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Conserved domains on  [gi|1928162936|gb|QOX06120|]
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copper-transporting ATPase 1, partial [Caiman latirostris]

Protein Classification

heavy-metal-associated domain-containing protein( domain architecture ID 10086127)

heavy-metal-associated domain-containing protein such as heavy metal-associated isoprenylated plant proteins and Saccharomyces cerevisiae copper transport protein ATX1, which shuttles copper to the transport ATPase CCC2 and protects against oxygen toxicity

CATH:  3.30.70.100
Gene Ontology:  GO:0046872
PubMed:  12443926|8905098
SCOP:  4001253

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CopZ COG2608
Copper chaperone CopZ [Inorganic ion transport and metabolism];
67-128 1.08e-14

Copper chaperone CopZ [Inorganic ion transport and metabolism];


:

Pssm-ID: 442020 [Multi-domain]  Cd Length: 71  Bit Score: 66.47  E-value: 1.08e-14
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1928162936  67 KTIVFRVNGMHCNSCISNIQSTISALPSVASIVVSLEKKSALVKYNPNLIHVDALRRAIEAV 128
Cdd:COG2608     2 KTVTLKVEGMTCGHCVARVEKALKALDGVASVEVDLATGTATVTYDPEKVSLEDIKAAIEEA 63
HMA cd00371
Heavy-metal-associated domain (HMA) is a conserved domain of approximately 30 amino acid ...
 170-226 1.95e-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: 65.70  E-value: 1.95e-14
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1928162936 170 VINIAGMTCNSCAQSIEGVISQKPGVKSIHVSLVNHNGTIEYDPlLTSPEDLISSIK 226
Cdd:cd00371     1 ELSVEGMTCAGCVSKIEKALEKLPGVESVEVDLETGKATVEYDP-EVSPEELLEAIE 56
copA super family cl32553
copper-exporting P-type ATPase CopA;
10-109 2.18e-04

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: 41.65  E-value: 2.18e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928162936  10 TAEEIKNQIEAAGFTASIKK-QLKPLKLGAIDVERLKntqTKSSEGMLQKSpkhmNDLKTIVFRVNGMHCNSCISNIQST 88
Cdd:PRK10671   48 SAEALIETIKQAGYDASVSHpKAKPLTESSIPSEALT---AASEELPAATA----DDDDSQQLLLSGMSCASCVSRVQNA 120

                          90       100
                  ....*....|....*....|.
gi 1928162936  89 ISALPSVASIVVSLEKKSALV 109
Cdd:PRK10671  121 LQSVPGVTQARVNLAERTALV 141
 
Name Accession Description Interval E-value
CopZ COG2608
Copper chaperone CopZ [Inorganic ion transport and metabolism];
67-128 1.08e-14

Copper chaperone CopZ [Inorganic ion transport and metabolism];


Pssm-ID: 442020 [Multi-domain]  Cd Length: 71  Bit Score: 66.47  E-value: 1.08e-14
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1928162936  67 KTIVFRVNGMHCNSCISNIQSTISALPSVASIVVSLEKKSALVKYNPNLIHVDALRRAIEAV 128
Cdd:COG2608     2 KTVTLKVEGMTCGHCVARVEKALKALDGVASVEVDLATGTATVTYDPEKVSLEDIKAAIEEA 63
HMA cd00371
Heavy-metal-associated domain (HMA) is a conserved domain of approximately 30 amino acid ...
 170-226 1.95e-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: 65.70  E-value: 1.95e-14
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1928162936 170 VINIAGMTCNSCAQSIEGVISQKPGVKSIHVSLVNHNGTIEYDPlLTSPEDLISSIK 226
Cdd:cd00371     1 ELSVEGMTCAGCVSKIEKALEKLPGVESVEVDLETGKATVEYDP-EVSPEELLEAIE 56
CopZ COG2608
Copper chaperone CopZ [Inorganic ion transport and metabolism];
166-226 4.59e-14

Copper chaperone CopZ [Inorganic ion transport and metabolism];


Pssm-ID: 442020 [Multi-domain]  Cd Length: 71  Bit Score: 64.93  E-value: 4.59e-14
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1928162936 166 TQVTVINIAGMTCNSCAQSIEGVISQKPGVKSIHVSLVNHNGTIEYDPLLTSPEDLISSIK 226
Cdd:COG2608     1 MKTVTLKVEGMTCGHCVARVEKALKALDGVASVEVDLATGTATVTYDPEKVSLEDIKAAIE 61
HMA cd00371
Heavy-metal-associated domain (HMA) is a conserved domain of approximately 30 amino acid ...
 70-127 1.72e-13

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: 63.01  E-value: 1.72e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1928162936  70 VFRVNGMHCNSCISNIQSTISALPSVASIVVSLEKKSALVKYNPNlIHVDALRRAIEA 127
Cdd:cd00371     1 ELSVEGMTCAGCVSKIEKALEKLPGVESVEVDLETGKATVEYDPE-VSPEELLEAIED 57
HMA pfam00403
Heavy-metal-associated domain;
70-127 2.34e-13

Heavy-metal-associated domain;


Pssm-ID: 459804 [Multi-domain]  Cd Length: 58  Bit Score: 62.64  E-value: 2.34e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1928162936  70 VFRVNGMHCNSCISNIQSTISALPSVASIVVSLEKKSALVKYNPNLIHVDALRRAIEA 127
Cdd:pfam00403   1 TFRVSGMHCGGCAAKVEKALSELPGVLSVSVDLATKTVTVTGDAESTKLEKLVEAIEK 58
HMA pfam00403
Heavy-metal-associated domain;
170-226 4.59e-12

Heavy-metal-associated domain;


Pssm-ID: 459804 [Multi-domain]  Cd Length: 58  Bit Score: 59.17  E-value: 4.59e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1928162936 170 VINIAGMTCNSCAQSIEGVISQKPGVKSIHVSLVNHNGTIEYDPLLTSPEDLISSIK 226
Cdd:pfam00403   1 TFRVSGMHCGGCAAKVEKALSELPGVLSVSVDLATKTVTVTGDAESTKLEKLVEAIE 57
TIGR00003 TIGR00003
copper ion binding protein; This model describes an apparently copper-specific subfamily of ...
 69-126 7.00e-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: 45.22  E-value: 7.00e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1928162936  69 IVFRVNGMHCNSCISNIQSTISALPSVASIVVSLEKKSALVKYNPNLIHVDALRRAIE 126
Cdd:TIGR00003   2 QTFQVKGMSCNHCVDKIEKFVGEIEGVSKVKVQLEKEKVVVEFDAPNVSATEICEAIL 59
PRK13748 PRK13748
putative mercuric reductase; Provisional
 69-178 9.04e-07

putative mercuric reductase; Provisional


Pssm-ID: 184298 [Multi-domain]  Cd Length: 561  Bit Score: 48.99  E-value: 9.04e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928162936  69 IVFRVNGMHCNSCISNIQSTISALPSVASIVVSLEKKSALVKYNPNlIHVDALRRAIEAVSpetYKVSLPDE----YEDA 144
Cdd:PRK13748    2 TTLKITGMTCDSCAAHVKDALEKVPGVQSADVSYPKGSAQLAIEVG-TSPDALTAAVAGLG---YRATLADApptdNRGG 77

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1928162936 145 ELLNTQASPVKSPLNRNKWPLTQVTVINI--AGMTC 178
Cdd:PRK13748   78 LLDKMRGWLGGADKHSGNERPLHVAVIGSggAAMAA 113
PRK13748 PRK13748
putative mercuric reductase; Provisional
 169-226 2.05e-06

putative mercuric reductase; Provisional


Pssm-ID: 184298 [Multi-domain]  Cd Length: 561  Bit Score: 47.84  E-value: 2.05e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1928162936 169 TVINIAGMTCNSCAQSIEGVISQKPGVKSIHVSLVNHNGTIEYDPlLTSPEDLISSIK 226
Cdd:PRK13748    2 TTLKITGMTCDSCAAHVKDALEKVPGVQSADVSYPKGSAQLAIEV-GTSPDALTAAVA 58
copA PRK10671
copper-exporting P-type ATPase CopA;
10-109 2.18e-04

copper-exporting P-type ATPase CopA;


Pssm-ID: 182635 [Multi-domain]  Cd Length: 834  Bit Score: 41.65  E-value: 2.18e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928162936  10 TAEEIKNQIEAAGFTASIKK-QLKPLKLGAIDVERLKntqTKSSEGMLQKSpkhmNDLKTIVFRVNGMHCNSCISNIQST 88
Cdd:PRK10671   48 SAEALIETIKQAGYDASVSHpKAKPLTESSIPSEALT---AASEELPAATA----DDDDSQQLLLSGMSCASCVSRVQNA 120

                          90       100
                  ....*....|....*....|.
gi 1928162936  89 ISALPSVASIVVSLEKKSALV 109
Cdd:PRK10671  121 LQSVPGVTQARVNLAERTALV 141
TIGR00003 TIGR00003
copper ion binding protein; This model describes an apparently copper-specific subfamily of ...
 171-225 4.61e-04

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: 37.52  E-value: 4.61e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1928162936 171 INIAGMTCNSCAQSIEGVISQKPGVKSIHVSLVNHNGTIEYDPLLTSPEDLISSI 225
Cdd:TIGR00003   4 FQVKGMSCNHCVDKIEKFVGEIEGVSKVKVQLEKEKVVVEFDAPNVSATEICEAI 58
UxxU_metal_bind NF041115
metal-binding (seleno)protein; Known members of this family are selenoproteins with an ...
 165-225 2.81e-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: 35.39  E-value: 2.81e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1928162936 165 LTQVTVINIAGMTCNSCAQSIEGVISQKPGVKSIHVSLVNHNGTIEYDPLLTSPEDLISSI 225
Cdd:NF041115    2 LAETVILAIEGMTUASUPLIAKKALEGLEGVEKADVSYKEGRAEVAFDPDKVSAAQMVDAV 62
 
Name Accession Description Interval E-value
CopZ COG2608
Copper chaperone CopZ [Inorganic ion transport and metabolism];
67-128 1.08e-14

Copper chaperone CopZ [Inorganic ion transport and metabolism];


Pssm-ID: 442020 [Multi-domain]  Cd Length: 71  Bit Score: 66.47  E-value: 1.08e-14
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1928162936  67 KTIVFRVNGMHCNSCISNIQSTISALPSVASIVVSLEKKSALVKYNPNLIHVDALRRAIEAV 128
Cdd:COG2608     2 KTVTLKVEGMTCGHCVARVEKALKALDGVASVEVDLATGTATVTYDPEKVSLEDIKAAIEEA 63
HMA cd00371
Heavy-metal-associated domain (HMA) is a conserved domain of approximately 30 amino acid ...
 170-226 1.95e-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: 65.70  E-value: 1.95e-14
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1928162936 170 VINIAGMTCNSCAQSIEGVISQKPGVKSIHVSLVNHNGTIEYDPlLTSPEDLISSIK 226
Cdd:cd00371     1 ELSVEGMTCAGCVSKIEKALEKLPGVESVEVDLETGKATVEYDP-EVSPEELLEAIE 56
CopZ COG2608
Copper chaperone CopZ [Inorganic ion transport and metabolism];
166-226 4.59e-14

Copper chaperone CopZ [Inorganic ion transport and metabolism];


Pssm-ID: 442020 [Multi-domain]  Cd Length: 71  Bit Score: 64.93  E-value: 4.59e-14
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1928162936 166 TQVTVINIAGMTCNSCAQSIEGVISQKPGVKSIHVSLVNHNGTIEYDPLLTSPEDLISSIK 226
Cdd:COG2608     1 MKTVTLKVEGMTCGHCVARVEKALKALDGVASVEVDLATGTATVTYDPEKVSLEDIKAAIE 61
HMA cd00371
Heavy-metal-associated domain (HMA) is a conserved domain of approximately 30 amino acid ...
 70-127 1.72e-13

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: 63.01  E-value: 1.72e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1928162936  70 VFRVNGMHCNSCISNIQSTISALPSVASIVVSLEKKSALVKYNPNlIHVDALRRAIEA 127
Cdd:cd00371     1 ELSVEGMTCAGCVSKIEKALEKLPGVESVEVDLETGKATVEYDPE-VSPEELLEAIED 57
HMA pfam00403
Heavy-metal-associated domain;
70-127 2.34e-13

Heavy-metal-associated domain;


Pssm-ID: 459804 [Multi-domain]  Cd Length: 58  Bit Score: 62.64  E-value: 2.34e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1928162936  70 VFRVNGMHCNSCISNIQSTISALPSVASIVVSLEKKSALVKYNPNLIHVDALRRAIEA 127
Cdd:pfam00403   1 TFRVSGMHCGGCAAKVEKALSELPGVLSVSVDLATKTVTVTGDAESTKLEKLVEAIEK 58
ZntA COG2217
Cation-transporting P-type ATPase [Inorganic ion transport and metabolism];
67-145 2.56e-12

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


Pssm-ID: 441819 [Multi-domain]  Cd Length: 717  Bit Score: 65.55  E-value: 2.56e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1928162936  67 KTIVFRVNGMHCNSCISNIQSTISALPSVASIVVSLEKKSALVKYNPNLIHVDALRRAIEAVSpetYKVSLPDEYEDAE 145
Cdd:COG2217     1 ERVRLRIEGMTCAACAWLIEKALRKLPGVLSARVNLATERARVEYDPGKVSLEELIAAVEKAG---YEAEPADADAAAE 76
HMA pfam00403
Heavy-metal-associated domain;
170-226 4.59e-12

Heavy-metal-associated domain;


Pssm-ID: 459804 [Multi-domain]  Cd Length: 58  Bit Score: 59.17  E-value: 4.59e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1928162936 170 VINIAGMTCNSCAQSIEGVISQKPGVKSIHVSLVNHNGTIEYDPLLTSPEDLISSIK 226
Cdd:pfam00403   1 TFRVSGMHCGGCAAKVEKALSELPGVLSVSVDLATKTVTVTGDAESTKLEKLVEAIE 57
ZntA COG2217
Cation-transporting P-type ATPase [Inorganic ion transport and metabolism];
167-226 2.31e-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: 2.31e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928162936 167 QVTVINIAGMTCNSCAQSIEGVISQKPGVKSIHVSLVNHNGTIEYDPLLTSPEDLISSIK 226
Cdd:COG2217     1 ERVRLRIEGMTCAACAWLIEKALRKLPGVLSARVNLATERARVEYDPGKVSLEELIAAVE 60
TIGR00003 TIGR00003
copper ion binding protein; This model describes an apparently copper-specific subfamily of ...
 69-126 7.00e-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: 45.22  E-value: 7.00e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1928162936  69 IVFRVNGMHCNSCISNIQSTISALPSVASIVVSLEKKSALVKYNPNLIHVDALRRAIE 126
Cdd:TIGR00003   2 QTFQVKGMSCNHCVDKIEKFVGEIEGVSKVKVQLEKEKVVVEFDAPNVSATEICEAIL 59
PRK13748 PRK13748
putative mercuric reductase; Provisional
 69-178 9.04e-07

putative mercuric reductase; Provisional


Pssm-ID: 184298 [Multi-domain]  Cd Length: 561  Bit Score: 48.99  E-value: 9.04e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928162936  69 IVFRVNGMHCNSCISNIQSTISALPSVASIVVSLEKKSALVKYNPNlIHVDALRRAIEAVSpetYKVSLPDE----YEDA 144
Cdd:PRK13748    2 TTLKITGMTCDSCAAHVKDALEKVPGVQSADVSYPKGSAQLAIEVG-TSPDALTAAVAGLG---YRATLADApptdNRGG 77

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1928162936 145 ELLNTQASPVKSPLNRNKWPLTQVTVINI--AGMTC 178
Cdd:PRK13748   78 LLDKMRGWLGGADKHSGNERPLHVAVIGSggAAMAA 113
PRK13748 PRK13748
putative mercuric reductase; Provisional
 169-226 2.05e-06

putative mercuric reductase; Provisional


Pssm-ID: 184298 [Multi-domain]  Cd Length: 561  Bit Score: 47.84  E-value: 2.05e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1928162936 169 TVINIAGMTCNSCAQSIEGVISQKPGVKSIHVSLVNHNGTIEYDPlLTSPEDLISSIK 226
Cdd:PRK13748    2 TTLKITGMTCDSCAAHVKDALEKVPGVQSADVSYPKGSAQLAIEV-GTSPDALTAAVA 58
copA PRK10671
copper-exporting P-type ATPase CopA;
10-109 2.18e-04

copper-exporting P-type ATPase CopA;


Pssm-ID: 182635 [Multi-domain]  Cd Length: 834  Bit Score: 41.65  E-value: 2.18e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928162936  10 TAEEIKNQIEAAGFTASIKK-QLKPLKLGAIDVERLKntqTKSSEGMLQKSpkhmNDLKTIVFRVNGMHCNSCISNIQST 88
Cdd:PRK10671   48 SAEALIETIKQAGYDASVSHpKAKPLTESSIPSEALT---AASEELPAATA----DDDDSQQLLLSGMSCASCVSRVQNA 120

                          90       100
                  ....*....|....*....|.
gi 1928162936  89 ISALPSVASIVVSLEKKSALV 109
Cdd:PRK10671  121 LQSVPGVTQARVNLAERTALV 141
TIGR00003 TIGR00003
copper ion binding protein; This model describes an apparently copper-specific subfamily of ...
 171-225 4.61e-04

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: 37.52  E-value: 4.61e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1928162936 171 INIAGMTCNSCAQSIEGVISQKPGVKSIHVSLVNHNGTIEYDPLLTSPEDLISSI 225
Cdd:TIGR00003   4 FQVKGMSCNHCVDKIEKFVGEIEGVSKVKVQLEKEKVVVEFDAPNVSATEICEAI 58
MerP TIGR02052
mercuric transport protein periplasmic component; This model represents the periplasmic ...
 161-212 5.50e-04

mercuric transport protein periplasmic component; This model represents the periplasmic mercury (II) binding protein of the bacterial mercury detoxification system which passes mercuric ion to the MerT transporter for subsequent reduction to Hg(0) by the mercuric reductase MerA. MerP contains a distinctive GMTCXXC motif associated with metal binding. MerP is related to a larger family of metal binding proteins (pfam00403). [Cellular processes, Detoxification]


Pssm-ID: 131107 [Multi-domain]  Cd Length: 92  Bit Score: 38.09  E-value: 5.50e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1928162936 161 NKWPLTQVTVINIAGMTCNSCAQSIEGVISQKPGVKSIHVSLVNHNGTIEYD 212
Cdd:TIGR02052  17 PAWAATQTVTLEVPGMTCVACPITVETALQKVDGVSKAEVTFKTKLAVVTFD 68
copA PRK10671
copper-exporting P-type ATPase CopA;
67-226 1.40e-03

copper-exporting P-type ATPase CopA;


Pssm-ID: 182635 [Multi-domain]  Cd Length: 834  Bit Score: 39.34  E-value: 1.40e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928162936  67 KTIVFRVNGMHCNSCISNIQSTISALPSVASIVVSLEKKSALVKYNPNLIhVDALRRA---IEAVSPETYKVSLPDEYED 143
Cdd:PRK10671    3 QTIDLTLDGLSCGHCVKRVKESLEQRPDVEQADVSITEAHVTGTASAEAL-IETIKQAgydASVSHPKAKPLTESSIPSE 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928162936 144 AELLNTQASPVKSPLNRNKWPLTqvtvinIAGMTCNSCAQSIEGVISQKPGVKSIHVSLVNHNGTIEYDPlltSPEDLIS 223
Cdd:PRK10671   82 ALTAASEELPAATADDDDSQQLL------LSGMSCASCVSRVQNALQSVPGVTQARVNLAERTALVMGSA---SPQDLVQ 152


                  ...
gi 1928162936 224 SIK 226
Cdd:PRK10671  153 AVE 155
zntA PRK11033
zinc/cadmium/mercury/lead-transporting ATPase; Provisional
 173-200 1.63e-03

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


Pssm-ID: 236827 [Multi-domain]  Cd Length: 741  Bit Score: 39.21  E-value: 1.63e-03
                          10        20
                  ....*....|....*....|....*...
gi 1928162936 173 IAGMTCNSCAQSIEGVISQKPGVKSIHV 200
Cdd:PRK11033   59 VSGMDCPSCARKVENAVRQLAGVNQVQV 86
UxxU_metal_bind NF041115
metal-binding (seleno)protein; Known members of this family are selenoproteins with an ...
 165-225 2.81e-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: 35.39  E-value: 2.81e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1928162936 165 LTQVTVINIAGMTCNSCAQSIEGVISQKPGVKSIHVSLVNHNGTIEYDPLLTSPEDLISSI 225
Cdd:NF041115    2 LAETVILAIEGMTUASUPLIAKKALEGLEGVEKADVSYKEGRAEVAFDPDKVSAAQMVDAV 62
 
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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