ID   CYB_ALLMA               Reviewed;         382 AA.
AC   Q37395;
DT   06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   14-OCT-2015, entry version 77.
DE   RecName: Full=Cytochrome b;
DE   AltName: Full=Complex III subunit 3;
DE   AltName: Full=Complex III subunit III;
DE   AltName: Full=Cytochrome b-c1 complex subunit 3;
DE   AltName: Full=Ubiquinol-cytochrome-c reductase complex cytochrome b subunit;
GN   Name=cob; Synonyms=cytB;
OS   Allomyces macrogynus.
OG   Mitochondrion.
OC   Eukaryota; Fungi; Blastocladiomycota; Blastocladiomycetes;
OC   Blastocladiales; Blastocladiaceae; Allomyces.
OX   NCBI_TaxID=28583;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=8636971; DOI=10.1006/jmbi.1996.0056;
RA   Paquin B., Lang B.F.;
RT   "The mitochondrial DNA of Allomyces macrogynus: the complete genomic
RT   sequence from an ancestral fungus.";
RL   J. Mol. Biol. 255:688-701(1996).
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:0000250}.
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250};
CC       Note=Binds 2 heme groups non-covalently. {ECO:0000250};
CC   -!- SUBUNIT: Fungal cytochrome b-c1 complex contains 10 subunits; 3
CC       respiratory subunits, 2 core proteins and 5 low-molecular weight
CC       proteins. Cytochrome b-c1 complex is a homodimer (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250};
CC       Multi-pass membrane protein {ECO:0000250}.
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. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the cytochrome b family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00967, ECO:0000255|PROSITE-
CC       ProRule:PRU00968}.
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DR   EMBL; U41288; AAC49221.1; -; Genomic_DNA.
DR   PIR; S63638; S63638.
DR   RefSeq; NP_043720.1; NC_001715.1.
DR   ProteinModelPortal; Q37395; -.
DR   SMR; Q37395; 1-377.
DR   GeneID; 801884; -.
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:0009055; F:electron carrier activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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   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; IPR030689; Cytochrome_b.
DR   InterPro; IPR016174; Di-haem_cyt_TM.
DR   Pfam; PF00032; Cytochrom_B_C; 1.
DR   Pfam; PF13631; Cytochrom_B_N_2; 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; Heme; Iron; Membrane; Metal-binding;
KW   Mitochondrion; Mitochondrion inner membrane; Respiratory chain;
KW   Transmembrane; Transmembrane helix; Transport.
FT   CHAIN         1    382       Cytochrome b.
FT                                /FTId=PRO_0000061733.
FT   TRANSMEM     32     52       Helical. {ECO:0000255}.
FT   TRANSMEM     75     95       Helical. {ECO:0000255}.
FT   TRANSMEM    111    131       Helical. {ECO:0000255}.
FT   TRANSMEM    151    171       Helical. {ECO:0000255}.
FT   TRANSMEM    179    199       Helical. {ECO:0000255}.
FT   TRANSMEM    230    250       Helical. {ECO:0000255}.
FT   TRANSMEM    262    282       Helical. {ECO:0000255}.
FT   TRANSMEM    289    309       Helical. {ECO:0000255}.
FT   TRANSMEM    321    341       Helical. {ECO:0000255}.
FT   TRANSMEM    354    374       Helical. {ECO:0000255}.
FT   METAL        82     82       Iron 1 (heme b562 axial ligand).
FT                                {ECO:0000255|PROSITE-ProRule:PRU00968}.
FT   METAL        96     96       Iron 2 (heme b566 axial ligand).
FT                                {ECO:0000255|PROSITE-ProRule:PRU00968}.
FT   METAL       183    183       Iron 1 (heme b562 axial ligand).
FT                                {ECO:0000255|PROSITE-ProRule:PRU00968}.
FT   METAL       197    197       Iron 2 (heme b566 axial ligand).
FT                                {ECO:0000255|PROSITE-ProRule:PRU00968}.
SQ   SEQUENCE   382 AA;  43468 MW;  A892A1A46A6915FA CRC64;
     MRFLKSHPVL SLANSFLIDS PLPSNITYLW NFGSLLGLCL VIQIVTGVTL AMHYAPSTSL
     AFVSVEHIMR DVFYGWLIRY AHANGASFFF ICVYIHMARG LYFNSYTKPR VLLWSVGVVI
     YILMMATAFL GYVLPWGQMS FWGATVITNL LSAIPYIGTA LVEFVWGGFS VDNATLNRFF
     SLHYLLPFIL AALVVVHLIA LHEHGSNNPL GISSKVDRLP FHPYFTYKDL VGFFVFFLIF
     FGFVFYQPNL MGHPDNYIPA NPLVTPVSIV PEWYFLPFYA ILRAIPSKLG GVIGMFGALL
     ILLALPWLET SKVRGAGFRP VMKFFFWLFV VNFFLLMYCG GQHAEEPFIT LSRICTAYYF
     MYFLVIIPVI GHLENLLHRC RD
//