NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|495198499|ref|WP_007923288|]
View 

MULTISPECIES: heavy-metal-associated domain-containing protein [Pseudomonas]

Protein Classification

heavy-metal-associated domain-containing protein( domain architecture ID 10006509)

heavy-metal-associated domain-containing protein may function as a heavy metal transporter and/or detoxification protein; similar to heavy metal-associated isoprenylated plant protein (HIPP), Synechocystis Pcc6803 zinc-transporting ATPase, and Salmonella enterica gold resistance metallochaperone GolB which exhibits selectivity toward the Au(I) cation

Gene Ontology:  GO:0046872
PubMed:  12443926|8905098|8091505|9437429

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
CopZ COG2608
Copper chaperone CopZ [Inorganic ion transport and metabolism];
1-65 4.57e-15

Copper chaperone CopZ [Inorganic ion transport and metabolism];


:

Pssm-ID: 442020 [Multi-domain]  Cd Length: 71  Bit Score: 62.23  E-value: 4.57e-15
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 495198499  1 MQVFNVEGMSCGHCVRAITQAVQSKDPAASVKVDLGAREVGVES---RLSADEVISLISEEGYAVKLA 65
Cdd:COG2608   3 TVTLKVEGMTCGHCVARVEKALKALDGVASVEVDLATGTATVTYdpeKVSLEDIKAAIEEAGYEVEKA 70
 
Name Accession Description Interval E-value
CopZ COG2608
Copper chaperone CopZ [Inorganic ion transport and metabolism];
1-65 4.57e-15

Copper chaperone CopZ [Inorganic ion transport and metabolism];


Pssm-ID: 442020 [Multi-domain]  Cd Length: 71  Bit Score: 62.23  E-value: 4.57e-15
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 495198499  1 MQVFNVEGMSCGHCVRAITQAVQSKDPAASVKVDLGAREVGVES---RLSADEVISLISEEGYAVKLA 65
Cdd:COG2608   3 TVTLKVEGMTCGHCVARVEKALKALDGVASVEVDLATGTATVTYdpeKVSLEDIKAAIEEAGYEVEKA 70
chaper_CopZ_Bs NF033795
copper chaperone CopZ; This model describes CopZ, a small copper chaperone, as found in ...
 3-63 3.11e-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: 57.49  E-value: 3.11e-13
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495198499  3 VFNVEGMSCGHCVRAITQAVQSKDPAASVKVDLGAREVGV---ESRLSADEVISLISEEGYAVK 63
Cdd:NF033795  3 TLNVEGMSCGHCVKAVEGALGELNGVSSVKVNLEEGKVDVefdESKVTLDQIKEAIEDQGYDVV 66
chaper_CopZ_Eh NF033794
copper chaperone CopZ; Copper chaperone CopZ, as the name is used in Enterococcus hirae and ...
 2-65 1.95e-09

copper chaperone CopZ; Copper chaperone CopZ, as the name is used in Enterococcus hirae and related species, is a small copper-binding protein with close homology to domains found, sometimes in multiple copies, in various copper-translocating copper-translocating P-type ATPases, and to distinct families of other small copper chaperones that also named CopZ.


Pssm-ID: 411374 [Multi-domain]  Cd Length: 68  Bit Score: 48.10  E-value: 1.95e-09
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 495198499  2 QVFNVEGMSCGHCVRAITQAVQSKDPAASVKVDLgAREVGV----ESRLSADEVISLISEEGYAVKLA 65
Cdd:NF033794  2 QTFSIKGMSCNHCVARVEKAVNELPGVKKVKVNL-KKENGVvkfdETQVTAEKIAQAVNELGYQAEVV 68
HMA cd00371
Heavy-metal-associated domain (HMA) is a conserved domain of approximately 30 amino acid ...
 3-63 1.57e-08

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: 45.67  E-value: 1.57e-08
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495198499  3 VFNVEGMSCGHCVRAITQAVQSKDPAASVKVDLGAREVGVE--SRLSADEVISLISEEGYAVK 63
Cdd:cd00371   1 ELSVEGMTCAGCVSKIEKALEKLPGVESVEVDLETGKATVEydPEVSPEELLEAIEDAGYKAR 63
HMA pfam00403
Heavy-metal-associated domain;
3-55 8.48e-07

Heavy-metal-associated domain;


Pssm-ID: 459804 [Multi-domain]  Cd Length: 58  Bit Score: 41.07  E-value: 8.48e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 495198499   3 VFNVEGMSCGHCVRAITQAVQSKDPAASVKVDLGAREVGVESRLSADEVISLI 55
Cdd:pfam00403  1 TFRVSGMHCGGCAAKVEKALSELPGVLSVSVDLATKTVTVTGDAESTKLEKLV 53
TIGR00003 TIGR00003
copper ion binding protein; This model describes an apparently copper-specific subfamily of ...
 2-62 1.45e-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: 40.60  E-value: 1.45e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495198499   2 QVFNVEGMSCGHCVRAITQAVQSKDPAASVKVDLGAREVGVE---SRLSADEVISLISEEGYAV 62
Cdd:TIGR00003  2 QTFQVKGMSCNHCVDKIEKFVGEIEGVSKVKVQLEKEKVVVEfdaPNVSATEICEAILDAGYEV 65
copA PRK10671
copper-exporting P-type ATPase CopA;
6-60 1.43e-04

copper-exporting P-type ATPase CopA;


Pssm-ID: 182635 [Multi-domain]  Cd Length: 834  Bit Score: 37.41  E-value: 1.43e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 495198499   6 VEGMSCGHCVRAITQAVQSKDPAASVKVDLGAREVGVESRLSADEVISLISEEGY 60
Cdd:PRK10671 105 LSGMSCASCVSRVQNALQSVPGVTQARVNLAERTALVMGSASPQDLVQAVEKAGY 159
 
Name Accession Description Interval E-value
CopZ COG2608
Copper chaperone CopZ [Inorganic ion transport and metabolism];
1-65 4.57e-15

Copper chaperone CopZ [Inorganic ion transport and metabolism];


Pssm-ID: 442020 [Multi-domain]  Cd Length: 71  Bit Score: 62.23  E-value: 4.57e-15
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 495198499  1 MQVFNVEGMSCGHCVRAITQAVQSKDPAASVKVDLGAREVGVES---RLSADEVISLISEEGYAVKLA 65
Cdd:COG2608   3 TVTLKVEGMTCGHCVARVEKALKALDGVASVEVDLATGTATVTYdpeKVSLEDIKAAIEEAGYEVEKA 70
chaper_CopZ_Bs NF033795
copper chaperone CopZ; This model describes CopZ, a small copper chaperone, as found in ...
 3-63 3.11e-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: 57.49  E-value: 3.11e-13
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495198499  3 VFNVEGMSCGHCVRAITQAVQSKDPAASVKVDLGAREVGV---ESRLSADEVISLISEEGYAVK 63
Cdd:NF033795  3 TLNVEGMSCGHCVKAVEGALGELNGVSSVKVNLEEGKVDVefdESKVTLDQIKEAIEDQGYDVV 66
chaper_CopZ_Eh NF033794
copper chaperone CopZ; Copper chaperone CopZ, as the name is used in Enterococcus hirae and ...
 2-65 1.95e-09

copper chaperone CopZ; Copper chaperone CopZ, as the name is used in Enterococcus hirae and related species, is a small copper-binding protein with close homology to domains found, sometimes in multiple copies, in various copper-translocating copper-translocating P-type ATPases, and to distinct families of other small copper chaperones that also named CopZ.


Pssm-ID: 411374 [Multi-domain]  Cd Length: 68  Bit Score: 48.10  E-value: 1.95e-09
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 495198499  2 QVFNVEGMSCGHCVRAITQAVQSKDPAASVKVDLgAREVGV----ESRLSADEVISLISEEGYAVKLA 65
Cdd:NF033794  2 QTFSIKGMSCNHCVARVEKAVNELPGVKKVKVNL-KKENGVvkfdETQVTAEKIAQAVNELGYQAEVV 68
HMA cd00371
Heavy-metal-associated domain (HMA) is a conserved domain of approximately 30 amino acid ...
 3-63 1.57e-08

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: 45.67  E-value: 1.57e-08
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495198499  3 VFNVEGMSCGHCVRAITQAVQSKDPAASVKVDLGAREVGVE--SRLSADEVISLISEEGYAVK 63
Cdd:cd00371   1 ELSVEGMTCAGCVSKIEKALEKLPGVESVEVDLETGKATVEydPEVSPEELLEAIEDAGYKAR 63
ZntA COG2217
Cation-transporting P-type ATPase [Inorganic ion transport and metabolism];
4-65 5.92e-07

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


Pssm-ID: 441819 [Multi-domain]  Cd Length: 717  Bit Score: 43.98  E-value: 5.92e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 495198499   4 FNVEGMSCGHCVRAITQAVQSKDPAASVKVDLGAREVGVE---SRLSADEVISLISEEGYAVKLA 65
Cdd:COG2217    5 LRIEGMTCAACAWLIEKALRKLPGVLSARVNLATERARVEydpGKVSLEELIAAVEKAGYEAEPA 69
HMA pfam00403
Heavy-metal-associated domain;
3-55 8.48e-07

Heavy-metal-associated domain;


Pssm-ID: 459804 [Multi-domain]  Cd Length: 58  Bit Score: 41.07  E-value: 8.48e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 495198499   3 VFNVEGMSCGHCVRAITQAVQSKDPAASVKVDLGAREVGVESRLSADEVISLI 55
Cdd:pfam00403  1 TFRVSGMHCGGCAAKVEKALSELPGVLSVSVDLATKTVTVTGDAESTKLEKLV 53
TIGR00003 TIGR00003
copper ion binding protein; This model describes an apparently copper-specific subfamily of ...
 2-62 1.45e-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: 40.60  E-value: 1.45e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495198499   2 QVFNVEGMSCGHCVRAITQAVQSKDPAASVKVDLGAREVGVE---SRLSADEVISLISEEGYAV 62
Cdd:TIGR00003  2 QTFQVKGMSCNHCVDKIEKFVGEIEGVSKVKVQLEKEKVVVEfdaPNVSATEICEAILDAGYEV 65
copA PRK10671
copper-exporting P-type ATPase CopA;
6-60 1.43e-04

copper-exporting P-type ATPase CopA;


Pssm-ID: 182635 [Multi-domain]  Cd Length: 834  Bit Score: 37.41  E-value: 1.43e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 495198499   6 VEGMSCGHCVRAITQAVQSKDPAASVKVDLGAREVGVESRLSADEVISLISEEGY 60
Cdd:PRK10671 105 LSGMSCASCVSRVQNALQSVPGVTQARVNLAERTALVMGSASPQDLVQAVEKAGY 159
PLN02957 PLN02957
copper, zinc superoxide dismutase
 4-64 1.70e-04

copper, zinc superoxide dismutase


Pssm-ID: 215516 [Multi-domain]  Cd Length: 238  Bit Score: 37.04  E-value: 1.70e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495198499   4 FNVEgMSCGHCVRAITQAVQSKDPAASVKVDLGAREVGVESRLSADEVISLISEEGYAVKL 64
Cdd:PLN02957  10 FMVD-MKCEGCVAAVKNKLETLEGVKAVEVDLSNQVVRVLGSSPVKAMTAALEQTGRKARL 69
PRK13748 PRK13748
putative mercuric reductase; Provisional
 1-65 6.77e-04

putative mercuric reductase; Provisional


Pssm-ID: 184298 [Multi-domain]  Cd Length: 561  Bit Score: 35.51  E-value: 6.77e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 495198499   1 MQVFNVEGMSCGHCVRAITQAVQsKDP---AASVKVDLGAREVGVESRLSADEVISLISEEGYAVKLA 65
Cdd:PRK13748   1 MTTLKITGMTCDSCAAHVKDALE-KVPgvqSADVSYPKGSAQLAIEVGTSPDALTAAVAGLGYRATLA 67
copA PRK10671
copper-exporting P-type ATPase CopA;
2-65 1.61e-03

copper-exporting P-type ATPase CopA;


Pssm-ID: 182635 [Multi-domain]  Cd Length: 834  Bit Score: 34.33  E-value: 1.61e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495198499   2 QVFNVEGMSCGHCVRAITQAVQSKDPAASVKVDLgaREVGVESRLSADEVISLISEEGYAVKLA 65
Cdd:PRK10671   5 IDLTLDGLSCGHCVKRVKESLEQRPDVEQADVSI--TEAHVTGTASAEALIETIKQAGYDASVS 66
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH