILLLGSAFVEQGVGTGWTVYPPLSAIQAHSGGAVDMAIFSLHLAGASSILGAMNFITTIFNMRAPGMTMDRLPLFVWSILITAFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGMVSQIIPTFSAKNQIFGYLGMVYAMLSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTG... | Cofactor: Binds 2 heme A groups non-covalently per subunit.
Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-... |
P41774 | MMKMLKKEEMGGYGEVESWWRRWLWSTNHKDIGTLYLYSGVWGGLFGASLSLMIRMQLGHPGAVFLKSDWFYNVVVTTHALMMIFFAVMPILIEAFGNWLIPLLVGGKDMIYPRMNNLSYWLSPNALYLLMLSFSTDKGVGAGWTIYPPLSVYPYHSGPSMDVLIVSLHLAGLSSLVGAINFASTNKNMPVLEMKGERAELYVLSISVTAVLLIISIPVLGGGITMILFDRNFNTTFFDPAGGGDPVLFQHLFWFFGHPEVYILILPAFGVMSKVIMHCSGKEAVFGLIGMVYAMIGIGGLGCMVWAHHMFTVGLNVDTR... | Cofactor: Binds 2 heme A groups non-covalently per subunit.
Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-... |
P03945 | MSSISIWTERWFLSTNAKDIGVLYLIFALFSGLLGTAFSVLIRMELSGPGVQYIADNQLYNAIITAHAILMIFFMVMPALIGGFGNFLLPLLVGGPDMAFPRLNNISFWLLPPSLLLLVFSACIEGGAGTGWTIYPPLSGVQSHSGPSVDLAIFALHLSGVSSLLGSINFITTIVNMRTPGIRLHKLALFGWAVVITAVLLLLSLPVLAGAITMLLTDRNFNTSFFETAGGGDPILFQHLFWFFGHPEVYILIIPGFGIISTTISAYSNKSVFGYIGMVYAMMSIGILGFIVWSHHMYTVGLDVDTRAYFTAATLIIAVP... | Cofactor: Binds 2 heme A groups non-covalently per subunit.
Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-... |
Q8NNK2 | MEQQNKRGLKRKALLGGVLGLGGLAMAGCEVAPPGGVLGDFLRMGWPDGITPEAVAMGNFWSWVWVAAWIIGIIMWGLFLTAIFAWGAKRAEKRGEGEFPKQLQYNVPLELVLTIVPIIIVMVLFFFTVQTQDKVTALDKNPEVTVDVTAYQWNWKFGYSEIDGSLAPGGQDYQGSDPERQAAAEASKKDPSGDNPIHGNSKSDVSYLEFNRIETLGTTDEIPVMVLPVNTPIEFNLASADVAHSFWVPEFLFKRDAYAHPEANKSQRVFQIEEITEEGAFVGRCAEMCGTYHAMMNFELRVVDRDSFAEYISFRDSNPD... | Cofactor: Binds a binuclear copper A center per subunit.
Function: Subunits I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B) (By similarity).
Catalytic Activity: 4 Fe(II)-[cytochrome c]... |
P27168 | MSFTGIFHFFTNSPCDAAEPWQLGSQDAATPMMQGIIDLHHDIFFFLILILVFVSRILVRALWHFHSKKNPIPQRIVHGTTIEILRTIFPSIIPMFIAIPSFALLYSMDEVVVDPAMTIKAIGHQWYRTYEYSDYNSSDEQSLTFDSYTIPEDDPELGQSRLLEVDNRVVVPAKTHLRIIVTSADVPHSWAVPSSGVKCDAVPGRLNQISISVQREGVYYGQCSEICGTNHAFTPIVVEAVSRKDYGSRVSNQLIPQTGEA | Cofactor: Binds a dinuclear copper A center per subunit.
Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cyt... |
P50657 | MAHQAHSYHMVDPSPWPIFGAAAALLTTSGLVMWFHYNSSILLAAGLLSMLLVMLQWWREIVRESTFQGHHTPTVQKGLRYGMILF | Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, comple... |
P34843 | MKKNFPFHMVTNSPWPIILSFSFMNTLISTVIWIYSSISMFMILNFINSILIMMLWFRDIIRESTFQGMHSMFITNFLKFSMILFILSELMFFISFFWTFFHSSISPNIEINMTWPPKNIKFFNPMEIPLLNSFILVSSGFTVTLSHYYLIINNLKLSKSYLLLTILLGIYFTILQTIEYSNSFFCFNDSIYGSIFFMATGFHGLHVLIGSIFLLISLYRMMNIHFSNMHNMNFELAIWYWHFVDVIWLFLYTFIYLLI | Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, comple... |
P92514 | MIESQRHSYHLVDPSPWPISGSLGALATTVGGVMYMHSFQGGARLLSLGLIFILYTMFVWWRDVLRESTLEGHHTKVVQLGLRYGFILFIVSEVMFFFAFFWAFFHSSLAPAVEIGGIWPPKGIEVLDPWEIPFLNTLILLSSGAAVTWAHHAILAGKEKRAVYALVATVLLALVFTGFQGMEYYQAPFTISDSIYGSTFFLATGFHGFHVIIGTLFLIICGIRQYLGHLTKEHHVGFEAAAWYWHFVDVVWLFLFVSIYWWGGI | Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, comple... |
Q33752 | AGNRTEAVQALFLTVALGIYFTILQAWEYYDSPFTIADSVYGSTFFVATGFHGLHVINSTTFLLVCLFRLINFHFSAHHHFGFEAAAWYWDFVDVVVAFSLYMHIWWGS | Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, comple... |
Q33845 | LSALLNTSILLRSGVTVTWAHHALMENNFDQCLQGLLFTVLLGLYFSFLQGLEYMEASFTIADSIYGSTFFLATGFHGLHVLIGTIFLMICILRHLSATFSQHHFGFEAAAWYWH | Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, comple... |
P24012 | MQVQEKFTAETFPASPEKVTLEGKNKFLGFWLFLGGETVLFASLFATFLALRNSNAGDPPTTEMFDVTLVFIATMLLLTSSLTSVYAMYHMKNFSFGKMQLWLGITILLGAGFLGLEIYEFKHYTHEFGFTITSSALGSAFYTLVGTHGAHVAFGLMWISTLMIRNAKRGLNLYTAPKFYVASLYWHFIDVVWVFIFTVVYLMGMVG | Catalytic Activity: 4 Fe(II)-[cytochrome c] + 8 H(+)(in) + O2 = 4 Fe(III)-[cytochrome c] + 4 H(+)(out) + 2 H2O
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 23266
Sequence Length: 207
Subcellular Location: Cell membrane
EC: 7.1.1.9
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O46588 | SVVKREDFSLPAYVDRRDYPLPDVAHVKHLSASQKALKEKEKASWSSLSMDEKVELYRIKFKETFAEMNRGSNEWKTVVGTATFFIGFTALIIMWQKRY | Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, comple... |
Q96KJ9 | MLPRAAWSLVLRKGGGGRRGMHSSEGTTRGGGKMSPYTNCYAQRYYPMPEEPFCTELNAEEQALKEKEKGSWTQLTHAEKVALYRLQFNETFAEMNRRSNEWKTVMGCVFFFIGFAALVIWWQRVYVFPPKPITLTDERKAQQLQRMLDMKVNPVQGLASRWDYEKKQWKK | Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, comple... |
Q91W29 | MFSRAARSLVMRTGLRTRGTGTHSPGDAAGSQRRMTPYVDCYAQRSYPMPDEPFCTELSEEQRALKEKEKGSWTQLSQAEKVALYRLQFHETFAEMNHRSNEWKTVMGCVFFFIGFTALVIWWQRVYVFPKKVVTLTEERKAQQLQRLLDMKSNPIQGLAAHWDYEKKEWKK | Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, comple... |
Q91Y94 | MFSRATRSLVMKTGGLRTQGTHSPGSAASSSQRRMTPYVDCYAQRSYPMPDEPYCTELSEEQRALKEKEKGSWAQLSQAEKVALYRLQFHETFAEMNHRSNEWKTVMGCVFFFIGFTALVIWWQRVYVFPKKVVTLTEERKAQQLQRLLDMKSNPIQGLSAHWDYEKKEWKK | Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, comple... |
P80971 | MLRLTAGRVRSLLAGRATAAFSTSSARMASHDLEVAESVDMSKPLYWDRLDTPLPDRPYKEDLTAADKSLKQKEKGPWGQLSKEEKIALYRLMFCQTYSEMKQPSSEWKTVFGGIFIFLGFTGLVVWWQALYVYPPRPRTFDDEWKAKQLKRMLDMRVNPIEGFSAKWDYEKGQWK | Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, comple... |
Q04452 | MADNLSQSFDKSAMTEEERRHIKKEIRKQIVVFALMIFLTLMSFMAVATDVIPRSFAIPFIFILAVIQFALQLFFFMHMKDKDHGWANAFMISGIFITVPTIAALMLLLGVNKI | Catalytic Activity: 4 Fe(II)-[cytochrome c] + 8 H(+)(in) + O2 = 4 Fe(III)-[cytochrome c] + 4 H(+)(out) + 2 H2O
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 13045
Sequence Length: 114
Subcellular Location: Cell membrane
EC: 7.1.1.9
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Q03440 | MANQTNSGNERVDLAYRRRKNAEEMRHQMIAFVLMILLTLIAFAAVGYEEFSHWFVVPFILLLAAVQVAFQLYYFMHMSHKGHEFPAMFIYGGVAVMLLLVWAFTTVVWW | Catalytic Activity: 4 Fe(II)-[cytochrome c] + 8 H(+)(in) + O2 = 4 Fe(III)-[cytochrome c] + 4 H(+)(out) + 2 H2O
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 12864
Sequence Length: 110
Subcellular Location: Cell membrane
EC: 7.1.1.9
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Q8NNK3 | MKSSAKLMYGPTVFMAAMAVIYIFATMHVSDGGSVKGVEWVGSVALVLSAGLTLMLGVYLHFTEVRVDVLPEDWEEAEVADKAGTLGFFSPSSIWPAAMSGAVGFLAFGVVYFHYWMIAVGLMLLIFTITKLNLQYGVPKEKH | Function: Part of cytochrome c oxidase, its function is unknown.
Catalytic Activity: 4 Fe(II)-[cytochrome c] + 8 H(+)(in) + O2 = 4 Fe(III)-[cytochrome c] + 4 H(+)(out) + 2 H2O
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 15545
Sequence Length: 143
Subcellular Location: Cell membrane
EC: 7.1.1.9
|
P30815 | MFALRSIRSATKAFQTTSIVSQRGFLQTTLKNVLFPTERQLRRQYLADNHIKVGSPEFDKFYEDLQPSELSKQSGLSDALLDDPILHICVIKYNKNIVQRYNLTPEQEKDIMENYNVSAGDPSLEQILPIPVPAHIFEELPIVKVLNN | Function: This protein is one of the nuclear-coded polypeptide chains of cytochrome c oxidase, the terminal oxidase in mitochondrial electron transport.
Catalytic Activity: 4 Fe(II)-[cytochrome c] + 8 H(+)(in) + O2 = 4 Fe(III)-[cytochrome c] + 4 H(+)(out) + 2 H2O
Sequence Mass (Da): 16944
Sequence Length: 148
Subcellul... |
Q9CCF0 | MHIEARLFEFVAVFFVIMAVLYGVLTSMFATGGVDWVGTTALALTGGLALIVATFFRFVARRLDIRPEDYEGAEISDGAGELGFFSPHSWWPVLVALSGSVAAVGIALWLPWLIVAGVVFVLASAAGLVFEYYVGPEKH | Function: Part of cytochrome c oxidase, its function is unknown.
Catalytic Activity: 4 Fe(II)-[cytochrome c] + 8 H(+)(in) + O2 = 4 Fe(III)-[cytochrome c] + 4 H(+)(out) + 2 H2O
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 14970
Sequence Length: 139
Subcellular Location: Cell membrane
EC: 7.1.1.9
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P06809 | MLLSRTAVAVARRATAAPALRRSIATTVVRCNAETKPVPHIKRLSEIKTKDDLFGPGAAPGTVPTDLEQATGLERLEILGKMEGVDVFDMKPLDASRRGTMENPISVRSAGDEQYAGCTGFPADSHNVIWLTMTRERPVERCPECGNVYKMDYVGPQDDHAHDHGHDHHGFEEPKTFADYVKPEYW | Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, comple... |
O74347 | MHPHLDVNNQKQCADLIRALEECHKSFGKFFGECNTIKYELKACLTKDRNDKARLNRENARMRKKVIEENRKKEEIEERILTDRILQQERKKSHANEGAGDNNN | Function: Required for mitochondrial cytochrome c oxidase (COX) assembly and respiration.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 12294
Sequence Length: 104
Domain: The twin Cx9C motifs are involved in the recognition by the mitochondrial mia40-erv1 disulfide relay system and the subsequent t... |
A6ZZI5 | MEQNKDPQMISKHSSRLPIWVLSPREEQQARKNLKTETYKKCANFVQAMADCAKANGMKVFPTCDKQRDEMKSCLLFYQTDEKYLDGERDKIVLEKINKLEKLCQKQSSTK | Function: Required for mitochondrial cytochrome c oxidase (COX) assembly and respiration. Binds copper. May be involved in copper trafficking and distribution to mitochondrial COX and SOD1 (By similarity).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 13007
Sequence Length: 111
Subcellular Location... |
G2TRU5 | MNKSPIEEEFDLRKQHQKLLKKNCQKEIEDFVKCATGRTFSVTWKCRSENKTMKDCLTKAADEISEWQIRSEYNKAKQESFIGKQDEKK | Function: Required for mitochondrial cytochrome c oxidase (COX) assembly and respiration.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 10591
Sequence Length: 89
Domain: The twin Cx9C motifs are involved in the recognition by the mitochondrial mia40-erv1 disulfide relay system and the subsequent tr... |
Q3E7A4 | MHPQLEAERFHSCLDFINALDKCHQKEYYKRIFGLCNNEKDALNKCLKEASLNNKKRAVIESRIKRADVEKRWKKIEEEEYGEDAILKTILDRQYAKKKQESDNDANSK | Function: Required for mitochondrial cytochrome c oxidase (COX) assembly and respiration. May be involved in copper trafficking and distribution to mitochondrial COX and SOD1.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 12947
Sequence Length: 109
Domain: The twin Cx9C motifs are involved in the r... |
P98053 | MAVALILLLIAIGSVLFHLFSPWWWTPIATNWGYIDDTINITFWITGFVFTAVILFMAYCVFRFHHKEGRQAAYNPENKKLEWWLSVGTGVGVAAMLAPGLVVWHQFVTVPADATEVEIMGQQWQWSFRLPGKDGRLGTSDVRNISPENPMGLNRDDPHGQDDVVIENGDLHLPIGKPVKVLLRSVDVLHDFYVPEFRAKMDMVPGMVTYFWIRPIRTGTFDVLCAELCGAAHYQMRAKVIVEAESDYHAWLEQQKTFAGLSGRNAVVRAKYNSGDD | Function: Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Subunits 1-3 form the functional core of the enzyme complex. Subunit 2 transfers the electrons from cytochrome c via its binuclear copper A center to the bimetallic center of the catalytic subunit 1... |
P80981 | SNTSHQDFHSFYGTNLMIGG | Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, comple... |
P98000 | MVDVPYDRIADIPPAEVPDVELYHPRSWWTRYVFSQDAKVIAIQYSLTASAIGLVALVLSWLMRLQLGFPGTFSFIDANQYLQFITMHGMIMVIYLLTALFLGGFGNYLIPLMVGARDMVFPYVNMLSYWVYLLAVLVLASAFFVPGGPTGAGWTLYPPQAILSGTPGQDWGIVLMLSSLILFIIGFTMGGLNYVVTVLQARTRGMTLMRLPLTVWGIFTATVMALLAFPALFVGSVMLLLDRLLGTSFFMPTLVEMGQLSKYGGGSPLLFQHLFWFFGHPEVYIVALPAFGIVSDLISTHARKNIFGYRMMVWAIVAIG... | Function: Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Subunits 1-3 form the functional core of the enzyme complex. Co I is the catalytic subunit of the enzyme. Electrons originating in cytochrome c are transferred via the copper A center of subunit 2 a... |
P80980 | SNTSHQDFHLFYGDNGMPVH | Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, comple... |
P20610 | MTHALPKVVKSQLVQDIGVALILGSIAGCFFKYGVDKKKQRERVAFYEKYDKEDL | Function: This protein is one of the nuclear-coded polypeptide chains of cytochrome c oxidase, the terminal oxidase in mitochondrial electron transport.
Catalytic Activity: 4 Fe(II)-[cytochrome c] + 8 H(+)(in) + O2 = 4 Fe(III)-[cytochrome c] + 4 H(+)(out) + 2 H2O
Sequence Mass (Da): 6275
Sequence Length: 55
Subcellular... |
B1Y6Q4 | MNAPSSAAGHVSSHWRQYVALTKPRVVQLIVFCAAIGMLLAVPGAPGLADLGKALWATLGIWLVASAAAAFNCLIEQQIDSRMKRTAWRPTARGELSRTQALIFSAVLCSAGMAVLHEAVNPLTAWLTLGTFVGYAVIYTVVLKPLTPQNIVIGGISGAMPPLLGWAAMTGEVGPEGLILCLIIFLWTPPHFWALALYRAEDYARAGLPMLPVTHGNEFTRLQILLYTFVLLAGTLLPFVQGMSGWLYLAAAFVLGLRFIHYAWRLWRNYSEALARQTFRFSIWHLSLLFAALLVDHYTQDLLTL | Function: Converts heme B (protoheme IX) to heme O by substitution of the vinyl group on carbon 2 of heme B porphyrin ring with a hydroxyethyl farnesyl side group.
Catalytic Activity: (2E,6E)-farnesyl diphosphate + H2O + heme b = diphosphate + Fe(II)-heme o
Location Topology: Multi-pass membrane protein
Sequence Mass (... |
B1ZKN8 | MTSLSNSLSADAGRASLASAAGGEVSDFFALLKPRVMVLVIFTALVGMVVSDATVNPVIAAISLLMIAVGAGASGCLNMWWDADIDALMTRTAKRPIPDGRIRPDEALAFGIVLSVGSVLILGLASNWLAAGLLAFTIVFYAVIYSMWLKRATAQNIVIGGAAGALPPVVGQAAVTGHVGIESLVLFAIIFIWTPPHFWALALVKSGEYARAGIPMMPNVAGPDSTRRQIVWYSLLLAPLALVPVWLGFGGWLYAVVGVLGGLGMLAGAVQVYRLREGEPERKAAMGLFAFSILYLFLLFSALLAEQGLGLFRAVAA | Function: Converts heme B (protoheme IX) to heme O by substitution of the vinyl group on carbon 2 of heme B porphyrin ring with a hydroxyethyl farnesyl side group.
Catalytic Activity: (2E,6E)-farnesyl diphosphate + H2O + heme b = diphosphate + Fe(II)-heme o
Location Topology: Multi-pass membrane protein
Sequence Mass (... |
Q5HA73 | MTQKAKNTIYLLILIILSMLCLVYASVPLYSIFCKVTGYGGTVRTATATQSKLGKTTIKIRFNADINKELPWKFYPEIPYTTVKPGEQKLIFYRAENLTNEYVSGMAVYNVTPYKVGKYFNKVACFCFTKQTLSPYQKTIMPVSFFIDPNIETDPETSDVKLITLSYTFFKYKENTK | Function: Exerts its effect at some terminal stage of cytochrome c oxidase synthesis, probably by being involved in the insertion of the copper B into subunit I.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 20314
Sequence Length: 177
Subcellular Location: Cell inner membrane
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Q1QHV9 | MTDAPQHPQQPATGTPATPKAAPRVGRDVRIGATCGLLVALMVGAAYAAVPFYNWFCRATGFNGTTQVAKVAPSAAPLARTVAVRFDSNISGGLPWKFEPEQTEINVRIGEVATVYYTVTNHAATATTGQAAYNVTPLTVGSYFTKINCFCFTEQTLAPGEKREMAVVFYVDPSFAADSENDGVRTITLSYTFFPVKDAAPKPVAASEPDRPGGSI | Function: Exerts its effect at some terminal stage of cytochrome c oxidase synthesis, probably by being involved in the insertion of the copper B into subunit I.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 22916
Sequence Length: 216
Subcellular Location: Cell inner membrane
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A1BA38 | MSGGKPRSNTRTVAMLAGVVVLMGALSWAAVPFYSWFCKVTGFAGTTNVAEAASDTVLDEKIRVRFDANADSNLGWTFRPMQREMELKIGENAIAFYEAINNTDEPVTGTASYNVAPDAAGYFFNKIECFCFTEQTLQPGERVEMPVSFFVDADLVNDRDAGRIRDITLSYTFHRTDPPAPKQAALDAKTEPTVN | Function: Exerts its effect at some terminal stage of cytochrome c oxidase synthesis, probably by being involved in the insertion of the copper B into subunit I.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 21439
Sequence Length: 195
Subcellular Location: Cell inner membrane
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O21243 | MFKNRKSIAILIAAVSITMIGFSYGSVPLYRIFCQVTGFGGTTQVADLESDILTLKDEQQENRIITVRFNGDVSDTMPWKFHPIQQEIKVMVGETALAFYSAENPTDSSIIGISTYNVNPQQAGIYFNKIQCFCFEEQRLKPHETIDMPVFFFIDPAILDDPKMSDIDSITLSYTFFNVEDL | Function: Exerts its effect at some terminal stage of cytochrome c oxidase synthesis, probably by being involved in the insertion of the copper B into subunit I.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 20622
Sequence Length: 182
Subcellular Location: Mitochondrion inner membrane
|
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