ID A0A2J7ZUT0_9CHLO Unreviewed; 366 AA. AC A0A2J7ZUT0; DT 28-MAR-2018, integrated into UniProtKB/TrEMBL. DT 28-MAR-2018, sequence version 1. DT 12-AUG-2020, entry version 12. DE RecName: Full=COX2_CUA domain-containing protein {ECO:0000259|PROSITE:PS50857}; GN ORFNames=TSOC_009846 {ECO:0000313|EMBL:PNH04037.1}; OS Tetrabaena socialis. OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae; OC Chlamydomonadales; Tetrabaenaceae; Tetrabaena. OX NCBI_TaxID=47790 {ECO:0000313|EMBL:PNH04037.1, ECO:0000313|Proteomes:UP000236333}; RN [1] {ECO:0000313|EMBL:PNH04037.1, ECO:0000313|Proteomes:UP000236333} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NIES-571 {ECO:0000313|EMBL:PNH04037.1, RC ECO:0000313|Proteomes:UP000236333}; RX PubMed=29294063; DOI=10.1093/molbev/msx332; RA Featherston J., Arakaki Y., Hanschen E.R., Ferris P.J., Michod R.E., RA Olson B.J.S.C., Nozaki H., Durand P.M.; RT "The 4-celled Tetrabaena socialis nuclear genome reveals the essential RT components for genetic control of cell number at the origin of RT multicellularity in the volvocine lineage."; RL Mol. Biol. Evol. 0:0-0(2017). CC -!- CATALYTIC ACTIVITY: CC Reaction=4 [Fe(II)cytochrome c] + 4 H(+) + O2 = 4 [Fe(III)cytochrome c] CC + 2 H2O; Xref=Rhea:RHEA:11436, Rhea:RHEA-COMP:10350, Rhea:RHEA- CC COMP:14399, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, CC ChEBI:CHEBI:29033, ChEBI:CHEBI:29034; EC=7.1.1.9; CC Evidence={ECO:0000256|ARBA:ARBA00000049}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11437; CC Evidence={ECO:0000256|ARBA:ARBA00000049}; CC -!- COFACTOR: CC Name=Cu cation; Xref=ChEBI:CHEBI:23378; CC Evidence={ECO:0000256|ARBA:ARBA00001935}; CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:PNH04037.1}. 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; PGGS01000432; PNH04037.1; -; Genomic_DNA. DR OrthoDB; 1183470at2759; -. DR Proteomes; UP000236333; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; 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 CDD; cd13912; CcO_II_C; 1. DR Gene3D; 2.60.40.420; -; 1. DR InterPro; IPR002429; CcO_II-like_C. DR InterPro; IPR034210; CcO_II_C. DR InterPro; IPR001505; Copper_CuA. DR InterPro; IPR008972; Cupredoxin. DR Pfam; PF00116; COX2; 1. DR SUPFAM; SSF49503; SSF49503; 1. DR PROSITE; PS00078; COX2; 1. DR PROSITE; PS50857; COX2_CUA; 1. PE 4: Predicted; KW Copper {ECO:0000256|ARBA:ARBA00023008}; Membrane {ECO:0000256|SAM:Phobius}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}; KW Reference proteome {ECO:0000313|Proteomes:UP000236333}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 313..332 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 1..147 FT /note="COX2_CUA" FT /evidence="ECO:0000259|PROSITE:PS50857" SQ SEQUENCE 366 AA; 40552 MW; 530343A1222CD2A3 CRC64; MSKEELKSKL KADPKYRSEL KERIKGALLS KVPASQAISY NFDSYMLTEV QPGQLRVLEV DERLVLPTNT LIRLLVTASD VIHSWAVPSL GVKMDAVPGR LNQVWMSINR EGVFYGQCSE LCGANHSFMP IVVEAISPRA FLTEGLLLAL AVLLAFSSRA EATTFRDGDY IHSSRKAQFH QSRTNWQDLL GQHCPRFGFD RLVAVPIPKP QLAFGKGDTY KLQFSFDGDR HLTPWLALLG EDAPAVPLVE VTLRRSGEEL LGATAEVRDA PAEYQERHPV LVAELRNVSH WPKHVLVHYR FDTRNDVDLD RGLYLLFPAG LLAVLALCLS ALRGVQPKLA QFLAEVTAEG GTAVAAVWKG SEGKGE //