ID   A0A3G4R2E0_OCHKO        Unreviewed;       379 AA.
AC   A0A3G4R2E0;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   03-JUL-2019, entry version 4.
DE   RecName: Full=Cytochrome b {ECO:0000256|RuleBase:RU362117};
GN   Name=CYTB {ECO:0000313|EMBL:AYU56860.1};
OS   Ochotona koslowi (Koslov's pika).
OG   Mitochondrion {ECO:0000313|EMBL:AYU56860.1}.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Lagomorpha; Ochotonidae;
OC   Ochotona.
OX   NCBI_TaxID=130835 {ECO:0000313|EMBL:AYU56860.1};
RN   [1] {ECO:0000313|EMBL:AYU56860.1}
RP   NUCLEOTIDE SEQUENCE.
RA   He J.Y., Ma G.Y., Xie C.H., Zhang Z.T., Su P.J.;
RT   "The complete mitochondrial DNA sequence of Ochotona koslowi.";
RL   Submitted (FEB-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Component of the ubiquinol-cytochrome c reductase
CC       complex (complex III or cytochrome b-c1 complex) that is part of
CC       the mitochondrial respiratory chain. The b-c1 complex mediates
CC       electron transfer from ubiquinol to cytochrome c. Contributes to
CC       the generation of a proton gradient across the mitochondrial
CC       membrane that is then used for ATP synthesis.
CC       {ECO:0000256|RuleBase:RU362117}.
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413;
CC         Evidence={ECO:0000256|PIRSR:PIRSR038885-2,
CC         ECO:0000256|RuleBase:RU362117};
CC       Note=Binds 2 heme groups non-covalently.
CC       {ECO:0000256|PIRSR:PIRSR038885-2, ECO:0000256|RuleBase:RU362117};
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC       {ECO:0000256|RuleBase:RU362117}.
CC   -!- SIMILARITY: Belongs to the cytochrome b family.
CC       {ECO:0000256|RuleBase:RU362117}.
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DR   EMBL; MG888668; AYU56860.1; -; Genomic_DNA.
DR   SMR; A0A3G4R2E0; -.
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:0045275; C:respiratory chain complex III; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008121; F:ubiquinol-cytochrome-c reductase activity; IEA:InterPro.
DR   GO; GO:0006122; P:mitochondrial electron transport, ubiquinol to cytochrome c; IEA:InterPro.
DR   CDD; cd00290; cytochrome_b_C; 1.
DR   CDD; cd00284; Cytochrome_b_N; 1.
DR   Gene3D; 1.20.810.10; -; 1.
DR   InterPro; IPR005798; Cyt_b/b6_C.
DR   InterPro; IPR036150; Cyt_b/b6_C_sf.
DR   InterPro; IPR005797; Cyt_b/b6_N.
DR   InterPro; IPR027387; Cytb/b6-like_sf.
DR   InterPro; IPR030689; Cytochrome_b.
DR   InterPro; IPR016174; Di-haem_cyt_TM.
DR   Pfam; PF00032; Cytochrom_B_C; 1.
DR   Pfam; PF00033; Cytochrome_B; 1.
DR   PIRSF; PIRSF038885; COB; 1.
DR   SUPFAM; SSF81342; SSF81342; 1.
DR   SUPFAM; SSF81648; SSF81648; 1.
DR   PROSITE; PS51003; CYTB_CTER; 1.
DR   PROSITE; PS51002; CYTB_NTER; 1.
PE   3: Inferred from homology;
KW   Electron transport {ECO:0000256|RuleBase:RU362117};
KW   Heme {ECO:0000256|PIRSR:PIRSR038885-2, ECO:0000256|RuleBase:RU362117};
KW   Iron {ECO:0000256|PIRSR:PIRSR038885-2, ECO:0000256|RuleBase:RU362117};
KW   Membrane {ECO:0000256|RuleBase:RU362117};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR038885-2,
KW   ECO:0000256|RuleBase:RU362117};
KW   Mitochondrion {ECO:0000256|RuleBase:RU362117,
KW   ECO:0000313|EMBL:AYU56860.1};
KW   Respiratory chain {ECO:0000256|RuleBase:RU362117};
KW   Transmembrane {ECO:0000256|RuleBase:RU362117};
KW   Transmembrane helix {ECO:0000256|RuleBase:RU362117};
KW   Transport {ECO:0000256|RuleBase:RU362117}.
FT   TRANSMEM     30     52       Helical. {ECO:0000256|RuleBase:RU362117}.
FT   TRANSMEM     87    107       Helical. {ECO:0000256|RuleBase:RU362117}.
FT   TRANSMEM    113    133       Helical. {ECO:0000256|RuleBase:RU362117}.
FT   TRANSMEM    140    158       Helical. {ECO:0000256|RuleBase:RU362117}.
FT   TRANSMEM    178    200       Helical. {ECO:0000256|RuleBase:RU362117}.
FT   TRANSMEM    229    246       Helical. {ECO:0000256|RuleBase:RU362117}.
FT   TRANSMEM    288    307       Helical. {ECO:0000256|RuleBase:RU362117}.
FT   TRANSMEM    319    340       Helical. {ECO:0000256|RuleBase:RU362117}.
FT   TRANSMEM    346    372       Helical. {ECO:0000256|RuleBase:RU362117}.
FT   DOMAIN        1    209       CYTB_NTER. {ECO:0000259|PROSITE:PS51002}.
FT   DOMAIN      210    379       CYTB_CTER. {ECO:0000259|PROSITE:PS51003}.
FT   METAL        83     83       Iron 1 (heme b562 axial ligand).
FT                                {ECO:0000256|PIRSR:PIRSR038885-2}.
FT   METAL        97     97       Iron 2 (heme b566 axial ligand).
FT                                {ECO:0000256|PIRSR:PIRSR038885-2}.
FT   METAL       182    182       Iron 1 (heme b562 axial ligand).
FT                                {ECO:0000256|PIRSR:PIRSR038885-2}.
FT   METAL       196    196       Iron 2 (heme b566 axial ligand).
FT                                {ECO:0000256|PIRSR:PIRSR038885-2}.
FT   BINDING     201    201       Ubiquinone. {ECO:0000256|PIRSR:
FT                                PIRSR038885-1}.
SQ   SEQUENCE   379 AA;  42716 MW;  42268E04B8C06E10 CRC64;
     MTNIRKTHPL MKIVNHSFID LPAPSNISAW WNFGSLLGLC LGIQIITGLF LAMHYTSDTL
     TAFSSVTHIC RDVNYGWIIR YMHANGASMF FICLFLHVGR GIYYGSYTYS ETWNIGILLL
     FTVMATAFMG YVLPWGQMSF WGATVITNLL SAIPYIGTDL VQWIWGGFSV DKATLTRFFA
     FHFILPFVIA ALVLVHLLFL HETGSNNPTG IISDADKIPF HPYYTIKDAL GFLLLISLLL
     SLVLFHPDLL GDPDNYTPAN PLNTPPHIKP EWYFLFAYAI LRSIPNKLGG VLALVLSIAI
     LAAMPFLHTS KQRSMMFRPM SQTLFWILVA DLLTLTWIGG QPVEHPFIII GQLASFLYFL
     LILALMPICS LIENKLLKW
//