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Conserved domains on  [gi|522083889|ref|WP_020595098|]
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DNA repair protein RadC [Spirosoma panaciterrae]

Protein Classification

RadC family protein( domain architecture ID 11449512)

RadC family protein is a JAB or Mpr1p, Pad1p N-terminal (MPN) domain-containing protein that contains the signature JAB1/MPN/Mov34 metalloenzyme (JAMM) motif, which is involved in zinc ion coordination; a function as a nuclease has been suggested

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
RadC COG2003
DNA repair protein RadC, contains a helix-hairpin-helix DNA-binding motif [Replication, ...
8-231 3.97e-103

DNA repair protein RadC, contains a helix-hairpin-helix DNA-binding motif [Replication, recombination and repair];


:

Pssm-ID: 441606 [Multi-domain]  Cd Length: 224  Bit Score: 297.74  E-value: 3.97e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522083889   8 TIQSWAEEDRPREKLMLKGKAALSEAELIAILINSGTVDLTAVDVAKIILKSVNNnLNDLARLSIKDLSKFRGIGEAKAI 87
Cdd:COG2003    2 KIKDLPHRERPRERLLAKGAAALSDAELLAILLRTGTPGKDAVELAKELLARFGS-LRGLLRASVEELRKIKGIGEAKAA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522083889  88 SIVAALELGRRRKEQDRPQRARVTCSRDAYNEMIPHLIDKPHEEFWILLMNRANEILRPVQISSGGISGTVADPKIIFKQ 167
Cdd:COG2003   81 QLKAALELGRRLLREELEERPVISSPEDVADYLRARLAHLPREVFRVLFLDTKNRLIADEELSIGTLNHTPVYPREVFKR 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 522083889 168 AIEYLASSIILFHNHPSGNLMPSQADKDLTRKLKDAGRILDIPVLDHLIFTDKAYYSFADEGIL 231
Cdd:COG2003  161 ALRLNAAAIILAHNHPSGDPEPSRADIELTRRLKEAGELLGIRLLDHIIIGDGGYVSFAEEGLL 224
 
Name Accession Description Interval E-value
RadC COG2003
DNA repair protein RadC, contains a helix-hairpin-helix DNA-binding motif [Replication, ...
8-231 3.97e-103

DNA repair protein RadC, contains a helix-hairpin-helix DNA-binding motif [Replication, recombination and repair];


Pssm-ID: 441606 [Multi-domain]  Cd Length: 224  Bit Score: 297.74  E-value: 3.97e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522083889   8 TIQSWAEEDRPREKLMLKGKAALSEAELIAILINSGTVDLTAVDVAKIILKSVNNnLNDLARLSIKDLSKFRGIGEAKAI 87
Cdd:COG2003    2 KIKDLPHRERPRERLLAKGAAALSDAELLAILLRTGTPGKDAVELAKELLARFGS-LRGLLRASVEELRKIKGIGEAKAA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522083889  88 SIVAALELGRRRKEQDRPQRARVTCSRDAYNEMIPHLIDKPHEEFWILLMNRANEILRPVQISSGGISGTVADPKIIFKQ 167
Cdd:COG2003   81 QLKAALELGRRLLREELEERPVISSPEDVADYLRARLAHLPREVFRVLFLDTKNRLIADEELSIGTLNHTPVYPREVFKR 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 522083889 168 AIEYLASSIILFHNHPSGNLMPSQADKDLTRKLKDAGRILDIPVLDHLIFTDKAYYSFADEGIL 231
Cdd:COG2003  161 ALRLNAAAIILAHNHPSGDPEPSRADIELTRRLKEAGELLGIRLLDHIIIGDGGYVSFAEEGLL 224
PRK00024 PRK00024
DNA repair protein RadC;
9-231 7.00e-79

DNA repair protein RadC;


Pssm-ID: 178801 [Multi-domain]  Cd Length: 224  Bit Score: 236.12  E-value: 7.00e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522083889   9 IQSWAEEDRPREKLMLKGKAALSEAELIAILINSGTVDLTAVDVAKIILKSvNNNLNDLARLSIKDLSKFRGIGEAKAIS 88
Cdd:PRK00024   3 IKDWPEEERPRERLLKYGAAALSDAELLAILLRTGTKGKSVLDLARELLQR-FGSLRGLLDASLEELQSIKGIGPAKAAQ 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522083889  89 IVAALELGRRRKEQDRPQRARVTCSRDAYNEMIPHLIDKPHEEFWILLMNRANEILRPVQISSGGISGTVADPKIIFKQA 168
Cdd:PRK00024  82 LKAALELARRILAERLREREVLLSPEDVADYLMAELRDEEQEHFVVLFLDTKNRVIADEELFIGTLNSSIVHPREIVKRA 161
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 522083889 169 IEYLASSIILFHNHPSGNLMPSQADKDLTRKLKDAGRILDIPVLDHLIFTDKAYYSFADEGIL 231
Cdd:PRK00024 162 LKLNAAALILAHNHPSGDPEPSQADILITKRLKEAGELLGIRLLDHIIIGDGEYVSFAERGLL 224
MPN_DUF2466 cd08071
Mov34/MPN/PAD-1 family; Mov34 DUF2466 (also known as DNA repair protein RadC) domain of ...
114-226 5.28e-54

Mov34/MPN/PAD-1 family; Mov34 DUF2466 (also known as DNA repair protein RadC) domain of unknown function contains the signature JAB1/MPN/Mov34 metalloenzyme (JAMM) motif, EXnHS/THX7SXXD, which is involved in zinc ion coordination and provides the active site for isopeptidase activity. However, to date, the name RadC has been misleading and no function has been determined.


Pssm-ID: 163702  Cd Length: 113  Bit Score: 169.09  E-value: 5.28e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522083889 114 RDAYNEMIPHLIDKPHEEFWILLMNRANEILRPVQISSGGISGTVADPKIIFKQAIEYLASSIILFHNHPSGNLMPSQAD 193
Cdd:cd08071    1 EDVAEYLREELGDLDQEEFVVLLLDTKNRLIAVETISVGTLNSSLVHPREIFKEALRHNAAAIILAHNHPSGDPTPSRED 80
                         90       100       110
                 ....*....|....*....|....*....|...
gi 522083889 194 KDLTRKLKDAGRILDIPVLDHLIFTDKAYYSFA 226
Cdd:cd08071   81 IELTKRLKEAGELLGIRLLDHIIVGDGGYFSFR 113
radc TIGR00608
DNA repair protein radc; The genes in this family for which the functions are known have an as ...
17-231 3.77e-51

DNA repair protein radc; The genes in this family for which the functions are known have an as yet porrly defined role in determining sensitivity to DNA damaging agents such as UV irradiation. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 273171 [Multi-domain]  Cd Length: 218  Bit Score: 165.30  E-value: 3.77e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522083889   17 RPREKLMLKGKAALSEAELIAILINSGTVD-LTAVDVAKIILKSV--NNNLNDLARLSIKDLSKFRGIGEAKAISIVAAL 93
Cdd:TIGR00608   1 MPREKLLKFGAEALSDYELLAIILRTGTPKgLDVLSLSKRLLDVFgrQDSLGHLLSAPPEELSSVPGIGEAKAIQLKAAV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522083889   94 ELGRRRKEQDRPQRARVTCSRDAYNEMIPHLIDKPHEEFWILLMNRANEILRPVQISSGGISGTVADPKIIFKQAIEYLA 173
Cdd:TIGR00608  81 ELAKRYAKSRMLERPVIRSPEAAAEFLHTDLAHETREHFMVLFLDRKNRLIAKEVVFIGTVNHVPVHPREIFKEALKLSA 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 522083889  174 SSIILFHNHPSGNLMPSQADKDLTRKLKDAGRILDIPVLDHLIFTDKAYYSFADEGIL 231
Cdd:TIGR00608 161 SALILAHNHPSGEPSPSQEDILITERLRKAAELLGIELLDHLIIGKGRYVSFREEGLL 218
RadC pfam04002
RadC-like JAB domain; A family of proteins present widely across the bacteria. This family was ...
110-222 1.96e-50

RadC-like JAB domain; A family of proteins present widely across the bacteria. This family was named initially with reference to the E. coli radC102 mutation which suggested that RadC was involved in repair of DNA lesions. However the relevant mutation has subsequently been shown to be in recG, where radC is in fact an allele of recG. In addition, a personal communication from Claverys, J-P, et al, indicates a total failure of all attempts to characterize a radiation-related function for RadC in Streptococcus pneumoniae, suggesting that it is not involved in repair of DNA lesions, in recombination during transformation, in gene conversion, nor in mismatch repair. Computational analysis, however, provides a possible function. The RadC-like family belong to the JAB superfamily of metalloproteins. The domain shows fusions to an N-terminal Helix-hairpin-Helix (HhH) domain in most instances. Other domain combinations include fusions to the anti-restriction module ArdC, the DinG/RAD3-like superfamily II helicases and the DNAG-like primase. In some bacteria, closely related DinG/Rad3- like superfamily II helicases are fused to a 3'-5' exonuclease in the same position as the RadC-like JAB domain. These conserved domain associations lead to the hypothesis that the RadC-like JAB domains might function as a nuclease.


Pssm-ID: 461124  Cd Length: 113  Bit Score: 159.88  E-value: 1.96e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522083889  110 VTCSRDAYNEMIPHLIDKPHEEFWILLMNRANEILRPVQISSGGISGTVADPKIIFKQAIEYLASSIILFHNHPSGNLMP 189
Cdd:pfam04002   1 ITSPEDVAEYLMEELRDLDQEVFRVLFLDTKNRLIADEELSEGTLNSTLVHPREIFKRALRLNAAAVILAHNHPSGDPEP 80
                          90       100       110
                  ....*....|....*....|....*....|...
gi 522083889  190 SQADKDLTRKLKDAGRILDIPVLDHLIFTDKAY 222
Cdd:pfam04002  81 SREDIELTRRLKEAGELLGIRLLDHIIIGDGGY 113
 
Name Accession Description Interval E-value
RadC COG2003
DNA repair protein RadC, contains a helix-hairpin-helix DNA-binding motif [Replication, ...
8-231 3.97e-103

DNA repair protein RadC, contains a helix-hairpin-helix DNA-binding motif [Replication, recombination and repair];


Pssm-ID: 441606 [Multi-domain]  Cd Length: 224  Bit Score: 297.74  E-value: 3.97e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522083889   8 TIQSWAEEDRPREKLMLKGKAALSEAELIAILINSGTVDLTAVDVAKIILKSVNNnLNDLARLSIKDLSKFRGIGEAKAI 87
Cdd:COG2003    2 KIKDLPHRERPRERLLAKGAAALSDAELLAILLRTGTPGKDAVELAKELLARFGS-LRGLLRASVEELRKIKGIGEAKAA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522083889  88 SIVAALELGRRRKEQDRPQRARVTCSRDAYNEMIPHLIDKPHEEFWILLMNRANEILRPVQISSGGISGTVADPKIIFKQ 167
Cdd:COG2003   81 QLKAALELGRRLLREELEERPVISSPEDVADYLRARLAHLPREVFRVLFLDTKNRLIADEELSIGTLNHTPVYPREVFKR 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 522083889 168 AIEYLASSIILFHNHPSGNLMPSQADKDLTRKLKDAGRILDIPVLDHLIFTDKAYYSFADEGIL 231
Cdd:COG2003  161 ALRLNAAAIILAHNHPSGDPEPSRADIELTRRLKEAGELLGIRLLDHIIIGDGGYVSFAEEGLL 224
PRK00024 PRK00024
DNA repair protein RadC;
9-231 7.00e-79

DNA repair protein RadC;


Pssm-ID: 178801 [Multi-domain]  Cd Length: 224  Bit Score: 236.12  E-value: 7.00e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522083889   9 IQSWAEEDRPREKLMLKGKAALSEAELIAILINSGTVDLTAVDVAKIILKSvNNNLNDLARLSIKDLSKFRGIGEAKAIS 88
Cdd:PRK00024   3 IKDWPEEERPRERLLKYGAAALSDAELLAILLRTGTKGKSVLDLARELLQR-FGSLRGLLDASLEELQSIKGIGPAKAAQ 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522083889  89 IVAALELGRRRKEQDRPQRARVTCSRDAYNEMIPHLIDKPHEEFWILLMNRANEILRPVQISSGGISGTVADPKIIFKQA 168
Cdd:PRK00024  82 LKAALELARRILAERLREREVLLSPEDVADYLMAELRDEEQEHFVVLFLDTKNRVIADEELFIGTLNSSIVHPREIVKRA 161
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 522083889 169 IEYLASSIILFHNHPSGNLMPSQADKDLTRKLKDAGRILDIPVLDHLIFTDKAYYSFADEGIL 231
Cdd:PRK00024 162 LKLNAAALILAHNHPSGDPEPSQADILITKRLKEAGELLGIRLLDHIIIGDGEYVSFAERGLL 224
MPN_DUF2466 cd08071
Mov34/MPN/PAD-1 family; Mov34 DUF2466 (also known as DNA repair protein RadC) domain of ...
114-226 5.28e-54

Mov34/MPN/PAD-1 family; Mov34 DUF2466 (also known as DNA repair protein RadC) domain of unknown function contains the signature JAB1/MPN/Mov34 metalloenzyme (JAMM) motif, EXnHS/THX7SXXD, which is involved in zinc ion coordination and provides the active site for isopeptidase activity. However, to date, the name RadC has been misleading and no function has been determined.


Pssm-ID: 163702  Cd Length: 113  Bit Score: 169.09  E-value: 5.28e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522083889 114 RDAYNEMIPHLIDKPHEEFWILLMNRANEILRPVQISSGGISGTVADPKIIFKQAIEYLASSIILFHNHPSGNLMPSQAD 193
Cdd:cd08071    1 EDVAEYLREELGDLDQEEFVVLLLDTKNRLIAVETISVGTLNSSLVHPREIFKEALRHNAAAIILAHNHPSGDPTPSRED 80
                         90       100       110
                 ....*....|....*....|....*....|...
gi 522083889 194 KDLTRKLKDAGRILDIPVLDHLIFTDKAYYSFA 226
Cdd:cd08071   81 IELTKRLKEAGELLGIRLLDHIIVGDGGYFSFR 113
radc TIGR00608
DNA repair protein radc; The genes in this family for which the functions are known have an as ...
17-231 3.77e-51

DNA repair protein radc; The genes in this family for which the functions are known have an as yet porrly defined role in determining sensitivity to DNA damaging agents such as UV irradiation. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 273171 [Multi-domain]  Cd Length: 218  Bit Score: 165.30  E-value: 3.77e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522083889   17 RPREKLMLKGKAALSEAELIAILINSGTVD-LTAVDVAKIILKSV--NNNLNDLARLSIKDLSKFRGIGEAKAISIVAAL 93
Cdd:TIGR00608   1 MPREKLLKFGAEALSDYELLAIILRTGTPKgLDVLSLSKRLLDVFgrQDSLGHLLSAPPEELSSVPGIGEAKAIQLKAAV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522083889   94 ELGRRRKEQDRPQRARVTCSRDAYNEMIPHLIDKPHEEFWILLMNRANEILRPVQISSGGISGTVADPKIIFKQAIEYLA 173
Cdd:TIGR00608  81 ELAKRYAKSRMLERPVIRSPEAAAEFLHTDLAHETREHFMVLFLDRKNRLIAKEVVFIGTVNHVPVHPREIFKEALKLSA 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 522083889  174 SSIILFHNHPSGNLMPSQADKDLTRKLKDAGRILDIPVLDHLIFTDKAYYSFADEGIL 231
Cdd:TIGR00608 161 SALILAHNHPSGEPSPSQEDILITERLRKAAELLGIELLDHLIIGKGRYVSFREEGLL 218
RadC pfam04002
RadC-like JAB domain; A family of proteins present widely across the bacteria. This family was ...
110-222 1.96e-50

RadC-like JAB domain; A family of proteins present widely across the bacteria. This family was named initially with reference to the E. coli radC102 mutation which suggested that RadC was involved in repair of DNA lesions. However the relevant mutation has subsequently been shown to be in recG, where radC is in fact an allele of recG. In addition, a personal communication from Claverys, J-P, et al, indicates a total failure of all attempts to characterize a radiation-related function for RadC in Streptococcus pneumoniae, suggesting that it is not involved in repair of DNA lesions, in recombination during transformation, in gene conversion, nor in mismatch repair. Computational analysis, however, provides a possible function. The RadC-like family belong to the JAB superfamily of metalloproteins. The domain shows fusions to an N-terminal Helix-hairpin-Helix (HhH) domain in most instances. Other domain combinations include fusions to the anti-restriction module ArdC, the DinG/RAD3-like superfamily II helicases and the DNAG-like primase. In some bacteria, closely related DinG/Rad3- like superfamily II helicases are fused to a 3'-5' exonuclease in the same position as the RadC-like JAB domain. These conserved domain associations lead to the hypothesis that the RadC-like JAB domains might function as a nuclease.


Pssm-ID: 461124  Cd Length: 113  Bit Score: 159.88  E-value: 1.96e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522083889  110 VTCSRDAYNEMIPHLIDKPHEEFWILLMNRANEILRPVQISSGGISGTVADPKIIFKQAIEYLASSIILFHNHPSGNLMP 189
Cdd:pfam04002   1 ITSPEDVAEYLMEELRDLDQEVFRVLFLDTKNRLIADEELSEGTLNSTLVHPREIFKRALRLNAAAVILAHNHPSGDPEP 80
                          90       100       110
                  ....*....|....*....|....*....|...
gi 522083889  190 SQADKDLTRKLKDAGRILDIPVLDHLIFTDKAY 222
Cdd:pfam04002  81 SREDIELTRRLKEAGELLGIRLLDHIIIGDGGY 113
UPF0758_N pfam20582
UPF0758 N-terminal; This domain is functionally uncharacterized, found at the N-terminal of ...
9-81 1.57e-28

UPF0758 N-terminal; This domain is functionally uncharacterized, found at the N-terminal of the uncharacterized UPF0758 proteins from bacteria and archaea, and is approximately 90 amino acids in length. UPF0758 was previously known as the radC family, a name that was assigned according to the radC102 mutant of E. coli which was later demonstrated to be an allele of the transcription-repair-coupling factor recG. UPF0758 has been described as a putative JAMM-family deubiquitinating enzyme, but its function remains to be determined. Structure prediction using Colab notebook from AlphaFold DB suggests that it has an alpha bundle fold. It may contain two helix-hairpin-helix (HhH) motifs. This domain is found in association with pfam04002.


Pssm-ID: 466731 [Multi-domain]  Cd Length: 71  Bit Score: 102.36  E-value: 1.57e-28
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 522083889    9 IQSWAEEDRPREKLMLKGKAALSEAELIAILINSGTVDLTAVDVAKIILKSvnNNLNDLARLSIKDLSKFRGI 81
Cdd:pfam20582   1 IKDWPEDERPREKLLRYGAEALSDAELLAILLGSGTKGESAVDLARRLLHF--GGLRGLLKASVEELMKIKGI 71
MPN_prok_mb cd08059
Mpr1p, Pad1p N-terminal (MPN) domains with catalytic isopeptidase activity (metal-binding); ...
128-200 3.20e-06

Mpr1p, Pad1p N-terminal (MPN) domains with catalytic isopeptidase activity (metal-binding); prokaryotic; This family contains bacterial and archaeal MPN (also known as Mov34, PAD-1, JAMM, JAB, MPN+)-like domains. These catalytically active domains contain the signature JAB1/MPN/Mov34 metalloenzyme (JAMM) motif, EXnHS/THX7SXXD, which is involved in zinc ion coordination and provides the active site for isopeptidase activity for the release of ubiquitin from ubiquitinated proteins (thus having deubiquitinating (DUB) activity) that are tagged for degradation. The JAMM proteins likely hydrolyze ubiquitin conjugates in a manner similar to thermolysin, in which the zinc-polarized aqua ligand serves as the nucleophile, compared with the classical DUBs that do so with a cysteine residue in the active site.


Pssm-ID: 163690  Cd Length: 101  Bit Score: 44.47  E-value: 3.20e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 522083889 128 PHEEFWILLMNRANEILRPVQISSGgiSGTVAdpKIIFKQAIEYLASSIILFHNHPSGNLMPSQADKDLTRKL 200
Cdd:cd08059   15 PDEFCGFLSGSKDNVMDELIFLPFV--SGSVS--AVIDLAALEIGMKVVGLVHSHPSGSCRPSEADLSLFTRF 83
 
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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