(data stored in ACNUC7421 zone)

HOGENOM: BACMQ_1_PE23

ID   BACMQ_1_PE23                         STANDARD;      PRT;   705 AA.
AC   BACMQ_1_PE23; D5E3D7;
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   SubName: Full=Cadmium-translocating P-type ATPase; EC=3.6.3 -;
DE   (BACMQ_1.PE23).
GN   Name=cadA; OrderedLocusNames=BMQ_pBM40023;
OS   BACILLUS MEGATERIUM QM B1551.
OC   Bacteria; Firmicutes; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=545693;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS BACMQ_1.PE23.
CC       Bacillus megaterium QM B1551 plasmid pBM400, complete sequence.
CC       sequence.
CC   -!- ANNOTATIONS ORIGIN:D5E3D7_BACMQ
CC   -!- SIMILARITY: Belongs to the cation transport ATPase (P-type)
CC       family.
CC   -!- GENE_FAMILY: HOG000285828 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; D5E3D7; -.
DR   EMBL; CP001987; ADE72312.1; -; Genomic_DNA.
DR   RefSeq; YP_003565992.1; NC_004604.2.
DR   ProteinModelPortal; D5E3D7; -.
DR   EnsemblBacteria; EBBACT00000390598; EBBACP00000382872; EBBACG00000391461.
DR   GeneID; 4267609; -.
DR   GenomeReviews; CP001987_GR; BMQ_pBM40023.
DR   KEGG; bmq:BMQ_pBM40023; -.
DR   GeneTree; EBGT00070000033441; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0015662; F:ATPase activity, coupled to transmembrane movement of ions, phosphorylative mechanism; IEA:InterPDR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0046873; F:metal ion transmembrane transporter activity; IEA:InterPro.
DR   GO; GO:0006754; P:ATP biosynthetic process; IEA:InterPro.
DR   InterPro; IPR008250; ATPase_P-typ_ATPase-assoc-dom.
DR   InterPro; IPR006404; ATPase_P-typ_Cd/Co/Hg/Pb/Zn.
DR   InterPro; IPR023300; ATPase_P-typ_cyto_domA.
DR   InterPro; IPR023299; ATPase_P-typ_cyto_domN.
DR   InterPro; IPR006416; ATPase_P-typ_heavy-metal.
DR   InterPro; IPR001757; ATPase_P-typ_ion-transptr.
DR   InterPro; IPR018303; ATPase_P-typ_P_site.
DR   InterPro; IPR005834; Dehalogen-like_hydro.
DR   InterPro; IPR023214; HAD-like_dom.
DR   Gene3D; G3DSA:2.70.150.10; ATPase_P-typ_cyto_domA; 1.
DR   Gene3D; G3DSA:3.40.1110.10; ATPase_P-typ_cyto_domN; 1.
DR   Gene3D; G3DSA:3.40.50.1000; HAD-like_dom; 2.
DR   Pfam; PF00122; E1-E2_ATPase; 1.
DR   Pfam; PF00702; Hydrolase; 1.
DR   PRINTS; PR00119; CATATPASE.
DR   SUPFAM; SSF56784; HAD-like_dom; 1.
DR   TIGRFAMs; TIGR01512; ATPase-IB2_Cd; 1.
DR   TIGRFAMs; TIGR01525; ATPase-IB_hvy; 1.
DR   TIGRFAMs; TIGR01494; ATPase_P-type; 1.
DR   PROSITE; PS00154; ATPASE_E1_E2; 1.
DR   HOGENOMDNA; BACMQ_1.PE23; -.
KW   cadmium-translocating P-type ATPase;
KW   ATP-binding; Complete proteome; Hydrolase; Nucleotide-binding;
KW   Phosphoprotein; Plasmid; Transmembrane.
SQ   SEQUENCE   705 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MMMFGVKVAH SLPGRTRFYI PKQLETIHIE TWLRSFPGVY SASYNQVTGS LLIYHHITLS
     LYSLKSFIHK YKHTLKQAAC SWKKAIPIIA CGTIFLVNWY LQRSSYPAIV KALSYWVSTF
     TAIGTSYEVI KDGVIHVLKE RKGNANTLTA ASIFASLYMK NPGSALIITL MSTISELLTD
     YTSEQTKHYI HSVLKLDVSY AWRVKEKGVE EKVLVEDIEV GDKVVVFTGE KIPVDGIIIE
     GNGTADEASI TGEYMPREVS GGDNVYAGSV LQSGHVTVTV EKVGEDTSLS KIVKLLEEAQ
     DKRAPIQNIA DTVAEKMVPV SFGLALLTFF FTRNLNRAMS MLVIDFICGI KLSTATALYA
     SIGRAAKEGA IVKGSDHIEK MSKLNTVILD KTGTITEGTP VVQQVIAAEG FNQEDVIRLA
     AAAEKNSTHP IADAIMKQAK DWNILIPIRD NNAQVETTVG KGISTWLNGK RVIVGSLRFM
     NELKVKTTNL LQHMQNDENV IYVAYDQTLV GVVSIFDKIR SGMHRAVNNL RHQGINDIIM
     LTGDKRTVAR EMARRLKLNW YHAEALPDDK AFYVKKYGRT GAVMMVGDGI NDAPALAHAH
     VGVTMGAKRT DIASEASDVI ITSDNPEMLS ELVGLSKKTM NIIKQNFIAT FAINGIAILF
     GALGIFSPIV GAAIHNAATI GVVINSARIL WLGRETNESQ ILRSA
//

If you have problems or comments...

PBIL Back to PBIL home page