(data stored in SCRATCH zone)

SWISSPROT: A1AZD9_PARDP

ID   A1AZD9_PARDP            Unreviewed;       807 AA.
AC   A1AZD9;
DT   23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT   23-JAN-2007, sequence version 1.
DT   08-MAY-2019, entry version 105.
DE   SubName: Full=Heavy metal translocating P-type ATPase {ECO:0000313|EMBL:ABL68633.1};
GN   OrderedLocusNames=Pden_0521 {ECO:0000313|EMBL:ABL68633.1};
OS   Paracoccus denitrificans (strain Pd 1222).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Paracoccus.
OX   NCBI_TaxID=318586 {ECO:0000313|EMBL:ABL68633.1, ECO:0000313|Proteomes:UP000000361};
RN   [1] {ECO:0000313|Proteomes:UP000000361}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pd 1222 {ECO:0000313|Proteomes:UP000000361};
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
RA   Pitluck S., Munk A.C., Brettin T., Bruce D., Han C., Tapia R.,
RA   Gilna P., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Lykidis A., Spiro S., Richardson D.J., Moir J.W.B., Ferguson S.J.,
RA   van Spanning R.J.M., Richardson P.;
RT   "Complete sequence of chromosome 1 of Paracoccus denitrificans
RT   PD1222.";
RL   Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Cell membrane
CC       {ECO:0000256|RuleBase:RU362081}.
CC   -!- SIMILARITY: Belongs to the cation transport ATPase (P-type)
CC       (TC 3.A.3) family. Type IB subfamily.
CC       {ECO:0000256|RuleBase:RU362081}.
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DR   EMBL; CP000489; ABL68633.1; -; Genomic_DNA.
DR   RefSeq; WP_011746866.1; NC_008686.1.
DR   STRING; 318586.Pden_0521; -.
DR   PRIDE; A1AZD9; -.
DR   EnsemblBacteria; ABL68633; ABL68633; Pden_0521.
DR   KEGG; pde:Pden_0521; -.
DR   eggNOG; ENOG4105C59; Bacteria.
DR   eggNOG; COG2217; LUCA.
DR   HOGENOM; HOG000250397; -.
DR   KO; K17686; -.
DR   OMA; KTGYEAR; -.
DR   BioCyc; PDEN318586:G1GW1-523-MONOMER; -.
DR   Proteomes; UP000000361; Chromosome 1.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-UniRule.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0019829; F:cation-transporting ATPase activity; IEA:InterPro.
DR   GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR   GO; GO:0030001; P:metal ion transport; IEA:InterPro.
DR   CDD; cd00371; HMA; 2.
DR   Gene3D; 3.40.1110.10; -; 1.
DR   Gene3D; 3.40.50.1000; -; 1.
DR   InterPro; IPR023299; ATPase_P-typ_cyto_dom_N.
DR   InterPro; IPR018303; ATPase_P-typ_P_site.
DR   InterPro; IPR023298; ATPase_P-typ_TM_dom_sf.
DR   InterPro; IPR008250; ATPase_P-typ_transduc_dom_A_sf.
DR   InterPro; IPR036412; HAD-like_sf.
DR   InterPro; IPR023214; HAD_sf.
DR   InterPro; IPR017969; Heavy-metal-associated_CS.
DR   InterPro; IPR006122; HMA_Cu_ion-bd.
DR   InterPro; IPR006121; HMA_dom.
DR   InterPro; IPR036163; HMA_dom_sf.
DR   InterPro; IPR027256; P-typ_ATPase_IB.
DR   InterPro; IPR001757; P_typ_ATPase.
DR   Pfam; PF00403; HMA; 2.
DR   SUPFAM; SSF55008; SSF55008; 2.
DR   SUPFAM; SSF56784; SSF56784; 1.
DR   SUPFAM; SSF81653; SSF81653; 1.
DR   SUPFAM; SSF81665; SSF81665; 1.
DR   TIGRFAMs; TIGR01525; ATPase-IB_hvy; 1.
DR   TIGRFAMs; TIGR01494; ATPase_P-type; 1.
DR   TIGRFAMs; TIGR00003; TIGR00003; 1.
DR   PROSITE; PS00154; ATPASE_E1_E2; 1.
DR   PROSITE; PS01047; HMA_1; 2.
DR   PROSITE; PS50846; HMA_2; 2.
PE   3: Inferred from homology;
DR   PRODOM; A1AZD9.
DR   SWISS-2DPAGE; A1AZD9.
KW   ATP-binding {ECO:0000256|RuleBase:RU362081};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000361};
KW   Membrane {ECO:0000256|RuleBase:RU362081};
KW   Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00280,
KW   ECO:0000256|RuleBase:RU362081};
KW   Nucleotide-binding {ECO:0000256|RuleBase:RU362081};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000361};
KW   Transmembrane {ECO:0000256|RuleBase:RU362081};
KW   Transmembrane helix {ECO:0000256|RuleBase:RU362081}.
FT   TRANSMEM    161    184       Helical. {ECO:0000256|RuleBase:RU362081}.
FT   TRANSMEM    196    221       Helical. {ECO:0000256|RuleBase:RU362081}.
FT   TRANSMEM    233    255       Helical. {ECO:0000256|RuleBase:RU362081}.
FT   TRANSMEM    261    281       Helical. {ECO:0000256|RuleBase:RU362081}.
FT   TRANSMEM    415    437       Helical. {ECO:0000256|RuleBase:RU362081}.
FT   TRANSMEM    443    464       Helical. {ECO:0000256|RuleBase:RU362081}.
FT   TRANSMEM    754    777       Helical. {ECO:0000256|RuleBase:RU362081}.
FT   TRANSMEM    783    801       Helical. {ECO:0000256|RuleBase:RU362081}.
FT   DOMAIN        7     72       HMA. {ECO:0000259|PROSITE:PS50846}.
FT   DOMAIN       74    139       HMA. {ECO:0000259|PROSITE:PS50846}.
FT   METAL        17     17       {ECO:0000256|PROSITE-ProRule:PRU00280}.
FT   METAL        20     20       {ECO:0000256|PROSITE-ProRule:PRU00280}.
FT   METAL        84     84       {ECO:0000256|PROSITE-ProRule:PRU00280}.
FT   METAL        87     87       {ECO:0000256|PROSITE-ProRule:PRU00280}.
SQ   SEQUENCE   807 AA;  82894 MW;  E95ED3F269461064 CRC64;
     MKHHQNDAEL TVTGMSCASC VGRVEKALAA VPGVEEPRVN LATGRAHFRL TAPEALPRAV
     EALAGAGYPA APLETRLSIE GMSCASCVGR VEKALAALPG VTSAQVNLTT ASATIHHSPG
     VAPQALADTV TAKGYPAELQ AEAGHHMHDH GGDAASMKRN FLVALVLTLP VFVAEMGGHA
     FPAFHHWLHM ALGQQTLWVL EFLLTTAVLA GPGRVFFRVG FPALMRRAPE MNSLVALGAS
     AAWLYSTVAT FAPGVLPADS VHVYFEAAAV IVTLILLGRW LEARAKGRAG NAIRRLIELA
     PDSAHVQRDG RIVEIPVAEL HPGDIVHLRP GERVAVDGVL TEGSGAIDES MLTGEPVPVA
     KQPGDTVTGG TVNGNAALAY RVTATGGNTV LARIIRMVED AQATKLPVQA LVDRITAVFV
     PVVIGLALLT FVLWMIFAGS LGQALVAAIS VLIIACPCAM GLAVPVSIMV GTGRGAELGV
     LFRRGDALQR LAEARIVALD KTGTLTQGAP ALTAIEAEDI EPLDALRLAA AAEARSEHPL
     AAAIVGAARD KGLDLPPAEA VQAAVGRGLS ARVEGRALLI GNAAALTEAG ITPSPALIAA
     AEGWAANGAT PVHLAVDGRH AAAMALADPI RPEAAETIAE LHTLGLQTAM ISGDVRATAE
     AVGRKLGIDT VTAGVLPEGK LAAIREMGGG TVFVGDGIND APALAAAETG IAIGTGTDVA
     IESAEVVLVG GDPMGVARAI RLSRSVMRNI RQNLFWAFGY NVALIPVAMG ALVPFGGPQM
     SPMLGAGAMA LSSVFVVSNA LRLRRAA
//

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