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Conserved domains on  [gi|18418230|ref|NP_567924|]
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P-type ATP-ase 1 [Arabidopsis thaliana]

Protein Classification

heavy-metal-associated domain-containing protein( domain architecture ID 10086127)

heavy-metal-associated domain-containing protein such as heavy metal-associated isoprenylated plant proteins and Saccharomyces cerevisiae copper transport protein ATX1, which shuttles copper to the transport ATPase CCC2 and protects against oxygen toxicity

CATH:  3.30.70.100
Gene Ontology:  GO:0046872
PubMed:  12443926|8905098
SCOP:  4001253

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
HMA cd00371
Heavy-metal-associated domain (HMA) is a conserved domain of approximately 30 amino acid ...
 152-207 2.44e-13

Heavy-metal-associated domain (HMA) is a conserved domain of approximately 30 amino acid residues found in a number of proteins that transport or detoxify heavy metals, for example, the CPx-type heavy metal ATPases and copper chaperones. HMA domain contains two cysteine residues that are important in binding and transfer of metal ions, such as copper, cadmium, cobalt and zinc. In the case of copper, stoichiometry of binding is one Cu+ ion per binding domain. Repeats of the HMA domain in copper chaperone has been associated with Menkes/Wilson disease due to binding of multiple copper ions.


:

Pssm-ID: 238219 [Multi-domain]  Cd Length: 63  Bit Score: 62.62  E-value: 2.44e-13
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 18418230 152 LDVGGMTCGGCSASVKKILESQPQVASASVNLTTETAIVWPVPE--AKSVPDWQKSLG 207
Cdd:cd00371   2 LSVEGMTCAGCVSKIEKALEKLPGVESVEVDLETGKATVEYDPEvsPEELLEAIEDAG 59
 
Name Accession Description Interval E-value
HMA cd00371
Heavy-metal-associated domain (HMA) is a conserved domain of approximately 30 amino acid ...
 152-207 2.44e-13

Heavy-metal-associated domain (HMA) is a conserved domain of approximately 30 amino acid residues found in a number of proteins that transport or detoxify heavy metals, for example, the CPx-type heavy metal ATPases and copper chaperones. HMA domain contains two cysteine residues that are important in binding and transfer of metal ions, such as copper, cadmium, cobalt and zinc. In the case of copper, stoichiometry of binding is one Cu+ ion per binding domain. Repeats of the HMA domain in copper chaperone has been associated with Menkes/Wilson disease due to binding of multiple copper ions.


Pssm-ID: 238219 [Multi-domain]  Cd Length: 63  Bit Score: 62.62  E-value: 2.44e-13
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 18418230 152 LDVGGMTCGGCSASVKKILESQPQVASASVNLTTETAIVWPVPE--AKSVPDWQKSLG 207
Cdd:cd00371   2 LSVEGMTCAGCVSKIEKALEKLPGVESVEVDLETGKATVEYDPEvsPEELLEAIEDAG 59
CopZ COG2608
Copper chaperone CopZ [Inorganic ion transport and metabolism];
150-190 1.46e-11

Copper chaperone CopZ [Inorganic ion transport and metabolism];


Pssm-ID: 442020 [Multi-domain]  Cd Length: 71  Bit Score: 58.38  E-value: 1.46e-11
                        10        20        30        40
                ....*....|....*....|....*....|....*....|.
gi 18418230 150 IILDVGGMTCGGCSASVKKILESQPQVASASVNLTTETAIV 190
Cdd:COG2608   4 VTLKVEGMTCGHCVARVEKALKALDGVASVEVDLATGTATV 44
HMA pfam00403
Heavy-metal-associated domain;
151-206 5.16e-09

Heavy-metal-associated domain;


Pssm-ID: 459804 [Multi-domain]  Cd Length: 58  Bit Score: 51.08  E-value: 5.16e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 18418230   151 ILDVGGMTCGGCSASVKKILESQPQVASASVNLTTETAIVWPVPEAKSVPDWQKSL 206
Cdd:pfam00403   1 TFRVSGMHCGGCAAKVEKALSELPGVLSVSVDLATKTVTVTGDAESTKLEKLVEAI 56
PRK13748 PRK13748
putative mercuric reductase; Provisional
 150-190 3.23e-04

putative mercuric reductase; Provisional


Pssm-ID: 184298 [Multi-domain]  Cd Length: 561  Bit Score: 41.29  E-value: 3.23e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 18418230  150 IILDVGGMTCGGCSASVKKILESQPQVASASVNLTTETAIV 190
Cdd:PRK13748   2 TTLKITGMTCDSCAAHVKDALEKVPGVQSADVSYPKGSAQL 42
 
Name Accession Description Interval E-value
HMA cd00371
Heavy-metal-associated domain (HMA) is a conserved domain of approximately 30 amino acid ...
 152-207 2.44e-13

Heavy-metal-associated domain (HMA) is a conserved domain of approximately 30 amino acid residues found in a number of proteins that transport or detoxify heavy metals, for example, the CPx-type heavy metal ATPases and copper chaperones. HMA domain contains two cysteine residues that are important in binding and transfer of metal ions, such as copper, cadmium, cobalt and zinc. In the case of copper, stoichiometry of binding is one Cu+ ion per binding domain. Repeats of the HMA domain in copper chaperone has been associated with Menkes/Wilson disease due to binding of multiple copper ions.


Pssm-ID: 238219 [Multi-domain]  Cd Length: 63  Bit Score: 62.62  E-value: 2.44e-13
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 18418230 152 LDVGGMTCGGCSASVKKILESQPQVASASVNLTTETAIVWPVPE--AKSVPDWQKSLG 207
Cdd:cd00371   2 LSVEGMTCAGCVSKIEKALEKLPGVESVEVDLETGKATVEYDPEvsPEELLEAIEDAG 59
CopZ COG2608
Copper chaperone CopZ [Inorganic ion transport and metabolism];
150-190 1.46e-11

Copper chaperone CopZ [Inorganic ion transport and metabolism];


Pssm-ID: 442020 [Multi-domain]  Cd Length: 71  Bit Score: 58.38  E-value: 1.46e-11
                        10        20        30        40
                ....*....|....*....|....*....|....*....|.
gi 18418230 150 IILDVGGMTCGGCSASVKKILESQPQVASASVNLTTETAIV 190
Cdd:COG2608   4 VTLKVEGMTCGHCVARVEKALKALDGVASVEVDLATGTATV 44
ZntA COG2217
Cation-transporting P-type ATPase [Inorganic ion transport and metabolism];
150-226 1.02e-09

Cation-transporting P-type ATPase [Inorganic ion transport and metabolism];


Pssm-ID: 441819 [Multi-domain]  Cd Length: 717  Bit Score: 57.85  E-value: 1.02e-09
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 18418230 150 IILDVGGMTCGGCSASVKKILESQPQVASASVNLTTETAIVWPVPEAKSVpdwqkslgETLANHLTNCGFQSTPRGE 226
Cdd:COG2217   3 VRLRIEGMTCAACAWLIEKALRKLPGVLSARVNLATERARVEYDPGKVSL--------EELIAAVEKAGYEAEPADA 71
HMA pfam00403
Heavy-metal-associated domain;
151-206 5.16e-09

Heavy-metal-associated domain;


Pssm-ID: 459804 [Multi-domain]  Cd Length: 58  Bit Score: 51.08  E-value: 5.16e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 18418230   151 ILDVGGMTCGGCSASVKKILESQPQVASASVNLTTETAIVWPVPEAKSVPDWQKSL 206
Cdd:pfam00403   1 TFRVSGMHCGGCAAKVEKALSELPGVLSVSVDLATKTVTVTGDAESTKLEKLVEAI 56
PRK13748 PRK13748
putative mercuric reductase; Provisional
 150-190 3.23e-04

putative mercuric reductase; Provisional


Pssm-ID: 184298 [Multi-domain]  Cd Length: 561  Bit Score: 41.29  E-value: 3.23e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 18418230  150 IILDVGGMTCGGCSASVKKILESQPQVASASVNLTTETAIV 190
Cdd:PRK13748   2 TTLKITGMTCDSCAAHVKDALEKVPGVQSADVSYPKGSAQL 42
copA PRK10671
copper-exporting P-type ATPase CopA;
146-190 2.77e-03

copper-exporting P-type ATPase CopA;


Pssm-ID: 182635 [Multi-domain]  Cd Length: 834  Bit Score: 38.57  E-value: 2.77e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 18418230  146 SSDIIILDVGGMTCGGCSASVKKILESQPQVASASVNLTTETAIV 190
Cdd:PRK10671  97 DDDSQQLLLSGMSCASCVSRVQNALQSVPGVTQARVNLAERTALV 141
copA PRK10671
copper-exporting P-type ATPase CopA;
147-184 3.44e-03

copper-exporting P-type ATPase CopA;


Pssm-ID: 182635 [Multi-domain]  Cd Length: 834  Bit Score: 38.18  E-value: 3.44e-03
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 18418230  147 SDIIILDVGGMTCGGCSASVKKILESQPQVASASVNLT 184
Cdd:PRK10671   2 SQTIDLTLDGLSCGHCVKRVKESLEQRPDVEQADVSIT 39
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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