ID   A0A0K0YD85_9ANNE        Unreviewed;       263 AA.
AC   A0A0K0YD85;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   14-DEC-2022, entry version 16.
DE   RecName: Full=Cytochrome c oxidase subunit 3 {ECO:0000256|ARBA:ARBA00015944, ECO:0000256|RuleBase:RU003375};
GN   Name=COX3 {ECO:0000313|EMBL:AKS48934.1};
OS   Trypanobia cryptica.
OG   Mitochondrion {ECO:0000313|EMBL:AKS48934.1}.
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Annelida; Polychaeta;
OC   Errantia; Phyllodocida; Syllidae; Trypanobia.
OX   NCBI_TaxID=2814713 {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 mitochondrial
RT   genome and ribosomal data of Ramisyllis multicaudata.";
RL   Sci. Rep. 5:12072-12072(2015).
CC   -!- FUNCTION: Component of the cytochrome c oxidase, the last enzyme in the
CC       mitochondrial electron transport chain which drives oxidative
CC       phosphorylation. The respiratory chain contains 3 multisubunit
CC       complexes succinate dehydrogenase (complex II, CII), ubiquinol-
CC       cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III,
CC       CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to
CC       transfer electrons derived from NADH and succinate to molecular oxygen,
CC       creating an electrochemical gradient over the inner membrane that
CC       drives transmembrane transport and the ATP synthase. Cytochrome c
CC       oxidase is the component of the respiratory chain that catalyzes the
CC       reduction of oxygen to water. Electrons originating from reduced
CC       cytochrome c in the intermembrane space (IMS) are transferred via the
CC       dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1
CC       to the active site in subunit 1, a binuclear center (BNC) formed by
CC       heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2
CC       water molecules using 4 electrons from cytochrome c in the IMS and 4
CC       protons from the mitochondrial matrix. {ECO:0000256|RuleBase:RU003375}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the cytochrome c oxidase subunit 3 family.
CC       {ECO:0000256|ARBA:ARBA00010581, ECO:0000256|RuleBase:RU003375}.
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DR   EMBL; KR534503; AKS48934.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0K0YD85; -.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
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; IPR035973; Cyt_c_oxidase_su3-like_sf.
DR   InterPro; IPR013833; Cyt_c_oxidase_su3_a-hlx.
DR   PANTHER; PTHR11403; CYTOCHROME C OXIDASE SUBUNIT III; 1.
DR   Pfam; PF00510; COX3; 1.
DR   SUPFAM; SSF81452; Cytochrome c oxidase subunit III-like; 1.
DR   PROSITE; PS50253; COX3; 1.
PE   3: Inferred from homology;
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Mitochondrion {ECO:0000256|RuleBase:RU003375, ECO:0000313|EMBL:AKS48934.1};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW   ECO:0000256|RuleBase:RU003375};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        12..36
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        42..59
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        79..103
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        128..148
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        160..180
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        192..219
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        240..260
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          5..262
FT                   /note="COX3"
FT                   /evidence="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
//