1FE4,2ROE,1P6T,2RML,1KQK,2VOY,2QIF,1P8G,6FF2,1KVI,2K1R,3CJK,2LQB,2AW0,1AW0,1OPZ,1P6T,1CPZ,2L3M,3J09,2G9O,4A48,2ROP,6A71,1Q8L,1S6O,1YJU,2XMW,2GCF,2RML,1YJR,3DXS,2EW9,2ROP,2EW9,2KT2,4A47,1OSD,1Y3K,2LDI,2XMV,1AFJ,1AFI,2GGP,2K2P,2N7Y,4Y2I,4Y2K,4Y2M,5F0U,2LQ9,3FRY,1SB6,4A46,1FE0,3CJK,4YDX,1YG0,2CRL,2RSQ,1CC8,1CC7,1JK9,5U9M,2AJ0,6FON,1QUP,6FP6,2KKH,4U9R,7B1I,7A8W,5A6P,5A6P,6G10,6R8K,6Q76,7A8X,7BNT,5ZNE,7NLJ,7NMM,6FU9


Conserved Protein Domain Family
HMA
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cd00371: HMA (This model is not part of the current CDD release)
heavy-metal-associated domain (HMA) found in CPx-type heavy metal ATPases and copper chaperones
The Heavy Metal-Associated domain (HMA) is a conserved domain of approximately 30 amino acid residues, identified in various proteins responsible for the transportation or detoxification of heavy metals. Notable examples include 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.
Links
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Statistics
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PSSM-Id: 501463
Aligned: 3394 rows
Threshold Bit Score: 27.1283
Created: 6-Mar-2002
Updated: 30-Oct-2024
Structure
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Program:
Drawing:
Aligned Rows:
Download Cn3D
 
metal-binding
Conserved site includes 2 residues -Click on image for an interactive view with Cn3D
Feature 1: metal-binding site [ion binding site], 2 residue positions
Conserved feature residue pattern:C CClick to see conserved feature residue pattern help
Evidence:
  • Comment:heavy metal-associated (HMA) domains bind metal ions at its Cys-x-x-Cys (CxxC) motif
  • Structure:1FE4; Homo sapiens Hah1 metallochaperone protein bound to Hg ion
  • Structure:Bacillus subtilis Copper-translocating P-type ATPase binds copper ion
  • Structure:4A46; Synechocystis sp. Ssr2857 protein binds zinc ion
Scroll to Sequence Alignment Display
Sequence Alignment
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Format: Row Display: Color Bits: Type Selection: 
Feature 1                   #     #                                                           
1FE4_A         4 HEFSVD---MTCg---GCAEAVSRVLNKLgg-vKYDIDLpnkKVCIESe----hSMDTLLATLKk------tGKTVS 63  human
QDV62269      35 TTITLKv--LTCe---NCAKKVAAKLNEVpgveSVKTDVkskTATVVPksnatpSPLKLWEAIEk------aGKEPV 100 Planctomycetes bac...
PAN31065      49 RITELHv-rMDCn---GCEHKVRKTLRAIdgvsEVYIDQanhKITVVGm----aDPERIVKAIRkt-----kRVPTI 112 Panicum hallii
EPS64000       8 RRIDLLm-rMDCe---GCVLKLSKALTSLkgveSVSVDVkqqKATVVGy----mEAEEVMKAVGkr----geIWPYV 72  Genlisea aurea
RYG42799      67 KTTVLAv-sMSCe---GCANTVKRLLGKVpgvsSVHTDVatqRVEVVSs----aEPPVLMEALSkwataggkTVELV 135 archaeon
XP_003078814   5 VTLRCD---FACd---GCANAVKRILSKDdavtSVRTSVedkLVVVVGag---lDAEDVRARVSk------cGRETT 66  Ostreococcus tauri
PWA32514      23 TKYELQi--IPCdmcnGCINKVKKVLRRLvgvkLLTTDFeneKFTISSvv---eHPEVIKFALEkkf--rqkRVILL 92  sweet wormwood
KVI09796      49 TTVDLQiipLHNc--tKCIRKVEKTLCRFdgvkLLDVDSengKFTIQTt----rHPEEIRDALQrkf---sgKSVIL 116 Cynara cardunculus...
NP_001329947  17 TMMKLKv-dLDCa---KCYKKVKKVLCKFpqirDQLFDEksnIVIIKVvc---cSPERIMDKLCskg---ggSIKTI 83  thale cress
PTQ43258     102 EIGVRR---FCCe---ECVIKVERKLQKLegvsSARCKMddgIITVVGs----vESRDVLATLKrir---ylDPDVC 165 liverwort

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