ID   CYB_CALKE               Reviewed;         371 AA.
AC   Q9MLD7;
DT   01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-MAR-2009, entry version 40.
DE   RecName: Full=Cytochrome b;
DE   AltName: Full=Ubiquinol-cytochrome-c reductase complex cytochrome b subunit;
DE   AltName: Full=Cytochrome b-c1 complex subunit 3;
DE   AltName: Full=Complex III subunit 3;
DE   AltName: Full=Complex III subunit III;
GN   Name=MT-CYB; Synonyms=COB, CYTB, MTCYB;
OS   Calliophis kelloggi (Kellogg's coral snake).
OG   Mitochondrion.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Scleroglossa; Serpentes; Colubroidea;
OC   Elapidae; Elapinae; Calliophis.
OX   NCBI_TaxID=114670;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Slowinski J.B., Boundy J., Lawson R.;
RT   "The phylogenetic relationships of Asian coral snakes (Elapidae:
RT   Calliophis and Maticora) based on morphological and molecular
RT   characters.";
RL   Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases.
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 (By similarity).
CC   -!- COFACTOR: Binds 2 heme groups non-covalently (By similarity).
CC   -!- SUBUNIT: The main subunits of complex b-c1 are: cytochrome b,
CC       cytochrome c1 and the Rieske protein (By similarity).
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane; Multi-pass
CC       membrane protein (By similarity).
CC   -!- MISCELLANEOUS: Heme 1 (or BL or b562) is low-potential and absorbs
CC       at about 562 nm, and heme 2 (or BH or b566) is high-potential and
CC       absorbs at about 566 nm (By similarity).
CC   -!- SIMILARITY: Belongs to the cytochrome b family.
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DR   EMBL; AF220408; AAF35311.1; -; Genomic_DNA.
DR   HOVERGEN; Q9MLD7; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005746; C:mitochondrial respiratory chain; IEA:UniProtKB-KW.
DR   GO; GO:0009055; F:electron carrier activity; IEA:InterPro.
DR   GO; GO:0005506; F:iron 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   GO; GO:0006810; P:transport; IEA:UniProtKB-KW.
DR   InterPro; IPR016175; Cyt_b/b6.
DR   InterPro; IPR005798; Cyt_b/b6_C.
DR   InterPro; IPR005797; Cyt_b/b6_N.
DR   Gene3D; G3DSA:1.20.810.10; Cytochrome_b/b6; 1.
DR   PANTHER; PTHR19271; Cytochrome_b/b6; 1.
DR   Pfam; PF00032; Cytochrom_B_C; 1.
DR   Pfam; PF00033; Cytochrom_B_N; 1.
DR   PROSITE; PS51003; CYTB_CTER; 1.
DR   PROSITE; PS51002; CYTB_NTER; 1.
PE   3: Inferred from homology;
KW   Electron transport; Heme; Iron; Membrane; Metal-binding;
KW   Mitochondrion; Mitochondrion inner membrane; Respiratory chain;
KW   Transmembrane; Transport.
FT   CHAIN         1    371       Cytochrome b.
FT                                /FTId=PRO_0000060708.
FT   TRANSMEM     25     45       Potential.
FT   TRANSMEM     68     88       Potential.
FT   TRANSMEM    104    124       Potential.
FT   TRANSMEM    142    162       Potential.
FT   TRANSMEM    170    190       Potential.
FT   TRANSMEM    222    242       Potential.
FT   TRANSMEM    280    300       Potential.
FT   TRANSMEM    311    331       Potential.
FT   TRANSMEM    339    359       Potential.
FT   METAL        75     75       Iron 1 (heme b562 axial ligand).
FT   METAL        89     89       Iron 2 (heme b566 axial ligand).
FT   METAL       174    174       Iron 1 (heme b562 axial ligand).
FT   METAL       188    188       Iron 2 (heme b566 axial ligand).
SQ   SEQUENCE   371 AA;  42188 MW;  B6723C71E03BD70F CRC64;
     MSNQHTLLIS NLLPVGSNIS TWWNFGSMLL TCLILQITTG FFLAIHYTAN INLAFSSVTH
     IMRDVPYGWI MQNLHAIGAS MFFICIYIHI ARGLYYGLYM NKNVWLSGTT LLITLMATAF
     FGYVLPWGQM SFWAATVITN LLTAIPYLGT TITTWLWGGF SINDPTLTRF FALHFILPFA
     IISLSSIHII LLHNKGSNNP LGTNSDIDKI PFHPYHSYKD TLMTISLFIL MFTILSFSPD
     LFNDPENFSK ANPLVTPQHI KPEWYFLFAY GILRSIPNKL GGTLALLMSV TILMTAPFTH
     TSHMRPMTFR PLAQMAFWTL IATFITITWT ASKPVEPPFI IISQMTSILY FLFFIMNPLL
     GWTENKIMMN N
//