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Conserved domains on  [gi|594140153|gb|AHL83925|]
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ATPase-7A, partial [Sturnira lilium]

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 ...
 69-126 2.12e-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: 2.12e-17
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 594140153  69 TFTIDGMHCKSCVSNIESALSALQYVSSIAVSLENRSAVVKYNANlVTPEALRKAIEA 126
Cdd:cd00371    1 ELSVEGMTCAGCVSKIEKALEKLPGVESVEVDLETGKATVEYDPE-VSPEELLEAIED 57
HMA cd00371
Heavy-metal-associated domain (HMA) is a conserved domain of approximately 30 amino acid ...
 169-226 2.12e-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: 70.71  E-value: 2.12e-16
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 594140153 169 VINIDGMTCNSCVQSIEGFISKKAGVKSILVSLANSNGTVEYDPlLTSPETLRKAIED 226
Cdd:cd00371    1 ELSVEGMTCAGCVSKIEKALEKLPGVESVEVDLETGKATVEYDP-EVSPEELLEAIED 57
copA super family cl32553
copper-exporting P-type ATPase CopA;
11-125 3.13e-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: 50.51  E-value: 3.13e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594140153  11 EEIKKQIEAAGFPAfikkQPKYPKLGAIDIERLKNTPVKSSEGSQPrsLACADDYSTATFTIDGMHCKSCVSNIESALSA 90
Cdd:PRK10671  50 EALIETIKQAGYDA----SVSHPKAKPLTESSIPSEALTAASEELP--AATADDDDSQQLLLSGMSCASCVSRVQNALQS 123

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 594140153  91 LQYVSSIAVSLENRSAVVKYNANlvtPEALRKAIE 125
Cdd:PRK10671 124 VPGVTQARVNLAERTALVMGSAS---PQDLVQAVE 155
 
Name Accession Description Interval E-value
HMA cd00371
Heavy-metal-associated domain (HMA) is a conserved domain of approximately 30 amino acid ...
 69-126 2.12e-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: 2.12e-17
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 594140153  69 TFTIDGMHCKSCVSNIESALSALQYVSSIAVSLENRSAVVKYNANlVTPEALRKAIEA 126
Cdd:cd00371    1 ELSVEGMTCAGCVSKIEKALEKLPGVESVEVDLETGKATVEYDPE-VSPEELLEAIED 57
CopZ COG2608
Copper chaperone CopZ [Inorganic ion transport and metabolism];
67-127 1.39e-16

Copper chaperone CopZ [Inorganic ion transport and metabolism];


Pssm-ID: 442020 [Multi-domain]  Cd Length: 71  Bit Score: 71.47  E-value: 1.39e-16
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 594140153  67 TATFTIDGMHCKSCVSNIESALSALQYVSSIAVSLENRSAVVKYNANLVTPEALRKAIEAV 127
Cdd:COG2608    3 TVTLKVEGMTCGHCVARVEKALKALDGVASVEVDLATGTATVTYDPEKVSLEDIKAAIEEA 63
HMA cd00371
Heavy-metal-associated domain (HMA) is a conserved domain of approximately 30 amino acid ...
 169-226 2.12e-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: 70.71  E-value: 2.12e-16
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 594140153 169 VINIDGMTCNSCVQSIEGFISKKAGVKSILVSLANSNGTVEYDPlLTSPETLRKAIED 226
Cdd:cd00371    1 ELSVEGMTCAGCVSKIEKALEKLPGVESVEVDLETGKATVEYDP-EVSPEELLEAIED 57
CopZ COG2608
Copper chaperone CopZ [Inorganic ion transport and metabolism];
165-226 7.43e-16

Copper chaperone CopZ [Inorganic ion transport and metabolism];


Pssm-ID: 442020 [Multi-domain]  Cd Length: 71  Bit Score: 69.55  E-value: 7.43e-16
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 594140153 165 TQETVINIDGMTCNSCVQSIEGFISKKAGVKSILVSLANSNGTVEYDPLLTSPETLRKAIED 226
Cdd:COG2608    1 MKTVTLKVEGMTCGHCVARVEKALKALDGVASVEVDLATGTATVTYDPEKVSLEDIKAAIEE 62
HMA pfam00403
Heavy-metal-associated domain;
69-126 7.47e-16

Heavy-metal-associated domain;


Pssm-ID: 459804 [Multi-domain]  Cd Length: 58  Bit Score: 69.19  E-value: 7.47e-16
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 594140153   69 TFTIDGMHCKSCVSNIESALSALQYVSSIAVSLENRSAVVKYNANLVTPEALRKAIEA 126
Cdd:pfam00403   1 TFRVSGMHCGGCAAKVEKALSELPGVLSVSVDLATKTVTVTGDAESTKLEKLVEAIEK 58
chaper_CopZ_Bs NF033795
copper chaperone CopZ; This model describes CopZ, a small copper chaperone, as found in ...
 167-226 1.64e-13

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: 63.27  E-value: 1.64e-13
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 594140153 167 ETVINIDGMTCNSCVQSIEGFISKKAGVKSILVSLANSNGTVEYDPLLTSPETLRKAIED 226
Cdd:NF033795   1 KVTLNVEGMSCGHCVKAVEGALGELNGVSSVKVNLEEGKVDVEFDESKVTLDQIKEAIED 60
HMA pfam00403
Heavy-metal-associated domain;
169-226 1.88e-11

Heavy-metal-associated domain;


Pssm-ID: 459804 [Multi-domain]  Cd Length: 58  Bit Score: 57.63  E-value: 1.88e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 594140153  169 VINIDGMTCNSCVQSIEGFISKKAGVKSILVSLANSNGTVEYDPLLTSPETLRKAIED 226
Cdd:pfam00403   1 TFRVSGMHCGGCAAKVEKALSELPGVLSVSVDLATKTVTVTGDAESTKLEKLVEAIEK 58
TIGR00003 TIGR00003
copper ion binding protein; This model describes an apparently copper-specific subfamily of ...
 69-125 1.56e-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: 1.56e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 594140153   69 TFTIDGMHCKSCVSNIESALSALQYVSSIAVSLENRSAVVKYNANLVTPEALRKAIE 125
Cdd:TIGR00003   3 TFQVKGMSCNHCVDKIEKFVGEIEGVSKVKVQLEKEKVVVEFDAPNVSATEICEAIL 59
PRK13748 PRK13748
putative mercuric reductase; Provisional
 167-225 1.21e-07

putative mercuric reductase; Provisional


Pssm-ID: 184298 [Multi-domain]  Cd Length: 561  Bit Score: 51.69  E-value: 1.21e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 594140153 167 ETVINIDGMTCNSCVQSIEGFISKKAGVKSILVSLANSNGTVEYDPlLTSPETLRKAIE 225
Cdd:PRK13748   1 MTTLKITGMTCDSCAAHVKDALEKVPGVQSADVSYPKGSAQLAIEV-GTSPDALTAAVA 58
copA PRK10671
copper-exporting P-type ATPase CopA;
11-125 3.13e-07

copper-exporting P-type ATPase CopA;


Pssm-ID: 182635 [Multi-domain]  Cd Length: 834  Bit Score: 50.51  E-value: 3.13e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594140153  11 EEIKKQIEAAGFPAfikkQPKYPKLGAIDIERLKNTPVKSSEGSQPrsLACADDYSTATFTIDGMHCKSCVSNIESALSA 90
Cdd:PRK10671  50 EALIETIKQAGYDA----SVSHPKAKPLTESSIPSEALTAASEELP--AATADDDDSQQLLLSGMSCASCVSRVQNALQS 123

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 594140153  91 LQYVSSIAVSLENRSAVVKYNANlvtPEALRKAIE 125
Cdd:PRK10671 124 VPGVTQARVNLAERTALVMGSAS---PQDLVQAVE 155
PRK13748 PRK13748
putative mercuric reductase; Provisional
 69-126 3.72e-07

putative mercuric reductase; Provisional


Pssm-ID: 184298 [Multi-domain]  Cd Length: 561  Bit Score: 50.15  E-value: 3.72e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 594140153  69 TFTIDGMHCKSCVSNIESALSALQYVSSIAVSLENRSAVVKYNANlVTPEALRKAIEA 126
Cdd:PRK13748   3 TLKITGMTCDSCAAHVKDALEKVPGVQSADVSYPKGSAQLAIEVG-TSPDALTAAVAG 59
TIGR00003 TIGR00003
copper ion binding protein; This model describes an apparently copper-specific subfamily of ...
 170-226 9.95e-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: 44.84  E-value: 9.95e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 594140153  170 INIDGMTCNSCVQSIEGFISKKAGVKSILVSLANSNGTVEYDPLLTSPETLRKAIED 226
Cdd:TIGR00003   4 FQVKGMSCNHCVDKIEKFVGEIEGVSKVKVQLEKEKVVVEFDAPNVSATEICEAILD 60
 
Name Accession Description Interval E-value
HMA cd00371
Heavy-metal-associated domain (HMA) is a conserved domain of approximately 30 amino acid ...
 69-126 2.12e-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: 2.12e-17
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 594140153  69 TFTIDGMHCKSCVSNIESALSALQYVSSIAVSLENRSAVVKYNANlVTPEALRKAIEA 126
Cdd:cd00371    1 ELSVEGMTCAGCVSKIEKALEKLPGVESVEVDLETGKATVEYDPE-VSPEELLEAIED 57
CopZ COG2608
Copper chaperone CopZ [Inorganic ion transport and metabolism];
67-127 1.39e-16

Copper chaperone CopZ [Inorganic ion transport and metabolism];


Pssm-ID: 442020 [Multi-domain]  Cd Length: 71  Bit Score: 71.47  E-value: 1.39e-16
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 594140153  67 TATFTIDGMHCKSCVSNIESALSALQYVSSIAVSLENRSAVVKYNANLVTPEALRKAIEAV 127
Cdd:COG2608    3 TVTLKVEGMTCGHCVARVEKALKALDGVASVEVDLATGTATVTYDPEKVSLEDIKAAIEEA 63
HMA cd00371
Heavy-metal-associated domain (HMA) is a conserved domain of approximately 30 amino acid ...
 169-226 2.12e-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: 70.71  E-value: 2.12e-16
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 594140153 169 VINIDGMTCNSCVQSIEGFISKKAGVKSILVSLANSNGTVEYDPlLTSPETLRKAIED 226
Cdd:cd00371    1 ELSVEGMTCAGCVSKIEKALEKLPGVESVEVDLETGKATVEYDP-EVSPEELLEAIED 57
CopZ COG2608
Copper chaperone CopZ [Inorganic ion transport and metabolism];
165-226 7.43e-16

Copper chaperone CopZ [Inorganic ion transport and metabolism];


Pssm-ID: 442020 [Multi-domain]  Cd Length: 71  Bit Score: 69.55  E-value: 7.43e-16
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 594140153 165 TQETVINIDGMTCNSCVQSIEGFISKKAGVKSILVSLANSNGTVEYDPLLTSPETLRKAIED 226
Cdd:COG2608    1 MKTVTLKVEGMTCGHCVARVEKALKALDGVASVEVDLATGTATVTYDPEKVSLEDIKAAIEE 62
HMA pfam00403
Heavy-metal-associated domain;
69-126 7.47e-16

Heavy-metal-associated domain;


Pssm-ID: 459804 [Multi-domain]  Cd Length: 58  Bit Score: 69.19  E-value: 7.47e-16
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 594140153   69 TFTIDGMHCKSCVSNIESALSALQYVSSIAVSLENRSAVVKYNANLVTPEALRKAIEA 126
Cdd:pfam00403   1 TFRVSGMHCGGCAAKVEKALSELPGVLSVSVDLATKTVTVTGDAESTKLEKLVEAIEK 58
chaper_CopZ_Bs NF033795
copper chaperone CopZ; This model describes CopZ, a small copper chaperone, as found in ...
 167-226 1.64e-13

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: 63.27  E-value: 1.64e-13
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 594140153 167 ETVINIDGMTCNSCVQSIEGFISKKAGVKSILVSLANSNGTVEYDPLLTSPETLRKAIED 226
Cdd:NF033795   1 KVTLNVEGMSCGHCVKAVEGALGELNGVSSVKVNLEEGKVDVEFDESKVTLDQIKEAIED 60
ZntA COG2217
Cation-transporting P-type ATPase [Inorganic ion transport and metabolism];
66-127 7.11e-13

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


Pssm-ID: 441819 [Multi-domain]  Cd Length: 717  Bit Score: 67.09  E-value: 7.11e-13
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 594140153  66 STATFTIDGMHCKSCVSNIESALSALQYVSSIAVSLENRSAVVKYNANLVTPEALRKAIEAV 127
Cdd:COG2217    1 ERVRLRIEGMTCAACAWLIEKALRKLPGVLSARVNLATERARVEYDPGKVSLEELIAAVEKA 62
ZntA COG2217
Cation-transporting P-type ATPase [Inorganic ion transport and metabolism];
166-226 7.77e-12

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


Pssm-ID: 441819 [Multi-domain]  Cd Length: 717  Bit Score: 64.01  E-value: 7.77e-12
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 594140153 166 QETVINIDGMTCNSCVQSIEGFISKKAGVKSILVSLANSNGTVEYDPLLTSPETLRKAIED 226
Cdd:COG2217    1 ERVRLRIEGMTCAACAWLIEKALRKLPGVLSARVNLATERARVEYDPGKVSLEELIAAVEK 61
HMA pfam00403
Heavy-metal-associated domain;
169-226 1.88e-11

Heavy-metal-associated domain;


Pssm-ID: 459804 [Multi-domain]  Cd Length: 58  Bit Score: 57.63  E-value: 1.88e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 594140153  169 VINIDGMTCNSCVQSIEGFISKKAGVKSILVSLANSNGTVEYDPLLTSPETLRKAIED 226
Cdd:pfam00403   1 TFRVSGMHCGGCAAKVEKALSELPGVLSVSVDLATKTVTVTGDAESTKLEKLVEAIEK 58
TIGR00003 TIGR00003
copper ion binding protein; This model describes an apparently copper-specific subfamily of ...
 69-125 1.56e-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: 1.56e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 594140153   69 TFTIDGMHCKSCVSNIESALSALQYVSSIAVSLENRSAVVKYNANLVTPEALRKAIE 125
Cdd:TIGR00003   3 TFQVKGMSCNHCVDKIEKFVGEIEGVSKVKVQLEKEKVVVEFDAPNVSATEICEAIL 59
PRK13748 PRK13748
putative mercuric reductase; Provisional
 167-225 1.21e-07

putative mercuric reductase; Provisional


Pssm-ID: 184298 [Multi-domain]  Cd Length: 561  Bit Score: 51.69  E-value: 1.21e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 594140153 167 ETVINIDGMTCNSCVQSIEGFISKKAGVKSILVSLANSNGTVEYDPlLTSPETLRKAIE 225
Cdd:PRK13748   1 MTTLKITGMTCDSCAAHVKDALEKVPGVQSADVSYPKGSAQLAIEV-GTSPDALTAAVA 58
copA PRK10671
copper-exporting P-type ATPase CopA;
11-125 3.13e-07

copper-exporting P-type ATPase CopA;


Pssm-ID: 182635 [Multi-domain]  Cd Length: 834  Bit Score: 50.51  E-value: 3.13e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594140153  11 EEIKKQIEAAGFPAfikkQPKYPKLGAIDIERLKNTPVKSSEGSQPrsLACADDYSTATFTIDGMHCKSCVSNIESALSA 90
Cdd:PRK10671  50 EALIETIKQAGYDA----SVSHPKAKPLTESSIPSEALTAASEELP--AATADDDDSQQLLLSGMSCASCVSRVQNALQS 123

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 594140153  91 LQYVSSIAVSLENRSAVVKYNANlvtPEALRKAIE 125
Cdd:PRK10671 124 VPGVTQARVNLAERTALVMGSAS---PQDLVQAVE 155
PRK13748 PRK13748
putative mercuric reductase; Provisional
 69-126 3.72e-07

putative mercuric reductase; Provisional


Pssm-ID: 184298 [Multi-domain]  Cd Length: 561  Bit Score: 50.15  E-value: 3.72e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 594140153  69 TFTIDGMHCKSCVSNIESALSALQYVSSIAVSLENRSAVVKYNANlVTPEALRKAIEA 126
Cdd:PRK13748   3 TLKITGMTCDSCAAHVKDALEKVPGVQSADVSYPKGSAQLAIEVG-TSPDALTAAVAG 59
TIGR00003 TIGR00003
copper ion binding protein; This model describes an apparently copper-specific subfamily of ...
 170-226 9.95e-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: 44.84  E-value: 9.95e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 594140153  170 INIDGMTCNSCVQSIEGFISKKAGVKSILVSLANSNGTVEYDPLLTSPETLRKAIED 226
Cdd:TIGR00003   4 FQVKGMSCNHCVDKIEKFVGEIEGVSKVKVQLEKEKVVVEFDAPNVSATEICEAILD 60
copA PRK10671
copper-exporting P-type ATPase CopA;
67-225 1.77e-03

copper-exporting P-type ATPase CopA;


Pssm-ID: 182635 [Multi-domain]  Cd Length: 834  Bit Score: 38.95  E-value: 1.77e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594140153  67 TATFTIDGMHCKSCVSNIESALSALQYVSSIAVSLENRS-----------AVVK---YNANLVTPEALRKAIEAVPPgQY 132
Cdd:PRK10671   4 TIDLTLDGLSCGHCVKRVKESLEQRPDVEQADVSITEAHvtgtasaealiETIKqagYDASVSHPKAKPLTESSIPS-EA 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594140153 133 RVSITSgvdstsnspsssclqKLPLHVVSQPLTQETVIniDGMTCNSCVQSIEGFISKKAGVKSILVSLANSNGTVEYDP 212
Cdd:PRK10671  83 LTAASE---------------ELPAATADDDDSQQLLL--SGMSCASCVSRVQNALQSVPGVTQARVNLAERTALVMGSA 145

                        170
                 ....*....|...
gi 594140153 213 lltSPETLRKAIE 225
Cdd:PRK10671 146 ---SPQDLVQAVE 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.
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