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Conserved domains on  [gi|1063685749|ref|NP_001323007|]
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Heavy metal transport/detoxification superfamily protein [Arabidopsis thaliana]

Protein Classification

heavy-metal-associated domain-containing protein( domain architecture ID 10449815)

heavy-metal-associated domain-containing protein may function as a heavy metal transporter and/or detoxification protein; such as heavy metal-associated isoprenylated plant proteins

Gene Ontology:  GO:0046872
PubMed:  12443926|8905098

Graphical summary

 Zoom to residue level

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List of domain hits

 Name Accession Description Interval E-value
HMA pfam00403
Heavy-metal-associated domain;
79-130 9.08e-11

Heavy-metal-associated domain;


:

Pssm-ID: 459804 [Multi-domain]  Cd Length: 58  Bit Score: 56.86  E-value: 9.08e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1063685749  79 VNIHCEGCNKKVKKLLQRIEGVCHVKIEAEHQKVTVSGSVDSaTLINKLVKA 130
Cdd:pfam00403   5 SGMHCGGCAAKVEKALSELPGVLSVSVDLATKTVTVTGDAES-TKLEKLVEA 55
 
Name Accession Description Interval E-value
HMA pfam00403
Heavy-metal-associated domain;
79-130 9.08e-11

Heavy-metal-associated domain;


Pssm-ID: 459804 [Multi-domain]  Cd Length: 58  Bit Score: 56.86  E-value: 9.08e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1063685749  79 VNIHCEGCNKKVKKLLQRIEGVCHVKIEAEHQKVTVSGSVDSaTLINKLVKA 130
Cdd:pfam00403   5 SGMHCGGCAAKVEKALSELPGVLSVSVDLATKTVTVTGDAES-TKLEKLVEA 55
CopZ COG2608
Copper chaperone CopZ [Inorganic ion transport and metabolism];
72-135 2.90e-09

Copper chaperone CopZ [Inorganic ion transport and metabolism];


Pssm-ID: 442020 [Multi-domain]  Cd Length: 71  Bit Score: 52.98  E-value: 2.90e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1063685749  72 IQTFSLRV-NIHCEGCNKKVKKLLQRIEGVCHVKIEAEHQKVTVSGS---VDSATLINKLVKAGKHAE 135
Cdd:COG2608     1 MKTVTLKVeGMTCGHCVARVEKALKALDGVASVEVDLATGTATVTYDpekVSLEDIKAAIEEAGYEVE 68
HMA cd00371
Heavy-metal-associated domain (HMA) is a conserved domain of approximately 30 amino acid ...
 77-135 8.33e-09

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: 51.45  E-value: 8.33e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1063685749  77 LRV-NIHCEGCNKKVKKLLQRIEGVCHVKIEAEHQKVTVSG--SVDSATLINKLVKAGKHAE 135
Cdd:cd00371     2 LSVeGMTCAGCVSKIEKALEKLPGVESVEVDLETGKATVEYdpEVSPEELLEAIEDAGYKAR 63
PLN02957 PLN02957
copper, zinc superoxide dismutase
 79-136 1.90e-05

copper, zinc superoxide dismutase


Pssm-ID: 215516 [Multi-domain]  Cd Length: 238  Bit Score: 45.90  E-value: 1.90e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1063685749  79 VNIHCEGCNKKVKKLLQRIEGVCHVKIEAEHQKVTVSGSVDSATLINKLVKAGKHAEL 136
Cdd:PLN02957   12 VDMKCEGCVAAVKNKLETLEGVKAVEVDLSNQVVRVLGSSPVKAMTAALEQTGRKARL 69
TIGR00003 TIGR00003
copper ion binding protein; This model describes an apparently copper-specific subfamily of ...
 73-122 1.60e-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: 36.75  E-value: 1.60e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1063685749  73 QTFSLRvNIHCEGCNKKVKKLLQRIEGVCHVKIEAEHQKVTVSGSVDSAT 122
Cdd:TIGR00003   2 QTFQVK-GMSCNHCVDKIEKFVGEIEGVSKVKVQLEKEKVVVEFDAPNVS 50
 
Name Accession Description Interval E-value
HMA pfam00403
Heavy-metal-associated domain;
79-130 9.08e-11

Heavy-metal-associated domain;


Pssm-ID: 459804 [Multi-domain]  Cd Length: 58  Bit Score: 56.86  E-value: 9.08e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1063685749  79 VNIHCEGCNKKVKKLLQRIEGVCHVKIEAEHQKVTVSGSVDSaTLINKLVKA 130
Cdd:pfam00403   5 SGMHCGGCAAKVEKALSELPGVLSVSVDLATKTVTVTGDAES-TKLEKLVEA 55
CopZ COG2608
Copper chaperone CopZ [Inorganic ion transport and metabolism];
72-135 2.90e-09

Copper chaperone CopZ [Inorganic ion transport and metabolism];


Pssm-ID: 442020 [Multi-domain]  Cd Length: 71  Bit Score: 52.98  E-value: 2.90e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1063685749  72 IQTFSLRV-NIHCEGCNKKVKKLLQRIEGVCHVKIEAEHQKVTVSGS---VDSATLINKLVKAGKHAE 135
Cdd:COG2608     1 MKTVTLKVeGMTCGHCVARVEKALKALDGVASVEVDLATGTATVTYDpekVSLEDIKAAIEEAGYEVE 68
HMA cd00371
Heavy-metal-associated domain (HMA) is a conserved domain of approximately 30 amino acid ...
 77-135 8.33e-09

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: 51.45  E-value: 8.33e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1063685749  77 LRV-NIHCEGCNKKVKKLLQRIEGVCHVKIEAEHQKVTVSG--SVDSATLINKLVKAGKHAE 135
Cdd:cd00371     2 LSVeGMTCAGCVSKIEKALEKLPGVESVEVDLETGKATVEYdpEVSPEELLEAIEDAGYKAR 63
ZntA COG2217
Cation-transporting P-type ATPase [Inorganic ion transport and metabolism];
73-158 7.06e-06

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


Pssm-ID: 441819 [Multi-domain]  Cd Length: 717  Bit Score: 48.22  E-value: 7.06e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063685749  73 QTFSLRV-NIHCEGCNKKVKKLLQRIEGVCHVKIEAEHQKVTVS---GSVDSATLINKLVKAGKHAELWSPNPNQNQPQK 148
Cdd:COG2217     1 ERVRLRIeGMTCAACAWLIEKALRKLPGVLSARVNLATERARVEydpGKVSLEELIAAVEKAGYEAEPADADAAAEEARE 80

                          90
                  ....*....|
gi 1063685749 149 PKTNDFIKNV 158
Cdd:COG2217    81 KELRDLLRRL 90
PLN02957 PLN02957
copper, zinc superoxide dismutase
 79-136 1.90e-05

copper, zinc superoxide dismutase


Pssm-ID: 215516 [Multi-domain]  Cd Length: 238  Bit Score: 45.90  E-value: 1.90e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1063685749  79 VNIHCEGCNKKVKKLLQRIEGVCHVKIEAEHQKVTVSGSVDSATLINKLVKAGKHAEL 136
Cdd:PLN02957   12 VDMKCEGCVAAVKNKLETLEGVKAVEVDLSNQVVRVLGSSPVKAMTAALEQTGRKARL 69
copA PRK10671
copper-exporting P-type ATPase CopA;
83-142 1.32e-04

copper-exporting P-type ATPase CopA;


Pssm-ID: 182635 [Multi-domain]  Cd Length: 834  Bit Score: 44.35  E-value: 1.32e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063685749  83 CEGCNKKVKKLLQRIEGVCHVKIEAEHQKVTvsGSVDSATLINKLVKAGKHAELWSPNPN 142
Cdd:PRK10671   14 CGHCVKRVKESLEQRPDVEQADVSITEAHVT--GTASAEALIETIKQAGYDASVSHPKAK 71
copA PRK10671
copper-exporting P-type ATPase CopA;
83-136 4.59e-04

copper-exporting P-type ATPase CopA;


Pssm-ID: 182635 [Multi-domain]  Cd Length: 834  Bit Score: 42.42  E-value: 4.59e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1063685749  83 CEGCNKKVKKLLQRIEGVCHVKIEAEHQKVTVSGSVDSATLINKLVKAGKHAEL 136
Cdd:PRK10671  110 CASCVSRVQNALQSVPGVTQARVNLAERTALVMGSASPQDLVQAVEKAGYGAEA 163
TIGR00003 TIGR00003
copper ion binding protein; This model describes an apparently copper-specific subfamily of ...
 73-122 1.60e-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: 36.75  E-value: 1.60e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1063685749  73 QTFSLRvNIHCEGCNKKVKKLLQRIEGVCHVKIEAEHQKVTVSGSVDSAT 122
Cdd:TIGR00003   2 QTFQVK-GMSCNHCVDKIEKFVGEIEGVSKVKVQLEKEKVVVEFDAPNVS 50
 
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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