(data stored in ACNUC7421 zone)

HOGENOM: THEFY_1_PE1013

ID   THEFY_1_PE1013                       STANDARD;      PRT;   314 AA.
AC   THEFY_1_PE1013; Q47R64;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   RecName: Full=Cytochrome c oxidase subunit 2; EC=1.9.3 1;Flags:
DE   Precursor; (THEFY_1.PE1013).
GN   OrderedLocusNames=Tfu_1015;
OS   THERMOBIFIDA FUSCA YX.
OC   Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC   Streptosporangineae; Nocardiopsaceae; Thermobifida.
OX   NCBI_TaxID=269800;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS THEFY_1.PE1013.
CC       Thermobifida fusca YX, complete genome.
CC       genome.
CC   -!- ANNOTATIONS ORIGIN:Q47R64_THEFY
CC   -!- FUNCTION: Subunits I and II form the functional core of the enzyme
CC       complex. Electrons originating in cytochrome c are transferred via
CC       heme a and Cu(A) to the binuclear center formed by heme a3 and
CC       Cu(B) (By similarity).
CC   -!- CATALYTIC ACTIVITY: 4 ferrocytochrome c + O(2) + 4 H(+) = 4
CC       ferricytochrome c + 2 H(2)O.
CC   -!- COFACTOR: Copper A (By similarity).
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the cytochrome c oxidase subunit 2 family.
CC   -!- GENE_FAMILY: HOG000245527 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; Q47R64; -.
DR   EMBL; CP000088; AAZ55053.1; -; Genomic_DNA.
DR   RefSeq; YP_289076.1; NC_007333.1.
DR   ProteinModelPortal; Q47R64; -.
DR   STRING; Q47R64; -.
DR   GeneID; 3579275; -.
DR   GenomeReviews; CP000088_GR; Tfu_1015.
DR   KEGG; tfu:Tfu_1015; -.
DR   NMPDR; fig|269800.4.peg.1107; -.
DR   eggNOG; COG1622; -.
DR   OMA; GRCAEMC; -.
DR   PhylomeDB; Q47R64; -.
DR   ProtClustDB; CLSK2769118; -.
DR   BioCyc; TFUS269800:TFU_1015-MONOMER; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0070469; C:respiratory chain; IEA:UniProtKB-KW.
DR   GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR   GO; GO:0004129; F:cytochrome-c oxidase activity; IEA:InterPro.
DR   GO; GO:0009055; F:electron carrier activity; IEA:InterPro.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0022904; P:respiratory electron transport chain; IEA:InterPro.
DR   InterPro; IPR001505; Copper_CuA.
DR   InterPro; IPR008972; Cupredoxin.
DR   InterPro; IPR014222; Cyt_c_oxidase_su2.
DR   InterPro; IPR015964; Cyt_c_oxidase_su2-like_TM_dom.
DR   InterPro; IPR002429; Cyt_c_oxidase_su2_C.
DR   InterPro; IPR011759; Cyt_c_oxidase_su2_TM_dom.
DR   Gene3D; G3DSA:1.10.287.90; COX2_TM; 1.
DR   Gene3D; G3DSA:2.60.40.420; Cupredoxin; 1.
DR   Pfam; PF00116; COX2; 1.
DR   PRINTS; PR01166; CYCOXIDASEII.
DR   SUPFAM; SSF49503; Cupredoxin; 1.
DR   SUPFAM; SSF81464; Cyt_c_oxidase_II-like_TM; 1.
DR   TIGRFAMs; TIGR02866; CoxB; 1.
DR   PROSITE; PS00078; COX2; 1.
DR   PROSITE; PS50857; COX2_CUA; 1.
DR   PROSITE; PS50999; COX2_TM; 1.
DR   HOGENOMDNA; THEFY_1.PE1013; -.
KW   cytochrome c oxidase subunit II;
KW   Complete proteome; Copper; Electron transport; Metal-binding;
KW   Oxidoreductase; Respiratory chain; Transmembrane; Transport.
SQ   SEQUENCE   314 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MSPTRHRNRR HALRRWAPRG AVLAALAVAA TGCASNEFTR LGLPEPITEQ AERVVTLWQG
     SWVAAFAVGI LVWGLIIWSV IAYRKRSEQL PPQVRYNMPI EALYTVLPII VVSVLFYFTA
     RDQTYLLETD EPADVYVDVN AFQWSWQFTY EDELDVNGNP VSVAGVPSTS KDELPVLVLP
     SDSVVHFDLE APDVIHSFWI PAFAFKLDVI PGHPNEFQVK IKPGVEGDYE GRCAELCGYD
     HSRMLFTLRV VTPEEYRAWI EEQKANPQEL PAVPDLEEEA PAPNPGPATA TQDSSDTAAT
     ADDAATTAEE EDGQ
//

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