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Conserved domains on  [gi|1002265819|ref|XP_015637237|]
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heavy metal-associated isoprenylated plant protein 27 [Oryza sativa Japonica Group]

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

Gene Ontology:  GO:0046872
PubMed:  12594858|10404590|8091505|9437429

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 ...
 35-90 1.24e-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: 1.24e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1002265819  35 IDCEGCERKIKKALEDMKGVSSVEVTAKQNKVTVTGYVDAG-KVMRRVAYKTGKRVE 90
Cdd:cd00371     7 MTCAGCVSKIEKALEKLPGVESVEVDLETGKATVEYDPEVSpEELLEAIEDAGYKAR 63
 
Name Accession Description Interval E-value
HMA cd00371
Heavy-metal-associated domain (HMA) is a conserved domain of approximately 30 amino acid ...
 35-90 1.24e-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: 1.24e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1002265819  35 IDCEGCERKIKKALEDMKGVSSVEVTAKQNKVTVTGYVDAG-KVMRRVAYKTGKRVE 90
Cdd:cd00371     7 MTCAGCVSKIEKALEKLPGVESVEVDLETGKATVEYDPEVSpEELLEAIEDAGYKAR 63
CopZ COG2608
Copper chaperone CopZ [Inorganic ion transport and metabolism];
27-91 2.62e-08

Copper chaperone CopZ [Inorganic ion transport and metabolism];


Pssm-ID: 442020 [Multi-domain]  Cd Length: 71  Bit Score: 47.98  E-value: 2.62e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1002265819  27 QTVEMKVR-IDCEGCERKIKKALEDMKGVSSVEVTAKQNKVTVTG---YVDAGKVMRRVAyKTGKRVEP 91
Cdd:COG2608     2 KTVTLKVEgMTCGHCVARVEKALKALDGVASVEVDLATGTATVTYdpeKVSLEDIKAAIE-EAGYEVEK 69
HMA pfam00403
Heavy-metal-associated domain;
29-77 7.30e-08

Heavy-metal-associated domain;


Pssm-ID: 459804 [Multi-domain]  Cd Length: 58  Bit Score: 46.46  E-value: 7.30e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1002265819  29 VEMKVRIDCEGCERKIKKALEDMKGVSSVEVTAKQNKVTVTGYVDAGKV 77
Cdd:pfam00403   1 TFRVSGMHCGGCAAKVEKALSELPGVLSVSVDLATKTVTVTGDAESTKL 49
PLN02957 PLN02957
copper, zinc superoxide dismutase
 29-88 2.27e-04

copper, zinc superoxide dismutase


Pssm-ID: 215516 [Multi-domain]  Cd Length: 238  Bit Score: 39.73  E-value: 2.27e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002265819  29 VEMKvridCEGCERKIKKALEDMKGVSSVEVTAKQNKVTVTGyVDAGKVMRRVAYKTGKR 88
Cdd:PLN02957   12 VDMK----CEGCVAAVKNKLETLEGVKAVEVDLSNQVVRVLG-SSPVKAMTAALEQTGRK 66
 
Name Accession Description Interval E-value
HMA cd00371
Heavy-metal-associated domain (HMA) is a conserved domain of approximately 30 amino acid ...
 35-90 1.24e-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: 1.24e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1002265819  35 IDCEGCERKIKKALEDMKGVSSVEVTAKQNKVTVTGYVDAG-KVMRRVAYKTGKRVE 90
Cdd:cd00371     7 MTCAGCVSKIEKALEKLPGVESVEVDLETGKATVEYDPEVSpEELLEAIEDAGYKAR 63
CopZ COG2608
Copper chaperone CopZ [Inorganic ion transport and metabolism];
27-91 2.62e-08

Copper chaperone CopZ [Inorganic ion transport and metabolism];


Pssm-ID: 442020 [Multi-domain]  Cd Length: 71  Bit Score: 47.98  E-value: 2.62e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1002265819  27 QTVEMKVR-IDCEGCERKIKKALEDMKGVSSVEVTAKQNKVTVTG---YVDAGKVMRRVAyKTGKRVEP 91
Cdd:COG2608     2 KTVTLKVEgMTCGHCVARVEKALKALDGVASVEVDLATGTATVTYdpeKVSLEDIKAAIE-EAGYEVEK 69
HMA pfam00403
Heavy-metal-associated domain;
29-77 7.30e-08

Heavy-metal-associated domain;


Pssm-ID: 459804 [Multi-domain]  Cd Length: 58  Bit Score: 46.46  E-value: 7.30e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1002265819  29 VEMKVRIDCEGCERKIKKALEDMKGVSSVEVTAKQNKVTVTGYVDAGKV 77
Cdd:pfam00403   1 TFRVSGMHCGGCAAKVEKALSELPGVLSVSVDLATKTVTVTGDAESTKL 49
ZntA COG2217
Cation-transporting P-type ATPase [Inorganic ion transport and metabolism];
27-91 1.90e-04

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


Pssm-ID: 441819 [Multi-domain]  Cd Length: 717  Bit Score: 40.51  E-value: 1.90e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1002265819  27 QTVEMKVR-IDCEGCERKIKKALEDMKGVSSVEVTAKQNKVTVT---GYVDAGKVMRRVAyKTGKRVEP 91
Cdd:COG2217     1 ERVRLRIEgMTCAACAWLIEKALRKLPGVLSARVNLATERARVEydpGKVSLEELIAAVE-KAGYEAEP 68
PLN02957 PLN02957
copper, zinc superoxide dismutase
 29-88 2.27e-04

copper, zinc superoxide dismutase


Pssm-ID: 215516 [Multi-domain]  Cd Length: 238  Bit Score: 39.73  E-value: 2.27e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002265819  29 VEMKvridCEGCERKIKKALEDMKGVSSVEVTAKQNKVTVTGyVDAGKVMRRVAYKTGKR 88
Cdd:PLN02957   12 VDMK----CEGCVAAVKNKLETLEGVKAVEVDLSNQVVRVLG-SSPVKAMTAALEQTGRK 66
 
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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