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Conserved domains on  [gi|452075|gb|AAA79211|]
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putative [Homo sapiens]

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 ...
 212-274 4.25e-23

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: 90.74  E-value: 4.25e-23
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 452075   212 IAIAGMTCASCVHSIEGMISQLEGVQQISVSLAEGTATVLYNPSViSPEELRAAIEDMGFEAS 274
Cdd:cd00371   2 LSVEGMTCAGCVSKIEKALEKLPGVESVEVDLETGKATVEYDPEV-SPEELLEAIEDAGYKAR 63
HMA cd00371
Heavy-metal-associated domain (HMA) is a conserved domain of approximately 30 amino acid ...
 109-167 4.97e-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: 79.57  E-value: 4.97e-19
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 452075   109 QLRIDGMHCKSCVLNIEENIGQLLGVQSIQVSLENKTAQVKYDPScTSPVALQRAIEAL 167
Cdd:cd00371   1 ELSVEGMTCAGCVSKIEKALEKLPGVESVEVDLETGKATVEYDPE-VSPEELLEAIEDA 58
HMA cd00371
Heavy-metal-associated domain (HMA) is a conserved domain of approximately 30 amino acid ...
 1-58 8.96e-17

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: 73.41  E-value: 8.96e-17
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 452075     1 MTCQSCVSSIEGKVRKLQGVVRVKVSLSNQEAVITYQPYlIQPEDLRDHVNDMGFEAA 58
Cdd:cd00371   7 MTCAGCVSKIEKALEKLPGVESVEVDLETGKATVEYDPE-VSPEELLEAIEDAGYKAR 63
 
Name Accession Description Interval E-value
HMA cd00371
Heavy-metal-associated domain (HMA) is a conserved domain of approximately 30 amino acid ...
 212-274 4.25e-23

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: 90.74  E-value: 4.25e-23
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 452075   212 IAIAGMTCASCVHSIEGMISQLEGVQQISVSLAEGTATVLYNPSViSPEELRAAIEDMGFEAS 274
Cdd:cd00371   2 LSVEGMTCAGCVSKIEKALEKLPGVESVEVDLETGKATVEYDPEV-SPEELLEAIEDAGYKAR 63
CopZ COG2608
Copper chaperone CopZ [Inorganic ion transport and metabolism];
209-277 4.21e-22

Copper chaperone CopZ [Inorganic ion transport and metabolism];


Pssm-ID: 442020 [Multi-domain]  Cd Length: 71  Bit Score: 88.42  E-value: 4.21e-22
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 452075   209 TTLIAIAGMTCASCVHSIEGMISQLEGVQQISVSLAEGTATVLYNPSVISPEELRAAIEDMGFEASVVS 277
Cdd:COG2608   3 TVTLKVEGMTCGHCVARVEKALKALDGVASVEVDLATGTATVTYDPEKVSLEDIKAAIEEAGYEVEKAE 71
HMA cd00371
Heavy-metal-associated domain (HMA) is a conserved domain of approximately 30 amino acid ...
 109-167 4.97e-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: 79.57  E-value: 4.97e-19
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 452075   109 QLRIDGMHCKSCVLNIEENIGQLLGVQSIQVSLENKTAQVKYDPScTSPVALQRAIEAL 167
Cdd:cd00371   1 ELSVEGMTCAGCVSKIEKALEKLPGVESVEVDLETGKATVEYDPE-VSPEELLEAIEDA 58
HMA cd00371
Heavy-metal-associated domain (HMA) is a conserved domain of approximately 30 amino acid ...
 1-58 8.96e-17

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: 73.41  E-value: 8.96e-17
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 452075     1 MTCQSCVSSIEGKVRKLQGVVRVKVSLSNQEAVITYQPYlIQPEDLRDHVNDMGFEAA 58
Cdd:cd00371   7 MTCAGCVSKIEKALEKLPGVESVEVDLETGKATVEYDPE-VSPEELLEAIEDAGYKAR 63
CopZ COG2608
Copper chaperone CopZ [Inorganic ion transport and metabolism];
107-167 3.68e-16

Copper chaperone CopZ [Inorganic ion transport and metabolism];


Pssm-ID: 442020 [Multi-domain]  Cd Length: 71  Bit Score: 72.24  E-value: 3.68e-16
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 452075   107 TLQLRIDGMHCKSCVLNIEENIGQLLGVQSIQVSLENKTAQVKYDPSCTSPVALQRAIEAL 167
Cdd:COG2608   3 TVTLKVEGMTCGHCVARVEKALKALDGVASVEVDLATGTATVTYDPEKVSLEDIKAAIEEA 63
CopZ COG2608
Copper chaperone CopZ [Inorganic ion transport and metabolism];
1-58 1.48e-14

Copper chaperone CopZ [Inorganic ion transport and metabolism];


Pssm-ID: 442020 [Multi-domain]  Cd Length: 71  Bit Score: 67.62  E-value: 1.48e-14
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 452075     1 MTCQSCVSSIEGKVRKLQGVVRVKVSLSNQEAVITYQPYLIQPEDLRDHVNDMGFEAA 58
Cdd:COG2608  11 MTCGHCVARVEKALKALDGVASVEVDLATGTATVTYDPEKVSLEDIKAAIEEAGYEVE 68
UxxU_metal_bind NF041115
metal-binding (seleno)protein; Known members of this family are selenoproteins with an ...
 208-278 3.84e-14

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: 66.59  E-value: 3.84e-14
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 452075    208 STTLIAIAGMTCASCVHSIEGMISQLEGVQQISVSLAEGTATVLYNPSVISPEELRAAIEDMGFEASVVSE 278
Cdd:NF041115   4 ETVILAIEGMTUASUPLIAKKALEGLEGVEKADVSYKEGRAEVAFDPDKVSAAQMVDAVNRIGFRASVIEE 74
HMA pfam00403
Heavy-metal-associated domain;
212-268 4.73e-14

Heavy-metal-associated domain;


Pssm-ID: 459804 [Multi-domain]  Cd Length: 58  Bit Score: 65.72  E-value: 4.73e-14
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 452075     212 IAIAGMTCASCVHSIEGMISQLEGVQQISVSLAEGTATVLYNPSVISPEELRAAIED 268
Cdd:pfam00403   2 FRVSGMHCGGCAAKVEKALSELPGVLSVSVDLATKTVTVTGDAESTKLEKLVEAIEK 58
HMA pfam00403
Heavy-metal-associated domain;
110-166 2.82e-13

Heavy-metal-associated domain;


Pssm-ID: 459804 [Multi-domain]  Cd Length: 58  Bit Score: 63.79  E-value: 2.82e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 452075     110 LRIDGMHCKSCVLNIEENIGQLLGVQSIQVSLENKTAQVKYDPSCTSPVALQRAIEA 166
Cdd:pfam00403   2 FRVSGMHCGGCAAKVEKALSELPGVLSVSVDLATKTVTVTGDAESTKLEKLVEAIEK 58
PRK13748 PRK13748
putative mercuric reductase; Provisional
 210-286 5.44e-11

putative mercuric reductase; Provisional


Pssm-ID: 184298 [Multi-domain]  Cd Length: 561  Bit Score: 63.63  E-value: 5.44e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 452075    210 TLIAIAGMTCASCVHSIEGMISQLEGVQQISVSLAEGTATVLYNPSViSPEELRAAIEDMGFEASVVSESCSTNPLG 286
Cdd:PRK13748   2 TTLKITGMTCDSCAAHVKDALEKVPGVQSADVSYPKGSAQLAIEVGT-SPDALTAAVAGLGYRATLADAPPTDNRGG 77
TIGR00003 TIGR00003
copper ion binding protein; This model describes an apparently copper-specific subfamily of ...
 212-273 3.36e-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: 52.54  E-value: 3.36e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 452075     212 IAIAGMTCASCVHSIEGMISQLEGVQQISVSLAEGTATVLYNPSVISPEELRAAIEDMGFEA 273
Cdd:TIGR00003   4 FQVKGMSCNHCVDKIEKFVGEIEGVSKVKVQLEKEKVVVEFDAPNVSATEICEAILDAGYEV 65
TIGR00003 TIGR00003
copper ion binding protein; This model describes an apparently copper-specific subfamily of ...
 1-58 1.44e-08

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: 50.62  E-value: 1.44e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 452075       1 MTCQSCVSSIEGKVRKLQGVVRVKVSLSNQEAVITYQPYLIQPEDLRDHVNDMGFEAA 58
Cdd:TIGR00003   9 MSCNHCVDKIEKFVGEIEGVSKVKVQLEKEKVVVEFDAPNVSATEICEAILDAGYEVE 66
PRK13748 PRK13748
putative mercuric reductase; Provisional
 110-167 2.52e-08

putative mercuric reductase; Provisional


Pssm-ID: 184298 [Multi-domain]  Cd Length: 561  Bit Score: 55.16  E-value: 2.52e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 452075    110 LRIDGMHCKSCVLNIEENIGQLLGVQSIQVSLENKTAQVKYDPScTSPVALQRAIEAL 167
Cdd:PRK13748   4 LKITGMTCDSCAAHVKDALEKVPGVQSADVSYPKGSAQLAIEVG-TSPDALTAAVAGL 60
TIGR00003 TIGR00003
copper ion binding protein; This model describes an apparently copper-specific subfamily of ...
 110-165 2.94e-08

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: 49.85  E-value: 2.94e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 452075     110 LRIDGMHCKSCVLNIEENIGQLLGVQSIQVSLENKTAQVKYDPSCTSPVALQRAIE 165
Cdd:TIGR00003   4 FQVKGMSCNHCVDKIEKFVGEIEGVSKVKVQLEKEKVVVEFDAPNVSATEICEAIL 59
HMA pfam00403
Heavy-metal-associated domain;
1-47 7.93e-07

Heavy-metal-associated domain;


Pssm-ID: 459804 [Multi-domain]  Cd Length: 58  Bit Score: 45.69  E-value: 7.93e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 452075       1 MTCQSCVSSIEGKVRKLQGVVRVKVSLSNQEAVITYQPYLIQPEDLR 47
Cdd:pfam00403   7 MHCGGCAAKVEKALSELPGVLSVSVDLATKTVTVTGDAESTKLEKLV 53
UxxU_metal_bind NF041115
metal-binding (seleno)protein; Known members of this family are selenoproteins with an ...
 107-156 3.78e-04

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: 38.47  E-value: 3.78e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 452075    107 TLQLRIDGMHCKSCVLNIEENIGQLLGVQSIQVSLENKTAQVKYDPSCTS 156
Cdd:NF041115   5 TVILAIEGMTUASUPLIAKKALEGLEGVEKADVSYKEGRAEVAFDPDKVS 54
PLN02957 PLN02957
copper, zinc superoxide dismutase
 1-57 5.86e-04

copper, zinc superoxide dismutase


Pssm-ID: 215516 [Multi-domain]  Cd Length: 238  Bit Score: 40.89  E-value: 5.86e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 452075      1 MTCQSCVSSIEGKVRKLQGVVRVKVSLSNQEA-VITYQPYliqpEDLRDHVNDMGFEA 57
Cdd:PLN02957  14 MKCEGCVAAVKNKLETLEGVKAVEVDLSNQVVrVLGSSPV----KAMTAALEQTGRKA 67
 
Name Accession Description Interval E-value
HMA cd00371
Heavy-metal-associated domain (HMA) is a conserved domain of approximately 30 amino acid ...
 212-274 4.25e-23

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: 90.74  E-value: 4.25e-23
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 452075   212 IAIAGMTCASCVHSIEGMISQLEGVQQISVSLAEGTATVLYNPSViSPEELRAAIEDMGFEAS 274
Cdd:cd00371   2 LSVEGMTCAGCVSKIEKALEKLPGVESVEVDLETGKATVEYDPEV-SPEELLEAIEDAGYKAR 63
CopZ COG2608
Copper chaperone CopZ [Inorganic ion transport and metabolism];
209-277 4.21e-22

Copper chaperone CopZ [Inorganic ion transport and metabolism];


Pssm-ID: 442020 [Multi-domain]  Cd Length: 71  Bit Score: 88.42  E-value: 4.21e-22
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 452075   209 TTLIAIAGMTCASCVHSIEGMISQLEGVQQISVSLAEGTATVLYNPSVISPEELRAAIEDMGFEASVVS 277
Cdd:COG2608   3 TVTLKVEGMTCGHCVARVEKALKALDGVASVEVDLATGTATVTYDPEKVSLEDIKAAIEEAGYEVEKAE 71
HMA cd00371
Heavy-metal-associated domain (HMA) is a conserved domain of approximately 30 amino acid ...
 109-167 4.97e-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: 79.57  E-value: 4.97e-19
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 452075   109 QLRIDGMHCKSCVLNIEENIGQLLGVQSIQVSLENKTAQVKYDPScTSPVALQRAIEAL 167
Cdd:cd00371   1 ELSVEGMTCAGCVSKIEKALEKLPGVESVEVDLETGKATVEYDPE-VSPEELLEAIEDA 58
ZntA COG2217
Cation-transporting P-type ATPase [Inorganic ion transport and metabolism];
212-279 4.74e-17

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


Pssm-ID: 441819 [Multi-domain]  Cd Length: 717  Bit Score: 82.11  E-value: 4.74e-17
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 452075   212 IAIAGMTCASCVHSIEGMISQLEGVQQISVSLAEGTATVLYNPSVISPEELRAAIEDMGFEASVVSES 279
Cdd:COG2217   5 LRIEGMTCAACAWLIEKALRKLPGVLSARVNLATERARVEYDPGKVSLEELIAAVEKAGYEAEPADAD 72
HMA cd00371
Heavy-metal-associated domain (HMA) is a conserved domain of approximately 30 amino acid ...
 1-58 8.96e-17

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: 73.41  E-value: 8.96e-17
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 452075     1 MTCQSCVSSIEGKVRKLQGVVRVKVSLSNQEAVITYQPYlIQPEDLRDHVNDMGFEAA 58
Cdd:cd00371   7 MTCAGCVSKIEKALEKLPGVESVEVDLETGKATVEYDPE-VSPEELLEAIEDAGYKAR 63
CopZ COG2608
Copper chaperone CopZ [Inorganic ion transport and metabolism];
107-167 3.68e-16

Copper chaperone CopZ [Inorganic ion transport and metabolism];


Pssm-ID: 442020 [Multi-domain]  Cd Length: 71  Bit Score: 72.24  E-value: 3.68e-16
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 452075   107 TLQLRIDGMHCKSCVLNIEENIGQLLGVQSIQVSLENKTAQVKYDPSCTSPVALQRAIEAL 167
Cdd:COG2608   3 TVTLKVEGMTCGHCVARVEKALKALDGVASVEVDLATGTATVTYDPEKVSLEDIKAAIEEA 63
CopZ COG2608
Copper chaperone CopZ [Inorganic ion transport and metabolism];
1-58 1.48e-14

Copper chaperone CopZ [Inorganic ion transport and metabolism];


Pssm-ID: 442020 [Multi-domain]  Cd Length: 71  Bit Score: 67.62  E-value: 1.48e-14
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 452075     1 MTCQSCVSSIEGKVRKLQGVVRVKVSLSNQEAVITYQPYLIQPEDLRDHVNDMGFEAA 58
Cdd:COG2608  11 MTCGHCVARVEKALKALDGVASVEVDLATGTATVTYDPEKVSLEDIKAAIEEAGYEVE 68
UxxU_metal_bind NF041115
metal-binding (seleno)protein; Known members of this family are selenoproteins with an ...
 208-278 3.84e-14

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: 66.59  E-value: 3.84e-14
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 452075    208 STTLIAIAGMTCASCVHSIEGMISQLEGVQQISVSLAEGTATVLYNPSVISPEELRAAIEDMGFEASVVSE 278
Cdd:NF041115   4 ETVILAIEGMTUASUPLIAKKALEGLEGVEKADVSYKEGRAEVAFDPDKVSAAQMVDAVNRIGFRASVIEE 74
HMA pfam00403
Heavy-metal-associated domain;
212-268 4.73e-14

Heavy-metal-associated domain;


Pssm-ID: 459804 [Multi-domain]  Cd Length: 58  Bit Score: 65.72  E-value: 4.73e-14
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 452075     212 IAIAGMTCASCVHSIEGMISQLEGVQQISVSLAEGTATVLYNPSVISPEELRAAIED 268
Cdd:pfam00403   2 FRVSGMHCGGCAAKVEKALSELPGVLSVSVDLATKTVTVTGDAESTKLEKLVEAIEK 58
HMA pfam00403
Heavy-metal-associated domain;
110-166 2.82e-13

Heavy-metal-associated domain;


Pssm-ID: 459804 [Multi-domain]  Cd Length: 58  Bit Score: 63.79  E-value: 2.82e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 452075     110 LRIDGMHCKSCVLNIEENIGQLLGVQSIQVSLENKTAQVKYDPSCTSPVALQRAIEA 166
Cdd:pfam00403   2 FRVSGMHCGGCAAKVEKALSELPGVLSVSVDLATKTVTVTGDAESTKLEKLVEAIEK 58
ZntA COG2217
Cation-transporting P-type ATPase [Inorganic ion transport and metabolism];
107-167 4.10e-13

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


Pssm-ID: 441819 [Multi-domain]  Cd Length: 717  Bit Score: 70.17  E-value: 4.10e-13
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 452075   107 TLQLRIDGMHCKSCVLNIEENIGQLLGVQSIQVSLENKTAQVKYDPSCTSPVALQRAIEAL 167
Cdd:COG2217   2 RVRLRIEGMTCAACAWLIEKALRKLPGVLSARVNLATERARVEYDPGKVSLEELIAAVEKA 62
ZntA COG2217
Cation-transporting P-type ATPase [Inorganic ion transport and metabolism];
1-61 2.02e-11

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


Pssm-ID: 441819 [Multi-domain]  Cd Length: 717  Bit Score: 65.16  E-value: 2.02e-11
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 452075     1 MTCQSCVSSIEGKVRKLQGVVRVKVSLSNQEAVITYQPYLIQPEDLRDHVNDMGFEAAIKS 61
Cdd:COG2217  10 MTCAACAWLIEKALRKLPGVLSARVNLATERARVEYDPGKVSLEELIAAVEKAGYEAEPAD 70
PRK13748 PRK13748
putative mercuric reductase; Provisional
 210-286 5.44e-11

putative mercuric reductase; Provisional


Pssm-ID: 184298 [Multi-domain]  Cd Length: 561  Bit Score: 63.63  E-value: 5.44e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 452075    210 TLIAIAGMTCASCVHSIEGMISQLEGVQQISVSLAEGTATVLYNPSViSPEELRAAIEDMGFEASVVSESCSTNPLG 286
Cdd:PRK13748   2 TTLKITGMTCDSCAAHVKDALEKVPGVQSADVSYPKGSAQLAIEVGT-SPDALTAAVAGLGYRATLADAPPTDNRGG 77
copA PRK10671
copper-exporting P-type ATPase CopA;
107-276 5.76e-10

copper-exporting P-type ATPase CopA;


Pssm-ID: 182635 [Multi-domain]  Cd Length: 834  Bit Score: 60.53  E-value: 5.76e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 452075    107 TLQLRIDGMHCKSCVLNIEENIGQLLGVQSIQVSLE--------------NKTAQVKYDPSCTSPVALQRAIEALPPGNF 172
Cdd:PRK10671   4 TIDLTLDGLSCGHCVKRVKESLEQRPDVEQADVSITeahvtgtasaealiETIKQAGYDASVSHPKAKPLTESSIPSEAL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 452075    173 KVSLPDGAEGSGTDHRsssshspgspprnqvqgtcSTTLIaIAGMTCASCVHSIEGMISQLEGVQQISVSLAEGTATVLY 252
Cdd:PRK10671  84 TAASEELPAATADDDD-------------------SQQLL-LSGMSCASCVSRVQNALQSVPGVTQARVNLAERTALVMG 143

                        170       180
                 ....*....|....*....|....
gi 452075    253 NPsviSPEELRAAIEDMGFEASVV 276
Cdd:PRK10671 144 SA---SPQDLVQAVEKAGYGAEAI 164
TIGR00003 TIGR00003
copper ion binding protein; This model describes an apparently copper-specific subfamily of ...
 212-273 3.36e-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: 52.54  E-value: 3.36e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 452075     212 IAIAGMTCASCVHSIEGMISQLEGVQQISVSLAEGTATVLYNPSVISPEELRAAIEDMGFEA 273
Cdd:TIGR00003   4 FQVKGMSCNHCVDKIEKFVGEIEGVSKVKVQLEKEKVVVEFDAPNVSATEICEAILDAGYEV 65
TIGR00003 TIGR00003
copper ion binding protein; This model describes an apparently copper-specific subfamily of ...
 1-58 1.44e-08

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: 50.62  E-value: 1.44e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 452075       1 MTCQSCVSSIEGKVRKLQGVVRVKVSLSNQEAVITYQPYLIQPEDLRDHVNDMGFEAA 58
Cdd:TIGR00003   9 MSCNHCVDKIEKFVGEIEGVSKVKVQLEKEKVVVEFDAPNVSATEICEAILDAGYEVE 66
PRK13748 PRK13748
putative mercuric reductase; Provisional
 110-167 2.52e-08

putative mercuric reductase; Provisional


Pssm-ID: 184298 [Multi-domain]  Cd Length: 561  Bit Score: 55.16  E-value: 2.52e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 452075    110 LRIDGMHCKSCVLNIEENIGQLLGVQSIQVSLENKTAQVKYDPScTSPVALQRAIEAL 167
Cdd:PRK13748   4 LKITGMTCDSCAAHVKDALEKVPGVQSADVSYPKGSAQLAIEVG-TSPDALTAAVAGL 60
TIGR00003 TIGR00003
copper ion binding protein; This model describes an apparently copper-specific subfamily of ...
 110-165 2.94e-08

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: 49.85  E-value: 2.94e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 452075     110 LRIDGMHCKSCVLNIEENIGQLLGVQSIQVSLENKTAQVKYDPSCTSPVALQRAIE 165
Cdd:TIGR00003   4 FQVKGMSCNHCVDKIEKFVGEIEGVSKVKVQLEKEKVVVEFDAPNVSATEICEAIL 59
HMA pfam00403
Heavy-metal-associated domain;
1-47 7.93e-07

Heavy-metal-associated domain;


Pssm-ID: 459804 [Multi-domain]  Cd Length: 58  Bit Score: 45.69  E-value: 7.93e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 452075       1 MTCQSCVSSIEGKVRKLQGVVRVKVSLSNQEAVITYQPYLIQPEDLR 47
Cdd:pfam00403   7 MHCGGCAAKVEKALSELPGVLSVSVDLATKTVTVTGDAESTKLEKLV 53
UxxU_metal_bind NF041115
metal-binding (seleno)protein; Known members of this family are selenoproteins with an ...
 107-156 3.78e-04

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: 38.47  E-value: 3.78e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 452075    107 TLQLRIDGMHCKSCVLNIEENIGQLLGVQSIQVSLENKTAQVKYDPSCTS 156
Cdd:NF041115   5 TVILAIEGMTUASUPLIAKKALEGLEGVEKADVSYKEGRAEVAFDPDKVS 54
zntA PRK11033
zinc/cadmium/mercury/lead-transporting ATPase; Provisional
 214-272 5.50e-04

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


Pssm-ID: 236827 [Multi-domain]  Cd Length: 741  Bit Score: 41.90  E-value: 5.50e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 452075    214 IAGMTCASCVHSIEGMISQLEGVQQISVSLAEGTATVLYNPSVISPEElrAAIEDMGFE 272
Cdd:PRK11033  59 VSGMDCPSCARKVENAVRQLAGVNQVQVLFATEKLVVDADNDIRAQVE--SAVQKAGFS 115
PLN02957 PLN02957
copper, zinc superoxide dismutase
 1-57 5.86e-04

copper, zinc superoxide dismutase


Pssm-ID: 215516 [Multi-domain]  Cd Length: 238  Bit Score: 40.89  E-value: 5.86e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 452075      1 MTCQSCVSSIEGKVRKLQGVVRVKVSLSNQEA-VITYQPYliqpEDLRDHVNDMGFEA 57
Cdd:PLN02957  14 MKCEGCVAAVKNKLETLEGVKAVEVDLSNQVVrVLGSSPV----KAMTAALEQTGRKA 67
PLN02957 PLN02957
copper, zinc superoxide dismutase
 217-273 7.16e-04

copper, zinc superoxide dismutase


Pssm-ID: 215516 [Multi-domain]  Cd Length: 238  Bit Score: 40.50  E-value: 7.16e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 452075    217 MTCASCVHSIEGMISQLEGVQQISVSLAEGTATVLYNPSVispEELRAAIEDMGFEA 273
Cdd:PLN02957  14 MKCEGCVAAVKNKLETLEGVKAVEVDLSNQVVRVLGSSPV---KAMTAALEQTGRKA 67
 
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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