ID A0A2U9IB08_9STRA Unreviewed; 193 AA. AC A0A2U9IB08; DT 12-SEP-2018, integrated into UniProtKB/TrEMBL. DT 12-SEP-2018, sequence version 1. DT 10-OCT-2018, entry version 2. DE RecName: Full=Cytochrome c oxidase subunit 2 {ECO:0000256|RuleBase:RU000457}; DE Flags: Fragment; GN Name=cox2 {ECO:0000313|EMBL:AWR93156.1}; OS Perofascia lepidii. OG Mitochondrion {ECO:0000313|EMBL:AWR93156.1}. OC Eukaryota; Stramenopiles; Oomycetes; Peronosporales; Peronosporaceae; OC Perofascia. OX NCBI_TaxID=184465 {ECO:0000313|EMBL:AWR93156.1}; RN [1] {ECO:0000313|EMBL:AWR93156.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=BISAK TM5 {ECO:0000313|EMBL:AWR93156.1}; RA Soylu E.M., Kara M., Kurt S., Uysal A., Shin H.D., Choi Y.J., RA Soylu S.; RT "First Report of Downy Mildew Disease Caused by Perofascia lepidii on RT Garden Cress Lepidium sativum in Turkey."; RL Plant Dis. 101:1827-1827(2017). RN [2] {ECO:0000313|EMBL:AWR93156.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=BISAK TM5 {ECO:0000313|EMBL:AWR93156.1}; RA Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I., RA Dimitrov K.M., Suarez D.L., Swayne D.E.; RL Submitted (APR-2017) to the EMBL/GenBank/DDBJ databases. 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; KY962511; AWR93156.1; -; Genomic_DNA. DR Gene3D; 1.10.287.90; -; 1. DR Gene3D; 2.60.40.420; -; 1. DR InterPro; IPR002429; CcO_II-like_C. DR InterPro; IPR008972; Cupredoxin. DR InterPro; IPR011759; Cyt_c_oxidase_su2_TM_dom. DR InterPro; IPR036257; Cyt_c_oxidase_su2_TM_sf. 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}; KW Electron transport {ECO:0000256|RuleBase:RU000457}; KW Membrane {ECO:0000256|RuleBase:RU000457, KW ECO:0000256|SAAS:SAAS00883094, ECO:0000256|SAM:Phobius}; KW Metal-binding {ECO:0000256|RuleBase:RU000457}; KW Mitochondrion {ECO:0000256|RuleBase:RU000457, KW ECO:0000313|EMBL:AWR93156.1}; KW Mitochondrion inner membrane {ECO:0000256|RuleBase:RU000457}; KW Respiratory chain {ECO:0000256|RuleBase:RU000457}; KW Transmembrane {ECO:0000256|RuleBase:RU000457, KW ECO:0000256|SAAS:SAAS00882981, ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00883111, KW ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|RuleBase:RU000457}. FT TRANSMEM 20 39 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 60 82 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 1 88 COX2_TM. {ECO:0000259|PROSITE:PS50999}. FT DOMAIN 89 193 COX2_CUA. {ECO:0000259|PROSITE:PS50857}. FT NON_TER 1 1 {ECO:0000313|EMBL:AWR93156.1}. FT NON_TER 193 193 {ECO:0000313|EMBL:AWR93156.1}. SQ SEQUENCE 193 AA; 22028 MW; 46AE23B48E35103B CRC64; FQDPATPVME GIINFHHDLM FFLIIITVFV CWMLFRVITL FNEKKNKIPA TVVHGATIEI IWTSIPALIL LIIAIPSFAL LYSMDEVIDP IITIKVIGSQ WYWSYEYSDN LEFADEPLIF DSYMIQEDDL AVGQFRLLEV DNRVVVPTNS HIRVLITASD VLHSWAIPSL GIKLDACPGR LNQTSMFIKR EGV //