UniProt: Q3Z7X1

Database: UniProt
Entry: Q3Z7X1_DEHM1

LinkDB:  Q3Z7X1_DEHM1 
Original site:  Q3Z7X1_DEHM1

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Ontology (5)   
   GO (5)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (1)   
   KEGG GENES (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (16)   
   InterPro (11)   
   Pfam (3)   
   PROSITE (2)   
Literature (1)   
   PubMed (1)   
All databases (26)   

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ID   Q3Z7X1_DEHM1            Unreviewed;       828 AA.
AC   Q3Z7X1;
DT   27-SEP-2005, integrated into UniProtKB/TrEMBL.
DT   27-SEP-2005, sequence version 1.
DT   27-MAR-2024, entry version 132.
DE   SubName: Full=Copper-translocating P-type ATPase {ECO:0000313|EMBL:AAW39748.1};
DE            EC=3.6.3.4 {ECO:0000313|EMBL:AAW39748.1};
GN   OrderedLocusNames=DET0953 {ECO:0000313|EMBL:AAW39748.1};
OS   Dehalococcoides mccartyi (strain ATCC BAA-2266 / KCTC 15142 / 195)
OS   (Dehalococcoides ethenogenes (strain 195)).
OC   Bacteria; Chloroflexota; Dehalococcoidia; Dehalococcoidales;
OC   Dehalococcoidaceae; Dehalococcoides.
OX   NCBI_TaxID=243164 {ECO:0000313|EMBL:AAW39748.1, ECO:0000313|Proteomes:UP000008289};
RN   [1] {ECO:0000313|EMBL:AAW39748.1, ECO:0000313|Proteomes:UP000008289}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-2266 / KCTC 15142 / 195
RC   {ECO:0000313|Proteomes:UP000008289};
RX   PubMed=15637277; DOI=10.1126/science.1102226;
RA   Seshadri R., Adrian L., Fouts D.E., Eisen J.A., Phillippy A.M., Methe B.A.,
RA   Ward N.L., Nelson W.C., Deboy R.T., Khouri H.M., Kolonay J.F., Dodson R.J.,
RA   Daugherty S.C., Brinkac L.M., Sullivan S.A., Madupu R., Nelson K.E.,
RA   Kang K.H., Impraim M., Tran K., Robinson J.M., Forberger H.A., Fraser C.M.,
RA   Zinder S.H., Heidelberg J.F.;
RT   "Genome sequence of the PCE-dechlorinating bacterium Dehalococcoides
RT   ethenogenes.";
RL   Science 307:105-108(2005).
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|RuleBase:RU362081}.
CC   -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC       family. Type IB subfamily. {ECO:0000256|ARBA:ARBA00006024,
CC       ECO:0000256|RuleBase:RU362081}.
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DR   EMBL; CP000027; AAW39748.1; -; Genomic_DNA.
DR   RefSeq; WP_010936657.1; NC_002936.3.
DR   AlphaFoldDB; Q3Z7X1; -.
DR   STRING; 243164.DET0953; -.
DR   KEGG; det:DET0953; -.
DR   PATRIC; fig|243164.10.peg.904; -.
DR   eggNOG; COG2217; Bacteria.
DR   HOGENOM; CLU_001771_0_3_0; -.
DR   InParanoid; Q3Z7X1; -.
DR   Proteomes; UP000008289; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0019829; F:ATPase-coupled monoatomic cation transmembrane transporter activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   CDD; cd00371; HMA; 2.
DR   CDD; cd02094; P-type_ATPase_Cu-like; 1.
DR   Gene3D; 3.30.70.100; -; 2.
DR   Gene3D; 3.40.1110.10; Calcium-transporting ATPase, cytoplasmic domain N; 1.
DR   Gene3D; 2.70.150.10; Calcium-transporting ATPase, cytoplasmic transduction domain A; 1.
DR   Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 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; IPR006121; HMA_dom.
DR   InterPro; IPR036163; HMA_dom_sf.
DR   InterPro; IPR027256; P-typ_ATPase_IB.
DR   InterPro; IPR001757; P_typ_ATPase.
DR   InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR   NCBIfam; TIGR01511; ATPase-IB1_Cu; 1.
DR   NCBIfam; TIGR01525; ATPase-IB_hvy; 1.
DR   NCBIfam; TIGR01494; ATPase_P-type; 1.
DR   PANTHER; PTHR43520; ATP7, ISOFORM B; 1.
DR   PANTHER; PTHR43520:SF8; COPPER-TRANSPORTING ATPASE 2; 1.
DR   Pfam; PF00122; E1-E2_ATPase; 1.
DR   Pfam; PF00403; HMA; 2.
DR   Pfam; PF00702; Hydrolase; 1.
DR   PRINTS; PR00119; CATATPASE.
DR   PRINTS; PR00941; CDATPASE.
DR   SFLD; SFLDS00003; Haloacid_Dehalogenase; 1.
DR   SFLD; SFLDF00027; p-type_atpase; 1.
DR   SUPFAM; SSF81653; Calcium ATPase, transduction domain A; 1.
DR   SUPFAM; SSF81665; Calcium ATPase, transmembrane domain M; 1.
DR   SUPFAM; SSF56784; HAD-like; 1.
DR   SUPFAM; SSF55008; HMA, heavy metal-associated domain; 2.
DR   PROSITE; PS00154; ATPASE_E1_E2; 1.
DR   PROSITE; PS50846; HMA_2; 2.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|RuleBase:RU362081};
KW   Cell membrane {ECO:0000256|RuleBase:RU362081};
KW   Hydrolase {ECO:0000313|EMBL:AAW39748.1};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU362081};
KW   Metal-binding {ECO:0000256|RuleBase:RU362081};
KW   Nucleotide-binding {ECO:0000256|RuleBase:RU362081};
KW   Translocase {ECO:0000256|ARBA:ARBA00022967};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW   ECO:0000256|RuleBase:RU362081};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|RuleBase:RU362081}.
FT   TRANSMEM        168..186
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        192..210
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        222..245
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        257..276
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        410..432
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        438..461
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        753..773
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        793..811
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   DOMAIN          11..77
FT                   /note="HMA"
FT                   /evidence="ECO:0000259|PROSITE:PS50846"
FT   DOMAIN          79..144
FT                   /note="HMA"
FT                   /evidence="ECO:0000259|PROSITE:PS50846"
SQ   SEQUENCE   828 AA;  89075 MW;  7161EE7B6D4E198F CRC64;
     MPEKNLPDTL PKIIMGISGM SCTRCAASIE ARLSKTDGIT DPKLNFASAK LIFSYDPAVI
     SLADIKSIIS GLGYGVISRK SIFPIKGLHC ASCVARAEKA LKNTNGVLSA SVNLANQTAN
     VEYLDFISYR ELSQAIKNTG YELLSEETPQ NELNSSENAE TRKLQQELTV ALVLGISLMI
     IGFLPAFGGK EFIMFLLATP VQFWAGLRFY RGAFAALKNR TSDMNTLIAL GTSAAYLYSL
     TALVFPSIFD SPLLEKHLYF DTSAMIIALI LTGRFLEARA KGRTSDAIRR LVGLQPSTAS
     IIRDGKEILV GISEVVAGDK IVIRPGERLP VDGLILEGYS SLDESMVTGE SIPAEKKAGD
     YVIGGTFNQT GAFTYEAQKV GADTALARII RLVEEAQGSK APIQRLADKI ASVFVPAVIS
     IAILTFVFWL VFGPEPSFTY AALNMIAVLV IACPCALGLA TPTALIVGMG KGAENGILIR
     SAVALEKMHK LDTIVLDKTG TLTRGKPVLS NLVSHTMDKD SFLTLVASAE QFSEHPLAKA
     VVKEAARKKL KITSSSEFSA LPGAGLKATV SGKQILIGNA NLMQSNRISL AEYQSEADKL
     WEAGENLIFV AADGKLEGMV AVRDILKRES QAVVAELKAN KLRTIMLTGD NQRAAKRIAD
     ELGLDQYISE VKPEDKSRLV QELQDQGHFV AMVGDGINDA PALAKADVGI AIGTGTDIAM
     ETGDITLISG DLFGLTKAIV LSKATFNTIR QNLFWAFFYN IILIPVAAGV LYLFLSHSGV
     PQSLHFFLGE YGFLNPILAA LAMAVSSLTV VSNSLRLRRV KLNTYLKQ
//

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