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Conserved domains on  [gi|295872338|gb|ADG50094|]
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CG1886, partial [Drosophila melanogaster]

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 ...
 93-155 1.80e-19

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: 79.19  E-value: 1.80e-19
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 295872338  93 IRVVGMTCQSCVRNIEGNIGTKPGIHSIEVQLAAKNARVQYDPAQyDPAQIAELIDDMGFEAS 155
Cdd:cd00371    2 LSVEGMTCAGCVSKIEKALEKLPGVESVEVDLETGKATVEYDPEV-SPEELLEAIEDAGYKAR 63
CopZ COG2608
Copper chaperone CopZ [Inorganic ion transport and metabolism];
7-72 1.25e-10

Copper chaperone CopZ [Inorganic ion transport and metabolism];


:

Pssm-ID: 442020 [Multi-domain]  Cd Length: 71  Bit Score: 56.07  E-value: 1.25e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 295872338   7 MSTVRLPIVGMTCQSCVRNITEHIGQKSGILGVRVILEENAGYFDYDPRQTDPARIASDIDDMGFE 72
Cdd:COG2608    1 MKTVTLKVEGMTCGHCVARVEKALKALDGVASVEVDLATGTATVTYDPEKVSLEDIKAAIEEAGYE 66
HMA cd00371
Heavy-metal-associated domain (HMA) is a conserved domain of approximately 30 amino acid ...
 210-251 1.12e-07

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: 47.60  E-value: 1.12e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 295872338 210 IRGMTCASCVAAIEKHCKKIYGLDSILVALLAAKAEVKFNAN 251
Cdd:cd00371    4 VEGMTCAGCVSKIEKALEKLPGVESVEVDLETGKATVEYDPE 45
 
Name Accession Description Interval E-value
HMA cd00371
Heavy-metal-associated domain (HMA) is a conserved domain of approximately 30 amino acid ...
 93-155 1.80e-19

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: 79.19  E-value: 1.80e-19
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 295872338  93 IRVVGMTCQSCVRNIEGNIGTKPGIHSIEVQLAAKNARVQYDPAQyDPAQIAELIDDMGFEAS 155
Cdd:cd00371    2 LSVEGMTCAGCVSKIEKALEKLPGVESVEVDLETGKATVEYDPEV-SPEELLEAIEDAGYKAR 63
CopZ COG2608
Copper chaperone CopZ [Inorganic ion transport and metabolism];
91-158 1.01e-15

Copper chaperone CopZ [Inorganic ion transport and metabolism];


Pssm-ID: 442020 [Multi-domain]  Cd Length: 71  Bit Score: 69.55  E-value: 1.01e-15
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 295872338  91 TNIRVVGMTCQSCVRNIEGNIGTKPGIHSIEVQLAAKNARVQYDPAQYDPAQIAELIDDMGFEASVQE 158
Cdd:COG2608    4 VTLKVEGMTCGHCVARVEKALKALDGVASVEVDLATGTATVTYDPEKVSLEDIKAAIEEAGYEVEKAE 71
HMA pfam00403
Heavy-metal-associated domain;
93-149 2.13e-12

Heavy-metal-associated domain;


Pssm-ID: 459804 [Multi-domain]  Cd Length: 58  Bit Score: 60.33  E-value: 2.13e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 295872338   93 IRVVGMTCQSCVRNIEGNIGTKPGIHSIEVQLAAKNARVQYDPAQYDPAQIAELIDD 149
Cdd:pfam00403   2 FRVSGMHCGGCAAKVEKALSELPGVLSVSVDLATKTVTVTGDAESTKLEKLVEAIEK 58
CopZ COG2608
Copper chaperone CopZ [Inorganic ion transport and metabolism];
7-72 1.25e-10

Copper chaperone CopZ [Inorganic ion transport and metabolism];


Pssm-ID: 442020 [Multi-domain]  Cd Length: 71  Bit Score: 56.07  E-value: 1.25e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 295872338   7 MSTVRLPIVGMTCQSCVRNITEHIGQKSGILGVRVILEENAGYFDYDPRQTDPARIASDIDDMGFE 72
Cdd:COG2608    1 MKTVTLKVEGMTCGHCVARVEKALKALDGVASVEVDLATGTATVTYDPEKVSLEDIKAAIEEAGYE 66
HMA cd00371
Heavy-metal-associated domain (HMA) is a conserved domain of approximately 30 amino acid ...
 12-74 1.35e-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: 52.99  E-value: 1.35e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 295872338  12 LPIVGMTCQSCVRNITEHIGQKSGILGVRVILEENAGYFDYDPRqTDPARIASDIDDMGFECS 74
Cdd:cd00371    2 LSVEGMTCAGCVSKIEKALEKLPGVESVEVDLETGKATVEYDPE-VSPEELLEAIEDAGYKAR 63
TIGR00003 TIGR00003
copper ion binding protein; This model describes an apparently copper-specific subfamily of ...
 93-154 5.68e-09

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: 51.39  E-value: 5.68e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 295872338   93 IRVVGMTCQSCVRNIEGNIGTKPGIHSIEVQLAAKNARVQYDPAQYDPAQIAELIDDMGFEA 154
Cdd:TIGR00003   4 FQVKGMSCNHCVDKIEKFVGEIEGVSKVKVQLEKEKVVVEFDAPNVSATEICEAILDAGYEV 65
HMA cd00371
Heavy-metal-associated domain (HMA) is a conserved domain of approximately 30 amino acid ...
 210-251 1.12e-07

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: 47.60  E-value: 1.12e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 295872338 210 IRGMTCASCVAAIEKHCKKIYGLDSILVALLAAKAEVKFNAN 251
Cdd:cd00371    4 VEGMTCAGCVSKIEKALEKLPGVESVEVDLETGKATVEYDPE 45
CopZ COG2608
Copper chaperone CopZ [Inorganic ion transport and metabolism];
208-251 2.71e-06

Copper chaperone CopZ [Inorganic ion transport and metabolism];


Pssm-ID: 442020 [Multi-domain]  Cd Length: 71  Bit Score: 44.13  E-value: 2.71e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 295872338 208 LHIRGMTCASCVAAIEKHCKKIYGLDSILVALLAAKAEVKFNAN 251
Cdd:COG2608    6 LKVEGMTCGHCVARVEKALKALDGVASVEVDLATGTATVTYDPE 49
TIGR00003 TIGR00003
copper ion binding protein; This model describes an apparently copper-specific subfamily of ...
 10-72 4.96e-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: 40.22  E-value: 4.96e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 295872338   10 VRLPIVGMTCQSCVRNITEHIGQKSGILGVRVILEENAGYFDYDPRQTDPARIASDIDDMGFE 72
Cdd:TIGR00003   2 QTFQVKGMSCNHCVDKIEKFVGEIEGVSKVKVQLEKEKVVVEFDAPNVSATEICEAILDAGYE 64
UxxU_metal_bind NF041115
metal-binding (seleno)protein; Known members of this family are selenoproteins with an ...
 93-158 6.96e-05

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: 40.01  E-value: 6.96e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 295872338  93 IRVVGMTCQSCVRNIEGNIGTKPGIHSIEVQLAAKNARVQYDPAQYDPAQIAELIDDMGFEASVQE 158
Cdd:NF041115   8 LAIEGMTUASUPLIAKKALEGLEGVEKADVSYKEGRAEVAFDPDKVSAAQMVDAVNRIGFRASVIE 73
TIGR00003 TIGR00003
copper ion binding protein; This model describes an apparently copper-specific subfamily of ...
 208-250 8.47e-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: 8.47e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 295872338  208 LHIRGMTCASCVAAIEKHCKKIYGLDSILVALLAAKAEVKFNA 250
Cdd:TIGR00003   4 FQVKGMSCNHCVDKIEKFVGEIEGVSKVKVQLEKEKVVVEFDA 46
chaper_CopZ_Eh NF033794
copper chaperone CopZ; Copper chaperone CopZ, as the name is used in Enterococcus hirae and ...
 208-248 8.57e-05

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.


Pssm-ID: 411374 [Multi-domain]  Cd Length: 68  Bit Score: 39.62  E-value: 8.57e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 295872338 208 LHIRGMTCASCVAAIEKHCKKIYGLDSILVALLAAKAEVKF 248
Cdd:NF033794   4 FSIKGMSCNHCVARVEKAVNELPGVKKVKVNLKKENGVVKF 44
HMA pfam00403
Heavy-metal-associated domain;
208-250 1.07e-04

Heavy-metal-associated domain;


Pssm-ID: 459804 [Multi-domain]  Cd Length: 58  Bit Score: 39.14  E-value: 1.07e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 295872338  208 LHIRGMTCASCVAAIEKHCKKIYGLDSILVALLAAKAEVKFNA 250
Cdd:pfam00403   2 FRVSGMHCGGCAAKVEKALSELPGVLSVSVDLATKTVTVTGDA 44
HMA pfam00403
Heavy-metal-associated domain;
11-68 1.32e-04

Heavy-metal-associated domain;


Pssm-ID: 459804 [Multi-domain]  Cd Length: 58  Bit Score: 38.75  E-value: 1.32e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 295872338   11 RLPIVGMTCQSCVRNITEHIGQKSGILGVRVILEENAGYFDYDPRQTDPARIASDIDD 68
Cdd:pfam00403   1 TFRVSGMHCGGCAAKVEKALSELPGVLSVSVDLATKTVTVTGDAESTKLEKLVEAIEK 58
PRK13748 PRK13748
putative mercuric reductase; Provisional
 91-156 1.98e-04

putative mercuric reductase; Provisional


Pssm-ID: 184298 [Multi-domain]  Cd Length: 561  Bit Score: 42.06  E-value: 1.98e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 295872338  91 TNIRVVGMTCQSCVRNIEGNIGTKPGIHSIEVQLAAKNARVQYDPAqYDPAQIAELIDDMGFEASV 156
Cdd:PRK13748   2 TTLKITGMTCDSCAAHVKDALEKVPGVQSADVSYPKGSAQLAIEVG-TSPDALTAAVAGLGYRATL 66
PRK13748 PRK13748
putative mercuric reductase; Provisional
 208-250 1.21e-03

putative mercuric reductase; Provisional


Pssm-ID: 184298 [Multi-domain]  Cd Length: 561  Bit Score: 39.75  E-value: 1.21e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 295872338 208 LHIRGMTCASCVAAIEKHCKKIYGLDSILVALLAAKAEVKFNA 250
Cdd:PRK13748   4 LKITGMTCDSCAAHVKDALEKVPGVQSADVSYPKGSAQLAIEV 46
 
Name Accession Description Interval E-value
HMA cd00371
Heavy-metal-associated domain (HMA) is a conserved domain of approximately 30 amino acid ...
 93-155 1.80e-19

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: 79.19  E-value: 1.80e-19
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 295872338  93 IRVVGMTCQSCVRNIEGNIGTKPGIHSIEVQLAAKNARVQYDPAQyDPAQIAELIDDMGFEAS 155
Cdd:cd00371    2 LSVEGMTCAGCVSKIEKALEKLPGVESVEVDLETGKATVEYDPEV-SPEELLEAIEDAGYKAR 63
CopZ COG2608
Copper chaperone CopZ [Inorganic ion transport and metabolism];
91-158 1.01e-15

Copper chaperone CopZ [Inorganic ion transport and metabolism];


Pssm-ID: 442020 [Multi-domain]  Cd Length: 71  Bit Score: 69.55  E-value: 1.01e-15
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 295872338  91 TNIRVVGMTCQSCVRNIEGNIGTKPGIHSIEVQLAAKNARVQYDPAQYDPAQIAELIDDMGFEASVQE 158
Cdd:COG2608    4 VTLKVEGMTCGHCVARVEKALKALDGVASVEVDLATGTATVTYDPEKVSLEDIKAAIEEAGYEVEKAE 71
ZntA COG2217
Cation-transporting P-type ATPase [Inorganic ion transport and metabolism];
91-177 5.89e-13

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


Pssm-ID: 441819 [Multi-domain]  Cd Length: 717  Bit Score: 67.86  E-value: 5.89e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295872338  91 TNIRVVGMTCQSCVRNIEGNIGTKPGIHSIEVQLAAKNARVQYDPAQYDPAQIAELIDDMGFEASVQEPRSPSQSPSPAP 170
Cdd:COG2217    3 VRLRIEGMTCAACAWLIEKALRKLPGVLSARVNLATERARVEYDPGKVSLEELIAAVEKAGYEAEPADADAAAEEAREKE 82


                 ....*..
gi 295872338 171 ASSPKKR 177
Cdd:COG2217   83 LRDLLRR 89
HMA pfam00403
Heavy-metal-associated domain;
93-149 2.13e-12

Heavy-metal-associated domain;


Pssm-ID: 459804 [Multi-domain]  Cd Length: 58  Bit Score: 60.33  E-value: 2.13e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 295872338   93 IRVVGMTCQSCVRNIEGNIGTKPGIHSIEVQLAAKNARVQYDPAQYDPAQIAELIDD 149
Cdd:pfam00403   2 FRVSGMHCGGCAAKVEKALSELPGVLSVSVDLATKTVTVTGDAESTKLEKLVEAIEK 58
CopZ COG2608
Copper chaperone CopZ [Inorganic ion transport and metabolism];
7-72 1.25e-10

Copper chaperone CopZ [Inorganic ion transport and metabolism];


Pssm-ID: 442020 [Multi-domain]  Cd Length: 71  Bit Score: 56.07  E-value: 1.25e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 295872338   7 MSTVRLPIVGMTCQSCVRNITEHIGQKSGILGVRVILEENAGYFDYDPRQTDPARIASDIDDMGFE 72
Cdd:COG2608    1 MKTVTLKVEGMTCGHCVARVEKALKALDGVASVEVDLATGTATVTYDPEKVSLEDIKAAIEEAGYE 66
HMA cd00371
Heavy-metal-associated domain (HMA) is a conserved domain of approximately 30 amino acid ...
 12-74 1.35e-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: 52.99  E-value: 1.35e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 295872338  12 LPIVGMTCQSCVRNITEHIGQKSGILGVRVILEENAGYFDYDPRqTDPARIASDIDDMGFECS 74
Cdd:cd00371    2 LSVEGMTCAGCVSKIEKALEKLPGVESVEVDLETGKATVEYDPE-VSPEELLEAIEDAGYKAR 63
TIGR00003 TIGR00003
copper ion binding protein; This model describes an apparently copper-specific subfamily of ...
 93-154 5.68e-09

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: 51.39  E-value: 5.68e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 295872338   93 IRVVGMTCQSCVRNIEGNIGTKPGIHSIEVQLAAKNARVQYDPAQYDPAQIAELIDDMGFEA 154
Cdd:TIGR00003   4 FQVKGMSCNHCVDKIEKFVGEIEGVSKVKVQLEKEKVVVEFDAPNVSATEICEAILDAGYEV 65
ZntA COG2217
Cation-transporting P-type ATPase [Inorganic ion transport and metabolism];
8-89 1.01e-08

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


Pssm-ID: 441819 [Multi-domain]  Cd Length: 717  Bit Score: 55.15  E-value: 1.01e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295872338   8 STVRLPIVGMTCQSCVRNITEHIGQKSGILGVRVILEENAGYFDYDPRQTDPARIASDIDDMGFEcSYPGDAADPPETPA 87
Cdd:COG2217    1 ERVRLRIEGMTCAACAWLIEKALRKLPGVLSARVNLATERARVEYDPGKVSLEELIAAVEKAGYE-AEPADADAAAEEAR 79


                 ..
gi 295872338  88 SA 89
Cdd:COG2217   80 EK 81
HMA cd00371
Heavy-metal-associated domain (HMA) is a conserved domain of approximately 30 amino acid ...
 210-251 1.12e-07

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: 47.60  E-value: 1.12e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 295872338 210 IRGMTCASCVAAIEKHCKKIYGLDSILVALLAAKAEVKFNAN 251
Cdd:cd00371    4 VEGMTCAGCVSKIEKALEKLPGVESVEVDLETGKATVEYDPE 45
CopZ COG2608
Copper chaperone CopZ [Inorganic ion transport and metabolism];
208-251 2.71e-06

Copper chaperone CopZ [Inorganic ion transport and metabolism];


Pssm-ID: 442020 [Multi-domain]  Cd Length: 71  Bit Score: 44.13  E-value: 2.71e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 295872338 208 LHIRGMTCASCVAAIEKHCKKIYGLDSILVALLAAKAEVKFNAN 251
Cdd:COG2608    6 LKVEGMTCGHCVARVEKALKALDGVASVEVDLATGTATVTYDPE 49
ZntA COG2217
Cation-transporting P-type ATPase [Inorganic ion transport and metabolism];
208-250 6.39e-06

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


Pssm-ID: 441819 [Multi-domain]  Cd Length: 717  Bit Score: 46.67  E-value: 6.39e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 295872338 208 LHIRGMTCASCVAAIEKHCKKIYGLDSILVALLAAKAEVKFNA 250
Cdd:COG2217    5 LRIEGMTCAACAWLIEKALRKLPGVLSARVNLATERARVEYDP 47
TIGR00003 TIGR00003
copper ion binding protein; This model describes an apparently copper-specific subfamily of ...
 10-72 4.96e-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: 40.22  E-value: 4.96e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 295872338   10 VRLPIVGMTCQSCVRNITEHIGQKSGILGVRVILEENAGYFDYDPRQTDPARIASDIDDMGFE 72
Cdd:TIGR00003   2 QTFQVKGMSCNHCVDKIEKFVGEIEGVSKVKVQLEKEKVVVEFDAPNVSATEICEAILDAGYE 64
UxxU_metal_bind NF041115
metal-binding (seleno)protein; Known members of this family are selenoproteins with an ...
 93-158 6.96e-05

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: 40.01  E-value: 6.96e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 295872338  93 IRVVGMTCQSCVRNIEGNIGTKPGIHSIEVQLAAKNARVQYDPAQYDPAQIAELIDDMGFEASVQE 158
Cdd:NF041115   8 LAIEGMTUASUPLIAKKALEGLEGVEKADVSYKEGRAEVAFDPDKVSAAQMVDAVNRIGFRASVIE 73
TIGR00003 TIGR00003
copper ion binding protein; This model describes an apparently copper-specific subfamily of ...
 208-250 8.47e-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: 8.47e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 295872338  208 LHIRGMTCASCVAAIEKHCKKIYGLDSILVALLAAKAEVKFNA 250
Cdd:TIGR00003   4 FQVKGMSCNHCVDKIEKFVGEIEGVSKVKVQLEKEKVVVEFDA 46
chaper_CopZ_Eh NF033794
copper chaperone CopZ; Copper chaperone CopZ, as the name is used in Enterococcus hirae and ...
 208-248 8.57e-05

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.


Pssm-ID: 411374 [Multi-domain]  Cd Length: 68  Bit Score: 39.62  E-value: 8.57e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 295872338 208 LHIRGMTCASCVAAIEKHCKKIYGLDSILVALLAAKAEVKF 248
Cdd:NF033794   4 FSIKGMSCNHCVARVEKAVNELPGVKKVKVNLKKENGVVKF 44
HMA pfam00403
Heavy-metal-associated domain;
208-250 1.07e-04

Heavy-metal-associated domain;


Pssm-ID: 459804 [Multi-domain]  Cd Length: 58  Bit Score: 39.14  E-value: 1.07e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 295872338  208 LHIRGMTCASCVAAIEKHCKKIYGLDSILVALLAAKAEVKFNA 250
Cdd:pfam00403   2 FRVSGMHCGGCAAKVEKALSELPGVLSVSVDLATKTVTVTGDA 44
HMA pfam00403
Heavy-metal-associated domain;
11-68 1.32e-04

Heavy-metal-associated domain;


Pssm-ID: 459804 [Multi-domain]  Cd Length: 58  Bit Score: 38.75  E-value: 1.32e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 295872338   11 RLPIVGMTCQSCVRNITEHIGQKSGILGVRVILEENAGYFDYDPRQTDPARIASDIDD 68
Cdd:pfam00403   1 TFRVSGMHCGGCAAKVEKALSELPGVLSVSVDLATKTVTVTGDAESTKLEKLVEAIEK 58
PRK13748 PRK13748
putative mercuric reductase; Provisional
 91-156 1.98e-04

putative mercuric reductase; Provisional


Pssm-ID: 184298 [Multi-domain]  Cd Length: 561  Bit Score: 42.06  E-value: 1.98e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 295872338  91 TNIRVVGMTCQSCVRNIEGNIGTKPGIHSIEVQLAAKNARVQYDPAqYDPAQIAELIDDMGFEASV 156
Cdd:PRK13748   2 TTLKITGMTCDSCAAHVKDALEKVPGVQSADVSYPKGSAQLAIEVG-TSPDALTAAVAGLGYRATL 66
copA PRK10671
copper-exporting P-type ATPase CopA;
97-239 1.14e-03

copper-exporting P-type ATPase CopA;


Pssm-ID: 182635 [Multi-domain]  Cd Length: 834  Bit Score: 40.11  E-value: 1.14e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295872338  97 GMTCQSCVRNIEGNIGTKPGIHSIEVQLAakNARVQYDPaqyDPAQIAELIDDMGFEASVQeprspsqspspapasSPKK 176
Cdd:PRK10671  11 GLSCGHCVKRVKESLEQRPDVEQADVSIT--EAHVTGTA---SAEALIETIKQAGYDASVS---------------HPKA 70

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 295872338 177 RATPTPPPPSYAQNGSAVAIPVEQELLTKCF-LHIRGMTCASCVAAIEKHCKKIYGLDSILVAL 239
Cdd:PRK10671  71 KPLTESSIPSEALTAASEELPAATADDDDSQqLLLSGMSCASCVSRVQNALQSVPGVTQARVNL 134
PRK13748 PRK13748
putative mercuric reductase; Provisional
 208-250 1.21e-03

putative mercuric reductase; Provisional


Pssm-ID: 184298 [Multi-domain]  Cd Length: 561  Bit Score: 39.75  E-value: 1.21e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 295872338 208 LHIRGMTCASCVAAIEKHCKKIYGLDSILVALLAAKAEVKFNA 250
Cdd:PRK13748   4 LKITGMTCDSCAAHVKDALEKVPGVQSADVSYPKGSAQLAIEV 46
copA PRK10671
copper-exporting P-type ATPase CopA;
7-158 5.84e-03

copper-exporting P-type ATPase CopA;


Pssm-ID: 182635 [Multi-domain]  Cd Length: 834  Bit Score: 37.80  E-value: 5.84e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295872338   7 MS-TVRLPIVGMTCQSCVRNITEHIGQKSGILGVRVILEE-----------------NAGYFDYDPR-QTDPARIaSDID 67
Cdd:PRK10671   1 MSqTIDLTLDGLSCGHCVKRVKESLEQRPDVEQADVSITEahvtgtasaealietikQAGYDASVSHpKAKPLTE-SSIP 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295872338  68 DMGFecsypgdAADPPETPASAWTN-----IRVVGMTCQSCVRNIEGNIGTKPGIHSIEVQLAAKNARVQYDPaqyDPAQ 142
Cdd:PRK10671  80 SEAL-------TAASEELPAATADDddsqqLLLSGMSCASCVSRVQNALQSVPGVTQARVNLAERTALVMGSA---SPQD 149

                        170
                 ....*....|....*.
gi 295872338 143 IAELIDDMGFEASVQE 158
Cdd:PRK10671 150 LVQAVEKAGYGAEAIE 165
 
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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