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Conserved domains on  [gi|347453622|gb|AEO95409|]
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ATP7A, partial [Abrocoma bennettii]

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 ...
 168-225 3.63e-18

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: 75.33  E-value: 3.63e-18
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 347453622 168 VINIDGMTCNSCVQSIEGVISKKKGVKSIQVSLENSNGTIEYDPlLTSPETLKEAIED 225
Cdd:cd00371    1 ELSVEGMTCAGCVSKIEKALEKLPGVESVEVDLETGKATVEYDP-EVSPEELLEAIED 57
HMA cd00371
Heavy-metal-associated domain (HMA) is a conserved domain of approximately 30 amino acid ...
 71-125 3.02e-15

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: 67.63  E-value: 3.02e-15
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 347453622  71 IDGMHCKSCVSNIENALSTLHYVSSVAVSLENRSAIVKYSANlATPEILRKAIEA 125
Cdd:cd00371    4 VEGMTCAGCVSKIEKALEKLPGVESVEVDLETGKATVEYDPE-VSPEELLEAIED 57
copA super family cl32553
copper-exporting P-type ATPase CopA;
9-135 2.34e-07

copper-exporting P-type ATPase CopA;


The actual alignment was detected with superfamily member PRK10671:

Pssm-ID: 182635 [Multi-domain]  Cd Length: 834  Bit Score: 50.90  E-value: 2.34e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347453622   9 TVEEIKKQIEALGFPAYV---KKQPkhLKLGAIDVERLKKTPVRSPEGSQQRSPSYTndltsiFIIDGMHCKSCVSNIEN 85
Cdd:PRK10671  48 SAEALIETIKQAGYDASVshpKAKP--LTESSIPSEALTAASEELPAATADDDDSQQ------LLLSGMSCASCVSRVQN 119

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 347453622  86 ALSTLHYVSSVAVSLENRSAIVKYSANlatPEILrkaIEAVSPGQYTVSI 135
Cdd:PRK10671 120 ALQSVPGVTQARVNLAERTALVMGSAS---PQDL---VQAVEKAGYGAEA 163
 
Name Accession Description Interval E-value
HMA cd00371
Heavy-metal-associated domain (HMA) is a conserved domain of approximately 30 amino acid ...
 168-225 3.63e-18

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: 75.33  E-value: 3.63e-18
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 347453622 168 VINIDGMTCNSCVQSIEGVISKKKGVKSIQVSLENSNGTIEYDPlLTSPETLKEAIED 225
Cdd:cd00371    1 ELSVEGMTCAGCVSKIEKALEKLPGVESVEVDLETGKATVEYDP-EVSPEELLEAIED 57
CopZ COG2608
Copper chaperone CopZ [Inorganic ion transport and metabolism];
166-225 5.74e-17

Copper chaperone CopZ [Inorganic ion transport and metabolism];


Pssm-ID: 442020 [Multi-domain]  Cd Length: 71  Bit Score: 72.24  E-value: 5.74e-17
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 347453622 166 ETVINIDGMTCNSCVQSIEGVISKKKGVKSIQVSLENSNGTIEYDPLLTSPETLKEAIED 225
Cdd:COG2608    3 TVTLKVEGMTCGHCVARVEKALKALDGVASVEVDLATGTATVTYDPEKVSLEDIKAAIEE 62
chaper_CopZ_Bs NF033795
copper chaperone CopZ; This model describes CopZ, a small copper chaperone, as found in ...
 166-225 1.93e-15

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: 68.28  E-value: 1.93e-15
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 347453622 166 ETVINIDGMTCNSCVQSIEGVISKKKGVKSIQVSLENSNGTIEYDPLLTSPETLKEAIED 225
Cdd:NF033795   1 KVTLNVEGMSCGHCVKAVEGALGELNGVSSVKVNLEEGKVDVEFDESKVTLDQIKEAIED 60
HMA cd00371
Heavy-metal-associated domain (HMA) is a conserved domain of approximately 30 amino acid ...
 71-125 3.02e-15

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: 67.63  E-value: 3.02e-15
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 347453622  71 IDGMHCKSCVSNIENALSTLHYVSSVAVSLENRSAIVKYSANlATPEILRKAIEA 125
Cdd:cd00371    4 VEGMTCAGCVSKIEKALEKLPGVESVEVDLETGKATVEYDPE-VSPEELLEAIED 57
CopZ COG2608
Copper chaperone CopZ [Inorganic ion transport and metabolism];
66-126 1.26e-13

Copper chaperone CopZ [Inorganic ion transport and metabolism];


Pssm-ID: 442020 [Multi-domain]  Cd Length: 71  Bit Score: 63.77  E-value: 1.26e-13
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 347453622  66 TSIFIIDGMHCKSCVSNIENALSTLHYVSSVAVSLENRSAIVKYSANLATPEILRKAIEAV 126
Cdd:COG2608    3 TVTLKVEGMTCGHCVARVEKALKALDGVASVEVDLATGTATVTYDPEKVSLEDIKAAIEEA 63
HMA pfam00403
Heavy-metal-associated domain;
168-225 1.39e-13

Heavy-metal-associated domain;


Pssm-ID: 459804 [Multi-domain]  Cd Length: 58  Bit Score: 63.02  E-value: 1.39e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 347453622  168 VINIDGMTCNSCVQSIEGVISKKKGVKSIQVSLENSNGTIEYDPLLTSPETLKEAIED 225
Cdd:pfam00403   1 TFRVSGMHCGGCAAKVEKALSELPGVLSVSVDLATKTVTVTGDAESTKLEKLVEAIEK 58
HMA pfam00403
Heavy-metal-associated domain;
68-125 8.56e-13

Heavy-metal-associated domain;


Pssm-ID: 459804 [Multi-domain]  Cd Length: 58  Bit Score: 61.10  E-value: 8.56e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 347453622   68 IFIIDGMHCKSCVSNIENALSTLHYVSSVAVSLENRSAIVKYSANLATPEILRKAIEA 125
Cdd:pfam00403   1 TFRVSGMHCGGCAAKVEKALSELPGVLSVSVDLATKTVTVTGDAESTKLEKLVEAIEK 58
TIGR00003 TIGR00003
copper ion binding protein; This model describes an apparently copper-specific subfamily of ...
 169-225 9.48e-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: 47.54  E-value: 9.48e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 347453622  169 INIDGMTCNSCVQSIEGVISKKKGVKSIQVSLENSNGTIEYDPLLTSPETLKEAIED 225
Cdd:TIGR00003   4 FQVKGMSCNHCVDKIEKFVGEIEGVSKVKVQLEKEKVVVEFDAPNVSATEICEAILD 60
copA PRK10671
copper-exporting P-type ATPase CopA;
9-135 2.34e-07

copper-exporting P-type ATPase CopA;


Pssm-ID: 182635 [Multi-domain]  Cd Length: 834  Bit Score: 50.90  E-value: 2.34e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347453622   9 TVEEIKKQIEALGFPAYV---KKQPkhLKLGAIDVERLKKTPVRSPEGSQQRSPSYTndltsiFIIDGMHCKSCVSNIEN 85
Cdd:PRK10671  48 SAEALIETIKQAGYDASVshpKAKP--LTESSIPSEALTAASEELPAATADDDDSQQ------LLLSGMSCASCVSRVQN 119

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 347453622  86 ALSTLHYVSSVAVSLENRSAIVKYSANlatPEILrkaIEAVSPGQYTVSI 135
Cdd:PRK10671 120 ALQSVPGVTQARVNLAERTALVMGSAS---PQDL---VQAVEKAGYGAEA 163
PRK13748 PRK13748
putative mercuric reductase; Provisional
 166-224 5.77e-07

putative mercuric reductase; Provisional


Pssm-ID: 184298 [Multi-domain]  Cd Length: 561  Bit Score: 49.38  E-value: 5.77e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 347453622 166 ETVINIDGMTCNSCVQSIEGVISKKKGVKSIQVSLENSNGTIEYDPlLTSPETLKEAIE 224
Cdd:PRK13748   1 MTTLKITGMTCDSCAAHVKDALEKVPGVQSADVSYPKGSAQLAIEV-GTSPDALTAAVA 58
TIGR00003 TIGR00003
copper ion binding protein; This model describes an apparently copper-specific subfamily of ...
 69-124 1.40e-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: 44.45  E-value: 1.40e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 347453622   69 FIIDGMHCKSCVSNIENALSTLHYVSSVAVSLENRSAIVKYSANLATPEILRKAIE 124
Cdd:TIGR00003   4 FQVKGMSCNHCVDKIEKFVGEIEGVSKVKVQLEKEKVVVEFDAPNVSATEICEAIL 59
UxxU_metal_bind NF041115
metal-binding (seleno)protein; Known members of this family are selenoproteins with an ...
 163-224 1.33e-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: 39.24  E-value: 1.33e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 347453622 163 LTHETVINIDGMTCNSCVQSIEGVISKKKGVKSIQVSLENSNGTIEYDPLLTSPETLKEAIE 224
Cdd:NF041115   2 LAETVILAIEGMTUASUPLIAKKALEGLEGVEKADVSYKEGRAEVAFDPDKVSAAQMVDAVN 63
PRK13748 PRK13748
putative mercuric reductase; Provisional
 71-125 5.60e-04

putative mercuric reductase; Provisional


Pssm-ID: 184298 [Multi-domain]  Cd Length: 561  Bit Score: 40.52  E-value: 5.60e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 347453622  71 IDGMHCKSCVSNIENALSTLHYVSSVAVSLENRSAIVKYSANLAtPEILRKAIEA 125
Cdd:PRK13748   6 ITGMTCDSCAAHVKDALEKVPGVQSADVSYPKGSAQLAIEVGTS-PDALTAAVAG 59
 
Name Accession Description Interval E-value
HMA cd00371
Heavy-metal-associated domain (HMA) is a conserved domain of approximately 30 amino acid ...
 168-225 3.63e-18

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: 75.33  E-value: 3.63e-18
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 347453622 168 VINIDGMTCNSCVQSIEGVISKKKGVKSIQVSLENSNGTIEYDPlLTSPETLKEAIED 225
Cdd:cd00371    1 ELSVEGMTCAGCVSKIEKALEKLPGVESVEVDLETGKATVEYDP-EVSPEELLEAIED 57
CopZ COG2608
Copper chaperone CopZ [Inorganic ion transport and metabolism];
166-225 5.74e-17

Copper chaperone CopZ [Inorganic ion transport and metabolism];


Pssm-ID: 442020 [Multi-domain]  Cd Length: 71  Bit Score: 72.24  E-value: 5.74e-17
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 347453622 166 ETVINIDGMTCNSCVQSIEGVISKKKGVKSIQVSLENSNGTIEYDPLLTSPETLKEAIED 225
Cdd:COG2608    3 TVTLKVEGMTCGHCVARVEKALKALDGVASVEVDLATGTATVTYDPEKVSLEDIKAAIEE 62
chaper_CopZ_Bs NF033795
copper chaperone CopZ; This model describes CopZ, a small copper chaperone, as found in ...
 166-225 1.93e-15

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: 68.28  E-value: 1.93e-15
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 347453622 166 ETVINIDGMTCNSCVQSIEGVISKKKGVKSIQVSLENSNGTIEYDPLLTSPETLKEAIED 225
Cdd:NF033795   1 KVTLNVEGMSCGHCVKAVEGALGELNGVSSVKVNLEEGKVDVEFDESKVTLDQIKEAIED 60
HMA cd00371
Heavy-metal-associated domain (HMA) is a conserved domain of approximately 30 amino acid ...
 71-125 3.02e-15

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: 67.63  E-value: 3.02e-15
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 347453622  71 IDGMHCKSCVSNIENALSTLHYVSSVAVSLENRSAIVKYSANlATPEILRKAIEA 125
Cdd:cd00371    4 VEGMTCAGCVSKIEKALEKLPGVESVEVDLETGKATVEYDPE-VSPEELLEAIED 57
CopZ COG2608
Copper chaperone CopZ [Inorganic ion transport and metabolism];
66-126 1.26e-13

Copper chaperone CopZ [Inorganic ion transport and metabolism];


Pssm-ID: 442020 [Multi-domain]  Cd Length: 71  Bit Score: 63.77  E-value: 1.26e-13
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 347453622  66 TSIFIIDGMHCKSCVSNIENALSTLHYVSSVAVSLENRSAIVKYSANLATPEILRKAIEAV 126
Cdd:COG2608    3 TVTLKVEGMTCGHCVARVEKALKALDGVASVEVDLATGTATVTYDPEKVSLEDIKAAIEEA 63
HMA pfam00403
Heavy-metal-associated domain;
168-225 1.39e-13

Heavy-metal-associated domain;


Pssm-ID: 459804 [Multi-domain]  Cd Length: 58  Bit Score: 63.02  E-value: 1.39e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 347453622  168 VINIDGMTCNSCVQSIEGVISKKKGVKSIQVSLENSNGTIEYDPLLTSPETLKEAIED 225
Cdd:pfam00403   1 TFRVSGMHCGGCAAKVEKALSELPGVLSVSVDLATKTVTVTGDAESTKLEKLVEAIEK 58
HMA pfam00403
Heavy-metal-associated domain;
68-125 8.56e-13

Heavy-metal-associated domain;


Pssm-ID: 459804 [Multi-domain]  Cd Length: 58  Bit Score: 61.10  E-value: 8.56e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 347453622   68 IFIIDGMHCKSCVSNIENALSTLHYVSSVAVSLENRSAIVKYSANLATPEILRKAIEA 125
Cdd:pfam00403   1 TFRVSGMHCGGCAAKVEKALSELPGVLSVSVDLATKTVTVTGDAESTKLEKLVEAIEK 58
ZntA COG2217
Cation-transporting P-type ATPase [Inorganic ion transport and metabolism];
166-225 1.34e-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: 1.34e-11
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 347453622 166 ETVINIDGMTCNSCVQSIEGVISKKKGVKSIQVSLENSNGTIEYDPLLTSPETLKEAIED 225
Cdd:COG2217    2 RVRLRIEGMTCAACAWLIEKALRKLPGVLSARVNLATERARVEYDPGKVSLEELIAAVEK 61
ZntA COG2217
Cation-transporting P-type ATPase [Inorganic ion transport and metabolism];
69-142 2.94e-11

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


Pssm-ID: 441819 [Multi-domain]  Cd Length: 717  Bit Score: 62.47  E-value: 2.94e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 347453622  69 FIIDGMHCKSCVSNIENALSTLHYVSSVAVSLENRSAIVKYSANLATPEILRKAIEAVSpgqYTVSIASEGENT 142
Cdd:COG2217    5 LRIEGMTCAACAWLIEKALRKLPGVLSARVNLATERARVEYDPGKVSLEELIAAVEKAG---YEAEPADADAAA 75
TIGR00003 TIGR00003
copper ion binding protein; This model describes an apparently copper-specific subfamily of ...
 169-225 9.48e-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: 47.54  E-value: 9.48e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 347453622  169 INIDGMTCNSCVQSIEGVISKKKGVKSIQVSLENSNGTIEYDPLLTSPETLKEAIED 225
Cdd:TIGR00003   4 FQVKGMSCNHCVDKIEKFVGEIEGVSKVKVQLEKEKVVVEFDAPNVSATEICEAILD 60
copA PRK10671
copper-exporting P-type ATPase CopA;
9-135 2.34e-07

copper-exporting P-type ATPase CopA;


Pssm-ID: 182635 [Multi-domain]  Cd Length: 834  Bit Score: 50.90  E-value: 2.34e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347453622   9 TVEEIKKQIEALGFPAYV---KKQPkhLKLGAIDVERLKKTPVRSPEGSQQRSPSYTndltsiFIIDGMHCKSCVSNIEN 85
Cdd:PRK10671  48 SAEALIETIKQAGYDASVshpKAKP--LTESSIPSEALTAASEELPAATADDDDSQQ------LLLSGMSCASCVSRVQN 119

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 347453622  86 ALSTLHYVSSVAVSLENRSAIVKYSANlatPEILrkaIEAVSPGQYTVSI 135
Cdd:PRK10671 120 ALQSVPGVTQARVNLAERTALVMGSAS---PQDL---VQAVEKAGYGAEA 163
PRK13748 PRK13748
putative mercuric reductase; Provisional
 166-224 5.77e-07

putative mercuric reductase; Provisional


Pssm-ID: 184298 [Multi-domain]  Cd Length: 561  Bit Score: 49.38  E-value: 5.77e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 347453622 166 ETVINIDGMTCNSCVQSIEGVISKKKGVKSIQVSLENSNGTIEYDPlLTSPETLKEAIE 224
Cdd:PRK13748   1 MTTLKITGMTCDSCAAHVKDALEKVPGVQSADVSYPKGSAQLAIEV-GTSPDALTAAVA 58
TIGR00003 TIGR00003
copper ion binding protein; This model describes an apparently copper-specific subfamily of ...
 69-124 1.40e-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: 44.45  E-value: 1.40e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 347453622   69 FIIDGMHCKSCVSNIENALSTLHYVSSVAVSLENRSAIVKYSANLATPEILRKAIE 124
Cdd:TIGR00003   4 FQVKGMSCNHCVDKIEKFVGEIEGVSKVKVQLEKEKVVVEFDAPNVSATEICEAIL 59
UxxU_metal_bind NF041115
metal-binding (seleno)protein; Known members of this family are selenoproteins with an ...
 163-224 1.33e-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: 39.24  E-value: 1.33e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 347453622 163 LTHETVINIDGMTCNSCVQSIEGVISKKKGVKSIQVSLENSNGTIEYDPLLTSPETLKEAIE 224
Cdd:NF041115   2 LAETVILAIEGMTUASUPLIAKKALEGLEGVEKADVSYKEGRAEVAFDPDKVSAAQMVDAVN 63
PRK13748 PRK13748
putative mercuric reductase; Provisional
 71-125 5.60e-04

putative mercuric reductase; Provisional


Pssm-ID: 184298 [Multi-domain]  Cd Length: 561  Bit Score: 40.52  E-value: 5.60e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 347453622  71 IDGMHCKSCVSNIENALSTLHYVSSVAVSLENRSAIVKYSANLAtPEILRKAIEA 125
Cdd:PRK13748   6 ITGMTCDSCAAHVKDALEKVPGVQSADVSYPKGSAQLAIEVGTS-PDALTAAVAG 59
copA PRK10671
copper-exporting P-type ATPase CopA;
60-224 7.61e-04

copper-exporting P-type ATPase CopA;


Pssm-ID: 182635 [Multi-domain]  Cd Length: 834  Bit Score: 40.11  E-value: 7.61e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347453622  60 SYTNDLTsifiIDGMHCKSCVSNIENALSTLHYVSSVAVSLENRSAIVKysanlATPEILrkaIEAVSPGQYTVSIASEG 139
Cdd:PRK10671   2 SQTIDLT----LDGLSCGHCVKRVKESLEQRPDVEQADVSITEAHVTGT-----ASAEAL---IETIKQAGYDASVSHPK 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347453622 140 EN------TSNSLSSSSLQTIPlniVTQPLTHETV-INIDGMTCNSCVQSIEGVISKKKGVKSIQVSLEnsngtiEYDPL 212
Cdd:PRK10671  70 AKpltessIPSEALTAASEELP---AATADDDDSQqLLLSGMSCASCVSRVQNALQSVPGVTQARVNLA------ERTAL 140

                        170
                 ....*....|....*
gi 347453622 213 LT---SPETLKEAIE 224
Cdd:PRK10671 141 VMgsaSPQDLVQAVE 155
PLN02957 PLN02957
copper, zinc superoxide dismutase
 64-124 1.59e-03

copper, zinc superoxide dismutase


Pssm-ID: 215516 [Multi-domain]  Cd Length: 238  Bit Score: 38.58  E-value: 1.59e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 347453622  64 DLTSIFIIDgMHCKSCVSNIENALSTLHYVSSVAVSLENRSAIVKYSANLATpeiLRKAIE 124
Cdd:PLN02957   5 ELLTEFMVD-MKCEGCVAAVKNKLETLEGVKAVEVDLSNQVVRVLGSSPVKA---MTAALE 61
 
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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