(data stored in ACNUC7421 zone)

HOGENOM: DEMUC1_1_PE157

ID   DEMUC1_1_PE157                       STANDARD;      PRT;   777 AA.
AC   DEMUC1_1_PE157; E8R7I1;
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=ATPase, P-type (DEMUC1_1.PE157) (Transporting), HAD
DE   superfamily, subfamily IC; .
GN   OrderedLocusNames=Desmu_0157;
OS   DESULFUROCOCCUS MUCOSUS DSM 2162.
OC   Archaea; Crenarchaeota; Thermoprotei; Desulfurococcales;
OC   Desulfurococcaceae; Desulfurococcus.
OX   NCBI_TaxID=765177;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS DEMUC1_1.PE157.
CC       Desulfurococcus mucosus DSM 2162 chromosome, complete genome.
CC       / IFO 0083) chromosome G, complete sequence.
CC   -!- ANNOTATIONS ORIGIN:E8R7I1_DESM0
CC   -!- GENE_FAMILY: HOG000160005 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; E8R7I1; -.
DR   EMBL; CP002363; ADV64476.1; -; Genomic_DNA.
DR   RefSeq; YP_004175958.1; NC_014961.1.
DR   GeneID; 10152845; -.
DR   GenomeReviews; CP002363_GR; Desmu_0157.
DR   KEGG; dmu:Desmu_0157; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
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:0006754; P:ATP biosynthetic process; IEA:InterPro.
DR   GO; GO:0006812; P:cation transport; IEA:InterPro.
DR   InterPro; IPR008250; ATPase_P-typ_ATPase-assoc-dom.
DR   InterPro; IPR004014; ATPase_P-typ_cation-transptr_N.
DR   InterPro; IPR023300; ATPase_P-typ_cyto_domA.
DR   InterPro; IPR023299; ATPase_P-typ_cyto_domN.
DR   InterPro; IPR000695; ATPase_P-typ_H-transp.
DR   InterPro; IPR001757; ATPase_P-typ_ion-transptr.
DR   InterPro; IPR018303; ATPase_P-typ_P_site.
DR   InterPro; IPR006534; ATPase_P-typ_PM_proton-efflux.
DR   InterPro; IPR023298; ATPase_P-typ_TM_dom.
DR   InterPro; IPR005834; Dehalogen-like_hydro.
DR   InterPro; IPR023214; HAD-like_dom.
DR   Gene3D; G3DSA:2.70.150.10; ATPase_P-typ_cyto_domA; 2.
DR   Gene3D; G3DSA:3.40.1110.10; ATPase_P-typ_cyto_domN; 2.
DR   Gene3D; G3DSA:1.20.1110.10; ATPase_P-typ_TM_dom; 2.
DR   Pfam; PF00690; Cation_ATPase_N; 1.
DR   Pfam; PF00122; E1-E2_ATPase; 1.
DR   Pfam; PF00702; Hydrolase; 1.
DR   PRINTS; PR00119; CATATPASE.
DR   PRINTS; PR00120; HATPASE.
DR   SMART; SM00831; Cation_ATPase_N; 1.
DR   SUPFAM; SSF56784; HAD-like_dom; 1.
DR   TIGRFAMs; TIGR01647; ATPase-IIIA_H; 1.
DR   TIGRFAMs; TIGR01494; ATPase_P-type; 2.
DR   PROSITE; PS00154; ATPASE_E1_E2; 1.
DR   HOGENOMDNA; DEMUC1_1.PE157; -.
KW   HAD superfamily P-type ATPase;
KW   Complete proteome.
SQ   SEQUENCE   777 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MRGLTGLSSS EVEEKLRIYG FNTVPEKKES TLKIFVKKLQ GLTAYTIEAA AVISFILGRY
     IDAAIMILLL LLNAFIGVLH EQRAGKAVEM LKSRLKIVVK ALRDGEWRDI PSEYIVPGDV
     VKVRLGDIIP ADGVVLEGHL LVDESTLTGE SMPVEKNPGD PVYAGTAVAR GEAIIRITAT
     GPRTRYGRTV ELVEAGKPRL LIEEITSSIT RWLLAVDVFF VVLVVVRLLI TQTPVVDALP
     FTLTLLIASI PIALPAMTTI TLALGSVELA RAGVIVRRLE AVEAASMMEV ICLDKTGTIT
     ENKLVVKDII PLREGFTEHD VILYAALASE PDGRDPIDKA ILEKAGELGV DLGSVSVMEF
     KPFSPESKRS EALVSMGGRI LKAVKGAPQV LVDVDTTLDR ERFNEAVRTL GDRGMRPLAV
     GVEENGSLRV IGLIGIYDKP REDSQRFIEE IKSMGVKPVM VTGDNYYVAK SIARSVGIEG
     RVVSLKGVPR EELADLLDSA GVFAEVVPED KYEIVRLYQS KGKVVGMTGD GVNDAPALKQ
     ADLGVAVSNA TDIAKSVASV VLTKPGLGNI VDVIRLGRVV YRRIVVWAIN KIVKTFQVVY
     FVSASTLLLG APILTPTHMI LMLFLYDFVT LSISTDRLRP SSKPEKWNVR RLVKVSVILG
     LVKIAELFLA LYLGLHVLSL QLEQARTFVF YTLLTSGLFN ILNFRETGWF WHSKPSKVMT
     IALTTDILAG TIIAWKGWII QPIPPPVILI AFVYTVAVTL ILTDAVKIAV FKLFKYS
//

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