(data stored in ACNUC30567 zone)

HOGENOM: ACAM1_1_PE1760

ID   ACAM1_1_PE1760                       STANDARD;      PRT;   794 AA.
AC   ACAM1_1_PE1760; B0CDC6;
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=Copper-translocating P-type ATPase; (ACAM1_1.PE1760).
GN   Name=synA; OrderedLocusNames=AM1_1831;
OS   ACARYOCHLORIS MARINA MBIC11017.
OC   Bacteria; Cyanobacteria; Acaryochloris.
OX   NCBI_TaxID=329726;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS ACAM1_1.PE1760.
CC       Acaryochloris marina MBIC11017, complete genome.
CC   -!- ANNOTATIONS ORIGIN:B0CDC6_ACAM1
CC   -!- SIMILARITY: Belongs to the cation transport ATPase (P-type)
CC       family.
CC   -!- GENE_FAMILY: HOG000250397 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; B0CDC6; -.
DR   EMBL; CP000828; ABW26851.1; -; Genomic_DNA.
DR   RefSeq; YP_001516165.1; NC_009925.1.
DR   ProteinModelPortal; B0CDC6; -.
DR   STRING; B0CDC6; -.
DR   GeneID; 5680647; -.
DR   GenomeReviews; CP000828_GR; AM1_1831.
DR   KEGG; amr:AM1_1831; -.
DR   OMA; GTHHPLA; -.
DR   ProtClustDB; CLSK893343; -.
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:0005261; F:cation channel activity; IEA:InterPro.
DR   GO; GO:0005261; F:cation channel activity; 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:0030001; P:metal ion transport; IEA:InterPro.
DR   InterPro; IPR008250; ATPase_P-typ_ATPase-assoc-dom.
DR   InterPro; IPR001366; ATPase_P-typ_Cd-transp.
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   InterPro; IPR017969; Heavy-metal-associated_CS.
DR   InterPro; IPR006121; HeavyMe-assoc_HMA.
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; PF00403; HMA; 1.
DR   Pfam; PF00702; Hydrolase; 1.
DR   PRINTS; PR00119; CATATPASE.
DR   PRINTS; PR00941; CDATPASE.
DR   SUPFAM; SSF56784; HAD-like_dom; 1.
DR   SUPFAM; SSF55008; HeavyMe_transpt; 1.
DR   TIGRFAMs; TIGR01525; ATPase-IB_hvy; 1.
DR   TIGRFAMs; TIGR01494; ATPase_P-type; 2.
DR   PROSITE; PS00154; ATPASE_E1_E2; 1.
DR   PROSITE; PS01047; HMA_1; 1.
DR   PROSITE; PS50846; HMA_2; 1.
DR   HOGENOMDNA; ACAM1_1.PE1760; -.
KW   copper-translocating P-type ATPase;
KW   ATP-binding; Complete proteome; Hydrolase; Nucleotide-binding;
KW   Phosphoprotein; Transmembrane.
SQ   SEQUENCE   794 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MTSLSPPPST QQVVLAVSGM KCAGCVQAVE KRLQQQPGVA TAVVNLVMEQ AAIEYVPQEI
     EPASLAQVLT IAGFPSHIQN REEEAEPLPP QPLKEIQPLV LATVLVVLSG VGHLGHIPGF
     TLPWLTSIQF HWGLATLALL GPGRPILQEG WQGLWQNRPN MNTLISLGSI TAYLASVVAV
     VWPQLYWDCF FDAPVMIVGL ILLGRALEAQ ARGRTKASLE KLLALQPMVA RWLPNPETQP
     DRTVDIPVRD VQIGAWLQVL PGDKFPVDGR VLEGSTLVDE AMLTGEAMPV PKASGDEVVA
     GTLNQSALIT IEATRTGQQT TLAQIIDLVE TAQTRKAPIQ QFADRVAGYF TYGVLAIATL
     TFLFWVGIGV HLWPDVLASG TLPMMHSPDV GMAEMAPRSA GILLGLKLAI AVLVIACPCA
     LGLATPTAIL VGTSLGAERG LLIRGGDVLE QVDRLDTLIF DKTGTLTTGH PQVTDYWVSE
     GLPALPVGDH LSSQTVLQLA ASLEKGSRHP LATAIVEQAD AQDLAYASAT ALETVPGCGI
     KGQLEGTFIR LGSAQWLQDC GIVIPPQDQH QGHHLAQAGK TLIHLATDQT YVGGVAVQDT
     LRSDAAQTLK DLKGLGLRIQ MLTGDQAETA HIVAQELGLD PTAVRAGVTP GDKAAVIADL
     QAQGHQVGMV GDGINDAPAL AQADVGISLS GGTDVAIETA QIILMSGDAN PLYRLVDVLR
     LSRATFRKIQ QNLFWALIYN LIGLPIAAGI LLPKFGILLS PASSAALMAF SSVSVVTNSL
     QLRRLSLQAK YSSH
//

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