ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
Q87Q46 | MDCSFSADIQTRIDNKTKPLGALGVLEKVALQLALIQSQDQAQAVEEIVIRKPTMLVFAGDHGVAKEGISIAPSEVTQQMVANFLAGGAAINCFCDVNQIEFKVIDCGMLAPIEVMVPEFKSHPNLIEQRLGNGTANFSKQAAMSSEQVALGLEYGARVAQSTIYSGSNLLMFGEMGIGNTSSASALLAALSPLEVNHCVGLGTGINSEQLSRKLKLVAQGVSRCRGLDAKAVLSQVGGFEIVQMVGAFLEAKRLKTPVLVDGFIVSVAAYVATLLDEETRDYMLFAHRSEENGHKFVLESLKAEPLLDLGLRLGEGTGA... | Function: Catalyzes the synthesis of alpha-ribazole-5'-phosphate from nicotinate mononucleotide (NAMN) and 5,6-dimethylbenzimidazole (DMB).
Catalytic Activity: 5,6-dimethylbenzimidazole + nicotinate beta-D-ribonucleotide = alpha-ribazole 5'-phosphate + H(+) + nicotinate
Sequence Mass (Da): 36823
Sequence Length: 347
Pa... |
Q8PHR3 | MRSDWIFGACAVPDARMRSAALARQEQLTKPPGALGRLEHLAVQLAAWQRTERPGAQRVWIAVYAADHGVAAEGVSAFPQAVTGEMVRNFARGGAAIAVLARELGARLEVVNLGVVNDPGDLPRVRRAWIAPSSANICEQPAMTATQLRDAIAAGADSIAQARSCDTQLFVGGEMGIGNTTSAAALACALLSQFPQAMAGAGTGLDAEGIAHKATVITRALALHADASSPLERLRRLGGFEIAALVGAYIAAAQAGIPVLVDGFITTAAALVATRLNPGVREWLLFGHRSQERGHAALLRALDAEPLLQLDLRLGEASGA... | Function: Catalyzes the synthesis of alpha-ribazole-5'-phosphate from nicotinate mononucleotide (NAMN) and 5,6-dimethylbenzimidazole (DMB).
Catalytic Activity: 5,6-dimethylbenzimidazole + nicotinate beta-D-ribonucleotide = alpha-ribazole 5'-phosphate + H(+) + nicotinate
Sequence Mass (Da): 36034
Sequence Length: 348
Pa... |
O28218 | MRILIPFKANNPKSRLSSILSEEERKELARLMLLDVIDAAKPFGEIKVVCPSELDVEGVEVVVDTSDLNTTVNKVMDEAPLAVIMSDLPLLSEEVLKRFFETEGDVVVAPGRKGGTNMLLVRKRGFRVSYHFGSFFKHLEMARKMGMKAKIFDSFYSSVDIDDESDLLELMMHGSGKKSYEFLRKIGFSVSFEETPRLERRVFMQP | Function: Guanylyltransferase that catalyzes the activation of (2S)-2-phospholactate (2-PL) as (2S)-lactyl-2-diphospho-5'-guanosine, via the condensation of 2-PL with GTP. It is involved in the biosynthesis of coenzyme F420, a hydride carrier cofactor.
Catalytic Activity: (2S)-2-phospholactate + GTP + H(+) = (2S)-lacty... |
C7P363 | MRVVVPFSATEPKTRLAPVLDADERRAFARVMLADVLDALDTVGVDPTVLATEAIDLDRPVTVDDRPLDAAINGLLAASDEPVAVVMADLALATPDALDRLFAAEGDVVLAPGRGGGTNAFVARHPDFRVDYHDASIRDHRRIARDAGGTVTEIDSYRLSTDVDEPADLAEVLLHGEGRAADWLRGAGVQLTVADGRTTVERP | Function: Guanylyltransferase that catalyzes the activation of (2S)-2-phospholactate (2-PL) as (2S)-lactyl-2-diphospho-5'-guanosine, via the condensation of 2-PL with GTP. It is involved in the biosynthesis of coenzyme F420, a hydride carrier cofactor.
Catalytic Activity: (2S)-2-phospholactate + GTP + H(+) = (2S)-lacty... |
C7NN78 | MHVVVPFDGRDPKTRLAPVLDAPERRDFARAMLADVAETIESISFEPTILATTDVECEWPVVVDERSLDAAVNDQLAVADGPVAVVMADLALVTPDALDRLFRAGGEVVLAPGRGGGTNAFVARHHDFRVDYHDASITDHRSIAEEIGADTVEVDSFRLASDVDEPDDLAEVLLHGEGRAAAWLREHGFDLSMDEGRVSVQR | Function: Guanylyltransferase that catalyzes the activation of (2S)-2-phospholactate (2-PL) as (2S)-lactyl-2-diphospho-5'-guanosine, via the condensation of 2-PL with GTP. It is involved in the biosynthesis of coenzyme F420, a hydride carrier cofactor.
Catalytic Activity: (2S)-2-phospholactate + GTP + H(+) = (2S)-lacty... |
Q18FK8 | MHVIVPYTDVSPKTRLNSILTASERTAFAQAMLYDVISTLQSNGHTVELLIPTETVMQATDQRDQETIIDSTGVSTEAVSTSTSTHADTTEHNAASDNYVSQSPTHTLSVTPEAIMRILRDDDDPDNEASTQERDGDKEYIDITVDTAQNQIQSNQIVVTADDRALTPAVNSCLNRLSDTETPFSELAVVMADLALITPTAIERLFAREGDIVLAPGRGGGTNAIVVRHPAFRVDYHGTSYRDHYQAATDASLSVGVVDSMRLGTDIDKPTDLPEVLLHNNGMSSVWLQSAGIELNLDDNTGRVGITRKRKNEDVD | Function: Guanylyltransferase that catalyzes the activation of (2S)-2-phospholactate (2-PL) as (2S)-lactyl-2-diphospho-5'-guanosine, via the condensation of 2-PL with GTP. It is involved in the biosynthesis of coenzyme F420, a hydride carrier cofactor.
Catalytic Activity: (2S)-2-phospholactate + GTP + H(+) = (2S)-lacty... |
A4W7B7 | MARLAAFDMDGTLLMPDHRLGDKTLSTLKRLHDRDITLTFATGRHVLEMRHLLGALSLDAFLITGNGTRIHSVEGEVLHRQDLDPDVADLVLHSTWETEASIHVFNDTGWLTGKEIPELLHAHVYSGFRYQLTDLRRIPAHSVTKICFCGDHDDLCRLRIQLNDALGNRAHLTFSAMDCLEVLPVGCNKGSALAVLSDHLGLTLQDCMAFGDAMNDREMLGSVGRGLIMGNAMPQLIAELSHLPVIGHCRNEAVSHFLTHWLDQPNLPYSPE | Function: Catalyzes the hydrolysis of 4-amino-2-methyl-5-hydroxymethylpyrimidine pyrophosphate (HMP-PP) to 4-amino-2-methyl-5-hydroxymethylpyrimidine phosphate (HMP-P).
Catalytic Activity: 4-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine + H2O = 4-amino-2-methyl-5-(phosphooxymethyl)pyrimidine + H(+) + phosphate
Sequen... |
P43154 | MELKILSVAIATTLTSTGVFALSEPVSQVTEQHAHSAHTHGVEFNRVEYQPTATLPIQPSKATRVQSLESLDESSTACDLEALVTESSNQLISEILSQGATCVNQLFSAESRIQESVFSSDHMYNIAKHTTTLAKGYTGGGSDELETLFLYLRAGYYAEFYNDNISFIEWVTPAVKESVDAFVNTASFYENSDRHGKVLSEVIITMDSAGLQHAYLPQVTQWLTRWNDQYAQHWYMRNAVNGVFTILFGGQWNEQFVQIIGNQTDLAKALGDFALRASSIGAEDEFMAANAGRELGRLTKYTGNASSVVKSQLSRIFEQY... | Cofactor: Binds 1 zinc ion.
PTM: Proteolytic cleavage might yield three different active forms.
Catalytic Activity: Digestion of native collagen in the triple helical region at Xaa-|-Gly bonds. With synthetic peptides, a preference is shown for Gly at P3 and P1', Pro and Ala at P2 and P2', and hydroxyproline, Ala or Ar... |
Q9KRJ0 | MSFQQRIQHHPIAWACVIAGLSYSSYSQAACEIQDLQPARDLPAQIAVATQACYNSWFYAPTATLDNLYSEASLAHLQTVLDAEIARYTGEAQQARRLENYGEFIRAAYYVRYNAGREPYSQALSQRFAQSIDRFLRHPHAFDQGREQVGAMKSLSLMVDNVKQLPLTMDAMILALHRFNRETAQDTQWVDGLNNLFRAMSGHVGNSEFYRYLAANTQHIDTLYRFALDNEWALETDAEFLVYNALRETGRLLISPDAITKQKARHVMRQVIARYPLGSKHDKLWLAAVEMLHYYAPEVLQQLGIDLDAAKRDLAARILP... | Cofactor: Binds 1 zinc ion.
Function: Possesses gelatinolytic activity.
Catalytic Activity: Digestion of native collagen in the triple helical region at Xaa-|-Gly bonds. With synthetic peptides, a preference is shown for Gly at P3 and P1', Pro and Ala at P2 and P2', and hydroxyproline, Ala or Arg at P3'.
Sequence Mass ... |
Q2M2T5 | MAAELEGSKCLSGLLSGLAQDTFYGHPGITEELLRSQLYPEVSLEEFRPFLAKMKGILKSIASADMDFNQLEAFLTALTKKQGGITSEQAAVISKFWKSHKTKIRESLMNQSCWDRGLRSLSWRVDGKSQSRHSAQIHTPVAIMELEIGKSGQESEFLCLEFDEVKVNQVLKKLSEVEESISTLMQPA | Function: Proposed scaffold protein that is implicated in diverse physiological processes and whose function may be in part linked to its ability to regulate ubiquitination of specific cellular proteins. Can modulate activity of cullin-RING E3 ubiquitin ligase (CRL) complexes by displacing CAND1; in vitro promotes CRL ... |
Q8N668 | MAAGELEGGKPLSGLLNALAQDTFHGYPGITEELLRSQLYPEVPPEEFRPFLAKMRGILKSIASADMDFNQLEAFLTAQTKKQGGITSDQAAVISKFWKSHKTKIRESLMNQSRWNSGLRGLSWRVDGKSQSRHSAQIHTPVAIIELELGKYGQESEFLCLEFDEVKVNQILKTLSEVEESISTLISQPN | Function: Proposed scaffold protein that is implicated in diverse physiological processes and whose function may be in part linked to its ability to regulate ubiquitination of specific cellular proteins. Can modulate activity of cullin-RING E3 ubiquitin ligase (CRL) complexes by displacing CAND1; in vitro promotes CRL ... |
Q8K4M5 | MAGDLEGGKSLSGLLSGLAQNAFHGHSGVTEELLHSQLYPEVPPEEFRPFLAKMRGLLKSIASADMDFNQLEAFLTAQTKKQGGITSEQAAVISKFWKSHKIKIRESLMKQSRWDNGLRGLSWRVDGKSQSRHSTQIHSPVAIIELEFGKNGQESEFLCLEFDEVKVKQILKKLSEVEESINRLMQAA | Function: Proposed scaffold protein that is implicated in diverse physiological processes and whose function may be in part linked to its ability to regulate ubiquitination of specific cellular proteins. Can modulate activity of cullin-RING E3 ubiquitin ligase (CRL) complexes by displacing CAND1; in vitro promotes CRL ... |
Q9SV21 | MDKSSTMLVHYDKGTPAVANEIKEALEGNDVEAKVDAMKKAIMLLLNGETIPQLFITIIRYVLPSEDHTIQKLLLLYLELIEKTDSKGKVLPEMILICQNLRNNLQHPNEYIRGVTLRFLCRMKETEIVEPLTPSVLQNLEHRHPFVRRNAILAIMSIYKLPQGDQLFVDAPEMIEKVLSTEQDPSAKRNAFLMLFTCAEERAVNYLLSNVDKVSDWNESLQMVVLELIRSVCKTKPAEKGKYIKIIISLLSATSSAVIYECAGTLVSLSSAPTAIRAAANTYCQLLLSQSDNNVKLILLDRLYELKTLHRDIMVELIID... | 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... |
Q53PC7 | MEKPCTLLVHFDKGSPSMANEIKADLEGSDVAAKVDAMKRAIMLLLNGETLPHLFITVVRYVLPSEDHTIQKLLLLYLEIVDKRDVASGKVLPEMILICQNLRNNLQHPNEYIRGVTLRFLCRLNEPELLEPLIPSILANLDHRHHFIRRHALSAISAIYRLPHGDQLLPDAPEVVERALTGEQDASARRNGFLMLCACAQERAVAYLLTNAERVAEWPDLLQMAAVDLIRKVCRSPNRADKGRYIKIIISLLSAPNSAVVYESAGALVSLSSAPTAVRAAANTYCQLLSSQSDNNVKLIVLDRLHELRASHRDVMVDVV... | 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... |
Q9SV20 | MDKSSTMLVHYDKGTPAVANEIKEALEGNDVEAKVDAMKKAIMLLLNGETIPQLFITIIRYVLPSEDHTIQKLLLLYLELIEKTDSKGKVLPEMILICQNLRNNLQHPNEYIRGVTLRFLCRMKETEIVEPLTPSVLQNLEHRHPFVRRNAILAIMSIYKLPHGDQLFVDAPEMIEKVLSTEQDPSAKRNAFLMLFTCAEERAVNYLLSNVDKVSDWNESLQMVVLELIRSVCKTKPAEKGKYIKIIISLLSATSSAVIYECAGTLVSLSSAPTAIRAAANTYCQLLLSQSDNNVKLILLDRLYELKTLHRDIMVELIID... | 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... |
Q20168 | MPLRLDVKRKLLARSDRVKCVDLHPVETWLLAALYNGNVHIWNYETQTLVKSFEVCDVPVRAAKFVPRKSWVVTGSDDMHIRVFNYNTLERVHQFEAHSDYLRSLVVHPTLPYVISSSDDMLVKMWDWDNKWAMKQSFEGHTHYVMQIAINPKDNNTFATASLDKTVKVWQFGSNVPNFTLEGHEKGVNCVDYYHGGEKPYIISGADDHLVKIWDYQNKTCVQTLDGHAQNVSSVCFHPELPLIITGSEDSTVRLWHANTYRLETTLNYGLERVWCIQAQKGANTIAIGYDEGSVTLKLGREEPAVSMDSSGKILWAKHS... | 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... |
Q54YD8 | MPLRLDIKKKLSTRSDRVKSVDIHPTEPWILASLYDGNVYIWNYETQNMVKSFEVSPNNPVRTARFIAKKQWIVTGSDDTYIRVYNYNTMEKIKSFEAHADYIRCIIVHPTLPYILSSSDDMFIKLWDYEKGWSNTQVFEGHSHYVMSIAWNPKDTNQFATASLDKTVKVWSINSPHPHFTLEGHEKGINSVEYFSGGEKPYLISGADDKLVKIWDYQSKTCVQTLEGHSNNVSVVCYHPELPLILSGSEDGTVKLWHSSTYRLERTLNYGMGFVWSMNFLRGSNFIGLGYDDGTVVLKIGKNKPPVSMDQGGKVIYAKH... | 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... |
O62621 | MPLKLDIKRRLTSRSDRVKCVDLHPAEPWMLCALYNGHVHIMNYENQQMVKDFEVCDVPVRSARFVARKNWILTGSDDMQIRVFNYNTLEKVHSFEAHSDYLRCIAVHPTQPLVLTSSDDMLIKLWNWEKMWACQRVFEGHTHYVMQIVFNPKDNNTFASASLDRTVKVWQLGSNFANFTLEGHEKGVNCVDYYHGGDKPYLISGADDRLVKIWDYQNKTCVQTLEGHAQNISAVCFHPELPIVLTGSEDGTVRIWHSGTYRLETCLNYGFERVWTISSMRGTNNVALGYDEGSIIIKVGREEPAMSMDVVGSKIIWAKH... | 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... |
P35606 | MPLRLDIKRKLTARSDRVKSVDLHPTEPWMLASLYNGSVCVWNHETQTLVKTFEVCDLPVRAAKFVARKNWVVTGADDMQIRVFNYNTLERVHMFEAHSDYIRCIAVHPTQPFILTSSDDMLIKLWDWDKKWSCSQVFEGHTHYVMQIVINPKDNNQFASASLDRTIKVWQLGSSSPNFTLEGHEKGVNCIDYYSGGDKPYLISGADDRLVKIWDYQNKTCVQTLEGHAQNVSCASFHPELPIIITGSEDGTVRIWHSSTYRLESTLNYGMERVWCVASLRGSNNVALGYDEGSIIVKLGREEPAMSMDANGKIIWAKHS... | 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... |
O35142 | MPLRLDIKRKLTAMSDRVKSVDLHPTEPWMLASLYNGSVCVWNHETQTLVKTFEVCDLPVRAAKFVARKNWVVTGADDMQIRVFNYNTLERVHMFEAHSDYIRCIAVHPTQPFILTSSDDMLIKLWDWDKKWSCSQVFEGHTHYVMQIVINPKDNNQFASASLDRTIKVWQLGSSSPNFTLEGHEKGVNCIDYYSGGDKPYLISGADDRLVKIWDYQNKTCVQTPEGHAQNVSCATFHPELPIIITGSEDGTVRIWHSSTYRLESTLNYGMERVWCVASLRGSNNVALGYDEGSIIVKLGREEPAMSMDANGKIIWAKHS... | 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... |
Q1HPV1 | MYLRKPIQKIKSEVQIRLIRYYTASENAKVTYHEEMQNNFIATNIFQKALLTCGSAVIALLDPHRGDMIACLGEVTGENAIKYMHSKMLQTEEGQDILKNKPRINSKTIAFETLSQMPENSLGRVYADFMKDNNITADSRLPVQFIADPELAYVMQRYREVHDLVHASLFMKTNMLGEVTVKWVEGIQTKLPMCIGGGIWGAARLRPKHRQMYLKYYLPWAIRTGNNAKFLQGIYFEKRWEQDIDDFHKEMNIVRLLKK | Function: Component of the coenzyme Q biosynthetic pathway. May play a role in organizing a multi-subunit COQ enzyme complex required for coenzyme Q biosynthesis. Required for steady-state levels of other COQ polypeptides.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 30097
Sequence Length: 259
Pat... |
Q05B52 | MATLLRGVLRPLCAFRGGPGPPAGVPFRAVSHGTGLLYPEHIPTSVLQKVLLAAGSAGMALYDPYRHDMVAVLGETTGRRTLKVLRDQMKRDPEGAQILQERPRISLSTLDMGKLRSLPEGSFGCAYLHFLDVNVASGRGMTVCTEDFIQC | Function: Component of the coenzyme Q biosynthetic pathway. May play a role in organizing a multi-subunit COQ enzyme complex required for coenzyme Q biosynthesis. Required for steady-state levels of other COQ polypeptides (By similarity).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 16337
Sequence... |
P91428 | MSAQKLYASHVPLAPLSRMLLGIGSAVTAISDPKRGDMVAAMGETTAIGPVLENIRKRMESDVVGKRLLLEKPRISNGTIDRKWLRQLPDGTLGKLYSNFLDRLNTSPDARPTVKYIDNLEHLYVMQRYRETHDFTHIALEQKTNMLGEVTVKYFEGIQYGLPMCVTGGIFGGARLLTKNRQELVDRNLPWVVEQATNARFFMAFDWENHFEKQLSEVQKELNITPLSVNM | Function: Component of the coenzyme Q biosynthetic pathway. May play a role in organizing a multi-subunit COQ enzyme complex required for coenzyme Q biosynthesis. Required for steady-state levels of other COQ polypeptides.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 26224
Sequence Length: 231
Pat... |
Q2H4H9 | MANKFPFWAAAISSQQQQPSDPPQQHSLQAPNSRSLLPSRSLTRPAGPTTLGHDLIAAFAEATATPYFIYRLRDAMLASPTGRRILRDRPRITSTSLNLPYLRSLPPGTVGHTYVAWLDREGVSPDTRSAVRYIDDAECAYVMQRYRECHDFYHALTGLPVVREGEVALKAFEFANTLLPMTGLSVFAAATLKRSERRRFGEIYLPWALRNGLRAAEVINMYWEEPLERDVVGS | Function: Component of the coenzyme Q biosynthetic pathway. May play a role in organizing a multi-subunit COQ enzyme complex required for coenzyme Q biosynthesis. Required for steady-state levels of other COQ polypeptides.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 26309
Sequence Length: 234
Pat... |
Q1EAH9 | MAIAKSVRARAVGLRSLRVLCAQRSVAREFSVLNRPQPNYPGHIPLTPIERGALAIGSAVGSLLNPRRGDLIATVGETTATPFFIYRLRDAMLADPTGRRILRDRPRITSQTLSLPYLRSLPKNTVGYTYATWLDREGVSPDTRSSVQYIDDEECAYVMQRYRECHDFYHAVTGLPIVVEGEIALKAFEFMNTLIPMTGLSVFAAIRLKPEEKQRFWSIHLPWAIRSGLASKELINVYWEEQLERDVNELREELNIEKPPDLRDIRKKVREQKKAAKEAVIKS | Function: Component of the coenzyme Q biosynthetic pathway. May play a role in organizing a multi-subunit COQ enzyme complex required for coenzyme Q biosynthesis. Required for steady-state levels of other COQ polypeptides.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 32233
Sequence Length: 283
Pat... |
A8P488 | MLGRRSVSLLRGLTELPVSSRAHTALRALSVPQTRRNVATKPNYEGHIPLNWFENALLTAGAAYMSITDPRRGDMVAALGETTAGPTVSWLRDQMLASPEGRQILKDRPRITSSTVDMDKLAQMPEGTFGRAYINWLERCGVTPDTREPVHYIDDPELAYVMQRYRECHDFYHCICNMPVNVESELAVKYFEFANLGLPMAGLAALFGPLRLNAQKRNWLFTEAVPWALKCGSSARSLITVYWEKRWEEQVEDMKKEFGIWDGPEARWSKPLNEAKEAAERRSKTTQNQIY | Function: Component of the coenzyme Q biosynthetic pathway. May play a role in organizing a multi-subunit COQ enzyme complex required for coenzyme Q biosynthesis. Required for steady-state levels of other COQ polypeptides.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 33140
Sequence Length: 291
Pat... |
Q5CHB0 | MNKFTNLLIKRTASSLKGGDFRELFRKNYIPITQFEKVLLSVTSCVEGLKNPTDSNSVACITELTSNRALRKLQILMNSTPDGRRIIKNRPLIDSSKYSIKDLMAFPDDSLGRRYGEFLTTYNLEIDRAPVRYVNSEDLAYVLTRFRQVSLNDYK | Function: Component of the coenzyme Q biosynthetic pathway. May play a role in organizing a multi-subunit COQ enzyme complex required for coenzyme Q biosynthesis. Required for steady-state levels of other COQ polypeptides (By similarity).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 17839
Sequence... |
P0CM82 | MTLAIPLELSLFDPTSADFLVPLISFSAYFSVKSFTMRPCPRLLTRKLNYPGHIPLSPAQNALLAVGSGVVGVLDVTRGDLIASLSESTAGIFLPALHEKMKMTPEGRQIMKDRPEITNKTIEKLKELKRGTLGREYVEWLGGGGLEPESRAPVQYIDSPLLAYTMLRYRQTHDLYHTLFSLPPTLPHELSLKVLEFSNMSLPVALLSSVFGPLRLKRKETWTRDWVPWALRTGREGRSLVTVYWEKRWEQGIGELRRELGVERNDAEGVEARWGGYRKIREVERELRRKGEWVDEPEDW | Function: Component of the coenzyme Q biosynthetic pathway. May play a role in organizing a multi-subunit COQ enzyme complex required for coenzyme Q biosynthesis. Required for steady-state levels of other COQ polypeptides.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 34287
Sequence Length: 300
Pat... |
P97478 | MSAAGAIAAASVGRLRTGVRRPFSEYGRGLIIRCHSSGMTLDNINRAAVDRIIRVDHAGEYGANRIYAGQMAVLGRTSVGPVIQKMWDQEKNHLKKFNELMIAFRVRPTVLMPLWNVAGFALGAGTALLGKEGAMACTVAVEESIANHYNNQIRMLMEEDPEKYEELLQVIKQFRDEELEHHDTGLDHDAELAPAYALLKRIIQAGCSAAIYLSERF | Cofactor: Binds 2 iron ions per subunit.
Function: Catalyzes the hydroxylation of 2-polyprenyl-3-methyl-6-methoxy-1,4-benzoquinol (DMQH2) during ubiquinone biosynthesis. Has also a structural role in the COQ enzyme complex, stabilizing other COQ polypeptides (By similarity). Involved in lifespan determination in a ubiq... |
Q3JCJ6 | MEGRRLSQLDRVIINFDDALRTVFGQPRTTERASPASGIAEGALSEKERRLSGCLMRVNHAGEVAAQALYQGQALTARLTEIRKAMENAAREENEHLVWCQQRVQELGAHTSYLGPFWYGGSFVIGALAGMAGDKWSLGFVAETEHQVVKHIERHLDRISAQDAPSRAILEQMKEDEARHATVALEAGGVELPSSIKALMGAASKVMTRTAYWI | 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... |
A4SV64 | MSLIDRFIAEFDTALRSVVGGAHSRRPTPGSGEISHANLDVAQRKHAAGLMRVNHVGEVCAQALYQSQKMLARNPQIQVMLEHSGQEEMDHLAWCETRLQELGSHPSYLNPFWYAGSFAIGMLAGLAGDRWSLGFVAETEKQVENHLESHLETLPQEDLRSRAIVDQMRIDEIEHGQAALHAGGVVLPDPVQKVMQAMSKVMTTAAYRI | 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... |
A1VJY7 | MTTALDLALNAADGALRTLFAKPRASRTCPTVPAQATELSLEDKALSGALMRVNHVGEVCAQALYAAQALGTRDAVLRKHFLKASQEEGDHLAWTKDRLDELGARPSLLNPLWYAGAFGLGLVASRLGDRLSLGFVVETERQVEAHLASHLERLPEGDHESRAIVAQMKDDEALHASAAEDAGALQLPAPVKMLMRSAAKVMTTVAHRI | 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... |
Q12FJ1 | MTPALDTALNAADGALRTLFAKPQASRTCPTVAGQRTELSTQEKALSGALMRVNHVGEVCAQALYAAQAVTTRDPALRRHFLAASREEGDHLAWTRERLDELGARPSLLNPLWYAGAFGLGLLAGRLGDRVSLGFVVETERQVEAHLASHLERLPEGDHDSRAIVAQMKDDEARHAQDAQNAGALPMPAPVKALMQASARLMTTTAHYL | 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... |
Q960N3 | MFVEMSVCDSPNKNSKLDKKSLTPFKKVRRKNWKQEAAYKSDTSKGQEVSYVGERFIPNRFERENIEFNLKYIGKRKERDILETGVTLTASYWRQSGFISNINRTFGIGERRLFQFSSQQGTRSRVVDNDSADSDWPCNPRARPYAIQNATHEMPGICSPVDYNMMDWSSGGMVAMSSGQDVMLWRNLDESTMVFSVESPTSLKYSPDGKHLAIGCMDRNYPVLDLWEVRSPTEFLVSYRKLFFKSMGYISCIEWSHDGKEVICGTQCGVIIVLAMPTLNTLMQLREHRHTVKKMKFAPTHKYFASSDTDGKIFIFDAVL... | Function: Female meiosis-specific activator of the anaphase promoting complex/cyclosome (APC/C) . Required for the completion of meiosis in oocytes . Activates the ubiquitin ligase activity and substrate specificity of APC/C and triggers the sequential degradation of mitotic cyclins in meiosis . Promotes the ubiquitina... |
Q4I5G1 | MRPPRCLFPAAEILLKAPPSRRCMSSAAAFQPPKIVAAIPWKGSSFFLSNRLFDRSTCLDFVVLRRANGIRSTSASASTTHDSTLSSSPTANHSTSAHKDHKIAPHRKRQAQRREKAAAEAAAAAARGEKPLPPDASSLLAAHAASQTSPLRRHLSACLSLAKPRLTMLVVLTAMATYALYPVPEMLSPSTTETPSLSPLTLLFLTIGTTFCSASANALNMLYEPSTDAKMTRTRNRPLVRNLISKRAAVLFAILSGFVGTGALYFGVNPTVSGLGFANIVIYAGMYTPLKAVTAFNTWIGAVVGGIPPLMGWAAAAGET... | Function: Converts protoheme IX and farnesyl diphosphate to heme O.
Catalytic Activity: (2E,6E)-farnesyl diphosphate + H2O + heme b = diphosphate + Fe(II)-heme o
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 55397
Sequence Length: 507
Subcellular Location: Mitochondrion membrane
EC: 2.5.1.141
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Q12887 | MAASPHTLSSRLLTGCVGGSVWYLERRTIQDSPHKFLHLLRNVNKQWITFQHFSFLKRMYVTQLNRSHNQQVRPKPEPVASPFLEKTSSGQAKAEIYEMRPLSPPSLSLSRKPNEKELIELEPDSVIEDSIDVGKETKEEKRWKEMKLQVYDLPGILARLSKIKLTALVVSTTAAGFALAPGPFDWPCFLLTSVGTGLASCAANSINQFFEVPFDSNMNRTKNRPLVRGQISPLLAVSFATCCAVPGVAILTLGVNPLTGALGLFNIFLYTCCYTPLKRISIANTWVGAVVGAIPPVMGWTAATGSLDAGAFLLGGILYS... | Function: Converts protoheme IX and farnesyl diphosphate to heme O.
Catalytic Activity: (2E,6E)-farnesyl diphosphate + H2O + heme b = diphosphate + Fe(II)-heme o
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 48910
Sequence Length: 443
Subcellular Location: Mitochondrion membrane
EC: 2.5.1.141
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Q8CFY5 | MAASPHTISSRLLTGSVGGCIWYLERRAIQGLPHRVTRLFRNVSNQWVTLQHLSFLKRMYVTQLHRGLSQRVKPKPEPPASPFLEHTSSGQARADEDELPSFPAPSRPLSRKPNEELVELEATSIVDHSLDTAKEKKEERQWKEMKLHTDDLPGILARLSKIKLTALVVSTTSAGFALAPGPFDWSCFLLTSLGTGLASCAANSINQFFEVPFDSNMNRTKNRPLVRGQISPLLAVSFATCCAVPGVALLTWGVNPLTGALGVFNIFLYTCCYTPLKRVSITNTWVGAVVGAIPPVMGWTAATGSLDAGALLLGGILYSW... | Function: Converts protoheme IX and farnesyl diphosphate to heme O.
Catalytic Activity: (2E,6E)-farnesyl diphosphate + H2O + heme b = diphosphate + Fe(II)-heme o
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 48884
Sequence Length: 443
Subcellular Location: Mitochondrion membrane
EC: 2.5.1.141
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Q7S5E7 | MSSSTESLPGTLRRTLTTSRAPAATSSQRLKAGYFVSNAFLPRVKANGIHDSASSQRSTTVASTTSTTADAADGSSSTTQPTTAADLPPVDNTLLPHRRRQAQRKAAAAAAAAAANGETPTPLINPDAPTADLAPDASSQLAAAAASAPADSLKRRLSSLLSLSKPRLTVLVVLSAMVPYALYPVPSFLTSSALDTSLAPSLSPLTLLFLTTGTTLCSASANALNMLYEPDTDSKMTRTRTRPLVRRLLTTKAAVLFAVGCGLAGTLALYFGVNPTVSFLGAANIALYAGAYTPLKRISAVNTWVGAIVGGIPPLMGWAA... | Function: Converts protoheme IX and farnesyl diphosphate to heme O.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 54111
Sequence Length: 511
Subcellular Location: Mitochondrion membrane
EC: 2.5.1.-
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Q9Y7Y4 | MFHILNKGSSKSCIYTRPCLKRFYHQHYEHTGKLSRTFFSPTHIKYNRLSTLDTSTSTANAAPDPQVLTFLSKRMQAAPLYPKPSAFLELGKPRLTVLVVLSTMSSYALAPYPGLSFNTLAWLTMGTALCSISANAFNQSMEPMLDCQMARTRSRPIPRGAIRPEYAWLFATLTGIAGTSMSFLVNPTVGWLGLGNIVLYMGIYTPLKRISIVNTWVGSLVGAIPPLMGWAACSGGDLLSHPGGLITAAMLFAWQFPHFNAFSTMVKDDYKKCGYQMMAWKNPALNARVSLRYALAFLPLSYAYISTGLVGPWYAVPATG... | Function: Converts protoheme IX and farnesyl diphosphate to heme O.
Catalytic Activity: (2E,6E)-farnesyl diphosphate + H2O + heme b = diphosphate + Fe(II)-heme o
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 43130
Sequence Length: 387
Subcellular Location: Mitochondrion membrane
EC: 2.5.1.141
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Q6C0L2 | MLLSNVAVNRTVVHTQLVSGSRSALHALSRTSHSVPVTHTHQRRHIFSHKRRLSSSTLAIPFALSNTNSATTAPLQFLSNVSLCRVTPGTITTSAKATAPNLDKMSAEAATTAAQASASPVEDSFLKKAVSCQSETEREAVMAARAAKKALRETKETWWAPYVALTKPRLTVLVVLSAMSSYALTPEAVSLTNLLFLTVGTALCSGSANAINMGREPAYDSMMTRTRGRPVVRGAVTPNQAFTFAGITGTVGTAALYFGVNPTVAILGASNIALYGGLYTTLKRKHIINTWVGAVVGAIPPLMGWAASGGSLLHPGAWCL... | Function: Converts protoheme IX and farnesyl diphosphate to heme O.
Catalytic Activity: (2E,6E)-farnesyl diphosphate + H2O + heme b = diphosphate + Fe(II)-heme o
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 51187
Sequence Length: 471
Subcellular Location: Mitochondrion membrane
EC: 2.5.1.141
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P21592 | MSYFPRTYAHLMRNVLAHNKGNIYLQIGTQLHDTQIKIRFNGVRYISRNHGGKQQHINTAPIEFTPNFGYGDRTSNCNKKVESTAMKTLRCTDDISTSSGSEATTDASTQLPFNVKLVDPMVRKSKRPSHAISEGLNMKTLKKKVIMPYLQLTKPRLTILVMLSAICSYALSPYPASVNELLCLTVGTTLCSGSANAINMGREPEFDRQMVRTQARPVVRGDVTPTQAFEFAALIGTLGVSILYFGVNPTVAILGASNIALYGWAYTSMKRKHIINTWLGALVGMVPPLMGWAAASPLSHPGSWCLAGLLFAWQFPHFNT... | Function: Converts protoheme IX and farnesyl diphosphate to heme O.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 52148
Sequence Length: 462
Subcellular Location: Mitochondrion membrane
EC: 2.5.1.-
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Q8GWR0 | MSWSKACRGTRISSYLENLHRTSQYPRTILCSRYYTHGACKSNEHYLRSKRVFWGSSSSWSLNSHSATAKSMLDSAHRQYSTHSPSETKSQKMLYYLTAVVFGMVGLTYAAVPLYRTFCQATGYGGTVQRKETVEEKIARHSESGTVTEREIVVQFNADVADGMQWKFTPTQREVRVKPGESALAFYTAENKSSAPITGVSTYNVTPMKAGVYFNKIQCFCFEEQRLLPGEQIDMPVFFYIDPEFETDPRMDGINNLILSYTFFKVSEENTTETVNNNNSVPVQETN | 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): 32605
Sequence Length: 287
Subcellular Location: Mitochondrion inner membrane
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A3KMZ6 | MGGLWRPAWRRVVFCGWSWSHLGRPTRAAERAEPCLRPGRSGPAGTEQGLRRLGTWRRPSPAEQPARRPKSTNPYTRSQEEDWRRRNKTVLTYMAAAAVGMLGASYAAVPLYRLYCQTTGLGGSAVAGHASDQIENMVPVKDRIIKITFNADVHASLQWNFRPQQTEIYVVPGETALAFYKAKNPTDKPVIGISTYNVVPFEAGQYFNKIQCFCFEEQRLNPQEEVDMPVFFYIDPEFAEDPRMVNVDLITLSYTFFEAKEGHTLPVPGYNSNQQLSPASNL | 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): 31824
Sequence Length: 282
Subcellular Location: Mitochondrion inner membrane
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Q54HM6 | MSRLFNNFLLKTNKNQFIQSFSTKSQINNNIFNNLIKNEKISLPPPPFLSSSSPLSMNNIFNRNNKNLYTTNNFNYNKLQFTTQSPNPTPTPTPTPTPTPTPNNNENNNNKNNNNNNFKEEQKKILQEKNKAIGLYVLIAIIGILGLSYAAVPLYRIFCRATGYGGTTRDADDFDVIRKRNLDRTVYPIKVTFSASTANKIPWTFKPTQSTIECLPGEPVLCFYRATNNTDTPIIGVATYNITPMKAGTYFTKIQCFCFDEQRINAHETIDMPVLFVIEPELLDDKNMKGVSDITLSYTFFKSNDQGEYEEI | 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): 35485
Sequence Length: 312
Subcellular Location: Mitochondrion inner membrane
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Q9Y6N1 | MGGLWRPGWRCVPFCGWRWIHPGSPTRAAERVEPFLRPEWSGTGGAERGLRWLGTWKRCSLRARHPALQPPRRPKSSNPFTRAQEEERRRQNKTTLTYVAAVAVGMLGASYAAVPLYRLYCQTTGLGGSAVAGHASDKIENMVPVKDRIIKISFNADVHASLQWNFRPQQTEIYVVPGETALAFYRAKNPTDKPVIGISTYNIVPFEAGQYFNKIQCFCFEEQRLNPQEEVDMPVFFYIDPEFAEDPRMIKVDLITLSYTFFEAKEGHKLPVPGYN | 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): 31430
Sequence Length: 276
Subcellular Location: Mitochondrion inner membrane
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Q6P8I6 | MGGLWCPGWRLVASCGRGWRQPGWSGRTVVNAELVLRPGWDGLGGAERGLRRLGTWKRPCGVRGPATQPPRRPRSSNPFQRAQEDEWRRRNKTVLTYVAAAAVGMLGASYAAVPLYRLYCQTTGLGGSAVAGHSSDQIENMVPVKDRVIKVTFNADVHASLQWNFRPQQTEIYVVPGETALAFYKAKNPTDKPVIGISTYNVVPFEAGQYFNKIQCFCFEEQRLNPQEEVDMPVFFYIDPEFAEDPRMVNVDLITLSYTFFEAKEGHKLPVPGYN | 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): 30849
Sequence Length: 275
Subcellular Location: Mitochondrion inner membrane
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P19516 | MIRICPIVRSKVPLLGTFLRSDSWLAPHALALRRAICKNVALRSYSVNSEQPKHTFDISKLTRNEIQQLRELKRARERKFKDRTVAFYFSSVAVLFLGLAYAAVPLYRAICARTGFGGIPITDRRKFTDDKLIPVDTEKRIRISFTSEVSQILPWKFVPQQREVYVLPGETALAFYKAKNYSDKDIIGMATYSIAPGEAAQYFNKIQCFCFEEQKLAAGEEIDMPVFFFIDPDFASDPAMRNIDDIILHYTFFRAHYGDGTAVSDSKKEPEMNADEKAASLANAAILSPEVIDTRKDNSN | 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): 34044
Sequence Length: 300
Subcellular Location: Mitochondrion inner membrane
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O94581 | MSEQEDQEAPKQFTFGTVGFDARFPNTNQTKHCFQSYIDYFRCIKAKGEDFVPCKQFWHAYQSLCPMEWVERWDEQRENGTFPAPI | 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... |
Q9ZZM6 | MAITRWFFSTNHKDIGTLYLVFGAWAGMVGTALSLLIRAELSQPGALLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGISSILGAINFITTIINMKPPAISQYQTPLFVWAVLVTAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVAYYSGKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKV... | 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-... |
P07506 | MTNPVRWLFSTNHKDIGTLYFIFGAIAGVMGTCFSVLIRMELARPGDQILGGNHQLYNVLITAHAFLMIFFMVMPAMIGGSGNWSVPILIGAPDMAFPRLNNISFWLLPPSLLLLLSSALVEVGSGTGWTVYPPLSGITSHSGGAVDSAISSLHLSGVSSILGSINFITTISNMRGPGMTMHRSPLFVWSVPVTAFPLLLSLPVLAGAITMLLTDRNFNTTFSDPAGGGDPILYQHLFRFFGHPEVYIPILPGSGIISHIVSTFSGKPVFGYLGMVYAMISIGVLGFLVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGI... | 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-... |
P98003 | MFWISLVCLSVSHKMIGMCYLLVAILCGFLGYIYSLFIRLELSIIGCGVLFGDYQYYNVLVTTHGLVMVFAFIMPVMMGGLVNYFVPVLSGFPDMVFPRLNNMSFWMFMGGFGALVSGLLTEEGMGIGWTMYPTLICVDFHSSLACDFTVFAVHLLGVSSILNSINLLGTLFCCRRKFFSFLNWTLFIWGSLITALLLIITLPVLAGGVTLVLCDRNFNTSFYDVVGGGDLLLFQHLFWFFGHPEVYIIIIPVFGLISTMVEVLGFRCVFSSVAMIYSMILIAILGFFVWAHHMFVVGMDVDTRAYFGSVTVLIGLPTCI... | 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-... |
P15544 | MQLSRWLFSTNHKDIGTLYLIFGAWAGMVGTAMSVIIRAELAQPGSLLNDDQIYNVVVTAHALVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLIPPSFILLLASAGVENGAGTGWTIYPPLSSNITHAGSSVDLAIFSLHLAGASSILGLINFITTIINMRTPGMSLDRLPLFVWSVFVTAFLLLLSLPVLAGAITMLLTDRNINTTFFDPAGGGDPILFQHLFWLFGHPEVYILILPGFGMISHVIAHYSGKREPFGYLGLVYAMIAIGVLGFLVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGLKV... | 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-... |
P14573 | MATWSNLSLQDGASPLMEQLSFFHDHTMIDLLLITMIVGYSLSYMLLTKYTNRNMLHGHLIETIWTALPAITLIFIALPSLRLLYLLDDSSDAMITIKTIGRQWYWSYEYSDFINVEFDTYMTPENELNTDEFRLLEVDNRTTLPMNTEVRVLTSASDVLHSWAVPALVLKIDATPGRLNQGMFMINRPGLFFGQCSEICGANHSFMPIVIESTSIKLFIKWLSNMM | 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... |
P00412 | MILRLLECRFFTIALCDAAEPWQLGFQDAATPMMQGIIDLHHDIFFFLILILVFVLWMLVRALWHFNEQTNPIPQRIVHGTTIEIIWTIFPSVILLFIAIPSFALLYSMDGVLVDPAITIKAIGHQWYWTYEYSDYNSSDEQSLTFDSYMIPEDDLELGQLRLLEVDNRVVVPAKTHLRMIVTSADVLHSWAVPSLGVKCDAVPGRLNLTSILVQREGVYYGQCSEICGTNHAFMPIVVEAVTLKDYADWVSNQLILQTN | 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... |
P00414 | MTHQSHAYHMVKPSPWPLTGALSALLMTSGLAMWFHFHSMTLLMLGLLTNTLTMYQWWRDVTRESTYQGHHTPPVQKGLRYGMILFITSEVFFFAGFFWAFYHSSLAPTPQLGGHWPPTGITPLNPLEVPLLNTSVLLASGVSITWAHHSLMENNRNQMIQALLITILLGLYFTLLQASEYFESPFTISDGIYGSTFFVATGFHGLHVIIGSTFLTICFIRQLMFHFTSKHHFGFEAAAWYWHFVDVVWLFLYVSIYWWGS | 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... |
P80499 | TVSENVVKKVEDVMPIATGHEREXLXAQ | 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... |
P80974 | GTLKGIPTDDEQATGLERRT | 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... |
P00425 | MLRTSLTKGARLTGTRFVQTKALSKATLTDLPERWENMPNLEQKEIADNLTERQKLPWKTLNNEEIKAAWYISYGEWGPRRPVHGKGDVAFITKGVFLGLGISFGLFGLVRLLANPETPKTMNREWQLKSDEYLKSKNANPWGGYSQVQSK | 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... |
O93980 | MFLRSVTRAAARSSAVPTTGLRSYRTVSGPMACLNARPQTEKKSIAPQQTRAASEHAISNPTLAGIEKRWEAMPPQEQAELWMQLRDRMKVDWHQMTLQEKKAAYWISFGPHGPRSVPPKGENLKIFFKVAQLTLVSFGIFYVIHLFAKPQPKTMTKEWQEASNEYAKQEKINPIYGISAEGYEGKGFVQSPPAEKQ | 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... |
P29505 | MSKIVKFLKELATPSHSMEFFHKPASNSLLDASELNFVRRNIKREDFGHEVLTGAFGTLKSPVIVESIFHSRIVACEGGDGEEHDILFHTVAEKKPTICLDCGQVFKLKHISSEGEVMYY | 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... |
P06810 | MLRTPTVSALVRNVAVRAAKPTMAVRAASTMPISNPTLANIEKRWEQMPMQEQAELWMALRDRMKGNWADLTLQEKKAAYYIAFGPHGPRALPPPGEQKKVLAYTVAGVFLSFVIFATMRAFAKPPPATMTKEWQEATNEFLKAQKSDPLTGLTSEGYNGKGHVQSPSASA | 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... |
O74988 | MYLSKIICKKVPMKLLCTRNAATVSAAATNALQKEQPSGEAMIARPRLVDLDKRWGIMSQEEKDGLITDLYARQKQPWTTLSIEEKKAAYWIAFGEHGPRAFSHISQKTVFWGTVAGLTIGVVLFGLIRTQAAPSPRTMTREWQEKSNEYMKENKINPISGEASEGFKGRGQISGGIFSPSEKDKK | 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... |
Q20779 | MNRLAQPATRSVVKTFQRKSSGSFYGSNNVEGFKESYVTPLKQAHNASETWKKIFFIASIPCLALTMYAAFKDHKKHMSHERPEHVEYAFLNVRNKPFPWSDGNHSLFHNKAEQFVPGVGFEADREKH | 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... |
O13082 | MAMSPAATVARRRLAAASQGSHEGGARTWKILSFVLALPGVGVCMANAYMKMQAHSHDPPEFVPYPHLRIRTKPWPWGDGNHSLFHNAHTNALPTGYEGPHH | 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... |
O13085 | MASPASMAARRVLSAASHAGHEGGSARTWKILSFVLALPGVAVCIANAYMKMQQHSHEPPEFVAYSHLRIRTKKWPWGDGNHSLFHNPHENALPEGYEGPRH | 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... |
Q54P95 | MEGEQLQTAPYNPRFPQQNQTKHCWANYVDYYGCVKHYNGDNSKCQTFFNSMNSLCPAAWISEWDEQKAADLFPSDRV | 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... |
P80976 | KALYAPFDATFPNQNQTRNKAVDTAPCEWYRRVY | 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... |
Q02226 | ILCPLEAFIVQHILTISVMGLLSCFRSTVLRKCSKGSSGMSRFLYTNNFQRNLISSGGNESYYGYFNRRSYTSLYMGTGTVGGITSARIRVPNVGCEGFMCSSHLSITQRNSRLIHSTSKIVPNSEIQNITTEMVKTPEVSRWMDQVIPTIAPCDAAEPWQLGFQDAATPIMQGIIDLHHDIFFFVIQIGVFVSWVLLRALWHFRSKMNPIPQRIVHGTTIEILWTIFPSVILMFIAIPSFALLYSMDDIVVDPAITIKAIGHQWYWTYEYSDYNNSDEQSLAFDSYMIPEDDLELGQLRLLEVDNRVVVPAKTHLRVII... | 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... |
O31652 | MENTRDSAAISETKYIKASNRVTIYDFIKLAKPGIIISNSIAAFGGFWIAFASAEKTLTGLAFLMTMVTAMLGTAFVMASGTVYNNYFDRHMDAKMARTRSRASVTGKMPPAMILTYGSVLGIAGLAMLYSLNPLTAFLGLAAFIFYAIIYTVWVKRTSVWSTFVGSFPGAAPPLMGYCAVTGDFSMTAVLLYTIMFLWQPPHFWAIGIRRKEEYRAAGVPLLPVVKGNHVTKIKMMQYIAVLVPVTLLFPFSLGTGHISPFYFLAALVLGGIWIKKSIKGFKTDDDVKWAKDMFVYSLIYFCLLFFIMMIDSFMMFLIR | 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 (... |
A0RUY7 | MGAREILEVSKPRIVLLLVITAVTTMYAGDALSAGEPGPDLWDYAHLMAAGALASAGSSALNHYYDRDIDPKMRRTARRPIPSGRIGENIVLAYGLAISSAAVVYAYFLLNAPTAFFIALGIFSYVIIYTAWLKRTNRSNIVIGGIAGSAASWAGWTAATGTLDLLGFLIGFLVFVWTPSHFWCLAMKIREDYEAAGVPMLPVVIGMQRTSKYILGNTLLLLPYSLALYAFGMGLVYLVIAVASGGLMLVYHYKLTKTPTPDFAWKAYKVTAPYLTIIFAAVALDAAFHYPFPFPF | 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 (... |
Q7P0G0 | MSAVGLPLWRQHAHALWQLSKPRVVALIVFCAVIGMFLASPGVPDAAVVVPATLGIALVAGAAAMVNCLVERGVDVRMRRTAWRATATGEVGARETLLVALAVGGMGLALLLACCNALTAWLTLGTFVGYAIVYTLLLKPNTPQNIVIGGASGAMPPVLGWTAVNGQIDAFALALFLIIYTWTPPHFWALALYRRDDYARAGLPMLPVTHGQRYTTLSIVLYGFLLTAVTLLPVALGEAGAIYLGAVLLLDGRLLFLAVRLHRQYADALARRLFAWSIWYLTWLFAALLLDHYYLIPLN | 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 (... |
Q2W9D1 | MTFRQYIELLKPRIALMIALTAITGYGAVATKVDPVALLLLTLAMILGSAASAVFNHVWDRDIDRLMRRTSRRPMATGAGTPALGFALAVVLMVAGMALANAAFNWVVALHLFLGGFVYVAIYTVWLKRRHWTNIIIGGAAGSFAVLAGAAAVDQTQWLLPMVLALVLFLWTPSHFWSLAILLADDYRQAGVPMLPVVVGAKRTAWCILANTVILVGASLLPWGLGLLGNVYGFVAAVSGAVLLGFNVVLVRDTSRRWAGWNFAASMPYLLLLFIAVFADKHW | 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 (... |
P24009 | MANSRILNDTAIDGQIEETTAWKDFLSLIKIGIVNSNLITTFTGMWLALHISGLSFLGNINTVLLTLIGSSLIIAGSCAINNWYDRDIDHLMERTKVRPTVTGKIQPSQALWSGILLVALGLIMLLMTTVMAAVIGFIGVFTYVVLYTMWTKRRYTINTVVGSVSGAVPPLIGWTAVEGNIGVVAWVLFMILFIWQIPHFLALAIKKTEDYRAANIPMLPVVYGFEVTKRQIIVWVACLMPLPFFLGSLGLPIVILGLLLNIGWLILGLMGFRSKNIMKWATQMFVYSLNYMTIYFVAMVVLTLF | 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 (... |
A0RZ28 | MQREKAQSRVAVYYELSKPKIWYLLVFTAFGAAVAASGIYGIEISIATWALMLFSVAAGSASANVLTNYHDRDIDAIMKRTQKRPLPSGRVTPAGARNFGLFLAGASMVMAACIALTTTPVQGAWAAAFIAFGLFNNVLVYSYMLKRRSRSNIVLGGLCGGMPPMIGWVAVTTADLWTMGLVMGGLVFIWTPMHIWALTLHFRDDYNKVNVPMLTAVHSEGTSARVIAVSTVAMALFSLAPLLITLEDGAAAVGPVYLATAAASGALIIALSAWVVYKPTEKAAWVLFKFSSPYLAVLFIALMVDAGLRA | 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 (... |
Q1QHV7 | MPVVDQNAIELPPRISEASVADYFALLKPRVMSLVIFTALVGLMIAPGHVHPVLGFTAILCIAVGAGASGALNMALEGDIDVLMSRTANRPIPRGRITRGEAMGFGLTLSFFSVMTLGALVNWYAGGLLAFTIFFYVVIYTMGLKRRTAQNIVIGGAAGALPPVVAWAAATGSLSVEPLLLFLIIFFWTPPHFWALALFRSDDYARAGVPMLPVVAGPDATRLQILLYTIVLVAIAAAPWPLGYFDWVYGVTSLVLGAGMLVLAINVYRHRTGSTALRATRRLFAFSILYLFALFAVLLLDVLAKAVAPLIW | 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 (... |
Q310M2 | MLRAASSLFRFRVAGMVALSCVFGYLLAAGAAGPDMVTSAAGTFLLTCACSVFNQIQEKDLDARMPRTRNRPVASGRLPTTAARAVGMAALLPALILLHAAGGVRLVLLSAAVLALYNGVYTPMKKYTAFSLLAGAVPGALPPVFGWLAAGGNLYSPEIALLFIVYYLWQVPHFWLRAERDRQSYLAAGLPLPSVELPHRYHALLRLWYASYMVALLLLPVFPFIAETAVRIAVCLAGITGLAASGYLLASPVRGFHAVNVSMLFVMLLLVVDRLVTSGIIT | 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 (... |
B1ZMT0 | MSTTPASNAKFSDYLELTKPRLSMLSVMTALVGYLAARPPWDPIQLALLVLGTSAAAGGVAALNQWLEHDTDAHMKRTADRPIPAGKVATGSAFVLGVLMCIGSLFLLYALVHPLAALFTLLTIFSYLGWYTPAKRWSRWSTEIGAVAGAFPPLIGWSAGEGRVTALGWVLFGVLFFWQVPHFMAVAWTYRKDYSAVHFPMLPVRDESGERVALWSLINTAALLVTSLLPLLWGLTTWFYGVAAAVTGLWFLWQAIKFMQPATRDRAARKLFFASIGYLPLVLGALVIDRLFLVS | 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 (... |
B3CTF6 | MPNSHSTQSTPVKNFQNKFLVLTSTPKDFLLLMKPSVMLLAVFTAITGLFIAPNKIHPLLSSIAILCISTGAGAAGAINMWYDADIDSIMKRTRNRPTVTGKIPPSTALTFGIILAFFSVLVMAICVNYISSILLLISISFYIIVYTMWLKRRTAQNIVIGGAAGALPPVIGYSAVTNSIDTTCLMLFLIIFLWTPAHFWTLSLYYTNDYKLANVPILPLVKGINYTKYSILAYTFLTVISASLPYFTDIAGLLYLICSTISGIIFLCYASMLFNDRNNILARKMFKYSIIYLFNIFLYLIIEHCIKHFNIS | 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 (... |
A1R6I0 | MTAAVSTTDTPLNASPARGSIGISRKFKAYLALTKPRVIELLLVSTLPTMIFAQRGFPSIGLILATLVGGAFAAGSAGVFNCYIDRDIDKLMHRTEKRPLVTGEVTPREALVFAWILGAASIAILWFGANPLSAWLGLGAIVFYVVIYTMILKRRTAQNIVWGGAAGCFPVLIAWAAVTNTVEWPAIVLFMVIFLWTPPHYWPLSMRYGEDYRNAKVPMLGAIAGAKVVSVQVVLYAWAMVACSLLMVPVGGAGWVYTIAAVAAGAWFLYESHALYKRAQGGDVSNKGAMKVFHGSISYLTLLFIALAVDPFVGSAIVGS | 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 (... |
P08301 | MGPAEAGFGDYVALLKPRVMSLVVFTAFVGLWIAPQPVNPFVAFCAVLFIALGGGASGALNMWYDADIDAVMRRTAGRPVPSGRVTSQEPLAVGIALSGLSVMMLGAGGNWFAAGFLAFTIFFYAVVYTIWLKRSTPQNIVIGGAAGAFPPMIGWALPTGGIGIESLLMFALIFFWTPPHFWALALFMKDDYSKAGVPMLTVTHGRKVTRCHIFAYTLVLAPFALWLGFTSVGGPLYLAVSVVLNALFIAGGWQILRRSEDQAQADGYRVEKRYFRLSLYYTFLHFLALLVQHWVGGW | 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 (... |
Q6MBY2 | MINYYLLLTKPGIILGNLVTVMAGFLLASKGQFQFGLFFSTILGLAFIMASGCVFNNYIDLEKDRLMKRTQNRPLVIGVIFEKQAIVFGLALAIVGAIILYFYTNLLTLVIAELGFIIYVFFYSIWKSRTVYGTAIGSLAGAVPPLVGYCAVSNQLDLGAFILFAMMVFWQMPHFFSIAIYRLQDYSAANIPVLPLKKGIQITKIRILLYIIIFTLTSSLLTFFHFTGSLYLILTIGLGLTWLLMGLRGLKTSNDQQWAQQMFRFSLVIISVLSLTIPFDLVN | 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 (... |
Q167V9 | MALRGPAKTVAQTVSVVIFMGALAWASVPLYDWFCRVTGFGGVTGVSDVAPEDILDQTITIRFDGSLNNHMPWEFKPVVREMDVRIGESGLAFYEAYNPTDRPVAGSASYNVTPYQAGGFFNKIQCFCFEEQVLQPGERVQMPVTFYVDPEIVDDRDGKHVHTITLSYTFYEIDLPEEYADAQDIEENSDTSLN | 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): 21698
Sequence Length: 194
Subcellular Location: Cell inner membrane
|
Q1GE51 | MALNGPQKTVVQLVGVVVLMGGLAWASVPFYDWFCRVTGFGGVTQVAETGSDQVLDQTIKVRFDASKDRGMPWEFKPVERIMELKIGETGLAFYEAYNPTDRPVAGQASYNVAPFSAGYYFDKIQCFCFNEQVLQPGERVMMPVTFFVDPEIIEDPEAKYVHTITLSYTFHEIDLPEGYAALDTGDTSGAETELN | 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): 21678
Sequence Length: 195
Subcellular Location: Cell inner membrane
|
A7IPB8 | MDAGKAERRAGNGRRTDGRRHLVVAAACAAFIAAMVGVTYASVPLYAMFCALTGFGGATRVGAAPTSAPIEREITIRFDANVAPGLPWAFAPVERDVTVKVGATSLAHYTAANRSSMETHANATYNVSPPQAGAYFVKLQCFCFDEQTLAPNEKLEMPVVFYVDPAIAQDPDLKTLTDITLSYTFFPAKTPDKAAARASGTGG | 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): 21469
Sequence Length: 203
Subcellular Location: Cell inner membrane
|
Q6UWD8 | MPLTPEPPSGRVEGPPAWEAAPWPSLPCGPCIPIMLVLATLAALFILTTAVLAERLFRRALRPDPSHRAPTLVWRPGGELWIEPMGTARERSEDWYGSAVPLLTDRAPEPPTQVGTLEARATAPPAPSAPNSAPSNLGPQTVLEVPARSTFWGPQPWEGRPPATGLVSWAEPEQRPEASVQFGSPQARRQRPGSPDPEWGLQPRVTLEQISAFWKREGRTSVGF | PTM: O-glycosylated with core 1 or possibly core 8 glycans.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 24360
Sequence Length: 224
Subcellular Location: Membrane
|
Q6UW02 | MLDFAIFAVTFLLALVGAVLYLYPASRQAAGIPGITPTEEKDGNLPDIVNSGSLHEFLVNLHERYGPVVSFWFGRRLVVSLGTVDVLKQHINPNKTSDPFETMLKSLLRYQSGGGSVSENHMRKKLYENGVTDSLKSNFALLLKLSEELLDKWLSYPETQHVPLSQHMLGFAMKSVTQMVMGSTFEDDQEVIRFQKNHGTVWSEIGKGFLDGSLDKNMTRKKQYEDALMQLESVLRNIIKERKGRNFSQHIFIDSLVQGNLNDQQILEDSMIFSLASCIITAKLCTWAICFLTTSEEVQKKLYEEINQVFGNGPVTPEKI... | Location Topology: Single-pass membrane protein
Sequence Mass (Da): 52432
Sequence Length: 462
Subcellular Location: Membrane
EC: 1.14.-.-
|
P34791 | MASSSSMQMVHTSRSIAQIGFGVKSQLVSANRTTQSVCFGARSSGIALSSRLHYASPIKQFSGVYATTKHQRTACVKSMAAEEEEVIEPQAKVTNKVYFDVEIGGEVAGRIVMGLFGEVVPKTVENFRALCTGEKKYGYKGSSFHRIIKDFMIQGGDFTEGNGTGGISIYGAKFEDENFTLKHTGPGILSMANAGPNTNGSQFFICTVKTSWLDNKHVVFGQVIEGMKLVRTLESQETRAFDVPKKGCRIYACGELPLDA | Function: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Required for the light-induced increase of thiol accumulation. Assists the folding or assembly of SAT1 enzyme to form the cysteine synthase complex. Links light and redox sign... |
O49605 | MRREISFLLQPRCLLLLVALTIFLVFALFNTGKDEEKQVIEDHEITNRVFLDVDIDGQRLGRIVIGLYGTVVPKTVENFRALCTGEKGKTSSGKPLHYKGTPFHRIISGFVIQGGDIIHGDGKSSDSIYGGTFPDENFKIQHSHAGMVAMANTGPDSNGSQFFITTVKASWLEGEHVVLGKVIQGMDNVFAIEGGAGTYSGKPRKKVVIADSGEIPKDKWDEER | Function: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides (By similarity).
Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
Sequence Mass (Da): 24594
Sequence Length: 224
Subcellular Loca... |
P00191 | MVLAGLLLLLTLLAGAHLLWGRWKLRNLHLPPLVPGFLHLLQPNLPIHLLSLTQKLGPVYRLRLGLQEVVVLNSKRTIEEAMIRKWVDFAGRPQIPSYKLVSQRCQDISLGDYSLLWKAHKKLTRSALLLGTRSSMEPWVDQLTQEFCERMRVQAGAPVTIQKEFSLLTCSIICYLTFGNKEDTLVHAFHDCVQDLMKTWDHWSIQILDMVPFLRFFPNPGLWRLKQAIENRDHMVEKQLTRHKESMVAGQWRDMTDYMLQGVGRQRVEEGPGQLLEGHVHMSVVDLFIGGTETTASTLSWAVAFLLHHPEIQRRLQEEL... | Function: A cytochrome P450 monooxygenase that plays a major role in adrenal steroidogenesis. Catalyzes the hydroxylation at C-21 of progesterone and 17alpha-hydroxyprogesterone to respectively form 11-deoxycorticosterone and 11-deoxycortisol, intermediate metabolites in the biosynthetic pathway of mineralocorticoids a... |
P08686 | MLLLGLLLLPLLAGARLLWNWWKLRSLHLPPLAPGFLHLLQPDLPIYLLGLTQKFGPIYRLHLGLQDVVVLNSKRTIEEAMVKKWADFAGRPEPLTYKLVSKNYPDLSLGDYSLLWKAHKKLTRSALLLGIRDSMEPVVEQLTQEFCERMRAQPGTPVAIEEEFSLLTCSIICYLTFGDKIKDDNLMPAYYKCIQEVLKTWSHWSIQIVDVIPFLRFFPNPGLRRLKQAIEKRDHIVEMQLRQHKESLVAGQWRDMMDYMLQGVAQPSMEEGSGQLLEGHVHMAAVDLLIGGTETTANTLSWAVVFLLHHPEIQQRLQEE... | Function: A cytochrome P450 monooxygenase that plays a major role in adrenal steroidogenesis. Catalyzes the hydroxylation at C-21 of progesterone and 17alpha-hydroxyprogesterone to respectively form 11-deoxycorticosterone and 11-deoxycortisol, intermediate metabolites in the biosynthetic pathway of mineralocorticoids a... |
Q64562 | MLLPGLLLLLLLLLLAGTRWLWGQWKLWKLRLPPLAPGFLHFLQPNLPVYLFGLAQKLGPIYRIRLGLQDVVVLNSNKTIEEALIQKWVDFAGRPQILDGKMNFDLSMGDYSLTWKAHKKLSRSALVLGMRDSMEPLVEQLTQEFCERMRAQAGASVAIHKEFSLLTCSIISCLTFGDKQDSTLLNATHSCVRDLLKAWNHWSVQILDIIPFLRFFPNPGLWKLKQFQESRDHIVMQELKRHKDSLVAGQWKDMIDYMLQGVEKQRDARDPGQLHERHVHMSVVDLFVGGTETTAATLSWAVAFLLHHPEIQKRLQEELD... | Function: A cytochrome P450 monooxygenase that plays a major role in adrenal steroidogenesis. Catalyzes the hydroxylation at C-21 of progesterone and 17alpha-hydroxyprogesterone to respectively form 11-deoxycorticosterone and 11-deoxycortisol, intermediate metabolites in the biosynthetic pathway of mineralocorticoids a... |
Q94A16 | MAKIKPQALLQQSKKKKGPSRISITNIVIYTLAVLLLVFVLFSAYRRWTHRSEIPTHNGRSVLEDAAFPGMKNVDLPRFATLDTGKGSVTIELFKDTAPNVVDQFMKFCQDGYFKGFLFSRVVKHFVIQAGDSAEFDAVKDWALDRKNIDTSLKHEEFMVGTPKAKNEQGGFEFFIVSAQIKDLNEKLTVFGRVSKGQDVVQEIEEVETDDQYQPKSPIEIMSVTLLQDM | Function: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.
Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
Sequence Mass (Da): 26042
Sequence Length: 230
Subcellular Location: Mitochondr... |
Q9C835 | MAKIKPQALLNQSKKKKGPSRISISTIIVCNLVVAVVILSLVTTYRHWSQRSRNTIEHETRSQRFEDTNTASGQKTYDLPGFADINTSKGLITVELFKEGSPEVVDKFLDLCQKDHFKGMPFQRVIKNYLVQAGHSPSSIPVEEWTAKGKLRGRLHIGPKHEAFMLGTPKNKGNNKDFELLITTAPIPDLNDQLIVFGRVLKGEDVVQEIEEVDTDEHFQPKSPIGITGVVLKLET | Function: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides (By similarity).
Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
Location Topology: Single-pass type II membrane protein
Sequenc... |
P29981 | MEFITILLSTALFIVTFLFLFRQGAKRARFVYLVNKLPGPTAYPVVGNAIEAIVPRNKLFQVFDRRAKLYGPLYRIWAGPIAQVGLTRPEHVELILRDTKHIDKSLVYSFIRPWLGEGLLTGTGAKWHSHRKMITPTFHFKILDIFVDVFVEKSEILVKKLQSKVGGKDFDIYPFITHCALDIICETAMGIQMNAQEESESEYVKAVYEISELTMQRSVRPWLHPKVIFDLTTMGKRYAECLRILHGFTNKVIQERKSLRQMTGMKPTISNEEDELLGKKKRLAFLDLLLEASENGTKMSDTDIREEVDTFMFEGHDTTS... | Function: Involved in the metabolism of insect hormones and in the breakdown of synthetic insecticides.
Catalytic Activity: an organic molecule + O2 + reduced [NADPH--hemoprotein reductase] = an alcohol + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]
Location Topology: Peripheral membrane protein
Sequence Mass (... |
Q9VA27 | MSSKVITSLMAESILLSKVGQVISGYSPITVFLLGSILIFLVVYNKRRSRLVKYIEKIPGPAAMPFLGNAIEMNVDHDELFNRVIGMQKLWGTRIGINRVWQGTAPRVLLFEPETVEPILNSQKFVNKSHDYDYLHPWLGEGLLTSTDRKWHSRRKILTPAFHFKILDDFIDVFNEQSAVLARKLAVEVGSEAFNLFPYVTLCTLDIVCETAMGRRIYAQSNSESEYVKAVYGIGSIVQSRQAKIWLQSDFIFSLTAEYKLHQSYINTLHGFSNMVIRERKAELAILQENNNNNNNNAPDAYDDVGKKKRLAFLDLLIDA... | Function: May be involved in the metabolism of insect hormones and in the breakdown of synthetic insecticides.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 60757
Sequence Length: 535
Subcellular Location: Endoplasmic reticulum membrane
EC: 1.14.-.-
|
Q964T1 | MDITVFLSLTVVVFLAVIIFYGRNEERKRMLQKIPGAPSLPLIGTALPILYRRKEDRMTWIEEILEKYKPLILWYFGNRPFVNISSPELIEVVLRNTQLIDKAFLYDLFHSWLGTGLLTSSGAKWHQHRKIITPTFHFSILEGFITIFAEKSEILVRKLQKEVGRGPFFIRQYVSNCALDIICETAMGTSVNAQDEGFSEYVTAINKMTDVLSDRMANPLLYPEFIFKLTPYYWTHKKCLKVLNGFVNKIIQERKEERKKSKVTQTSEDADIGKKKRVPFLDTLLDASEDDNKLTDTDILEEVHTFMFEGHDTVSAAMTW... | Catalytic Activity: an organic molecule + O2 + reduced [NADPH--hemoprotein reductase] = an alcohol + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 58297
Sequence Length: 501
Subcellular Location: Endoplasmic reticulum membrane
EC: 1.14.14.1
|
P33269 | MFLVIGAILASALFVGLLLYHLKFKRLIDLISYMPGPPVLPLVGHGHHFIGKPPHEMVKKIFEFMETYSKDQVLKVWLGPELNVLMGNPKDVEVVLGTLRFNDKAGEYKALEPWLKEGLLVSRGRKWHKRRKIITPAFHFKILDQFVEVFEKGSRDLLRNMEQDRLKHGESGFSLYDWINLCTMDTICETAMGVSINAQSNADSEYVQAVKTISMVLHKRMFNILYRFDLTYMLTPLARAEKKALNVLHQFTEKIIVQRREELIREGSSQESSNDDADVGAKRKMAFLDILLQSTVDERPLSNLDIREEVDTFMFEGHDT... | Function: Involved in the metabolism of insect hormones and in the breakdown of synthetic insecticides.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 58691
Sequence Length: 512
Subcellular Location: Endoplasmic reticulum membrane
EC: 1.14.-.-
|
Q27589 | MLGVVGVLLLVAFATLLLWDFLWRRRGNGILPGPRPLPFLGNLLMYRGLDPEQIMDFVKKNQRKYGRLYRVWILHQLAVFSTDPRDIEFVLSSQQHITKNNLYKLLNCWLGDGLLMSTGRKWHGRRKIITPTFHFKILEQFVEIFDQQSAVMVEQLQSRADGKTPINIFPVICLTALDIIAETAMGTKINAQKNPNLPYVQAVNDVTNILIKRFIHAWQRVDWIFRLTQPTEAKRQDKAIKVMHDFTENIIRERRETLVNNSKETTPEEEVNFLGQKRRMALLDVLLQSTIDGAPLSDEDIREEVDTFMFEGHDTTTSAI... | Function: Involved in the metabolism of insect hormones and in the breakdown of synthetic insecticides.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 57914
Sequence Length: 501
Subcellular Location: Endoplasmic reticulum membrane
EC: 1.14.-.-
|
Q9VS79 | MQLMLRLNPKTFIKVGREYVLKFGHLQRVWIFNRLLIMSGDAELNEQLLSSQEHLVKHPVYKVLGQWLGNGLLLSDGKVWHQRRKIITPTFHFSILEQFVEVFDQQSNICVQRLAQKANGNTFDVYRSICAAALDIIAETAMGTKIYAQANESTPYAEAVNECTALLSWRFMSVYLQVELLFTLTHPHLKWRQTQLIRTMQEFTIKVIEKRRQALEDQQSKLMDTADEDVGSKRRMALLDVLLMSTVDGRPLTNDEIREEVDTFMFEGHDTTTSALSFCLHELSRHPEVQAKMLEEIVQVLGTDRSRPVSIRDLGELKYM... | Function: May be involved in the metabolism of insect hormones and in the breakdown of synthetic insecticides.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 53287
Sequence Length: 463
Subcellular Location: Endoplasmic reticulum membrane
EC: 1.14.-.-
|
O44221 | MWFIVYILLALPIMLFVFLSCEWPKRNDAEQIEWSSGVPFLGNAHQMGKTPAEILNTFFEFWHKYNKDNFRIWIGYYANILVSNPKHLEVIMNSTTLIEKLDIYDMLHPWLGEGLLTSKGSKWHKHRKMITPTFHFNILQDFHQVMNENSAKFIKRLKEVSAGDNIIDFQDETHYLTLDAICDTAMGVTINAIEKRDTVDVVKAFKDMCHIINMRAFRPLQRSDFLYRFSPEYATYAKTLKTLKDFTNDIIAKRIKVHRTAAAKTNQEGSEFSRKKMLPDTLLSATIDGRPLNQQEIYEEVSTFMFEGHDTTTSGVAFAG... | Function: Probably involved in steroid hormones biosynthesis.
Sequence Mass (Da): 60609
Sequence Length: 522
Subcellular Location: Mitochondrion
EC: 1.14.-.-
|
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