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Conserved domains on  [gi|1060647700|dbj|BAV56065|]
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ATPase, Cu++ transporting, alpha polypeptide, partial [Chodsigoa sodalis]

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
CopZ COG2608
Copper chaperone CopZ [Inorganic ion transport and metabolism];
163-223 6.64e-18

Copper chaperone CopZ [Inorganic ion transport and metabolism];


:

Pssm-ID: 442020 [Multi-domain]  Cd Length: 71  Bit Score: 74.94  E-value: 6.64e-18
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1060647700 163 TQETTINIDGMTCNSCVQSIESAISKKAGVKSISVSLANSNGTVEYDPLLTTPETLREAIE 223
Cdd:COG2608     1 MKTVTLKVEGMTCGHCVARVEKALKALDGVASVEVDLATGTATVTYDPEKVSLEDIKAAIE 61
HMA cd00371
Heavy-metal-associated domain (HMA) is a conserved domain of approximately 30 amino acid ...
 67-125 1.66e-16

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: 71.10  E-value: 1.66e-16
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1060647700  67 TFIIDGMHCKSCVSNIESALSTLQYVSSIVVSLENRTAIIKYKAsSVTPEALKRAIEAT 125
Cdd:cd00371     1 ELSVEGMTCAGCVSKIEKALEKLPGVESVEVDLETGKATVEYDP-EVSPEELLEAIEDA 58
copA super family cl32553
copper-exporting P-type ATPase CopA;
8-123 1.33e-06

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: 48.58  E-value: 1.33e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060647700   8 TVEEIKKQIESAGFPAfVKKQPKYLKLGLIDIerlknTPVKSSEGSQQKPLPCVSDSK-VTFIIDGMHCKSCVSNIESAL 86
Cdd:PRK10671   48 SAEALIETIKQAGYDA-SVSHPKAKPLTESSI-----PSEALTAASEELPAATADDDDsQQLLLSGMSCASCVSRVQNAL 121

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1060647700  87 STLQYVSSIVVSLENRTAIIkykASSVTPEALKRAIE 123
Cdd:PRK10671  122 QSVPGVTQARVNLAERTALV---MGSASPQDLVQAVE 155
 
Name Accession Description Interval E-value
CopZ COG2608
Copper chaperone CopZ [Inorganic ion transport and metabolism];
163-223 6.64e-18

Copper chaperone CopZ [Inorganic ion transport and metabolism];


Pssm-ID: 442020 [Multi-domain]  Cd Length: 71  Bit Score: 74.94  E-value: 6.64e-18
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1060647700 163 TQETTINIDGMTCNSCVQSIESAISKKAGVKSISVSLANSNGTVEYDPLLTTPETLREAIE 223
Cdd:COG2608     1 MKTVTLKVEGMTCGHCVARVEKALKALDGVASVEVDLATGTATVTYDPEKVSLEDIKAAIE 61
HMA cd00371
Heavy-metal-associated domain (HMA) is a conserved domain of approximately 30 amino acid ...
 167-223 3.39e-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: 72.64  E-value: 3.39e-17
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1060647700 167 TINIDGMTCNSCVQSIESAISKKAGVKSISVSLANSNGTVEYDPlLTTPETLREAIE 223
Cdd:cd00371     1 ELSVEGMTCAGCVSKIEKALEKLPGVESVEVDLETGKATVEYDP-EVSPEELLEAIE 56
HMA cd00371
Heavy-metal-associated domain (HMA) is a conserved domain of approximately 30 amino acid ...
 67-125 1.66e-16

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: 71.10  E-value: 1.66e-16
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1060647700  67 TFIIDGMHCKSCVSNIESALSTLQYVSSIVVSLENRTAIIKYKAsSVTPEALKRAIEAT 125
Cdd:cd00371     1 ELSVEGMTCAGCVSKIEKALEKLPGVESVEVDLETGKATVEYDP-EVSPEELLEAIEDA 58
chaper_CopZ_Bs NF033795
copper chaperone CopZ; This model describes CopZ, a small copper chaperone, as found in ...
 165-223 1.07e-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: 68.66  E-value: 1.07e-15
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1060647700 165 ETTINIDGMTCNSCVQSIESAISKKAGVKSISVSLANSNGTVEYDPLLTTPETLREAIE 223
Cdd:NF033795    1 KVTLNVEGMSCGHCVKAVEGALGELNGVSSVKVNLEEGKVDVEFDESKVTLDQIKEAIE 59
HMA pfam00403
Heavy-metal-associated domain;
67-124 4.19e-15

Heavy-metal-associated domain;


Pssm-ID: 459804 [Multi-domain]  Cd Length: 58  Bit Score: 67.26  E-value: 4.19e-15
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1060647700  67 TFIIDGMHCKSCVSNIESALSTLQYVSSIVVSLENRTAIIKYKASSVTPEALKRAIEA 124
Cdd:pfam00403   1 TFRVSGMHCGGCAAKVEKALSELPGVLSVSVDLATKTVTVTGDAESTKLEKLVEAIEK 58
CopZ COG2608
Copper chaperone CopZ [Inorganic ion transport and metabolism];
65-125 1.58e-14

Copper chaperone CopZ [Inorganic ion transport and metabolism];


Pssm-ID: 442020 [Multi-domain]  Cd Length: 71  Bit Score: 66.08  E-value: 1.58e-14
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1060647700  65 KVTFIIDGMHCKSCVSNIESALSTLQYVSSIVVSLENRTAIIKYKASSVTPEALKRAIEAT 125
Cdd:COG2608     3 TVTLKVEGMTCGHCVARVEKALKALDGVASVEVDLATGTATVTYDPEKVSLEDIKAAIEEA 63
HMA pfam00403
Heavy-metal-associated domain;
167-223 8.24e-14

Heavy-metal-associated domain;


Pssm-ID: 459804 [Multi-domain]  Cd Length: 58  Bit Score: 63.79  E-value: 8.24e-14
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1060647700 167 TINIDGMTCNSCVQSIESAISKKAGVKSISVSLANSNGTVEYDPLLTTPETLREAIE 223
Cdd:pfam00403   1 TFRVSGMHCGGCAAKVEKALSELPGVLSVSVDLATKTVTVTGDAESTKLEKLVEAIE 57
PRK13748 PRK13748
putative mercuric reductase; Provisional
 165-223 6.19e-09

putative mercuric reductase; Provisional


Pssm-ID: 184298 [Multi-domain]  Cd Length: 561  Bit Score: 55.16  E-value: 6.19e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1060647700 165 ETTINIDGMTCNSCVQSIESAISKKAGVKSISVSLANSNGTVEYDPlLTTPETLREAIE 223
Cdd:PRK13748    1 MTTLKITGMTCDSCAAHVKDALEKVPGVQSADVSYPKGSAQLAIEV-GTSPDALTAAVA 58
TIGR00003 TIGR00003
copper ion binding protein; This model describes an apparently copper-specific subfamily of ...
 65-123 1.20e-07

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: 1.20e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1060647700  65 KVTFIIDGMHCKSCVSNIESALSTLQYVSSIVVSLENRTAIIKYKASSVTPEALKRAIE 123
Cdd:TIGR00003   1 KQTFQVKGMSCNHCVDKIEKFVGEIEGVSKVKVQLEKEKVVVEFDAPNVSATEICEAIL 59
TIGR00003 TIGR00003
copper ion binding protein; This model describes an apparently copper-specific subfamily of ...
 167-223 5.98e-07

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: 45.61  E-value: 5.98e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1060647700 167 TINIDGMTCNSCVQSIESAISKKAGVKSISVSLANSNGTVEYDPLLTTPETLREAIE 223
Cdd:TIGR00003   3 TFQVKGMSCNHCVDKIEKFVGEIEGVSKVKVQLEKEKVVVEFDAPNVSATEICEAIL 59
copA PRK10671
copper-exporting P-type ATPase CopA;
8-123 1.33e-06

copper-exporting P-type ATPase CopA;


Pssm-ID: 182635 [Multi-domain]  Cd Length: 834  Bit Score: 48.58  E-value: 1.33e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060647700   8 TVEEIKKQIESAGFPAfVKKQPKYLKLGLIDIerlknTPVKSSEGSQQKPLPCVSDSK-VTFIIDGMHCKSCVSNIESAL 86
Cdd:PRK10671   48 SAEALIETIKQAGYDA-SVSHPKAKPLTESSI-----PSEALTAASEELPAATADDDDsQQLLLSGMSCASCVSRVQNAL 121

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1060647700  87 STLQYVSSIVVSLENRTAIIkykASSVTPEALKRAIE 123
Cdd:PRK10671  122 QSVPGVTQARVNLAERTALV---MGSASPQDLVQAVE 155
PRK13748 PRK13748
putative mercuric reductase; Provisional
 66-140 1.65e-05

putative mercuric reductase; Provisional


Pssm-ID: 184298 [Multi-domain]  Cd Length: 561  Bit Score: 45.14  E-value: 1.65e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1060647700  66 VTFIIDGMHCKSCVSNIESALSTLQYVSSIVVSLENRTAIIKYKAsSVTPEALKRAIEATSpgkYRVSITNEAEN 140
Cdd:PRK13748    2 TTLKITGMTCDSCAAHVKDALEKVPGVQSADVSYPKGSAQLAIEV-GTSPDALTAAVAGLG---YRATLADAPPT 72
UxxU_metal_bind NF041115
metal-binding (seleno)protein; Known members of this family are selenoproteins with an ...
 162-223 1.30e-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: 1.30e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1060647700 162 LTQETTINIDGMTCNSCVQSIESAISKKAGVKSISVSLANSNGTVEYDPLLTTPETLREAIE 223
Cdd:NF041115    2 LAETVILAIEGMTUASUPLIAKKALEGLEGVEKADVSYKEGRAEVAFDPDKVSAAQMVDAVN 63
 
Name Accession Description Interval E-value
CopZ COG2608
Copper chaperone CopZ [Inorganic ion transport and metabolism];
163-223 6.64e-18

Copper chaperone CopZ [Inorganic ion transport and metabolism];


Pssm-ID: 442020 [Multi-domain]  Cd Length: 71  Bit Score: 74.94  E-value: 6.64e-18
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1060647700 163 TQETTINIDGMTCNSCVQSIESAISKKAGVKSISVSLANSNGTVEYDPLLTTPETLREAIE 223
Cdd:COG2608     1 MKTVTLKVEGMTCGHCVARVEKALKALDGVASVEVDLATGTATVTYDPEKVSLEDIKAAIE 61
HMA cd00371
Heavy-metal-associated domain (HMA) is a conserved domain of approximately 30 amino acid ...
 167-223 3.39e-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: 72.64  E-value: 3.39e-17
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1060647700 167 TINIDGMTCNSCVQSIESAISKKAGVKSISVSLANSNGTVEYDPlLTTPETLREAIE 223
Cdd:cd00371     1 ELSVEGMTCAGCVSKIEKALEKLPGVESVEVDLETGKATVEYDP-EVSPEELLEAIE 56
HMA cd00371
Heavy-metal-associated domain (HMA) is a conserved domain of approximately 30 amino acid ...
 67-125 1.66e-16

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: 71.10  E-value: 1.66e-16
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1060647700  67 TFIIDGMHCKSCVSNIESALSTLQYVSSIVVSLENRTAIIKYKAsSVTPEALKRAIEAT 125
Cdd:cd00371     1 ELSVEGMTCAGCVSKIEKALEKLPGVESVEVDLETGKATVEYDP-EVSPEELLEAIEDA 58
chaper_CopZ_Bs NF033795
copper chaperone CopZ; This model describes CopZ, a small copper chaperone, as found in ...
 165-223 1.07e-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: 68.66  E-value: 1.07e-15
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1060647700 165 ETTINIDGMTCNSCVQSIESAISKKAGVKSISVSLANSNGTVEYDPLLTTPETLREAIE 223
Cdd:NF033795    1 KVTLNVEGMSCGHCVKAVEGALGELNGVSSVKVNLEEGKVDVEFDESKVTLDQIKEAIE 59
HMA pfam00403
Heavy-metal-associated domain;
67-124 4.19e-15

Heavy-metal-associated domain;


Pssm-ID: 459804 [Multi-domain]  Cd Length: 58  Bit Score: 67.26  E-value: 4.19e-15
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1060647700  67 TFIIDGMHCKSCVSNIESALSTLQYVSSIVVSLENRTAIIKYKASSVTPEALKRAIEA 124
Cdd:pfam00403   1 TFRVSGMHCGGCAAKVEKALSELPGVLSVSVDLATKTVTVTGDAESTKLEKLVEAIEK 58
CopZ COG2608
Copper chaperone CopZ [Inorganic ion transport and metabolism];
65-125 1.58e-14

Copper chaperone CopZ [Inorganic ion transport and metabolism];


Pssm-ID: 442020 [Multi-domain]  Cd Length: 71  Bit Score: 66.08  E-value: 1.58e-14
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1060647700  65 KVTFIIDGMHCKSCVSNIESALSTLQYVSSIVVSLENRTAIIKYKASSVTPEALKRAIEAT 125
Cdd:COG2608     3 TVTLKVEGMTCGHCVARVEKALKALDGVASVEVDLATGTATVTYDPEKVSLEDIKAAIEEA 63
ZntA COG2217
Cation-transporting P-type ATPase [Inorganic ion transport and metabolism];
164-223 5.46e-14

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


Pssm-ID: 441819 [Multi-domain]  Cd Length: 717  Bit Score: 70.17  E-value: 5.46e-14
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060647700 164 QETTINIDGMTCNSCVQSIESAISKKAGVKSISVSLANSNGTVEYDPLLTTPETLREAIE 223
Cdd:COG2217     1 ERVRLRIEGMTCAACAWLIEKALRKLPGVLSARVNLATERARVEYDPGKVSLEELIAAVE 60
HMA pfam00403
Heavy-metal-associated domain;
167-223 8.24e-14

Heavy-metal-associated domain;


Pssm-ID: 459804 [Multi-domain]  Cd Length: 58  Bit Score: 63.79  E-value: 8.24e-14
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1060647700 167 TINIDGMTCNSCVQSIESAISKKAGVKSISVSLANSNGTVEYDPLLTTPETLREAIE 223
Cdd:pfam00403   1 TFRVSGMHCGGCAAKVEKALSELPGVLSVSVDLATKTVTVTGDAESTKLEKLVEAIE 57
ZntA COG2217
Cation-transporting P-type ATPase [Inorganic ion transport and metabolism];
64-141 1.46e-12

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


Pssm-ID: 441819 [Multi-domain]  Cd Length: 717  Bit Score: 65.93  E-value: 1.46e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1060647700  64 SKVTFIIDGMHCKSCVSNIESALSTLQYVSSIVVSLENRTAIIKYKASSVTPEALKRAIEATSpgkYRVSITNEAENT 141
Cdd:COG2217     1 ERVRLRIEGMTCAACAWLIEKALRKLPGVLSARVNLATERARVEYDPGKVSLEELIAAVEKAG---YEAEPADADAAA 75
PRK13748 PRK13748
putative mercuric reductase; Provisional
 165-223 6.19e-09

putative mercuric reductase; Provisional


Pssm-ID: 184298 [Multi-domain]  Cd Length: 561  Bit Score: 55.16  E-value: 6.19e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1060647700 165 ETTINIDGMTCNSCVQSIESAISKKAGVKSISVSLANSNGTVEYDPlLTTPETLREAIE 223
Cdd:PRK13748    1 MTTLKITGMTCDSCAAHVKDALEKVPGVQSADVSYPKGSAQLAIEV-GTSPDALTAAVA 58
TIGR00003 TIGR00003
copper ion binding protein; This model describes an apparently copper-specific subfamily of ...
 65-123 1.20e-07

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: 1.20e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1060647700  65 KVTFIIDGMHCKSCVSNIESALSTLQYVSSIVVSLENRTAIIKYKASSVTPEALKRAIE 123
Cdd:TIGR00003   1 KQTFQVKGMSCNHCVDKIEKFVGEIEGVSKVKVQLEKEKVVVEFDAPNVSATEICEAIL 59
TIGR00003 TIGR00003
copper ion binding protein; This model describes an apparently copper-specific subfamily of ...
 167-223 5.98e-07

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: 45.61  E-value: 5.98e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1060647700 167 TINIDGMTCNSCVQSIESAISKKAGVKSISVSLANSNGTVEYDPLLTTPETLREAIE 223
Cdd:TIGR00003   3 TFQVKGMSCNHCVDKIEKFVGEIEGVSKVKVQLEKEKVVVEFDAPNVSATEICEAIL 59
copA PRK10671
copper-exporting P-type ATPase CopA;
8-123 1.33e-06

copper-exporting P-type ATPase CopA;


Pssm-ID: 182635 [Multi-domain]  Cd Length: 834  Bit Score: 48.58  E-value: 1.33e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060647700   8 TVEEIKKQIESAGFPAfVKKQPKYLKLGLIDIerlknTPVKSSEGSQQKPLPCVSDSK-VTFIIDGMHCKSCVSNIESAL 86
Cdd:PRK10671   48 SAEALIETIKQAGYDA-SVSHPKAKPLTESSI-----PSEALTAASEELPAATADDDDsQQLLLSGMSCASCVSRVQNAL 121

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1060647700  87 STLQYVSSIVVSLENRTAIIkykASSVTPEALKRAIE 123
Cdd:PRK10671  122 QSVPGVTQARVNLAERTALV---MGSASPQDLVQAVE 155
PRK13748 PRK13748
putative mercuric reductase; Provisional
 66-140 1.65e-05

putative mercuric reductase; Provisional


Pssm-ID: 184298 [Multi-domain]  Cd Length: 561  Bit Score: 45.14  E-value: 1.65e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1060647700  66 VTFIIDGMHCKSCVSNIESALSTLQYVSSIVVSLENRTAIIKYKAsSVTPEALKRAIEATSpgkYRVSITNEAEN 140
Cdd:PRK13748    2 TTLKITGMTCDSCAAHVKDALEKVPGVQSADVSYPKGSAQLAIEV-GTSPDALTAAVAGLG---YRATLADAPPT 72
copA PRK10671
copper-exporting P-type ATPase CopA;
70-223 1.13e-04

copper-exporting P-type ATPase CopA;


Pssm-ID: 182635 [Multi-domain]  Cd Length: 834  Bit Score: 42.81  E-value: 1.13e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060647700  70 IDGMHCKSCVSNIESALSTLQYVSSIVVSLENRTAIikykaSSVTPEALkraIEATSPGKYRVSITNEAEN--TSNSPSS 147
Cdd:PRK10671    9 LDGLSCGHCVKRVKESLEQRPDVEQADVSITEAHVT-----GTASAEAL---IETIKQAGYDASVSHPKAKplTESSIPS 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1060647700 148 SSLQKVPLNIVSQPLTQETTIN--IDGMTCNSCVQSIESAISKKAGVKSISVSLANSNGTVEYDPLlttPETLREAIE 223
Cdd:PRK10671   81 EALTAASEELPAATADDDDSQQllLSGMSCASCVSRVQNALQSVPGVTQARVNLAERTALVMGSAS---PQDLVQAVE 155
UxxU_metal_bind NF041115
metal-binding (seleno)protein; Known members of this family are selenoproteins with an ...
 162-223 1.30e-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: 1.30e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1060647700 162 LTQETTINIDGMTCNSCVQSIESAISKKAGVKSISVSLANSNGTVEYDPLLTTPETLREAIE 223
Cdd:NF041115    2 LAETVILAIEGMTUASUPLIAKKALEGLEGVEKADVSYKEGRAEVAFDPDKVSAAQMVDAVN 63
PLN02957 PLN02957
copper, zinc superoxide dismutase
 173-223 6.50e-04

copper, zinc superoxide dismutase


Pssm-ID: 215516 [Multi-domain]  Cd Length: 238  Bit Score: 39.73  E-value: 6.50e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1060647700 173 MTCNSCVQSIESAISKKAGVKSISVSLANSNGTVeydpLLTTPE-TLREAIE 223
Cdd:PLN02957   14 MKCEGCVAAVKNKLETLEGVKAVEVDLSNQVVRV----LGSSPVkAMTAALE 61
zntA PRK11033
zinc/cadmium/mercury/lead-transporting ATPase; Provisional
 170-223 1.49e-03

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


Pssm-ID: 236827 [Multi-domain]  Cd Length: 741  Bit Score: 39.21  E-value: 1.49e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1060647700 170 IDGMTCNSCVQSIESAISKKAGVKSISVSLANSNGTVEYDPllttpeTLREAIE 223
Cdd:PRK11033   59 VSGMDCPSCARKVENAVRQLAGVNQVQVLFATEKLVVDADN------DIRAQVE 106
 
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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