ID   H9TDH7_9TELE            Unreviewed;       261 AA.
AC   H9TDH7;
DT   13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT   13-JUN-2012, sequence version 1.
DT   01-OCT-2014, entry version 12.
DE   RecName: Full=Cytochrome b {ECO:0000256|RuleBase:RU000300};
DE   Flags: Fragment {ECO:0000313|EMBL:AFG19142.1};
GN   Name=cytb {ECO:0000313|EMBL:AFG19142.1};
OS   Liza macrolepis.
OG   Mitochondrion {ECO:0000313|EMBL:AFG19142.1}.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Mugilomorphae; Mugilidae; Liza.
OX   NCBI_TaxID=1111460 {ECO:0000313|EMBL:AFG19142.1};
RN   [1] {ECO:0000313|EMBL:AFG19142.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=150 {ECO:0000313|EMBL:AFG19142.1};
RX   PubMed=22445821; DOI=10.1016/j.ympev.2012.03.006;
RA   Durand J.-D., Shen K.-N., Chen W.-J., Jamandre B.W., Blel H., Diop K.,
RA   Nirchio M., Garcia de Leon F.J., Whitfield A.K., Chang C.-W.,
RA   Borsa P.;
RT   "Systematics of the grey mullets (Teleostei: Mugiliformes: Mugilidae):
RT   molecular phylogenetic evidence challenges two centuries of
RT   morphology-based taxonomy.";
RL   Mol. Phylogenet. Evol. 64:73-92(2012).
CC   -!- FUNCTION: Component of the ubiquinol-cytochrome c reductase
CC       complex (complex III or cytochrome b-c1 complex), which is a
CC       respiratory chain that generates an electrochemical potential
CC       coupled to ATP synthesis. {ECO:0000256|RuleBase:RU000300}.
CC   -!- COFACTOR: Binds 2 heme groups non-covalently.
CC       {ECO:0000256|RuleBase:RU000300}.
CC   -!- SIMILARITY: Belongs to the cytochrome b family.
CC       {ECO:0000256|RuleBase:RU000300}.
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DR   EMBL; JQ060168; AFG19142.1; -; 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:0070469; C:respiratory chain; IEA:UniProtKB-KW.
DR   GO; GO:0009055; F:electron carrier activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   GO; GO:0022904; P:respiratory electron transport chain; IEA:InterPro.
DR   Gene3D; 1.20.810.10; -; 1.
DR   InterPro; IPR005798; Cyt_b/b6_C.
DR   InterPro; IPR005797; Cyt_b/b6_N.
DR   InterPro; IPR027387; Cytb/b6-like.
DR   InterPro; IPR016174; Di-haem_cyt_TM.
DR   Pfam; PF00032; Cytochrom_B_C; 1.
DR   Pfam; PF13631; Cytochrom_B_N_2; 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:RU000300};
KW   Heme {ECO:0000256|RuleBase:RU000300};
KW   Iron {ECO:0000256|RuleBase:RU000300}; Membrane;
KW   Metal-binding {ECO:0000256|RuleBase:RU000300};
KW   Mitochondrion {ECO:0000256|RuleBase:RU000300,
KW   ECO:0000313|EMBL:AFG19142.1};
KW   Respiratory chain {ECO:0000256|RuleBase:RU000300};
KW   Transmembrane {ECO:0000256|RuleBase:RU000300};
KW   Transport {ECO:0000256|RuleBase:RU000300}.
FT   NON_TER       1      1       {ECO:0000313|EMBL:AFG19142.1}.
FT   NON_TER     261    261       {ECO:0000313|EMBL:AFG19142.1}.
SQ   SEQUENCE   261 AA;  29114 MW;  40AC6CB7B2279279 CRC64;
     FGSLRGLCLI AQIVTGLFLA KHYTPDTASA FSSVAHICRD VNYGWLIRNM HANGASFFFI
     CIYLHIGRGL YYGSYLYKET WNIGVILLLL VMMTAFVGYV LPWGQMSFWG ATVITNLLSA
     VPYIGDSLVQ WIWGGFSVNN ATLTRFFAFH FLLPFIILAM TLVHLIFLHK TGSNNPLGLN
     SNAKKISFHP YFTYKDLLGF AILLTALASL ALFAPNLLGD PDNFTLANPM VTPPHIKPEW
     YFLFAYAILR SIPNKLGGVL A
//