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Conserved domains on  [gi|2006698672|gb|QTA08600|]
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DNA repair protein RadC [Escherichia albertii]

Protein Classification

JAB domain-containing protein( domain architecture ID 11477685)

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

Gene Ontology:  GO:0046872|GO:0008237|GO:0006508

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK00024 PRK00024
DNA repair protein RadC;
8-222 1.43e-119

DNA repair protein RadC;


:

Pssm-ID: 178801 [Multi-domain]  Cd Length: 224  Bit Score: 338.97  E-value: 1.43e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006698672   8 LMPREKMLRLGISSLTDVELLALFLRTGTRGKDVLTLSKEMLENFGSLYGLLSSEYEQFSGVHGIGVAKFAQLKGIAELA 87
Cdd:PRK00024   10 ERPRERLLKYGAAALSDAELLAILLRTGTKGKSVLDLARELLQRFGSLRGLLDASLEELQSIKGIGPAKAAQLKAALELA 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006698672  88 RRYYNVRMREESPLLSPEMTREFLQSQLTGEEREIFMVIFLDSQHRVLTHSRLFSGTLNHVEVHPREIVREAIKINASAL 167
Cdd:PRK00024   90 RRILAERLREREVLLSPEDVADYLMAELRDEEQEHFVVLFLDTKNRVIADEELFIGTLNSSIVHPREIVKRALKLNAAAL 169

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2006698672 168 ILAHNHPSGCAEPSKADKLITERIIKSCQFMELRVLDHIVIGRGEYVSFAERGWI 222
Cdd:PRK00024  170 ILAHNHPSGDPEPSQADILITKRLKEAGELLGIRLLDHIIIGDGEYVSFAERGLL 224
 
Name Accession Description Interval E-value
PRK00024 PRK00024
DNA repair protein RadC;
8-222 1.43e-119

DNA repair protein RadC;


Pssm-ID: 178801 [Multi-domain]  Cd Length: 224  Bit Score: 338.97  E-value: 1.43e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006698672   8 LMPREKMLRLGISSLTDVELLALFLRTGTRGKDVLTLSKEMLENFGSLYGLLSSEYEQFSGVHGIGVAKFAQLKGIAELA 87
Cdd:PRK00024   10 ERPRERLLKYGAAALSDAELLAILLRTGTKGKSVLDLARELLQRFGSLRGLLDASLEELQSIKGIGPAKAAQLKAALELA 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006698672  88 RRYYNVRMREESPLLSPEMTREFLQSQLTGEEREIFMVIFLDSQHRVLTHSRLFSGTLNHVEVHPREIVREAIKINASAL 167
Cdd:PRK00024   90 RRILAERLREREVLLSPEDVADYLMAELRDEEQEHFVVLFLDTKNRVIADEELFIGTLNSSIVHPREIVKRALKLNAAAL 169

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2006698672 168 ILAHNHPSGCAEPSKADKLITERIIKSCQFMELRVLDHIVIGRGEYVSFAERGWI 222
Cdd:PRK00024  170 ILAHNHPSGDPEPSQADILITKRLKEAGELLGIRLLDHIIIGDGEYVSFAERGLL 224
radc TIGR00608
DNA repair protein radc; The genes in this family for which the functions are known have an as ...
 9-222 1.47e-117

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: 333.64  E-value: 1.47e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006698672   9 MPREKMLRLGISSLTDVELLALFLRTGTRGK-DVLTLSKEMLENFG---SLYGLLSSEYEQFSGVHGIGVAKFAQLKGIA 84
Cdd:TIGR00608   1 MPREKLLKFGAEALSDYELLAIILRTGTPKGlDVLSLSKRLLDVFGrqdSLGHLLSAPPEELSSVPGIGEAKAIQLKAAV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006698672  85 ELARRYYNVRMREESPLLSPEMTREFLQSQLTGEEREIFMVIFLDSQHRVLTHSRLFSGTLNHVEVHPREIVREAIKINA 164
Cdd:TIGR00608  81 ELAKRYAKSRMLERPVIRSPEAAAEFLHTDLAHETREHFMVLFLDRKNRLIAKEVVFIGTVNHVPVHPREIFKEALKLSA 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2006698672 165 SALILAHNHPSGCAEPSKADKLITERIIKSCQFMELRVLDHIVIGRGEYVSFAERGWI 222
Cdd:TIGR00608 161 SALILAHNHPSGEPSPSQEDILITERLRKAAELLGIELLDHLIIGKGRYVSFREEGLL 218
RadC COG2003
DNA repair protein RadC, contains a helix-hairpin-helix DNA-binding motif [Replication, ...
 1-222 2.00e-111

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: 318.16  E-value: 2.00e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006698672   1 MKSNTELLMPREKMLRLGISSLTDVELLALFLRTGTRGKDVLTLSKEMLENFGSLYGLLSSEYEQFSGVHGIGVAKFAQL 80
Cdd:COG2003     3 IKDLPHRERPRERLLAKGAAALSDAELLAILLRTGTPGKDAVELAKELLARFGSLRGLLRASVEELRKIKGIGEAKAAQL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006698672  81 KGIAELARRYYNVRMREESPLLSPEMTREFLQSQLTGEEREIFMVIFLDSQHRVLTHSRLFSGTLNHVEVHPREIVREAI 160
Cdd:COG2003    83 KAALELGRRLLREELEERPVISSPEDVADYLRARLAHLPREVFRVLFLDTKNRLIADEELSIGTLNHTPVYPREVFKRAL 162

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2006698672 161 KINASALILAHNHPSGCAEPSKADKLITERIIKSCQFMELRVLDHIVIGRGEYVSFAERGWI 222
Cdd:COG2003   163 RLNAAAIILAHNHPSGDPEPSRADIELTRRLKEAGELLGIRLLDHIIIGDGGYVSFAEEGLL 224
MPN_DUF2466 cd08071
Mov34/MPN/PAD-1 family; Mov34 DUF2466 (also known as DNA repair protein RadC) domain of ...
 105-217 1.36e-56

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: 175.26  E-value: 1.36e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006698672 105 EMTREFLQSQLTGEEREIFMVIFLDSQHRVLTHSRLFSGTLNHVEVHPREIVREAIKINASALILAHNHPSGCAEPSKAD 184
Cdd:cd08071     1 EDVAEYLREELGDLDQEEFVVLLLDTKNRLIAVETISVGTLNSSLVHPREIFKEALRHNAAAIILAHNHPSGDPTPSRED 80

                          90       100       110
                  ....*....|....*....|....*....|...
gi 2006698672 185 KLITERIIKSCQFMELRVLDHIVIGRGEYVSFA 217
Cdd:cd08071    81 IELTKRLKEAGELLGIRLLDHIIVGDGGYFSFR 113
RadC pfam04002
RadC-like JAB domain; A family of proteins present widely across the bacteria. This family was ...
 101-213 2.07e-55

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: 172.20  E-value: 2.07e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006698672 101 LLSPEMTREFLQSQLTGEEREIFMVIFLDSQHRVLTHSRLFSGTLNHVEVHPREIVREAIKINASALILAHNHPSGCAEP 180
Cdd:pfam04002   1 ITSPEDVAEYLMEELRDLDQEVFRVLFLDTKNRLIADEELSEGTLNSTLVHPREIFKRALRLNAAAVILAHNHPSGDPEP 80

                          90       100       110
                  ....*....|....*....|....*....|...
gi 2006698672 181 SKADKLITERIIKSCQFMELRVLDHIVIGRGEY 213
Cdd:pfam04002  81 SREDIELTRRLKEAGELLGIRLLDHIIIGDGGY 113
 
Name Accession Description Interval E-value
PRK00024 PRK00024
DNA repair protein RadC;
8-222 1.43e-119

DNA repair protein RadC;


Pssm-ID: 178801 [Multi-domain]  Cd Length: 224  Bit Score: 338.97  E-value: 1.43e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006698672   8 LMPREKMLRLGISSLTDVELLALFLRTGTRGKDVLTLSKEMLENFGSLYGLLSSEYEQFSGVHGIGVAKFAQLKGIAELA 87
Cdd:PRK00024   10 ERPRERLLKYGAAALSDAELLAILLRTGTKGKSVLDLARELLQRFGSLRGLLDASLEELQSIKGIGPAKAAQLKAALELA 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006698672  88 RRYYNVRMREESPLLSPEMTREFLQSQLTGEEREIFMVIFLDSQHRVLTHSRLFSGTLNHVEVHPREIVREAIKINASAL 167
Cdd:PRK00024   90 RRILAERLREREVLLSPEDVADYLMAELRDEEQEHFVVLFLDTKNRVIADEELFIGTLNSSIVHPREIVKRALKLNAAAL 169

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2006698672 168 ILAHNHPSGCAEPSKADKLITERIIKSCQFMELRVLDHIVIGRGEYVSFAERGWI 222
Cdd:PRK00024  170 ILAHNHPSGDPEPSQADILITKRLKEAGELLGIRLLDHIIIGDGEYVSFAERGLL 224
radc TIGR00608
DNA repair protein radc; The genes in this family for which the functions are known have an as ...
 9-222 1.47e-117

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: 333.64  E-value: 1.47e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006698672   9 MPREKMLRLGISSLTDVELLALFLRTGTRGK-DVLTLSKEMLENFG---SLYGLLSSEYEQFSGVHGIGVAKFAQLKGIA 84
Cdd:TIGR00608   1 MPREKLLKFGAEALSDYELLAIILRTGTPKGlDVLSLSKRLLDVFGrqdSLGHLLSAPPEELSSVPGIGEAKAIQLKAAV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006698672  85 ELARRYYNVRMREESPLLSPEMTREFLQSQLTGEEREIFMVIFLDSQHRVLTHSRLFSGTLNHVEVHPREIVREAIKINA 164
Cdd:TIGR00608  81 ELAKRYAKSRMLERPVIRSPEAAAEFLHTDLAHETREHFMVLFLDRKNRLIAKEVVFIGTVNHVPVHPREIFKEALKLSA 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2006698672 165 SALILAHNHPSGCAEPSKADKLITERIIKSCQFMELRVLDHIVIGRGEYVSFAERGWI 222
Cdd:TIGR00608 161 SALILAHNHPSGEPSPSQEDILITERLRKAAELLGIELLDHLIIGKGRYVSFREEGLL 218
RadC COG2003
DNA repair protein RadC, contains a helix-hairpin-helix DNA-binding motif [Replication, ...
 1-222 2.00e-111

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: 318.16  E-value: 2.00e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006698672   1 MKSNTELLMPREKMLRLGISSLTDVELLALFLRTGTRGKDVLTLSKEMLENFGSLYGLLSSEYEQFSGVHGIGVAKFAQL 80
Cdd:COG2003     3 IKDLPHRERPRERLLAKGAAALSDAELLAILLRTGTPGKDAVELAKELLARFGSLRGLLRASVEELRKIKGIGEAKAAQL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006698672  81 KGIAELARRYYNVRMREESPLLSPEMTREFLQSQLTGEEREIFMVIFLDSQHRVLTHSRLFSGTLNHVEVHPREIVREAI 160
Cdd:COG2003    83 KAALELGRRLLREELEERPVISSPEDVADYLRARLAHLPREVFRVLFLDTKNRLIADEELSIGTLNHTPVYPREVFKRAL 162

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2006698672 161 KINASALILAHNHPSGCAEPSKADKLITERIIKSCQFMELRVLDHIVIGRGEYVSFAERGWI 222
Cdd:COG2003   163 RLNAAAIILAHNHPSGDPEPSRADIELTRRLKEAGELLGIRLLDHIIIGDGGYVSFAEEGLL 224
MPN_DUF2466 cd08071
Mov34/MPN/PAD-1 family; Mov34 DUF2466 (also known as DNA repair protein RadC) domain of ...
 105-217 1.36e-56

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: 175.26  E-value: 1.36e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006698672 105 EMTREFLQSQLTGEEREIFMVIFLDSQHRVLTHSRLFSGTLNHVEVHPREIVREAIKINASALILAHNHPSGCAEPSKAD 184
Cdd:cd08071     1 EDVAEYLREELGDLDQEEFVVLLLDTKNRLIAVETISVGTLNSSLVHPREIFKEALRHNAAAIILAHNHPSGDPTPSRED 80

                          90       100       110
                  ....*....|....*....|....*....|...
gi 2006698672 185 KLITERIIKSCQFMELRVLDHIVIGRGEYVSFA 217
Cdd:cd08071    81 IELTKRLKEAGELLGIRLLDHIIVGDGGYFSFR 113
RadC pfam04002
RadC-like JAB domain; A family of proteins present widely across the bacteria. This family was ...
 101-213 2.07e-55

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: 172.20  E-value: 2.07e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006698672 101 LLSPEMTREFLQSQLTGEEREIFMVIFLDSQHRVLTHSRLFSGTLNHVEVHPREIVREAIKINASALILAHNHPSGCAEP 180
Cdd:pfam04002   1 ITSPEDVAEYLMEELRDLDQEVFRVLFLDTKNRLIADEELSEGTLNSTLVHPREIFKRALRLNAAAVILAHNHPSGDPEP 80

                          90       100       110
                  ....*....|....*....|....*....|...
gi 2006698672 181 SKADKLITERIIKSCQFMELRVLDHIVIGRGEY 213
Cdd:pfam04002  81 SREDIELTRRLKEAGELLGIRLLDHIIIGDGGY 113
UPF0758_N pfam20582
UPF0758 N-terminal; This domain is functionally uncharacterized, found at the N-terminal of ...
 10-72 3.05e-21

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: 83.48  E-value: 3.05e-21
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2006698672  10 PREKMLRLGISSLTDVELLALFLRTGTRGKDVLTLSKEMLEnFGSLYGLLSSEYEQFSGVHGI 72
Cdd:pfam20582  10 PREKLLRYGAEALSDAELLAILLGSGTKGESAVDLARRLLH-FGGLRGLLKASVEELMKIKGI 71
MPN_prok_mb cd08059
Mpr1p, Pad1p N-terminal (MPN) domains with catalytic isopeptidase activity (metal-binding); ...
 125-216 4.37e-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: 44.09  E-value: 4.37e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006698672 125 VIFLDSQHRVLTHSRLFSGTLnhvEVHPReIVREAIKINASALILAHNHPSGCAEPSKADKLITERIikscqfmelrVLD 204
Cdd:cd08059    21 FLSGSKDNVMDELIFLPFVSG---SVSAV-IDLAALEIGMKVVGLVHSHPSGSCRPSEADLSLFTRF----------GLY 86

                          90
                  ....*....|..
gi 2006698672 205 HIVIGRGEYVSF 216
Cdd:cd08059    87 HVIVCYPYENSW 98
 
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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