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Conserved domains on  [gi|14532548|gb|AAK64002|]
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At1g66240/T6J19_6 [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 ...
 36-93 2.77e-15

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: 64.16  E-value: 2.77e-15
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 14532548  36 VLRVA-MTCEGCVGAVKRVLGKMEGVESFDVDIKEQKVTVKGN--VQPDAVLQTVTKTGKK 93
Cdd:cd00371   1 ELSVEgMTCAGCVSKIEKALEKLPGVESVEVDLETGKATVEYDpeVSPEELLEAIEDAGYK 61
 
Name Accession Description Interval E-value
HMA cd00371
Heavy-metal-associated domain (HMA) is a conserved domain of approximately 30 amino acid ...
 36-93 2.77e-15

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: 64.16  E-value: 2.77e-15
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 14532548  36 VLRVA-MTCEGCVGAVKRVLGKMEGVESFDVDIKEQKVTVKGN--VQPDAVLQTVTKTGKK 93
Cdd:cd00371   1 ELSVEgMTCAGCVSKIEKALEKLPGVESVEVDLETGKATVEYDpeVSPEELLEAIEDAGYK 61
CopZ COG2608
Copper chaperone CopZ [Inorganic ion transport and metabolism];
32-91 7.80e-11

Copper chaperone CopZ [Inorganic ion transport and metabolism];


Pssm-ID: 442020 [Multi-domain]  Cd Length: 71  Bit Score: 53.37  E-value: 7.80e-11
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 14532548  32 SQTVVLRVA-MTCEGCVGAVKRVLGKMEGVESFDVDIKEQKVTVKGN---VQPDAVLQTVTKTG 91
Cdd:COG2608   1 MKTVTLKVEgMTCGHCVARVEKALKALDGVASVEVDLATGTATVTYDpekVSLEDIKAAIEEAG 64
PLN02957 PLN02957
copper, zinc superoxide dismutase
 39-93 4.22e-09

copper, zinc superoxide dismutase


Pssm-ID: 215516 [Multi-domain]  Cd Length: 238  Bit Score: 51.68  E-value: 4.22e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 14532548   39 VAMTCEGCVGAVKRVLGKMEGVESFDVDIKEQKVTVKGNVQPDAVLQTVTKTGKK 93
Cdd:PLN02957  12 VDMKCEGCVAAVKNKLETLEGVKAVEVDLSNQVVRVLGSSPVKAMTAALEQTGRK 66
HMA pfam00403
Heavy-metal-associated domain;
41-83 1.29e-08

Heavy-metal-associated domain;


Pssm-ID: 459804 [Multi-domain]  Cd Length: 58  Bit Score: 47.23  E-value: 1.29e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 14532548    41 MTCEGCVGAVKRVLGKMEGVESFDVDIKEQKVTVKGNVQPDAV 83
Cdd:pfam00403   7 MHCGGCAAKVEKALSELPGVLSVSVDLATKTVTVTGDAESTKL 49
TIGR00003 TIGR00003
copper ion binding protein; This model describes an apparently copper-specific subfamily of ...
 41-91 5.69e-04

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: 35.59  E-value: 5.69e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 14532548    41 MTCEGCVGAVKRVLGKMEGVESFDVDIKEQKVTVK---GNVQPDAVLQTVTKTG 91
Cdd:TIGR00003   9 MSCNHCVDKIEKFVGEIEGVSKVKVQLEKEKVVVEfdaPNVSATEICEAILDAG 62
UxxU_metal_bind NF041115
metal-binding (seleno)protein; Known members of this family are selenoproteins with an ...
 30-83 8.04e-03

metal-binding (seleno)protein; Known members of this family are selenoproteins with an exceptional UXXU motif, with two selenocysteines. Known members so far derive primarily from MAGs, and have an N-terminal signal peptide N-terminal to the region represented in the seed alignment. Note that this model represents a specific clade of a more widely distributed domain that frequently appears 3 or 4 times in a single protein, so the domain-specific cutoff is critical to identification. Homologous domains, outside the scope of this model, are found in CopZ family copper chaperones and heavy metal-translocating P-type ATPases.


Pssm-ID: 469038 [Multi-domain]  Cd Length: 74  Bit Score: 32.69  E-value: 8.04e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 14532548   30 AMSQTVVLRV-AMTCEGCVGAVKRVLGKMEGVESFDVDIKEQKVTVKgnVQPDAV 83
Cdd:NF041115   1 ALAETVILAIeGMTUASUPLIAKKALEGLEGVEKADVSYKEGRAEVA--FDPDKV 53
 
Name Accession Description Interval E-value
HMA cd00371
Heavy-metal-associated domain (HMA) is a conserved domain of approximately 30 amino acid ...
 36-93 2.77e-15

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: 64.16  E-value: 2.77e-15
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 14532548  36 VLRVA-MTCEGCVGAVKRVLGKMEGVESFDVDIKEQKVTVKGN--VQPDAVLQTVTKTGKK 93
Cdd:cd00371   1 ELSVEgMTCAGCVSKIEKALEKLPGVESVEVDLETGKATVEYDpeVSPEELLEAIEDAGYK 61
CopZ COG2608
Copper chaperone CopZ [Inorganic ion transport and metabolism];
32-91 7.80e-11

Copper chaperone CopZ [Inorganic ion transport and metabolism];


Pssm-ID: 442020 [Multi-domain]  Cd Length: 71  Bit Score: 53.37  E-value: 7.80e-11
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 14532548  32 SQTVVLRVA-MTCEGCVGAVKRVLGKMEGVESFDVDIKEQKVTVKGN---VQPDAVLQTVTKTG 91
Cdd:COG2608   1 MKTVTLKVEgMTCGHCVARVEKALKALDGVASVEVDLATGTATVTYDpekVSLEDIKAAIEEAG 64
PLN02957 PLN02957
copper, zinc superoxide dismutase
 39-93 4.22e-09

copper, zinc superoxide dismutase


Pssm-ID: 215516 [Multi-domain]  Cd Length: 238  Bit Score: 51.68  E-value: 4.22e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 14532548   39 VAMTCEGCVGAVKRVLGKMEGVESFDVDIKEQKVTVKGNVQPDAVLQTVTKTGKK 93
Cdd:PLN02957  12 VDMKCEGCVAAVKNKLETLEGVKAVEVDLSNQVVRVLGSSPVKAMTAALEQTGRK 66
HMA pfam00403
Heavy-metal-associated domain;
41-83 1.29e-08

Heavy-metal-associated domain;


Pssm-ID: 459804 [Multi-domain]  Cd Length: 58  Bit Score: 47.23  E-value: 1.29e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 14532548    41 MTCEGCVGAVKRVLGKMEGVESFDVDIKEQKVTVKGNVQPDAV 83
Cdd:pfam00403   7 MHCGGCAAKVEKALSELPGVLSVSVDLATKTVTVTGDAESTKL 49
copA PRK10671
copper-exporting P-type ATPase CopA;
31-106 4.38e-07

copper-exporting P-type ATPase CopA;


Pssm-ID: 182635 [Multi-domain]  Cd Length: 834  Bit Score: 46.27  E-value: 4.38e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 14532548   31 MSQTVVLRV-AMTCEGCVGAVKRVLGKMEGVESFDVDIKEQKVTvkGNVQPDAVLQTVTKTGkktafWEAEGETAKA 106
Cdd:PRK10671   1 MSQTIDLTLdGLSCGHCVKRVKESLEQRPDVEQADVSITEAHVT--GTASAEALIETIKQAG-----YDASVSHPKA 70
ZntA COG2217
Cation-transporting P-type ATPase [Inorganic ion transport and metabolism];
33-106 1.03e-06

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


Pssm-ID: 441819 [Multi-domain]  Cd Length: 717  Bit Score: 45.13  E-value: 1.03e-06
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 14532548  33 QTVVLRV-AMTCEGCVGAVKRVLGKMEGVESFDVDIKEQKVTV---KGNVQPDAVLQTVTKTGKKTAFWEAEGETAKA 106
Cdd:COG2217   1 ERVRLRIeGMTCAACAWLIEKALRKLPGVLSARVNLATERARVeydPGKVSLEELIAAVEKAGYEAEPADADAAAEEA 78
copA PRK10671
copper-exporting P-type ATPase CopA;
41-91 5.82e-05

copper-exporting P-type ATPase CopA;


Pssm-ID: 182635 [Multi-domain]  Cd Length: 834  Bit Score: 40.49  E-value: 5.82e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 14532548   41 MTCEGCVGAVKRVLGKMEGVESFDVDIKEQKVTVKGNVQPDAVLQTVTKTG 91
Cdd:PRK10671 108 MSCASCVSRVQNALQSVPGVTQARVNLAERTALVMGSASPQDLVQAVEKAG 158
PRK13748 PRK13748
putative mercuric reductase; Provisional
 41-106 3.25e-04

putative mercuric reductase; Provisional


Pssm-ID: 184298 [Multi-domain]  Cd Length: 561  Bit Score: 38.21  E-value: 3.25e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 14532548   41 MTCEGCVGAVKRVLGKMEGVESFDVDIKEQK--VTVKGNVQPDAVLQTVTKTGKKTAFWEAEGETAKA 106
Cdd:PRK13748   9 MTCDSCAAHVKDALEKVPGVQSADVSYPKGSaqLAIEVGTSPDALTAAVAGLGYRATLADAPPTDNRG 76
TIGR00003 TIGR00003
copper ion binding protein; This model describes an apparently copper-specific subfamily of ...
 41-91 5.69e-04

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: 35.59  E-value: 5.69e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 14532548    41 MTCEGCVGAVKRVLGKMEGVESFDVDIKEQKVTVK---GNVQPDAVLQTVTKTG 91
Cdd:TIGR00003   9 MSCNHCVDKIEKFVGEIEGVSKVKVQLEKEKVVVEfdaPNVSATEICEAILDAG 62
UxxU_metal_bind NF041115
metal-binding (seleno)protein; Known members of this family are selenoproteins with an ...
 30-83 8.04e-03

metal-binding (seleno)protein; Known members of this family are selenoproteins with an exceptional UXXU motif, with two selenocysteines. Known members so far derive primarily from MAGs, and have an N-terminal signal peptide N-terminal to the region represented in the seed alignment. Note that this model represents a specific clade of a more widely distributed domain that frequently appears 3 or 4 times in a single protein, so the domain-specific cutoff is critical to identification. Homologous domains, outside the scope of this model, are found in CopZ family copper chaperones and heavy metal-translocating P-type ATPases.


Pssm-ID: 469038 [Multi-domain]  Cd Length: 74  Bit Score: 32.69  E-value: 8.04e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 14532548   30 AMSQTVVLRV-AMTCEGCVGAVKRVLGKMEGVESFDVDIKEQKVTVKgnVQPDAV 83
Cdd:NF041115   1 ALAETVILAIeGMTUASUPLIAKKALEGLEGVEKADVSYKEGRAEVA--FDPDKV 53
 
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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