NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|347453654|gb|AEO95425|]
View 

ATP7A, partial [Laonastes aenigmamus]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
 168-225 3.11e-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: 73.02  E-value: 3.11e-17
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 347453654 168 VINIAGMTCNSCVQSIEGVISKKAGVKSIHVSLANGNGTVEYDPlLTSPETLREAIED 225
Cdd:cd00371    1 ELSVEGMTCAGCVSKIEKALEKLPGVESVEVDLETGKATVEYDP-EVSPEELLEAIED 57
HMA cd00371
Heavy-metal-associated domain (HMA) is a conserved domain of approximately 30 amino acid ...
 71-123 2.00e-14

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: 65.32  E-value: 2.00e-14
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 347453654  71 IDGMHCKSCVSNIESALSALQFVSNVAISLENKSAVIKYNAGlVTPETLRKAI 123
Cdd:cd00371    4 VEGMTCAGCVSKIEKALEKLPGVESVEVDLETGKATVEYDPE-VSPEELLEAI 55
 
Name Accession Description Interval E-value
HMA cd00371
Heavy-metal-associated domain (HMA) is a conserved domain of approximately 30 amino acid ...
 168-225 3.11e-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: 73.02  E-value: 3.11e-17
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 347453654 168 VINIAGMTCNSCVQSIEGVISKKAGVKSIHVSLANGNGTVEYDPlLTSPETLREAIED 225
Cdd:cd00371    1 ELSVEGMTCAGCVSKIEKALEKLPGVESVEVDLETGKATVEYDP-EVSPEELLEAIED 57
CopZ COG2608
Copper chaperone CopZ [Inorganic ion transport and metabolism];
164-225 5.50e-17

Copper chaperone CopZ [Inorganic ion transport and metabolism];


Pssm-ID: 442020 [Multi-domain]  Cd Length: 71  Bit Score: 72.63  E-value: 5.50e-17
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 347453654 164 TQETVINIAGMTCNSCVQSIEGVISKKAGVKSIHVSLANGNGTVEYDPLLTSPETLREAIED 225
Cdd:COG2608    1 MKTVTLKVEGMTCGHCVARVEKALKALDGVASVEVDLATGTATVTYDPEKVSLEDIKAAIEE 62
chaper_CopZ_Bs NF033795
copper chaperone CopZ; This model describes CopZ, a small copper chaperone, as found in ...
 166-225 8.33e-16

copper chaperone CopZ; This model describes CopZ, a small copper chaperone, as found in Bacillus subtilis and related species. A number of longer protein, such as copper-translocating P-type ATPases, contain multiple CopZ-like domains, with its signature invariant CxxC motif. CopZ from other species may be more different in sequence from this family than some of those domains of longer proteins.


Pssm-ID: 411375 [Multi-domain]  Cd Length: 66  Bit Score: 69.05  E-value: 8.33e-16
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 347453654 166 ETVINIAGMTCNSCVQSIEGVISKKAGVKSIHVSLANGNGTVEYDPLLTSPETLREAIED 225
Cdd:NF033795   1 KVTLNVEGMSCGHCVKAVEGALGELNGVSSVKVNLEEGKVDVEFDESKVTLDQIKEAIED 60
HMA cd00371
Heavy-metal-associated domain (HMA) is a conserved domain of approximately 30 amino acid ...
 71-123 2.00e-14

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: 65.32  E-value: 2.00e-14
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 347453654  71 IDGMHCKSCVSNIESALSALQFVSNVAISLENKSAVIKYNAGlVTPETLRKAI 123
Cdd:cd00371    4 VEGMTCAGCVSKIEKALEKLPGVESVEVDLETGKATVEYDPE-VSPEELLEAI 55
CopZ COG2608
Copper chaperone CopZ [Inorganic ion transport and metabolism];
67-123 9.79e-14

Copper chaperone CopZ [Inorganic ion transport and metabolism];


Pssm-ID: 442020 [Multi-domain]  Cd Length: 71  Bit Score: 63.77  E-value: 9.79e-14
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 347453654  67 AIFIIDGMHCKSCVSNIESALSALQFVSNVAISLENKSAVIKYNAGLVTPETLRKAI 123
Cdd:COG2608    4 VTLKVEGMTCGHCVARVEKALKALDGVASVEVDLATGTATVTYDPEKVSLEDIKAAI 60
HMA pfam00403
Heavy-metal-associated domain;
68-123 1.56e-13

Heavy-metal-associated domain;


Pssm-ID: 459804 [Multi-domain]  Cd Length: 58  Bit Score: 63.02  E-value: 1.56e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 347453654   68 IFIIDGMHCKSCVSNIESALSALQFVSNVAISLENKSAVIKYNAGLVTPETLRKAI 123
Cdd:pfam00403   1 TFRVSGMHCGGCAAKVEKALSELPGVLSVSVDLATKTVTVTGDAESTKLEKLVEAI 56
HMA pfam00403
Heavy-metal-associated domain;
168-225 4.63e-13

Heavy-metal-associated domain;


Pssm-ID: 459804 [Multi-domain]  Cd Length: 58  Bit Score: 61.87  E-value: 4.63e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 347453654  168 VINIAGMTCNSCVQSIEGVISKKAGVKSIHVSLANGNGTVEYDPLLTSPETLREAIED 225
Cdd:pfam00403   1 TFRVSGMHCGGCAAKVEKALSELPGVLSVSVDLATKTVTVTGDAESTKLEKLVEAIEK 58
TIGR00003 TIGR00003
copper ion binding protein; This model describes an apparently copper-specific subfamily of ...
 169-225 6.52e-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: 48.31  E-value: 6.52e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 347453654  169 INIAGMTCNSCVQSIEGVISKKAGVKSIHVSLANGNGTVEYDPLLTSPETLREAIED 225
Cdd:TIGR00003   4 FQVKGMSCNHCVDKIEKFVGEIEGVSKVKVQLEKEKVVVEFDAPNVSATEICEAILD 60
PRK13748 PRK13748
putative mercuric reductase; Provisional
 166-224 2.94e-07

putative mercuric reductase; Provisional


Pssm-ID: 184298 [Multi-domain]  Cd Length: 561  Bit Score: 50.54  E-value: 2.94e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 347453654 166 ETVINIAGMTCNSCVQSIEGVISKKAGVKSIHVSLANGNGTVEYDPlLTSPETLREAIE 224
Cdd:PRK13748   1 MTTLKITGMTCDSCAAHVKDALEKVPGVQSADVSYPKGSAQLAIEV-GTSPDALTAAVA 58
PRK13748 PRK13748
putative mercuric reductase; Provisional
 71-140 1.75e-06

putative mercuric reductase; Provisional


Pssm-ID: 184298 [Multi-domain]  Cd Length: 561  Bit Score: 47.84  E-value: 1.75e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347453654  71 IDGMHCKSCVSNIESALSALQFVSNVAISLENKSAVIKYNAGlVTPETLRKAIVAISpgkYRVSIASEEG 140
Cdd:PRK13748   6 ITGMTCDSCAAHVKDALEKVPGVQSADVSYPKGSAQLAIEVG-TSPDALTAAVAGLG---YRATLADAPP 71
TIGR00003 TIGR00003
copper ion binding protein; This model describes an apparently copper-specific subfamily of ...
 69-123 5.44e-06

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: 42.91  E-value: 5.44e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 347453654   69 FIIDGMHCKSCVSNIESALSALQFVSNVAISLENKSAVIKYNAGLVTPETLRKAI 123
Cdd:TIGR00003   4 FQVKGMSCNHCVDKIEKFVGEIEGVSKVKVQLEKEKVVVEFDAPNVSATEICEAI 58
UxxU_metal_bind NF041115
metal-binding (seleno)protein; Known members of this family are selenoproteins with an ...
 163-224 1.43e-03

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: 36.16  E-value: 1.43e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 347453654 163 LTQETVINIAGMTCNSCVQSIEGVISKKAGVKSIHVSLANGNGTVEYDPLLTSPETLREAIE 224
Cdd:NF041115   2 LAETVILAIEGMTUASUPLIAKKALEGLEGVEKADVSYKEGRAEVAFDPDKVSAAQMVDAVN 63
 
Name Accession Description Interval E-value
HMA cd00371
Heavy-metal-associated domain (HMA) is a conserved domain of approximately 30 amino acid ...
 168-225 3.11e-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: 73.02  E-value: 3.11e-17
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 347453654 168 VINIAGMTCNSCVQSIEGVISKKAGVKSIHVSLANGNGTVEYDPlLTSPETLREAIED 225
Cdd:cd00371    1 ELSVEGMTCAGCVSKIEKALEKLPGVESVEVDLETGKATVEYDP-EVSPEELLEAIED 57
CopZ COG2608
Copper chaperone CopZ [Inorganic ion transport and metabolism];
164-225 5.50e-17

Copper chaperone CopZ [Inorganic ion transport and metabolism];


Pssm-ID: 442020 [Multi-domain]  Cd Length: 71  Bit Score: 72.63  E-value: 5.50e-17
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 347453654 164 TQETVINIAGMTCNSCVQSIEGVISKKAGVKSIHVSLANGNGTVEYDPLLTSPETLREAIED 225
Cdd:COG2608    1 MKTVTLKVEGMTCGHCVARVEKALKALDGVASVEVDLATGTATVTYDPEKVSLEDIKAAIEE 62
chaper_CopZ_Bs NF033795
copper chaperone CopZ; This model describes CopZ, a small copper chaperone, as found in ...
 166-225 8.33e-16

copper chaperone CopZ; This model describes CopZ, a small copper chaperone, as found in Bacillus subtilis and related species. A number of longer protein, such as copper-translocating P-type ATPases, contain multiple CopZ-like domains, with its signature invariant CxxC motif. CopZ from other species may be more different in sequence from this family than some of those domains of longer proteins.


Pssm-ID: 411375 [Multi-domain]  Cd Length: 66  Bit Score: 69.05  E-value: 8.33e-16
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 347453654 166 ETVINIAGMTCNSCVQSIEGVISKKAGVKSIHVSLANGNGTVEYDPLLTSPETLREAIED 225
Cdd:NF033795   1 KVTLNVEGMSCGHCVKAVEGALGELNGVSSVKVNLEEGKVDVEFDESKVTLDQIKEAIED 60
HMA cd00371
Heavy-metal-associated domain (HMA) is a conserved domain of approximately 30 amino acid ...
 71-123 2.00e-14

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: 65.32  E-value: 2.00e-14
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 347453654  71 IDGMHCKSCVSNIESALSALQFVSNVAISLENKSAVIKYNAGlVTPETLRKAI 123
Cdd:cd00371    4 VEGMTCAGCVSKIEKALEKLPGVESVEVDLETGKATVEYDPE-VSPEELLEAI 55
CopZ COG2608
Copper chaperone CopZ [Inorganic ion transport and metabolism];
67-123 9.79e-14

Copper chaperone CopZ [Inorganic ion transport and metabolism];


Pssm-ID: 442020 [Multi-domain]  Cd Length: 71  Bit Score: 63.77  E-value: 9.79e-14
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 347453654  67 AIFIIDGMHCKSCVSNIESALSALQFVSNVAISLENKSAVIKYNAGLVTPETLRKAI 123
Cdd:COG2608    4 VTLKVEGMTCGHCVARVEKALKALDGVASVEVDLATGTATVTYDPEKVSLEDIKAAI 60
HMA pfam00403
Heavy-metal-associated domain;
68-123 1.56e-13

Heavy-metal-associated domain;


Pssm-ID: 459804 [Multi-domain]  Cd Length: 58  Bit Score: 63.02  E-value: 1.56e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 347453654   68 IFIIDGMHCKSCVSNIESALSALQFVSNVAISLENKSAVIKYNAGLVTPETLRKAI 123
Cdd:pfam00403   1 TFRVSGMHCGGCAAKVEKALSELPGVLSVSVDLATKTVTVTGDAESTKLEKLVEAI 56
HMA pfam00403
Heavy-metal-associated domain;
168-225 4.63e-13

Heavy-metal-associated domain;


Pssm-ID: 459804 [Multi-domain]  Cd Length: 58  Bit Score: 61.87  E-value: 4.63e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 347453654  168 VINIAGMTCNSCVQSIEGVISKKAGVKSIHVSLANGNGTVEYDPLLTSPETLREAIED 225
Cdd:pfam00403   1 TFRVSGMHCGGCAAKVEKALSELPGVLSVSVDLATKTVTVTGDAESTKLEKLVEAIEK 58
ZntA COG2217
Cation-transporting P-type ATPase [Inorganic ion transport and metabolism];
165-225 1.30e-12

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


Pssm-ID: 441819 [Multi-domain]  Cd Length: 717  Bit Score: 66.32  E-value: 1.30e-12
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 347453654 165 QETVINIAGMTCNSCVQSIEGVISKKAGVKSIHVSLANGNGTVEYDPLLTSPETLREAIED 225
Cdd:COG2217    1 ERVRLRIEGMTCAACAWLIEKALRKLPGVLSARVNLATERARVEYDPGKVSLEELIAAVEK 61
ZntA COG2217
Cation-transporting P-type ATPase [Inorganic ion transport and metabolism];
69-139 1.33e-11

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


Pssm-ID: 441819 [Multi-domain]  Cd Length: 717  Bit Score: 63.24  E-value: 1.33e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 347453654  69 FIIDGMHCKSCVSNIESALSALQFVSNVAISLENKSAVIKYNAGLVTPETLRKAIVAISpgkYRVSIASEE 139
Cdd:COG2217    5 LRIEGMTCAACAWLIEKALRKLPGVLSARVNLATERARVEYDPGKVSLEELIAAVEKAG---YEAEPADAD 72
TIGR00003 TIGR00003
copper ion binding protein; This model describes an apparently copper-specific subfamily of ...
 169-225 6.52e-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: 48.31  E-value: 6.52e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 347453654  169 INIAGMTCNSCVQSIEGVISKKAGVKSIHVSLANGNGTVEYDPLLTSPETLREAIED 225
Cdd:TIGR00003   4 FQVKGMSCNHCVDKIEKFVGEIEGVSKVKVQLEKEKVVVEFDAPNVSATEICEAILD 60
PRK13748 PRK13748
putative mercuric reductase; Provisional
 166-224 2.94e-07

putative mercuric reductase; Provisional


Pssm-ID: 184298 [Multi-domain]  Cd Length: 561  Bit Score: 50.54  E-value: 2.94e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 347453654 166 ETVINIAGMTCNSCVQSIEGVISKKAGVKSIHVSLANGNGTVEYDPlLTSPETLREAIE 224
Cdd:PRK13748   1 MTTLKITGMTCDSCAAHVKDALEKVPGVQSADVSYPKGSAQLAIEV-GTSPDALTAAVA 58
PRK13748 PRK13748
putative mercuric reductase; Provisional
 71-140 1.75e-06

putative mercuric reductase; Provisional


Pssm-ID: 184298 [Multi-domain]  Cd Length: 561  Bit Score: 47.84  E-value: 1.75e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347453654  71 IDGMHCKSCVSNIESALSALQFVSNVAISLENKSAVIKYNAGlVTPETLRKAIVAISpgkYRVSIASEEG 140
Cdd:PRK13748   6 ITGMTCDSCAAHVKDALEKVPGVQSADVSYPKGSAQLAIEVG-TSPDALTAAVAGLG---YRATLADAPP 71
TIGR00003 TIGR00003
copper ion binding protein; This model describes an apparently copper-specific subfamily of ...
 69-123 5.44e-06

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: 42.91  E-value: 5.44e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 347453654   69 FIIDGMHCKSCVSNIESALSALQFVSNVAISLENKSAVIKYNAGLVTPETLRKAI 123
Cdd:TIGR00003   4 FQVKGMSCNHCVDKIEKFVGEIEGVSKVKVQLEKEKVVVEFDAPNVSATEICEAI 58
copA PRK10671
copper-exporting P-type ATPase CopA;
63-123 4.06e-05

copper-exporting P-type ATPase CopA;


Pssm-ID: 182635 [Multi-domain]  Cd Length: 834  Bit Score: 43.96  E-value: 4.06e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 347453654  63 NDSVAIfIIDGMHCKSCVSNIESALSALQFVSNVAISLENKSAVIkynAGLVTPETLRKAI 123
Cdd:PRK10671  98 DDSQQL-LLSGMSCASCVSRVQNALQSVPGVTQARVNLAERTALV---MGSASPQDLVQAV 154
UxxU_metal_bind NF041115
metal-binding (seleno)protein; Known members of this family are selenoproteins with an ...
 163-224 1.43e-03

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: 36.16  E-value: 1.43e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 347453654 163 LTQETVINIAGMTCNSCVQSIEGVISKKAGVKSIHVSLANGNGTVEYDPLLTSPETLREAIE 224
Cdd:NF041115   2 LAETVILAIEGMTUASUPLIAKKALEGLEGVEKADVSYKEGRAEVAFDPDKVSAAQMVDAVN 63
PLN02957 PLN02957
copper, zinc superoxide dismutase
 69-104 6.41e-03

copper, zinc superoxide dismutase


Pssm-ID: 215516 [Multi-domain]  Cd Length: 238  Bit Score: 36.65  E-value: 6.41e-03
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 347453654  69 FIIDgMHCKSCVSNIESALSALQFVSNVAISLENKS 104
Cdd:PLN02957  10 FMVD-MKCEGCVAAVKNKLETLEGVKAVEVDLSNQV 44
copA PRK10671
copper-exporting P-type ATPase CopA;
68-224 6.42e-03

copper-exporting P-type ATPase CopA;


Pssm-ID: 182635 [Multi-domain]  Cd Length: 834  Bit Score: 37.41  E-value: 6.42e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347453654  68 IFIIDGMHCKSCVSNIESALSALQFVSNVAISLE--------NKSAVIK------YNAGLVTPETLRKAIVAISPGKyrV 133
Cdd:PRK10671   6 DLTLDGLSCGHCVKRVKESLEQRPDVEQADVSITeahvtgtaSAEALIEtikqagYDASVSHPKAKPLTESSIPSEA--L 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347453654 134 SIASEEgstsnspsssslqkIPLNIVTQPLTQETVINiaGMTCNSCVQSIEGVISKKAGVKSIHVSLAngngtvEYDPLL 213
Cdd:PRK10671  84 TAASEE--------------LPAATADDDDSQQLLLS--GMSCASCVSRVQNALQSVPGVTQARVNLA------ERTALV 141

                        170
                 ....*....|....
gi 347453654 214 T---SPETLREAIE 224
Cdd:PRK10671 142 MgsaSPQDLVQAVE 155
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH