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Conserved domains on  [gi|568063658|ref|WP_024051462|]
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MULTISPECIES: heavy-metal-associated domain-containing protein [Streptococcus]

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

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List of domain hits

 Name Accession Description Interval E-value
CopZ COG2608
Copper chaperone CopZ [Inorganic ion transport and metabolism];
1-69 5.83e-12

Copper chaperone CopZ [Inorganic ion transport and metabolism];


:

Pssm-ID: 442020 [Multi-domain]  Cd Length: 71  Bit Score: 54.53  E-value: 5.83e-12
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568063658  1 MKQIVTLENISCQNCVKHVTEHFLKLEGVSDVQIDLDTKVATVTTDHTH-SAEDYQVALAKTIYKVVTVA 69
Cdd:COG2608   2 KTVTLKVEGMTCGHCVARVEKALKALDGVASVEVDLATGTATVTYDPEKvSLEDIKAAIEEAGYEVEKAE 71
 
Name Accession Description Interval E-value
CopZ COG2608
Copper chaperone CopZ [Inorganic ion transport and metabolism];
1-69 5.83e-12

Copper chaperone CopZ [Inorganic ion transport and metabolism];


Pssm-ID: 442020 [Multi-domain]  Cd Length: 71  Bit Score: 54.53  E-value: 5.83e-12
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568063658  1 MKQIVTLENISCQNCVKHVTEHFLKLEGVSDVQIDLDTKVATVTTDHTH-SAEDYQVALAKTIYKVVTVA 69
Cdd:COG2608   2 KTVTLKVEGMTCGHCVARVEKALKALDGVASVEVDLATGTATVTYDPEKvSLEDIKAAIEEAGYEVEKAE 71
HMA cd00371
Heavy-metal-associated domain (HMA) is a conserved domain of approximately 30 amino acid ...
 5-65 1.27e-09

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: 48.37  E-value: 1.27e-09
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568063658  5 VTLENISCQNCVKHVTEHFLKLEGVSDVQIDLDTKVATVTTDHTHSAEDYQVALAKTIYKV 65
Cdd:cd00371   2 LSVEGMTCAGCVSKIEKALEKLPGVESVEVDLETGKATVEYDPEVSPEELLEAIEDAGYKA 62
HMA pfam00403
Heavy-metal-associated domain;
4-46 7.47e-07

Heavy-metal-associated domain;


Pssm-ID: 459804 [Multi-domain]  Cd Length: 58  Bit Score: 41.45  E-value: 7.47e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 568063658   4 IVTLENISCQNCVKHVTEHFLKLEGVSDVQIDLDTKVATVTTD 46
Cdd:pfam00403  1 TFRVSGMHCGGCAAKVEKALSELPGVLSVSVDLATKTVTVTGD 43
PLN02957 PLN02957
copper, zinc superoxide dismutase
 10-64 6.21e-04

copper, zinc superoxide dismutase


Pssm-ID: 215516 [Multi-domain]  Cd Length: 238  Bit Score: 35.88  E-value: 6.21e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 568063658  10 ISCQNCVKHVTEHFLKLEGVSDVQIDLDTKVATVTTdhTHSAEDYQVALAKTIYK 64
Cdd:PLN02957  14 MKCEGCVAAVKNKLETLEGVKAVEVDLSNQVVRVLG--SSPVKAMTAALEQTGRK 66
TIGR00003 TIGR00003
copper ion binding protein; This model describes an apparently copper-specific subfamily of ...
 2-66 1.03e-03

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: 33.67  E-value: 1.03e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568063658   2 KQIVTLENISCQNCVKHVTEHFLKLEGVSDVQIDLDTKVATVTTDHTH-SAEDYQVALAKTIYKVV 66
Cdd:TIGR00003  1 KQTFQVKGMSCNHCVDKIEKFVGEIEGVSKVKVQLEKEKVVVEFDAPNvSATEICEAILDAGYEVE 66
 
Name Accession Description Interval E-value
CopZ COG2608
Copper chaperone CopZ [Inorganic ion transport and metabolism];
1-69 5.83e-12

Copper chaperone CopZ [Inorganic ion transport and metabolism];


Pssm-ID: 442020 [Multi-domain]  Cd Length: 71  Bit Score: 54.53  E-value: 5.83e-12
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568063658  1 MKQIVTLENISCQNCVKHVTEHFLKLEGVSDVQIDLDTKVATVTTDHTH-SAEDYQVALAKTIYKVVTVA 69
Cdd:COG2608   2 KTVTLKVEGMTCGHCVARVEKALKALDGVASVEVDLATGTATVTYDPEKvSLEDIKAAIEEAGYEVEKAE 71
HMA cd00371
Heavy-metal-associated domain (HMA) is a conserved domain of approximately 30 amino acid ...
 5-65 1.27e-09

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: 48.37  E-value: 1.27e-09
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568063658  5 VTLENISCQNCVKHVTEHFLKLEGVSDVQIDLDTKVATVTTDHTHSAEDYQVALAKTIYKV 65
Cdd:cd00371   2 LSVEGMTCAGCVSKIEKALEKLPGVESVEVDLETGKATVEYDPEVSPEELLEAIEDAGYKA 62
HMA pfam00403
Heavy-metal-associated domain;
4-46 7.47e-07

Heavy-metal-associated domain;


Pssm-ID: 459804 [Multi-domain]  Cd Length: 58  Bit Score: 41.45  E-value: 7.47e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 568063658   4 IVTLENISCQNCVKHVTEHFLKLEGVSDVQIDLDTKVATVTTD 46
Cdd:pfam00403  1 TFRVSGMHCGGCAAKVEKALSELPGVLSVSVDLATKTVTVTGD 43
ZntA COG2217
Cation-transporting P-type ATPase [Inorganic ion transport and metabolism];
7-66 1.53e-06

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


Pssm-ID: 441819 [Multi-domain]  Cd Length: 717  Bit Score: 43.21  E-value: 1.53e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568063658   7 LENISCQNCVKHVTEHFLKLEGVSDVQIDLDTKVATVTTDHTH-SAEDYQVALAKTIYKVV 66
Cdd:COG2217    7 IEGMTCAACAWLIEKALRKLPGVLSARVNLATERARVEYDPGKvSLEELIAAVEKAGYEAE 67
PLN02957 PLN02957
copper, zinc superoxide dismutase
 10-64 6.21e-04

copper, zinc superoxide dismutase


Pssm-ID: 215516 [Multi-domain]  Cd Length: 238  Bit Score: 35.88  E-value: 6.21e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 568063658  10 ISCQNCVKHVTEHFLKLEGVSDVQIDLDTKVATVTTdhTHSAEDYQVALAKTIYK 64
Cdd:PLN02957  14 MKCEGCVAAVKNKLETLEGVKAVEVDLSNQVVRVLG--SSPVKAMTAALEQTGRK 66
TIGR00003 TIGR00003
copper ion binding protein; This model describes an apparently copper-specific subfamily of ...
 2-66 1.03e-03

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: 33.67  E-value: 1.03e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568063658   2 KQIVTLENISCQNCVKHVTEHFLKLEGVSDVQIDLDTKVATVTTDHTH-SAEDYQVALAKTIYKVV 66
Cdd:TIGR00003  1 KQTFQVKGMSCNHCVDKIEKFVGEIEGVSKVKVQLEKEKVVVEFDAPNvSATEICEAILDAGYEVE 66
PRK13748 PRK13748
putative mercuric reductase; Provisional
 3-65 2.41e-03

putative mercuric reductase; Provisional


Pssm-ID: 184298 [Multi-domain]  Cd Length: 561  Bit Score: 34.36  E-value: 2.41e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568063658   3 QIVTLENISCQNCVKHVTEHFLKLEGVSDVQIDLDTKVATVTTDHTHSAEDYQVALAKTIYKV 65
Cdd:PRK13748   2 TTLKITGMTCDSCAAHVKDALEKVPGVQSADVSYPKGSAQLAIEVGTSPDALTAAVAGLGYRA 64
 
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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