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Conserved domains on  [gi|332010777|gb|AED98160|]
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Heavy metal transport/detoxification superfamily protein [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 ...
22-82 8.38e-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: 59.16  E-value: 8.38e-13
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 332010777  22 EIKVK-MDCEGCERRVRKSVEGMKGVSKVTVDPKQSKLTVEG--FVQPSKVVHRVmHRTGKKAE 82
Cdd:cd00371    1 ELSVEgMTCAGCVSKIEKALEKLPGVESVEVDLETGKATVEYdpEVSPEELLEAI-EDAGYKAR 63
 
Name Accession Description Interval E-value
HMA cd00371
Heavy-metal-associated domain (HMA) is a conserved domain of approximately 30 amino acid ...
22-82 8.38e-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: 59.16  E-value: 8.38e-13
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 332010777  22 EIKVK-MDCEGCERRVRKSVEGMKGVSKVTVDPKQSKLTVEG--FVQPSKVVHRVmHRTGKKAE 82
Cdd:cd00371    1 ELSVEgMTCAGCVSKIEKALEKLPGVESVEVDLETGKATVEYdpEVSPEELLEAI-EDAGYKAR 63
CopZ COG2608
Copper chaperone CopZ [Inorganic ion transport and metabolism];
19-62 5.78e-10

Copper chaperone CopZ [Inorganic ion transport and metabolism];


Pssm-ID: 442020 [Multi-domain]  Cd Length: 71  Bit Score: 52.21  E-value: 5.78e-10
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 332010777  19 QKVEIKVK-MDCEGCERRVRKSVEGMKGVSKVTVDPKQSKLTVEG 62
Cdd:COG2608    2 KTVTLKVEgMTCGHCVARVEKALKALDGVASVEVDLATGTATVTY 46
HMA pfam00403
Heavy-metal-associated domain;
27-62 4.61e-09

Heavy-metal-associated domain;


Pssm-ID: 459804 [Multi-domain]  Cd Length: 58  Bit Score: 49.54  E-value: 4.61e-09
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 332010777   27 MDCEGCERRVRKSVEGMKGVSKVTVDPKQSKLTVEG 62
Cdd:pfam00403   7 MHCGGCAAKVEKALSELPGVLSVSVDLATKTVTVTG 42
PLN02957 PLN02957
copper, zinc superoxide dismutase
22-83 3.10e-06

copper, zinc superoxide dismutase


Pssm-ID: 215516 [Multi-domain]  Cd Length: 238  Bit Score: 45.13  E-value: 3.10e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 332010777  22 EIKVKMDCEGCERRVRKSVEGMKGVSKVTVDPKQSKLTVEGfVQPSKVVHRVMHRTGKKAEL 83
Cdd:PLN02957   9 EFMVDMKCEGCVAAVKNKLETLEGVKAVEVDLSNQVVRVLG-SSPVKAMTAALEQTGRKARL 69
TIGR00003 TIGR00003
copper ion binding protein; This model describes an apparently copper-specific subfamily of ...
20-61 1.59e-03

copper ion binding protein; This model describes an apparently copper-specific subfamily of the metal-binding domain HMA (pfam00403). Closely related sequences outside this model include mercury resistance proteins and repeated domains of eukaryotic eukaryotic copper transport proteins. Members of this family are strictly prokaryotic. The model identifies both small proteins consisting of just this domain and N-terminal regions of cation (probably copper) transporting ATPases. [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 188014 [Multi-domain]  Cd Length: 66  Bit Score: 35.21  E-value: 1.59e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 332010777   20 KVEIKVK-MDCEGCERRVRKSVEGMKGVSKVTVDPKQSKLTVE 61
Cdd:TIGR00003   1 KQTFQVKgMSCNHCVDKIEKFVGEIEGVSKVKVQLEKEKVVVE 43
 
Name Accession Description Interval E-value
HMA cd00371
Heavy-metal-associated domain (HMA) is a conserved domain of approximately 30 amino acid ...
22-82 8.38e-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: 59.16  E-value: 8.38e-13
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 332010777  22 EIKVK-MDCEGCERRVRKSVEGMKGVSKVTVDPKQSKLTVEG--FVQPSKVVHRVmHRTGKKAE 82
Cdd:cd00371    1 ELSVEgMTCAGCVSKIEKALEKLPGVESVEVDLETGKATVEYdpEVSPEELLEAI-EDAGYKAR 63
CopZ COG2608
Copper chaperone CopZ [Inorganic ion transport and metabolism];
19-62 5.78e-10

Copper chaperone CopZ [Inorganic ion transport and metabolism];


Pssm-ID: 442020 [Multi-domain]  Cd Length: 71  Bit Score: 52.21  E-value: 5.78e-10
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 332010777  19 QKVEIKVK-MDCEGCERRVRKSVEGMKGVSKVTVDPKQSKLTVEG 62
Cdd:COG2608    2 KTVTLKVEgMTCGHCVARVEKALKALDGVASVEVDLATGTATVTY 46
HMA pfam00403
Heavy-metal-associated domain;
27-62 4.61e-09

Heavy-metal-associated domain;


Pssm-ID: 459804 [Multi-domain]  Cd Length: 58  Bit Score: 49.54  E-value: 4.61e-09
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 332010777   27 MDCEGCERRVRKSVEGMKGVSKVTVDPKQSKLTVEG 62
Cdd:pfam00403   7 MHCGGCAAKVEKALSELPGVLSVSVDLATKTVTVTG 42
PLN02957 PLN02957
copper, zinc superoxide dismutase
22-83 3.10e-06

copper, zinc superoxide dismutase


Pssm-ID: 215516 [Multi-domain]  Cd Length: 238  Bit Score: 45.13  E-value: 3.10e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 332010777  22 EIKVKMDCEGCERRVRKSVEGMKGVSKVTVDPKQSKLTVEGfVQPSKVVHRVMHRTGKKAEL 83
Cdd:PLN02957   9 EFMVDMKCEGCVAAVKNKLETLEGVKAVEVDLSNQVVRVLG-SSPVKAMTAALEQTGRKARL 69
ZntA COG2217
Cation-transporting P-type ATPase [Inorganic ion transport and metabolism];
19-83 7.02e-05

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


Pssm-ID: 441819 [Multi-domain]  Cd Length: 717  Bit Score: 41.28  E-value: 7.02e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 332010777  19 QKVEIKVK-MDCEGCERRVRKSVEGMKGVSKVTVDPKQSKLTVE---GFVQPSKVVHRVmHRTGKKAEL 83
Cdd:COG2217    1 ERVRLRIEgMTCAACAWLIEKALRKLPGVLSARVNLATERARVEydpGKVSLEELIAAV-EKAGYEAEP 68
TIGR00003 TIGR00003
copper ion binding protein; This model describes an apparently copper-specific subfamily of ...
20-61 1.59e-03

copper ion binding protein; This model describes an apparently copper-specific subfamily of the metal-binding domain HMA (pfam00403). Closely related sequences outside this model include mercury resistance proteins and repeated domains of eukaryotic eukaryotic copper transport proteins. Members of this family are strictly prokaryotic. The model identifies both small proteins consisting of just this domain and N-terminal regions of cation (probably copper) transporting ATPases. [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 188014 [Multi-domain]  Cd Length: 66  Bit Score: 35.21  E-value: 1.59e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 332010777   20 KVEIKVK-MDCEGCERRVRKSVEGMKGVSKVTVDPKQSKLTVE 61
Cdd:TIGR00003   1 KQTFQVKgMSCNHCVDKIEKFVGEIEGVSKVKVQLEKEKVVVE 43
 
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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