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Conserved domains on  [gi|1172375513|ref|WP_080758783|]
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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

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List of domain hits

 Name Accession Description Interval E-value
CopZ COG2608
Copper chaperone CopZ [Inorganic ion transport and metabolism];
9-74 1.14e-21

Copper chaperone CopZ [Inorganic ion transport and metabolism];


:

Pssm-ID: 442020 [Multi-domain]  Cd Length: 71  Bit Score: 80.72  E-value: 1.14e-21
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1172375513   9 METLIIKIDGMHCGSCVAGVEKALIQVNGVQSAAVYLEAGQATVTYDPAYVSTADLVSAVVTAGYS 74
Cdd:COG2608     1 MKTVTLKVEGMTCGHCVARVEKALKALDGVASVEVDLATGTATVTYDPEKVSLEDIKAAIEEAGYE 66
 
Name Accession Description Interval E-value
CopZ COG2608
Copper chaperone CopZ [Inorganic ion transport and metabolism];
9-74 1.14e-21

Copper chaperone CopZ [Inorganic ion transport and metabolism];


Pssm-ID: 442020 [Multi-domain]  Cd Length: 71  Bit Score: 80.72  E-value: 1.14e-21
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1172375513   9 METLIIKIDGMHCGSCVAGVEKALIQVNGVQSAAVYLEAGQATVTYDPAYVSTADLVSAVVTAGYS 74
Cdd:COG2608     1 MKTVTLKVEGMTCGHCVARVEKALKALDGVASVEVDLATGTATVTYDPEKVSLEDIKAAIEEAGYE 66
HMA cd00371
Heavy-metal-associated domain (HMA) is a conserved domain of approximately 30 amino acid ...
 14-73 2.50e-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: 61.85  E-value: 2.50e-14
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172375513  14 IKIDGMHCGSCVAGVEKALIQVNGVQSAAVYLEAGQATVTYDPAyVSTADLVSAVVTAGY 73
Cdd:cd00371     2 LSVEGMTCAGCVSKIEKALEKLPGVESVEVDLETGKATVEYDPE-VSPEELLEAIEDAGY 60
PRK13748 PRK13748
putative mercuric reductase; Provisional
 13-73 1.14e-12

putative mercuric reductase; Provisional


Pssm-ID: 184298 [Multi-domain]  Cd Length: 561  Bit Score: 62.09  E-value: 1.14e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1172375513  13 IIKIDGMHCGSCVAGVEKALIQVNGVQSAAVYLEAGQATVTYDPAyVSTADLVSAVVTAGY 73
Cdd:PRK13748    3 TLKITGMTCDSCAAHVKDALEKVPGVQSADVSYPKGSAQLAIEVG-TSPDALTAAVAGLGY 62
HMA pfam00403
Heavy-metal-associated domain;
13-68 7.27e-12

Heavy-metal-associated domain;


Pssm-ID: 459804 [Multi-domain]  Cd Length: 58  Bit Score: 55.32  E-value: 7.27e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1172375513  13 IIKIDGMHCGSCVAGVEKALIQVNGVQSAAVYLEAGQATVTYDPAYVSTADLVSAV 68
Cdd:pfam00403   1 TFRVSGMHCGGCAAKVEKALSELPGVLSVSVDLATKTVTVTGDAESTKLEKLVEAI 56
UxxU_metal_bind NF041115
metal-binding (seleno)protein; Known members of this family are selenoproteins with an ...
 10-73 6.71e-11

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: 53.49  E-value: 6.71e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1172375513  10 ETLIIKIDGMHCGSCVAGVEKALIQVNGVQSAAVYLEAGQATVTYDPAYVSTADLVSAVVTAGY 73
Cdd:NF041115    4 ETVILAIEGMTUASUPLIAKKALEGLEGVEKADVSYKEGRAEVAFDPDKVSAAQMVDAVNRIGF 67
MerP TIGR02052
mercuric transport protein periplasmic component; This model represents the periplasmic ...
 10-73 5.28e-08

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: 46.57  E-value: 5.28e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1172375513  10 ETLIIKIDGMHCGSCVAGVEKALIQVNGVQSAAVYLEAGQATVTYDPAYVSTADLVSAVVTAGY 73
Cdd:TIGR02052  23 QTVTLEVPGMTCVACPITVETALQKVDGVSKAEVTFKTKLAVVTFDDEKTNVKALTEATTDAGY 86
 
Name Accession Description Interval E-value
CopZ COG2608
Copper chaperone CopZ [Inorganic ion transport and metabolism];
9-74 1.14e-21

Copper chaperone CopZ [Inorganic ion transport and metabolism];


Pssm-ID: 442020 [Multi-domain]  Cd Length: 71  Bit Score: 80.72  E-value: 1.14e-21
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1172375513   9 METLIIKIDGMHCGSCVAGVEKALIQVNGVQSAAVYLEAGQATVTYDPAYVSTADLVSAVVTAGYS 74
Cdd:COG2608     1 MKTVTLKVEGMTCGHCVARVEKALKALDGVASVEVDLATGTATVTYDPEKVSLEDIKAAIEEAGYE 66
ZntA COG2217
Cation-transporting P-type ATPase [Inorganic ion transport and metabolism];
10-74 4.33e-17

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


Pssm-ID: 441819 [Multi-domain]  Cd Length: 717  Bit Score: 74.79  E-value: 4.33e-17
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1172375513  10 ETLIIKIDGMHCGSCVAGVEKALIQVNGVQSAAVYLEAGQATVTYDPAYVSTADLVSAVVTAGYS 74
Cdd:COG2217     1 ERVRLRIEGMTCAACAWLIEKALRKLPGVLSARVNLATERARVEYDPGKVSLEELIAAVEKAGYE 65
HMA cd00371
Heavy-metal-associated domain (HMA) is a conserved domain of approximately 30 amino acid ...
 14-73 2.50e-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: 61.85  E-value: 2.50e-14
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172375513  14 IKIDGMHCGSCVAGVEKALIQVNGVQSAAVYLEAGQATVTYDPAyVSTADLVSAVVTAGY 73
Cdd:cd00371     2 LSVEGMTCAGCVSKIEKALEKLPGVESVEVDLETGKATVEYDPE-VSPEELLEAIEDAGY 60
PRK13748 PRK13748
putative mercuric reductase; Provisional
 13-73 1.14e-12

putative mercuric reductase; Provisional


Pssm-ID: 184298 [Multi-domain]  Cd Length: 561  Bit Score: 62.09  E-value: 1.14e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1172375513  13 IIKIDGMHCGSCVAGVEKALIQVNGVQSAAVYLEAGQATVTYDPAyVSTADLVSAVVTAGY 73
Cdd:PRK13748    3 TLKITGMTCDSCAAHVKDALEKVPGVQSADVSYPKGSAQLAIEVG-TSPDALTAAVAGLGY 62
HMA pfam00403
Heavy-metal-associated domain;
13-68 7.27e-12

Heavy-metal-associated domain;


Pssm-ID: 459804 [Multi-domain]  Cd Length: 58  Bit Score: 55.32  E-value: 7.27e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1172375513  13 IIKIDGMHCGSCVAGVEKALIQVNGVQSAAVYLEAGQATVTYDPAYVSTADLVSAV 68
Cdd:pfam00403   1 TFRVSGMHCGGCAAKVEKALSELPGVLSVSVDLATKTVTVTGDAESTKLEKLVEAI 56
UxxU_metal_bind NF041115
metal-binding (seleno)protein; Known members of this family are selenoproteins with an ...
 10-73 6.71e-11

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: 53.49  E-value: 6.71e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1172375513  10 ETLIIKIDGMHCGSCVAGVEKALIQVNGVQSAAVYLEAGQATVTYDPAYVSTADLVSAVVTAGY 73
Cdd:NF041115    4 ETVILAIEGMTUASUPLIAKKALEGLEGVEKADVSYKEGRAEVAFDPDKVSAAQMVDAVNRIGF 67
copA PRK10671
copper-exporting P-type ATPase CopA;
16-74 3.24e-09

copper-exporting P-type ATPase CopA;


Pssm-ID: 182635 [Multi-domain]  Cd Length: 834  Bit Score: 52.44  E-value: 3.24e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1172375513  16 IDGMHCGSCVAGVEKALIQVNGVQSAAVYLEAGQATVTydpAYVSTADLVSAVVTAGYS 74
Cdd:PRK10671  105 LSGMSCASCVSRVQNALQSVPGVTQARVNLAERTALVM---GSASPQDLVQAVEKAGYG 160
MerP TIGR02052
mercuric transport protein periplasmic component; This model represents the periplasmic ...
 10-73 5.28e-08

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: 46.57  E-value: 5.28e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1172375513  10 ETLIIKIDGMHCGSCVAGVEKALIQVNGVQSAAVYLEAGQATVTYDPAYVSTADLVSAVVTAGY 73
Cdd:TIGR02052  23 QTVTLEVPGMTCVACPITVETALQKVDGVSKAEVTFKTKLAVVTFDDEKTNVKALTEATTDAGY 86
TIGR00003 TIGR00003
copper ion binding protein; This model describes an apparently copper-specific subfamily of ...
 14-73 7.15e-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: 42.91  E-value: 7.15e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172375513  14 IKIDGMHCGSCVAGVEKALIQVNGVQSAAVYLEAGQATVTYDPAYVSTADLVSAVVTAGY 73
Cdd:TIGR00003   4 FQVKGMSCNHCVDKIEKFVGEIEGVSKVKVQLEKEKVVVEFDAPNVSATEICEAILDAGY 63
zntA PRK11033
zinc/cadmium/mercury/lead-transporting ATPase; Provisional
 15-74 2.90e-05

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


Pssm-ID: 236827 [Multi-domain]  Cd Length: 741  Bit Score: 41.13  E-value: 2.90e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172375513  15 KIDGMHCGSCVAGVEKALIQVNGVQSAAVYLEAGQATVTYDPAyvSTADLVSAVVTAGYS 74
Cdd:PRK11033   58 KVSGMDCPSCARKVENAVRQLAGVNQVQVLFATEKLVVDADND--IRAQVESAVQKAGFS 115
copA PRK10671
copper-exporting P-type ATPase CopA;
10-73 3.40e-05

copper-exporting P-type ATPase CopA;


Pssm-ID: 182635 [Multi-domain]  Cd Length: 834  Bit Score: 40.88  E-value: 3.40e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1172375513  10 ETLIIKIDGMHCGSCVAGVEKALIQVNGVQSAAVYLEagQATVTYDpayVSTADLVSAVVTAGY 73
Cdd:PRK10671    3 QTIDLTLDGLSCGHCVKRVKESLEQRPDVEQADVSIT--EAHVTGT---ASAEALIETIKQAGY 61
 
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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