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Conserved domains on  [gi|347453628|gb|AEO95412|]
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ATP7A, partial [Capromys pilorides]

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

Gene Ontology:  GO:0046872
PubMed:  12594858|10404590|8091505|9437429

Graphical summary

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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 ...
 168-225 6.36e-18

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: 74.56  E-value: 6.36e-18
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 347453628 168 VINIDGMTCNSCVQSIEGVISKKKGVKSIHVSLENSNGTIEYDPlLISPEILKEAIED 225
Cdd:cd00371    1 ELSVEGMTCAGCVSKIEKALEKLPGVESVEVDLETGKATVEYDP-EVSPEELLEAIED 57
HMA cd00371
Heavy-metal-associated domain (HMA) is a conserved domain of approximately 30 amino acid ...
 71-124 9.54e-10

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: 52.99  E-value: 9.54e-10
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 347453628  71 IDGMHCKSCVSNIENALSTLHYVSSVVVSLESRSAIVKYNANlVTPEILRKMIE 124
Cdd:cd00371    4 VEGMTCAGCVSKIEKALEKLPGVESVEVDLETGKATVEYDPE-VSPEELLEAIE 56
 
Name Accession Description Interval E-value
HMA cd00371
Heavy-metal-associated domain (HMA) is a conserved domain of approximately 30 amino acid ...
 168-225 6.36e-18

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: 74.56  E-value: 6.36e-18
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 347453628 168 VINIDGMTCNSCVQSIEGVISKKKGVKSIHVSLENSNGTIEYDPlLISPEILKEAIED 225
Cdd:cd00371    1 ELSVEGMTCAGCVSKIEKALEKLPGVESVEVDLETGKATVEYDP-EVSPEELLEAIED 57
CopZ COG2608
Copper chaperone CopZ [Inorganic ion transport and metabolism];
164-225 1.20e-16

Copper chaperone CopZ [Inorganic ion transport and metabolism];


Pssm-ID: 442020 [Multi-domain]  Cd Length: 71  Bit Score: 71.47  E-value: 1.20e-16
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 347453628 164 TQETVINIDGMTCNSCVQSIEGVISKKKGVKSIHVSLENSNGTIEYDPLLISPEILKEAIED 225
Cdd:COG2608    1 MKTVTLKVEGMTCGHCVARVEKALKALDGVASVEVDLATGTATVTYDPEKVSLEDIKAAIEE 62
chaper_CopZ_Bs NF033795
copper chaperone CopZ; This model describes CopZ, a small copper chaperone, as found in ...
 166-225 5.25e-15

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: 67.12  E-value: 5.25e-15
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 347453628 166 ETVINIDGMTCNSCVQSIEGVISKKKGVKSIHVSLENSNGTIEYDPLLISPEILKEAIED 225
Cdd:NF033795   1 KVTLNVEGMSCGHCVKAVEGALGELNGVSSVKVNLEEGKVDVEFDESKVTLDQIKEAIED 60
HMA pfam00403
Heavy-metal-associated domain;
168-225 1.05e-12

Heavy-metal-associated domain;


Pssm-ID: 459804 [Multi-domain]  Cd Length: 58  Bit Score: 60.71  E-value: 1.05e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 347453628  168 VINIDGMTCNSCVQSIEGVISKKKGVKSIHVSLENSNGTIEYDPLLISPEILKEAIED 225
Cdd:pfam00403   1 TFRVSGMHCGGCAAKVEKALSELPGVLSVSVDLATKTVTVTGDAESTKLEKLVEAIEK 58
HMA cd00371
Heavy-metal-associated domain (HMA) is a conserved domain of approximately 30 amino acid ...
 71-124 9.54e-10

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: 52.99  E-value: 9.54e-10
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 347453628  71 IDGMHCKSCVSNIENALSTLHYVSSVVVSLESRSAIVKYNANlVTPEILRKMIE 124
Cdd:cd00371    4 VEGMTCAGCVSKIEKALEKLPGVESVEVDLETGKATVEYDPE-VSPEELLEAIE 56
TIGR00003 TIGR00003
copper ion binding protein; This model describes an apparently copper-specific subfamily of ...
 169-225 5.97e-09

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: 51.00  E-value: 5.97e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 347453628  169 INIDGMTCNSCVQSIEGVISKKKGVKSIHVSLENSNGTIEYDPLLISPEILKEAIED 225
Cdd:TIGR00003   4 FQVKGMSCNHCVDKIEKFVGEIEGVSKVKVQLEKEKVVVEFDAPNVSATEICEAILD 60
HMA pfam00403
Heavy-metal-associated domain;
68-124 1.92e-07

Heavy-metal-associated domain;


Pssm-ID: 459804 [Multi-domain]  Cd Length: 58  Bit Score: 46.46  E-value: 1.92e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 347453628   68 IFIIDGMHCKSCVSNIENALSTLHYVSSVVVSLESRSAIVKYNANLVTPEILRKMIE 124
Cdd:pfam00403   1 TFRVSGMHCGGCAAKVEKALSELPGVLSVSVDLATKTVTVTGDAESTKLEKLVEAIE 57
CopZ COG2608
Copper chaperone CopZ [Inorganic ion transport and metabolism];
66-124 2.67e-07

Copper chaperone CopZ [Inorganic ion transport and metabolism];


Pssm-ID: 442020 [Multi-domain]  Cd Length: 71  Bit Score: 46.44  E-value: 2.67e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 347453628  66 TAIFIIDGMHCKSCVSNIENALSTLHYVSSVVVSLESRSAIVKYNANLVTPEILRKMIE 124
Cdd:COG2608    3 TVTLKVEGMTCGHCVARVEKALKALDGVASVEVDLATGTATVTYDPEKVSLEDIKAAIE 61
PRK13748 PRK13748
putative mercuric reductase; Provisional
 166-224 1.18e-05

putative mercuric reductase; Provisional


Pssm-ID: 184298 [Multi-domain]  Cd Length: 561  Bit Score: 45.53  E-value: 1.18e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 347453628 166 ETVINIDGMTCNSCVQSIEGVISKKKGVKSIHVSLENSNGTIEYDPlLISPEILKEAIE 224
Cdd:PRK13748   1 MTTLKITGMTCDSCAAHVKDALEKVPGVQSADVSYPKGSAQLAIEV-GTSPDALTAAVA 58
UxxU_metal_bind NF041115
metal-binding (seleno)protein; Known members of this family are selenoproteins with an ...
 163-224 5.40e-04

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: 37.31  E-value: 5.40e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 347453628 163 LTQETVINIDGMTCNSCVQSIEGVISKKKGVKSIHVSLENSNGTIEYDPLLISPEILKEAIE 224
Cdd:NF041115   2 LAETVILAIEGMTUASUPLIAKKALEGLEGVEKADVSYKEGRAEVAFDPDKVSAAQMVDAVN 63
copA PRK10671
copper-exporting P-type ATPase CopA;
70-135 1.36e-03

copper-exporting P-type ATPase CopA;


Pssm-ID: 182635 [Multi-domain]  Cd Length: 834  Bit Score: 39.34  E-value: 1.36e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 347453628  70 IIDGMHCKSCVSNIENALSTLHYVSSVVVSLESRSAIVKYNANlvtPEILrkmIETVSPGQYTVSI 135
Cdd:PRK10671 104 LLSGMSCASCVSRVQNALQSVPGVTQARVNLAERTALVMGSAS---PQDL---VQAVEKAGYGAEA 163
 
Name Accession Description Interval E-value
HMA cd00371
Heavy-metal-associated domain (HMA) is a conserved domain of approximately 30 amino acid ...
 168-225 6.36e-18

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: 74.56  E-value: 6.36e-18
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 347453628 168 VINIDGMTCNSCVQSIEGVISKKKGVKSIHVSLENSNGTIEYDPlLISPEILKEAIED 225
Cdd:cd00371    1 ELSVEGMTCAGCVSKIEKALEKLPGVESVEVDLETGKATVEYDP-EVSPEELLEAIED 57
CopZ COG2608
Copper chaperone CopZ [Inorganic ion transport and metabolism];
164-225 1.20e-16

Copper chaperone CopZ [Inorganic ion transport and metabolism];


Pssm-ID: 442020 [Multi-domain]  Cd Length: 71  Bit Score: 71.47  E-value: 1.20e-16
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 347453628 164 TQETVINIDGMTCNSCVQSIEGVISKKKGVKSIHVSLENSNGTIEYDPLLISPEILKEAIED 225
Cdd:COG2608    1 MKTVTLKVEGMTCGHCVARVEKALKALDGVASVEVDLATGTATVTYDPEKVSLEDIKAAIEE 62
chaper_CopZ_Bs NF033795
copper chaperone CopZ; This model describes CopZ, a small copper chaperone, as found in ...
 166-225 5.25e-15

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: 67.12  E-value: 5.25e-15
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 347453628 166 ETVINIDGMTCNSCVQSIEGVISKKKGVKSIHVSLENSNGTIEYDPLLISPEILKEAIED 225
Cdd:NF033795   1 KVTLNVEGMSCGHCVKAVEGALGELNGVSSVKVNLEEGKVDVEFDESKVTLDQIKEAIED 60
HMA pfam00403
Heavy-metal-associated domain;
168-225 1.05e-12

Heavy-metal-associated domain;


Pssm-ID: 459804 [Multi-domain]  Cd Length: 58  Bit Score: 60.71  E-value: 1.05e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 347453628  168 VINIDGMTCNSCVQSIEGVISKKKGVKSIHVSLENSNGTIEYDPLLISPEILKEAIED 225
Cdd:pfam00403   1 TFRVSGMHCGGCAAKVEKALSELPGVLSVSVDLATKTVTVTGDAESTKLEKLVEAIEK 58
ZntA COG2217
Cation-transporting P-type ATPase [Inorganic ion transport and metabolism];
165-225 7.25e-11

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


Pssm-ID: 441819 [Multi-domain]  Cd Length: 717  Bit Score: 61.31  E-value: 7.25e-11
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 347453628 165 QETVINIDGMTCNSCVQSIEGVISKKKGVKSIHVSLENSNGTIEYDPLLISPEILKEAIED 225
Cdd:COG2217    1 ERVRLRIEGMTCAACAWLIEKALRKLPGVLSARVNLATERARVEYDPGKVSLEELIAAVEK 61
HMA cd00371
Heavy-metal-associated domain (HMA) is a conserved domain of approximately 30 amino acid ...
 71-124 9.54e-10

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: 52.99  E-value: 9.54e-10
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 347453628  71 IDGMHCKSCVSNIENALSTLHYVSSVVVSLESRSAIVKYNANlVTPEILRKMIE 124
Cdd:cd00371    4 VEGMTCAGCVSKIEKALEKLPGVESVEVDLETGKATVEYDPE-VSPEELLEAIE 56
TIGR00003 TIGR00003
copper ion binding protein; This model describes an apparently copper-specific subfamily of ...
 169-225 5.97e-09

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: 51.00  E-value: 5.97e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 347453628  169 INIDGMTCNSCVQSIEGVISKKKGVKSIHVSLENSNGTIEYDPLLISPEILKEAIED 225
Cdd:TIGR00003   4 FQVKGMSCNHCVDKIEKFVGEIEGVSKVKVQLEKEKVVVEFDAPNVSATEICEAILD 60
HMA pfam00403
Heavy-metal-associated domain;
68-124 1.92e-07

Heavy-metal-associated domain;


Pssm-ID: 459804 [Multi-domain]  Cd Length: 58  Bit Score: 46.46  E-value: 1.92e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 347453628   68 IFIIDGMHCKSCVSNIENALSTLHYVSSVVVSLESRSAIVKYNANLVTPEILRKMIE 124
Cdd:pfam00403   1 TFRVSGMHCGGCAAKVEKALSELPGVLSVSVDLATKTVTVTGDAESTKLEKLVEAIE 57
CopZ COG2608
Copper chaperone CopZ [Inorganic ion transport and metabolism];
66-124 2.67e-07

Copper chaperone CopZ [Inorganic ion transport and metabolism];


Pssm-ID: 442020 [Multi-domain]  Cd Length: 71  Bit Score: 46.44  E-value: 2.67e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 347453628  66 TAIFIIDGMHCKSCVSNIENALSTLHYVSSVVVSLESRSAIVKYNANLVTPEILRKMIE 124
Cdd:COG2608    3 TVTLKVEGMTCGHCVARVEKALKALDGVASVEVDLATGTATVTYDPEKVSLEDIKAAIE 61
ZntA COG2217
Cation-transporting P-type ATPase [Inorganic ion transport and metabolism];
66-138 3.76e-06

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


Pssm-ID: 441819 [Multi-domain]  Cd Length: 717  Bit Score: 47.06  E-value: 3.76e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 347453628  66 TAIFIIDGMHCKSCVSNIENALSTLHYVSSVVVSLESRSAIVKYNANLVTPEILRKMIETVSpgqYTVSIASE 138
Cdd:COG2217    2 RVRLRIEGMTCAACAWLIEKALRKLPGVLSARVNLATERARVEYDPGKVSLEELIAAVEKAG---YEAEPADA 71
PRK13748 PRK13748
putative mercuric reductase; Provisional
 166-224 1.18e-05

putative mercuric reductase; Provisional


Pssm-ID: 184298 [Multi-domain]  Cd Length: 561  Bit Score: 45.53  E-value: 1.18e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 347453628 166 ETVINIDGMTCNSCVQSIEGVISKKKGVKSIHVSLENSNGTIEYDPlLISPEILKEAIE 224
Cdd:PRK13748   1 MTTLKITGMTCDSCAAHVKDALEKVPGVQSADVSYPKGSAQLAIEV-GTSPDALTAAVA 58
UxxU_metal_bind NF041115
metal-binding (seleno)protein; Known members of this family are selenoproteins with an ...
 163-224 5.40e-04

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: 37.31  E-value: 5.40e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 347453628 163 LTQETVINIDGMTCNSCVQSIEGVISKKKGVKSIHVSLENSNGTIEYDPLLISPEILKEAIE 224
Cdd:NF041115   2 LAETVILAIEGMTUASUPLIAKKALEGLEGVEKADVSYKEGRAEVAFDPDKVSAAQMVDAVN 63
copA PRK10671
copper-exporting P-type ATPase CopA;
70-135 1.36e-03

copper-exporting P-type ATPase CopA;


Pssm-ID: 182635 [Multi-domain]  Cd Length: 834  Bit Score: 39.34  E-value: 1.36e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 347453628  70 IIDGMHCKSCVSNIENALSTLHYVSSVVVSLESRSAIVKYNANlvtPEILrkmIETVSPGQYTVSI 135
Cdd:PRK10671 104 LLSGMSCASCVSRVQNALQSVPGVTQARVNLAERTALVMGSAS---PQDL---VQAVEKAGYGAEA 163
 
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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