ID U3LTB8_9STRA Unreviewed; 195 AA. AC U3LTB8; DT 11-DEC-2013, integrated into UniProtKB/TrEMBL. DT 11-DEC-2013, sequence version 1. DT 12-APR-2017, entry version 17. DE RecName: Full=Cytochrome c oxidase subunit 2 {ECO:0000256|RuleBase:RU000457}; DE Flags: Fragment; GN Name=COX2 {ECO:0000313|EMBL:AGK25033.1}; OS Pythium nagaii. OG Mitochondrion {ECO:0000313|EMBL:AGK25033.1}. OC Eukaryota; Stramenopiles; Oomycetes; Pythiales; Pythiaceae; Pythium. OX NCBI_TaxID=289625 {ECO:0000313|EMBL:AGK25033.1}; RN [1] {ECO:0000313|EMBL:AGK25033.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=P16712 {ECO:0000313|EMBL:AGK25033.1}; RX PubMed=23709523; DOI=10.3852/12-322; RA Bahramisharif A., Lamprecht S.C., Spies C.F., Botha W.J., McLeod A.; RT "Pythium cederbergense sp. nov. and related taxa from Pythium clade G RT associated with the South African indigenous plant Aspalathus linearis RT (rooibos)."; RL Mycologia 105:1174-1189(2013). CC -!- FUNCTION: Cytochrome c oxidase is the component of the respiratory CC chain that catalyzes the reduction of oxygen to water. Subunits 1- CC 3 form the functional core of the enzyme complex. Subunit 2 CC transfers the electrons from cytochrome c via its binuclear copper CC A center to the bimetallic center of the catalytic subunit 1. CC {ECO:0000256|RuleBase:RU000457}. CC -!- COFACTOR: CC Name=Cu cation; Xref=ChEBI:CHEBI:23378; CC Evidence={ECO:0000256|RuleBase:RU000457}; CC Note=Binds a copper A center. {ECO:0000256|RuleBase:RU000457}; CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane CC {ECO:0000256|RuleBase:RU000457}; Multi-pass membrane protein CC {ECO:0000256|RuleBase:RU000457}. CC -!- SIMILARITY: Belongs to the cytochrome c oxidase subunit 2 family. CC {ECO:0000256|RuleBase:RU000457}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; JX397984; AGK25033.1; -; Genomic_DNA. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell. DR GO; GO:0070469; C:respiratory chain; IEA:UniProtKB-KW. DR GO; GO:0005507; F:copper ion binding; IEA:InterPro. DR GO; GO:0004129; F:cytochrome-c oxidase activity; IEA:InterPro. DR GO; GO:0022900; P:electron transport chain; IEA:InterPro. DR CDD; cd13912; CcO_II_C; 1. DR Gene3D; 1.10.287.90; -; 1. DR Gene3D; 2.60.40.420; -; 1. DR InterPro; IPR002429; CcO_II-like_C. DR InterPro; IPR034210; CcO_II_C. DR InterPro; IPR008972; Cupredoxin. DR InterPro; IPR011759; Cyt_c_oxidase_su2_TM_dom. DR Pfam; PF00116; COX2; 1. DR Pfam; PF02790; COX2_TM; 1. DR SUPFAM; SSF49503; SSF49503; 1. DR SUPFAM; SSF81464; SSF81464; 1. DR PROSITE; PS50857; COX2_CUA; 1. DR PROSITE; PS50999; COX2_TM; 1. PE 3: Inferred from homology; KW Copper {ECO:0000256|RuleBase:RU000457, ECO:0000256|SAAS:SAAS00709548}; KW Electron transport {ECO:0000256|RuleBase:RU000457, KW ECO:0000256|SAAS:SAAS00644428}; KW Membrane {ECO:0000256|RuleBase:RU000457, KW ECO:0000256|SAAS:SAAS00644354, ECO:0000256|SAM:Phobius}; KW Metal-binding {ECO:0000256|RuleBase:RU000457, KW ECO:0000256|SAAS:SAAS00709462}; KW Mitochondrion {ECO:0000256|RuleBase:RU000457, KW ECO:0000313|EMBL:AGK25033.1}; KW Mitochondrion inner membrane {ECO:0000256|RuleBase:RU000457}; KW Respiratory chain {ECO:0000256|RuleBase:RU000457, KW ECO:0000256|SAAS:SAAS00709567}; KW Transmembrane {ECO:0000256|RuleBase:RU000457, KW ECO:0000256|SAAS:SAAS00106619, ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00106576, KW ECO:0000256|SAM:Phobius}; KW Transport {ECO:0000256|RuleBase:RU000457, KW ECO:0000256|SAAS:SAAS00644342}. FT TRANSMEM 16 36 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 57 79 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 1 85 COX2_TM. {ECO:0000259|PROSITE:PS50999}. FT DOMAIN 86 195 COX2_CUA. {ECO:0000259|PROSITE:PS50857}. FT NON_TER 1 1 {ECO:0000313|EMBL:AGK25033.1}. FT NON_TER 195 195 {ECO:0000313|EMBL:AGK25033.1}. SQ SEQUENCE 195 AA; 22258 MW; B9E9F027B274F643 CRC64; PATPVMEGII NFHHDLMFFL IVVTIFVCWM LFRVITLFDE KKNKIPSTVV HGATIEIIWT SVPALILLTV AVPSFALLYS MDEVIDPIIT LKVIGSQWYW SYEYSDNLEF SDEPLIFDSY MVQENDLEIG QFRLLEVDNR VVVPTNSHIR VLITASDVLH SWAIPSLGIK LDACPGRLNQ TSMFIKREGV FYGQC //