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.

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 295872360  79 IRVVGMTCQSCVRNIEGNIGTKPGIHSIEVQLAAKNARVQYDPAqYDPAQIAELIDDMGFEAS 141
Cdd:cd00371    2 LSVEGMTCAGCVSKIEKALEKLPGVESVEVDLETGKATVEYDPE-VSPEELLEAIEDAGYKAR 63

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.

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 295872360 196 IRGMTCASCVAAIEKHCKKIYGLDSILVALLAAKAEVKFNAN 237
Cdd:cd00371    4 VEGMTCAGCVSKIEKALEKLPGVESVEVDLETGKATVEYDPE 45

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.

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 295872360  79 IRVVGMTCQSCVRNIEGNIGTKPGIHSIEVQLAAKNARVQYDPAqYDPAQIAELIDDMGFEAS 141
Cdd:cd00371    2 LSVEGMTCAGCVSKIEKALEKLPGVESVEVDLETGKATVEYDPE-VSPEELLEAIEDAGYKAR 63

Heavy-metal-associated domain;

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 295872360   79 IRVVGMTCQSCVRNIEGNIGTKPGIHSIEVQLAAKNARVQYDPAQYDPAQIAELIDD 135
Cdd:pfam00403   2 FRVSGMHCGGCAAKVEKALSELPGVLSVSVDLATKTVTVTGDAESTKLEKLVEAIEK 58

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.

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 295872360   2 GMTCQSCVRNITEHIGQKSGILGVRVILEENAGYFDYDPRqTDPARIASDIDDMGFECS 60
Cdd:cd00371    6 GMTCAGCVSKIEKALEKLPGVESVEVDLETGKATVEYDPE-VSPEELLEAIEDAGYKAR 63

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.

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 295872360 196 IRGMTCASCVAAIEKHCKKIYGLDSILVALLAAKAEVKFNAN 237
Cdd:cd00371    4 VEGMTCAGCVSKIEKALEKLPGVESVEVDLETGKATVEYDPE 45

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.

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 295872360  79 IRVVGMTCQSCVRNIEGNIGTKPGIHSIEVQLAAKNARVQYDPAQYDPAQIAELIDDMGFEASVQE 144
Cdd:NF041115   8 LAIEGMTUASUPLIAKKALEGLEGVEKADVSYKEGRAEVAFDPDKVSAAQMVDAVNRIGFRASVIE 73

Heavy-metal-associated domain;

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 295872360  194 LHIRGMTCASCVAAIEKHCKKIYGLDSILVALLAAKAEVKFNA 236
Cdd:pfam00403   2 FRVSGMHCGGCAAKVEKALSELPGVLSVSVDLATKTVTVTGDA 44

putative mercuric reductase; Provisional

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 295872360  77 TNIRVVGMTCQSCVRNIEGNIGTKPGIHSIEVQLAAKNARVQYDPAqYDPAQIAELIDDMGFEASV 142
Cdd:PRK13748   2 TTLKITGMTCDSCAAHVKDALEKVPGVQSADVSYPKGSAQLAIEVG-TSPDALTAAVAGLGYRATL 66

Heavy-metal-associated domain;

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 295872360    1 VGMTCQSCVRNITEHIGQKSGILGVRVILEENAGYFDYDPRQTDPARIASDIDD 54
Cdd:pfam00403   5 SGMHCGGCAAKVEKALSELPGVLSVSVDLATKTVTVTGDAESTKLEKLVEAIEK 58

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.

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 295872360  79 IRVVGMTCQSCVRNIEGNIGTKPGIHSIEVQLAAKNARVQYDPAqYDPAQIAELIDDMGFEAS 141
Cdd:cd00371    2 LSVEGMTCAGCVSKIEKALEKLPGVESVEVDLETGKATVEYDPE-VSPEELLEAIEDAGYKAR 63

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

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295872360  77 TNIRVVGMTCQSCVRNIEGNIGTKPGIHSIEVQLAAKNARVQYDPAQYDPAQIAELIDDMGFEASVQEPRSPSQSPSPAP 156
Cdd:COG2217    3 VRLRIEGMTCAACAWLIEKALRKLPGVLSARVNLATERARVEYDPGKVSLEELIAAVEKAGYEAEPADADAAAEEAREKE 82

                 ....*..
gi 295872360 157 ASSPKKR 163
Cdd:COG2217   83 LRDLLRR 89

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]

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 295872360   79 IRVVGMTCQSCVRNIEGNIGTKPGIHSIEVQLAAKNARVQYDPAQYDPAQIAELIDDMGFEA 140
Cdd:TIGR00003   4 FQVKGMSCNHCVDKIEKFVGEIEGVSKVKVQLEKEKVVVEFDAPNVSATEICEAILDAGYEV 65

Copper chaperone CopZ [Inorganic ion transport and metabolism];

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 295872360   2 GMTCQSCVRNITEHIGQKSGILGVRVILEENAGYFDYDPRQTDPARIASDIDDMGFE 58
Cdd:COG2608   10 GMTCGHCVARVEKALKALDGVASVEVDLATGTATVTYDPEKVSLEDIKAAIEEAGYE 66

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

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 295872360   2 GMTCQSCVRNITEHIGQKSGILGVRVILEENAGYFDYDPRQTDPARIASDIDDMGFEcSYPGDAADPPETPASA 75
Cdd:COG2217    9 GMTCAACAWLIEKALRKLPGVLSARVNLATERARVEYDPGKVSLEELIAAVEKAGYE-AEPADADAAAEEAREK 81

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

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 295872360 194 LHIRGMTCASCVAAIEKHCKKIYGLDSILVALLAAKAEVKFNA 236
Cdd:COG2217    5 LRIEGMTCAACAWLIEKALRKLPGVLSARVNLATERARVEYDP 47

copper chaperone CopZ; Copper chaperone CopZ, as the name is used in Enterococcus hirae and related species, is a small copper-binding protein with close homology to domains found, sometimes in multiple copies, in various copper-translocating copper-translocating P-type ATPases, and to distinct families of other small copper chaperones that also named CopZ.

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 295872360 194 LHIRGMTCASCVAAIEKHCKKIYGLDSILVALLAAKAEVKF 234
Cdd:NF033794   4 FSIKGMSCNHCVARVEKAVNELPGVKKVKVNLKKENGVVKF 44

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]

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 295872360  194 LHIRGMTCASCVAAIEKHCKKIYGLDSILVALLAAKAEVKFNA 236
Cdd:TIGR00003   4 FQVKGMSCNHCVDKIEKFVGEIEGVSKVKVQLEKEKVVVEFDA 46

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]

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 295872360    2 GMTCQSCVRNITEHIGQKSGILGVRVILEENAGYFDYDPRQTDPARIASDIDDMGFE 58
Cdd:TIGR00003   8 GMSCNHCVDKIEKFVGEIEGVSKVKVQLEKEKVVVEFDAPNVSATEICEAILDAGYE 64

copper-exporting P-type ATPase CopA;

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295872360  83 GMTCQSCVRNIEGNIGTKPGIHSIEVQLAakNARVQYDPaqyDPAQIAELIDDMGFEASVQeprspsqspspapasSPKK 162
Cdd:PRK10671  11 GLSCGHCVKRVKESLEQRPDVEQADVSIT--EAHVTGTA---SAEALIETIKQAGYDASVS---------------HPKA 70

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 295872360 163 RATPTPPPPSYAQNGSAVAIPVEQELLTKCF-LHIRGMTCASCVAAIEKHCKKIYGLDSILVAL 225
Cdd:PRK10671  71 KPLTESSIPSEALTAASEELPAATADDDDSQqLLLSGMSCASCVSRVQNALQSVPGVTQARVNL 134