ID   CYB_ASPNG      STANDARD;      PRT;   385 AA.
AC   Q33798;
DT   15-DEC-1998 (Rel. 37, Created)
DT   15-DEC-1998 (Rel. 37, Last sequence update)
DT   05-JUL-2004 (Rel. 44, Last annotation update)
DE   Cytochrome b.
GN   Name=COB; Synonyms=COBA, CYTB;
OS   Aspergillus niger.
OG   Mitochondrion.
OC   Eukaryota; Fungi; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiales; Trichocomaceae; mitosporic Trichocomaceae; Aspergillus.
OX   NCBI_TaxID=5061;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=WU-2223L;
RA   Narusawa T., Kanayama S., Kirimura K., Usami S.;
RT   "Nucleotide sequence of the apocytochrome b gene of Aspergillus niger
RT   WU-2223L.";
RL   Submitted (JUL-1995) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE OF 142-286.
RC   STRAIN=IFM 40606, IFM 41398, IFM 41399, IFM 46897, IFM 5367, and
RC   IFM 5368;
RX   MEDLINE=99065785; PubMed=9776828;
RX   DOI=10.1046/j.1365-280X.1998.00145.x;
RA   Wang L., Yokoyama K., Miyaji M., Nishimura K.;
RT   "The identification and phylogenetic relationship of pathogenic
RT   species of Aspergillus based on the mitochondrial cytochrome b gene.";
RL   Med. Mycol. 36:153-164(1998).
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 two heme groups non-covalently. Heme 1 (or BL or
CC       b562) is low-potential and absorbs at about 562 nm, and heme 2 (or
CC       BH or b566) is high-potential and absorbs at about 566 nm (By
CC       similarity).
CC   -!- SUBUNIT: The main subunits of complex b-c1 are: cytochrome b,
CC       cytochrome c1 and the Rieske protein (By similarity).
CC   -!- SIMILARITY: Belongs to the cytochrome b family.
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DR   EMBL; D63375; BAA09690.1; -.
DR   EMBL; AB000575; BAA34142.1; -.
DR   EMBL; AB000576; BAA34143.1; -.
DR   EMBL; AB000577; BAA34144.1; -.
DR   EMBL; AB000578; BAA34145.1; -.
DR   EMBL; AB000583; BAA34150.2; -.
DR   EMBL; AB000597; BAA34162.1; -.
DR   HSSP; P00163; 1EZV.
DR   InterPro; IPR005798; Cytb_b6_C.
DR   InterPro; IPR005797; Cytb_b6_N.
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.
KW   Electron transport; Heme; Mitochondrion; Respiratory chain;
KW   Transmembrane.
FT   METAL        82     82       Iron 1 (heme b562 axial ligand).
FT   METAL        96     96       Iron 2 (heme b566 axial ligand).
FT   METAL       183    183       Iron 1 (heme b562 axial ligand).
FT   METAL       197    197       Iron 2 (heme b566 axial ligand).
SQ   SEQUENCE   385 AA;  43078 MW;  73980B1D34386EF3 CRC64;
     MRILKSHPLL KIVNSYMIDS PQPANISYLW NFGSLLALCL GIQIVTGVTL AMHYTPSVLE
     AFNSVEHIMR DVNNGWLVRY LHANTASAFF FLVYLHIGRG LYYGSYKSPR TLTWAIGTVI
     LIVMMATAFL GYVLPYGQMS LWGATVITNL MSAIPWIGQD IVEFIWGGFS VNNATLNRFF
     ALHFLLPFVL AALALMHLIA MHDTVGSGNP LGISGNYDRL PFAPYFIFKD LVTIFIFFIV
     LSIFVFFMPN ALGDSENYVM ANPMQTPPAI VPEWYLLPFY AILRSIPNKL LGVIAMFSAI
     LALMVMPITD LSKLRGVQFR PLSKVAFYIF VANFLVLMQI GAKHVETPFI ELGQISTVLY
     LAHFLVIVPV VSLIENSLVE LATKK
//