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Conserved domains on  [gi|18404191|ref|NP_566747|]
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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 ...
 77-130 9.25e-11

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: 53.76  E-value: 9.25e-11
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 18404191  77 ELKVS-MHCYGCAKKVEKHISKLDGVTWYKVELESKKVVVKGNIL--PVDVLESICK 130
Cdd:cd00371   1 ELSVEgMTCAGCVSKIEKALEKLPGVESVEVDLETGKATVEYDPEvsPEELLEAIED 57
 
Name Accession Description Interval E-value
HMA cd00371
Heavy-metal-associated domain (HMA) is a conserved domain of approximately 30 amino acid ...
 77-130 9.25e-11

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: 53.76  E-value: 9.25e-11
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 18404191  77 ELKVS-MHCYGCAKKVEKHISKLDGVTWYKVELESKKVVVKGNIL--PVDVLESICK 130
Cdd:cd00371   1 ELSVEgMTCAGCVSKIEKALEKLPGVESVEVDLETGKATVEYDPEvsPEELLEAIED 57
CopZ COG2608
Copper chaperone CopZ [Inorganic ion transport and metabolism];
76-124 1.41e-09

Copper chaperone CopZ [Inorganic ion transport and metabolism];


Pssm-ID: 442020 [Multi-domain]  Cd Length: 71  Bit Score: 51.06  E-value: 1.41e-09
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 18404191  76 VELKVS-MHCYGCAKKVEKHISKLDGVTWYKVELESKKVVVKGNILPVDV 124
Cdd:COG2608   4 VTLKVEgMTCGHCVARVEKALKALDGVASVEVDLATGTATVTYDPEKVSL 53
HMA pfam00403
Heavy-metal-associated domain;
82-124 3.53e-08

Heavy-metal-associated domain;


Pssm-ID: 459804 [Multi-domain]  Cd Length: 58  Bit Score: 46.84  E-value: 3.53e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 18404191    82 MHCYGCAKKVEKHISKLDGVTWYKVELESKKVVVKGNILPVDV 124
Cdd:pfam00403   7 MHCGGCAAKVEKALSELPGVLSVSVDLATKTVTVTGDAESTKL 49
TIGR00003 TIGR00003
copper ion binding protein; This model describes an apparently copper-specific subfamily of ...
 76-116 2.46e-05

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: 39.83  E-value: 2.46e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 18404191    76 VELKV-SMHCYGCAKKVEKHISKLDGVTWYKVELESKKVVVK 116
Cdd:TIGR00003   2 QTFQVkGMSCNHCVDKIEKFVGEIEGVSKVKVQLEKEKVVVE 43
zntA PRK11033
zinc/cadmium/mercury/lead-transporting ATPase; Provisional
 79-128 1.80e-04

zinc/cadmium/mercury/lead-transporting ATPase; Provisional


Pssm-ID: 236827 [Multi-domain]  Cd Length: 741  Bit Score: 39.98  E-value: 1.80e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 18404191   79 KVS-MHCYGCAKKVEKHISKLDGVTWYKVELESKKVVVKGNilpVDVLESI 128
Cdd:PRK11033  58 KVSgMDCPSCARKVENAVRQLAGVNQVQVLFATEKLVVDAD---NDIRAQV 105
 
Name Accession Description Interval E-value
HMA cd00371
Heavy-metal-associated domain (HMA) is a conserved domain of approximately 30 amino acid ...
 77-130 9.25e-11

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: 53.76  E-value: 9.25e-11
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 18404191  77 ELKVS-MHCYGCAKKVEKHISKLDGVTWYKVELESKKVVVKGNIL--PVDVLESICK 130
Cdd:cd00371   1 ELSVEgMTCAGCVSKIEKALEKLPGVESVEVDLETGKATVEYDPEvsPEELLEAIED 57
CopZ COG2608
Copper chaperone CopZ [Inorganic ion transport and metabolism];
76-124 1.41e-09

Copper chaperone CopZ [Inorganic ion transport and metabolism];


Pssm-ID: 442020 [Multi-domain]  Cd Length: 71  Bit Score: 51.06  E-value: 1.41e-09
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 18404191  76 VELKVS-MHCYGCAKKVEKHISKLDGVTWYKVELESKKVVVKGNILPVDV 124
Cdd:COG2608   4 VTLKVEgMTCGHCVARVEKALKALDGVASVEVDLATGTATVTYDPEKVSL 53
HMA pfam00403
Heavy-metal-associated domain;
82-124 3.53e-08

Heavy-metal-associated domain;


Pssm-ID: 459804 [Multi-domain]  Cd Length: 58  Bit Score: 46.84  E-value: 3.53e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 18404191    82 MHCYGCAKKVEKHISKLDGVTWYKVELESKKVVVKGNILPVDV 124
Cdd:pfam00403   7 MHCGGCAAKVEKALSELPGVLSVSVDLATKTVTVTGDAESTKL 49
ZntA COG2217
Cation-transporting P-type ATPase [Inorganic ion transport and metabolism];
76-131 3.59e-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: 3.59e-06
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 18404191  76 VELKVS-MHCYGCAKKVEKHISKLDGVTWYKVELESKKVVV---KGNILPVDVLESICKV 131
Cdd:COG2217   3 VRLRIEgMTCAACAWLIEKALRKLPGVLSARVNLATERARVeydPGKVSLEELIAAVEKA 62
TIGR00003 TIGR00003
copper ion binding protein; This model describes an apparently copper-specific subfamily of ...
 76-116 2.46e-05

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: 39.83  E-value: 2.46e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 18404191    76 VELKV-SMHCYGCAKKVEKHISKLDGVTWYKVELESKKVVVK 116
Cdd:TIGR00003   2 QTFQVkGMSCNHCVDKIEKFVGEIEGVSKVKVQLEKEKVVVE 43
zntA PRK11033
zinc/cadmium/mercury/lead-transporting ATPase; Provisional
 79-128 1.80e-04

zinc/cadmium/mercury/lead-transporting ATPase; Provisional


Pssm-ID: 236827 [Multi-domain]  Cd Length: 741  Bit Score: 39.98  E-value: 1.80e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 18404191   79 KVS-MHCYGCAKKVEKHISKLDGVTWYKVELESKKVVVKGNilpVDVLESI 128
Cdd:PRK11033  58 KVSgMDCPSCARKVENAVRQLAGVNQVQVLFATEKLVVDAD---NDIRAQV 105
MerP TIGR02052
mercuric transport protein periplasmic component; This model represents the periplasmic ...
 73-115 6.97e-03

mercuric transport protein periplasmic component; This model represents the periplasmic mercury (II) binding protein of the bacterial mercury detoxification system which passes mercuric ion to the MerT transporter for subsequent reduction to Hg(0) by the mercuric reductase MerA. MerP contains a distinctive GMTCXXC motif associated with metal binding. MerP is related to a larger family of metal binding proteins (pfam00403). [Cellular processes, Detoxification]


Pssm-ID: 131107 [Multi-domain]  Cd Length: 92  Bit Score: 33.86  E-value: 6.97e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 18404191    73 PKIVELKV-SMHCYGCAKKVEKHISKLDGVTWYKVELESKKVVV 115
Cdd:TIGR02052  22 TQTVTLEVpGMTCVACPITVETALQKVDGVSKAEVTFKTKLAVV 65
 
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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