ID   A0A0K0YD85_9ANNE        Unreviewed;       263 AA.
AC   A0A0K0YD85;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   12-APR-2017, entry version 6.
DE   RecName: Full=Cytochrome c oxidase subunit 3 {ECO:0000256|RuleBase:RU003375};
GN   Name=COX3 {ECO:0000313|EMBL:AKS48934.1};
OS   Trypanosyllis (Trypanobia) sp. CB-2015.
OG   Mitochondrion {ECO:0000313|EMBL:AKS48934.1}.
OC   Eukaryota; Metazoa; Lophotrochozoa; Annelida; Polychaeta; Palpata;
OC   Aciculata; Phyllodocida; Syllidae; Trypanosyllis.
OX   NCBI_TaxID=1648961 {ECO:0000313|EMBL:AKS48934.1};
RN   [1] {ECO:0000313|EMBL:AKS48934.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=26183383; DOI=10.1038/srep12072;
RA   Aguado M.T., Glasby C.J., Schroeder P.C., Weigert A., Bleidorn C.;
RT   "The making of a branching annelid: an analysis of complete
RT   mitochondrial genome and ribosomal data of Ramisyllis multicaudata.";
RL   Sci. Rep. 5:12072-12072(2015).
CC   -!- FUNCTION: Subunits I, II and III form the functional core of the
CC       enzyme complex. {ECO:0000256|RuleBase:RU003375}.
CC   -!- SIMILARITY: Belongs to the cytochrome c oxidase subunit 3 family.
CC       {ECO:0000256|RuleBase:RU003375, ECO:0000256|SAAS:SAAS00709834}.
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DR   EMBL; KR534503; AKS48934.1; -; Genomic_DNA.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-KW.
DR   GO; GO:0004129; F:cytochrome-c oxidase activity; IEA:InterPro.
DR   GO; GO:0019646; P:aerobic electron transport chain; IEA:InterPro.
DR   CDD; cd01665; Cyt_c_Oxidase_III; 1.
DR   Gene3D; 1.20.120.80; -; 1.
DR   InterPro; IPR024791; Cyt_c/ubiquinol_Oxase_su3.
DR   InterPro; IPR033945; Cyt_c_oxase_su3_dom.
DR   InterPro; IPR000298; Cyt_c_oxidase-like_su3.
DR   InterPro; IPR013833; Cyt_c_oxidase_su3_a-hlx.
DR   PANTHER; PTHR11403; PTHR11403; 1.
DR   Pfam; PF00510; COX3; 1.
DR   SUPFAM; SSF81452; SSF81452; 1.
DR   PROSITE; PS50253; COX3; 1.
PE   3: Inferred from homology;
KW   Membrane {ECO:0000256|SAAS:SAAS00709742, ECO:0000256|SAM:Phobius};
KW   Mitochondrion {ECO:0000256|RuleBase:RU003375,
KW   ECO:0000313|EMBL:AKS48934.1};
KW   Transmembrane {ECO:0000256|RuleBase:RU003375,
KW   ECO:0000256|SAAS:SAAS00709762, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAAS:SAAS00709799,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM     12     36       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM     42     59       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM     79    103       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    128    148       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    160    180       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    192    219       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    240    260       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN        5    262       COX3. {ECO:0000259|PROSITE:PS50253}.
SQ   SEQUENCE   263 AA;  30427 MW;  79C3D434C551417E CRC64;
     MMKKVFHPYH LVEFSPWPLT GSLGALTLMT GLVNWFHQDL TPTILVGILI ILMTMIQWWR
     DVTRESTYLG HHTTGVQQLL KWGMILFITS EVFFFLAFFW AFFHSSLAPT MELGCDWPPM
     GINPLDSFAI PLLNTAVLLS SGVTVTWAHH SIMSHKIKEF KLGLTYTILL GLYFTLLQVW
     EYLESSFTIA DSVYGSTFFV ATGFHGLHVI IGTSFLIVCR MRSNFNHYSP THHFGFEAAA
     WYWHFVDVVW IFLYLCIYWW GSM
//