NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|26450824|dbj|BAC42520|]
View 

putative isoprenylated protein [Arabidopsis thaliana]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
 36-90 8.88e-15

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: 64.55  E-value: 8.88e-15
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 26450824  36 MDCDGCERRVKNAVSSMKGVKSVEVNRKIHKVTVSGY--VEPKKVLKRIERTGKKAE 90
Cdd:cd00371   7 MTCAGCVSKIEKALEKLPGVESVEVDLETGKATVEYDpeVSPEELLEAIEDAGYKAR 63
 
Name Accession Description Interval E-value
HMA cd00371
Heavy-metal-associated domain (HMA) is a conserved domain of approximately 30 amino acid ...
 36-90 8.88e-15

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: 64.55  E-value: 8.88e-15
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 26450824  36 MDCDGCERRVKNAVSSMKGVKSVEVNRKIHKVTVSGY--VEPKKVLKRIERTGKKAE 90
Cdd:cd00371   7 MTCAGCVSKIEKALEKLPGVESVEVDLETGKATVEYDpeVSPEELLEAIEDAGYKAR 63
CopZ COG2608
Copper chaperone CopZ [Inorganic ion transport and metabolism];
27-90 3.47e-13

Copper chaperone CopZ [Inorganic ion transport and metabolism];


Pssm-ID: 442020 [Multi-domain]  Cd Length: 71  Bit Score: 60.69  E-value: 3.47e-13
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 26450824  27 MQTVNIKVK-MDCDGCERRVKNAVSSMKGVKSVEVNRKIHKVTVSG---YVEPKKVLKRIERTGKKAE 90
Cdd:COG2608   1 MKTVTLKVEgMTCGHCVARVEKALKALDGVASVEVDLATGTATVTYdpeKVSLEDIKAAIEEAGYEVE 68
HMA pfam00403
Heavy-metal-associated domain;
36-83 2.51e-10

Heavy-metal-associated domain;


Pssm-ID: 459804 [Multi-domain]  Cd Length: 58  Bit Score: 53.01  E-value: 2.51e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 26450824    36 MDCDGCERRVKNAVSSMKGVKSVEVNRKIHKVTVSGYVEP---KKVLKRIE 83
Cdd:pfam00403   7 MHCGGCAAKVEKALSELPGVLSVSVDLATKTVTVTGDAEStklEKLVEAIE 57
PLN02957 PLN02957
copper, zinc superoxide dismutase
 34-89 1.32e-08

copper, zinc superoxide dismutase


Pssm-ID: 215516 [Multi-domain]  Cd Length: 238  Bit Score: 51.68  E-value: 1.32e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 26450824   34 VKMDCDGCERRVKNAVSSMKGVKSVEVNRKIHKVTVSGYVEPKKVLKRIERTGKKA 89
Cdd:PLN02957  12 VDMKCEGCVAAVKNKLETLEGVKAVEVDLSNQVVRVLGSSPVKAMTAALEQTGRKA 67
 
Name Accession Description Interval E-value
HMA cd00371
Heavy-metal-associated domain (HMA) is a conserved domain of approximately 30 amino acid ...
 36-90 8.88e-15

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: 64.55  E-value: 8.88e-15
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 26450824  36 MDCDGCERRVKNAVSSMKGVKSVEVNRKIHKVTVSGY--VEPKKVLKRIERTGKKAE 90
Cdd:cd00371   7 MTCAGCVSKIEKALEKLPGVESVEVDLETGKATVEYDpeVSPEELLEAIEDAGYKAR 63
CopZ COG2608
Copper chaperone CopZ [Inorganic ion transport and metabolism];
27-90 3.47e-13

Copper chaperone CopZ [Inorganic ion transport and metabolism];


Pssm-ID: 442020 [Multi-domain]  Cd Length: 71  Bit Score: 60.69  E-value: 3.47e-13
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 26450824  27 MQTVNIKVK-MDCDGCERRVKNAVSSMKGVKSVEVNRKIHKVTVSG---YVEPKKVLKRIERTGKKAE 90
Cdd:COG2608   1 MKTVTLKVEgMTCGHCVARVEKALKALDGVASVEVDLATGTATVTYdpeKVSLEDIKAAIEEAGYEVE 68
HMA pfam00403
Heavy-metal-associated domain;
36-83 2.51e-10

Heavy-metal-associated domain;


Pssm-ID: 459804 [Multi-domain]  Cd Length: 58  Bit Score: 53.01  E-value: 2.51e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 26450824    36 MDCDGCERRVKNAVSSMKGVKSVEVNRKIHKVTVSGYVEP---KKVLKRIE 83
Cdd:pfam00403   7 MHCGGCAAKVEKALSELPGVLSVSVDLATKTVTVTGDAEStklEKLVEAIE 57
PLN02957 PLN02957
copper, zinc superoxide dismutase
 34-89 1.32e-08

copper, zinc superoxide dismutase


Pssm-ID: 215516 [Multi-domain]  Cd Length: 238  Bit Score: 51.68  E-value: 1.32e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 26450824   34 VKMDCDGCERRVKNAVSSMKGVKSVEVNRKIHKVTVSGYVEPKKVLKRIERTGKKA 89
Cdd:PLN02957  12 VDMKCEGCVAAVKNKLETLEGVKAVEVDLSNQVVRVLGSSPVKAMTAALEQTGRKA 67
ZntA COG2217
Cation-transporting P-type ATPase [Inorganic ion transport and metabolism];
28-91 3.27e-07

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


Pssm-ID: 441819 [Multi-domain]  Cd Length: 717  Bit Score: 48.22  E-value: 3.27e-07
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 26450824  28 QTVNIKVK-MDCDGCERRVKNAVSSMKGVKSVEVNRKIHKVTVS---GYVEPKKVLKRIERTGKKAEI 91
Cdd:COG2217   1 ERVRLRIEgMTCAACAWLIEKALRKLPGVLSARVNLATERARVEydpGKVSLEELIAAVEKAGYEAEP 68
zntA PRK11033
zinc/cadmium/mercury/lead-transporting ATPase; Provisional
 36-89 4.43e-04

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


Pssm-ID: 236827 [Multi-domain]  Cd Length: 741  Bit Score: 39.21  E-value: 4.43e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 26450824   36 MDCDGCERRVKNAVSSMKGVKSVEVNRKIHKVTVSGYVEpkkVLKRIERTGKKA 89
Cdd:PRK11033  62 MDCPSCARKVENAVRQLAGVNQVQVLFATEKLVVDADND---IRAQVESAVQKA 112
PRK13748 PRK13748
putative mercuric reductase; Provisional
 27-91 3.52e-03

putative mercuric reductase; Provisional


Pssm-ID: 184298 [Multi-domain]  Cd Length: 561  Bit Score: 36.67  E-value: 3.52e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 26450824   27 MQTVNIKvKMDCDGCERRVKNAVSSMKGVKSVEVN--RKIHKVTVSGYVEPKKVLKRIERTGKKAEI 91
Cdd:PRK13748   1 MTTLKIT-GMTCDSCAAHVKDALEKVPGVQSADVSypKGSAQLAIEVGTSPDALTAAVAGLGYRATL 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