NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|495291593|ref|WP_008016347|]
View 

DNA repair protein RadC [Pseudomonas sp. GM55]

Protein Classification

Mov34/MPN/PAD-1 family protein( domain architecture ID 1001617)

Mov34/MPN/PAD-1 family protein contains a protein domain of unknown function with 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

Gene Ontology:  GO:0046872|GO:0008237|GO:0006508
PubMed:  18556794|10369758

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
PRK00024 super family cl31993
DNA repair protein RadC;
26-165 2.54e-67

DNA repair protein RadC;


The actual alignment was detected with superfamily member PRK00024:

Pssm-ID: 178801 [Multi-domain]  Cd Length: 224  Bit Score: 204.15  E-value: 2.54e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495291593  26 ILQMAQQLAMSRLSKGRALTEPKQVFSHLQTLLQYHEYEVFALLLLDSKHRVIAFREIFRGTLDAASVYPREVVKIALEH 105
Cdd:PRK00024  85 ALELARRILAERLREREVLLSPEDVADYLMAELRDEEQEHFVVLFLDTKNRVIADEELFIGTLNSSIVHPREIVKRALKL 164

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 495291593 106 NAAAAILVHNHPSGDPEPSQSDRTLTTTLKNALNMVGTRILDHVVVGREGSVSLAEMGYL 165
Cdd:PRK00024 165 NAAALILAHNHPSGDPEPSQADILITKRLKEAGELLGIRLLDHIIIGDGEYVSFAERGLL 224
 
Name Accession Description Interval E-value
PRK00024 PRK00024
DNA repair protein RadC;
26-165 2.54e-67

DNA repair protein RadC;


Pssm-ID: 178801 [Multi-domain]  Cd Length: 224  Bit Score: 204.15  E-value: 2.54e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495291593  26 ILQMAQQLAMSRLSKGRALTEPKQVFSHLQTLLQYHEYEVFALLLLDSKHRVIAFREIFRGTLDAASVYPREVVKIALEH 105
Cdd:PRK00024  85 ALELARRILAERLREREVLLSPEDVADYLMAELRDEEQEHFVVLFLDTKNRVIADEELFIGTLNSSIVHPREIVKRALKL 164

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 495291593 106 NAAAAILVHNHPSGDPEPSQSDRTLTTTLKNALNMVGTRILDHVVVGREGSVSLAEMGYL 165
Cdd:PRK00024 165 NAAALILAHNHPSGDPEPSQADILITKRLKEAGELLGIRLLDHIIIGDGEYVSFAERGLL 224
RadC COG2003
DNA repair protein RadC, contains a helix-hairpin-helix DNA-binding motif [Replication, ...
 26-165 7.02e-64

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: 195.28  E-value: 7.02e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495291593  26 ILQMAQQLAMSRLSKGRALTEPKQVFSHLQTLLQYHEYEVFALLLLDSKHRVIAFREIFRGTLDAASVYPREVVKIALEH 105
Cdd:COG2003   85 ALELGRRLLREELEERPVISSPEDVADYLRARLAHLPREVFRVLFLDTKNRLIADEELSIGTLNHTPVYPREVFKRALRL 164

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 495291593 106 NAAAAILVHNHPSGDPEPSQSDRTLTTTLKNALNMVGTRILDHVVVGREGSVSLAEMGYL 165
Cdd:COG2003  165 NAAAIILAHNHPSGDPEPSRADIELTRRLKEAGELLGIRLLDHIIIGDGGYVSFAEEGLL 224
RadC pfam04002
RadC-like JAB domain; A family of proteins present widely across the bacteria. This family was ...
 44-155 1.16e-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: 170.66  E-value: 1.16e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495291593   44 LTEPKQVFSHLQTLLQYHEYEVFALLLLDSKHRVIAFREIFRGTLDAASVYPREVVKIALEHNAAAAILVHNHPSGDPEP 123
Cdd:pfam04002   1 ITSPEDVAEYLMEELRDLDQEVFRVLFLDTKNRLIADEELSEGTLNSTLVHPREIFKRALRLNAAAVILAHNHPSGDPEP 80

                          90       100       110
                  ....*....|....*....|....*....|..
gi 495291593  124 SQSDRTLTTTLKNALNMVGTRILDHVVVGREG 155
Cdd:pfam04002  81 SREDIELTRRLKEAGELLGIRLLDHIIIGDGG 112
MPN_DUF2466 cd08071
Mov34/MPN/PAD-1 family; Mov34 DUF2466 (also known as DNA repair protein RadC) domain of ...
 48-160 1.45e-53

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: 165.24  E-value: 1.45e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495291593  48 KQVFSHLQTLLQYHEYEVFALLLLDSKHRVIAFREIFRGTLDAASVYPREVVKIALEHNAAAAILVHNHPSGDPEPSQSD 127
Cdd:cd08071    1 EDVAEYLREELGDLDQEEFVVLLLDTKNRLIAVETISVGTLNSSLVHPREIFKEALRHNAAAIILAHNHPSGDPTPSRED 80

                         90       100       110
                 ....*....|....*....|....*....|...
gi 495291593 128 RTLTTTLKNALNMVGTRILDHVVVGREGSVSLA 160
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 ...
 26-165 3.69e-43

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: 142.58  E-value: 3.69e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495291593   26 ILQMAQQLAMSRLSKGRALTEPKQVFSHLQTLLQYHEYEVFALLLLDSKHRVIAFREIFRGTLDAASVYPREVVKIALEH 105
Cdd:TIGR00608  79 AVELAKRYAKSRMLERPVIRSPEAAAEFLHTDLAHETREHFMVLFLDRKNRLIAKEVVFIGTVNHVPVHPREIFKEALKL 158

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 495291593  106 NAAAAILVHNHPSGDPEPSQSDRTLTTTLKNALNMVGTRILDHVVVGREGSVSLAEMGYL 165
Cdd:TIGR00608 159 SASALILAHNHPSGEPSPSQEDILITERLRKAAELLGIELLDHLIIGKGRYVSFREEGLL 218
 
Name Accession Description Interval E-value
PRK00024 PRK00024
DNA repair protein RadC;
26-165 2.54e-67

DNA repair protein RadC;


Pssm-ID: 178801 [Multi-domain]  Cd Length: 224  Bit Score: 204.15  E-value: 2.54e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495291593  26 ILQMAQQLAMSRLSKGRALTEPKQVFSHLQTLLQYHEYEVFALLLLDSKHRVIAFREIFRGTLDAASVYPREVVKIALEH 105
Cdd:PRK00024  85 ALELARRILAERLREREVLLSPEDVADYLMAELRDEEQEHFVVLFLDTKNRVIADEELFIGTLNSSIVHPREIVKRALKL 164

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 495291593 106 NAAAAILVHNHPSGDPEPSQSDRTLTTTLKNALNMVGTRILDHVVVGREGSVSLAEMGYL 165
Cdd:PRK00024 165 NAAALILAHNHPSGDPEPSQADILITKRLKEAGELLGIRLLDHIIIGDGEYVSFAERGLL 224
RadC COG2003
DNA repair protein RadC, contains a helix-hairpin-helix DNA-binding motif [Replication, ...
 26-165 7.02e-64

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: 195.28  E-value: 7.02e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495291593  26 ILQMAQQLAMSRLSKGRALTEPKQVFSHLQTLLQYHEYEVFALLLLDSKHRVIAFREIFRGTLDAASVYPREVVKIALEH 105
Cdd:COG2003   85 ALELGRRLLREELEERPVISSPEDVADYLRARLAHLPREVFRVLFLDTKNRLIADEELSIGTLNHTPVYPREVFKRALRL 164

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 495291593 106 NAAAAILVHNHPSGDPEPSQSDRTLTTTLKNALNMVGTRILDHVVVGREGSVSLAEMGYL 165
Cdd:COG2003  165 NAAAIILAHNHPSGDPEPSRADIELTRRLKEAGELLGIRLLDHIIIGDGGYVSFAEEGLL 224
RadC pfam04002
RadC-like JAB domain; A family of proteins present widely across the bacteria. This family was ...
 44-155 1.16e-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: 170.66  E-value: 1.16e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495291593   44 LTEPKQVFSHLQTLLQYHEYEVFALLLLDSKHRVIAFREIFRGTLDAASVYPREVVKIALEHNAAAAILVHNHPSGDPEP 123
Cdd:pfam04002   1 ITSPEDVAEYLMEELRDLDQEVFRVLFLDTKNRLIADEELSEGTLNSTLVHPREIFKRALRLNAAAVILAHNHPSGDPEP 80

                          90       100       110
                  ....*....|....*....|....*....|..
gi 495291593  124 SQSDRTLTTTLKNALNMVGTRILDHVVVGREG 155
Cdd:pfam04002  81 SREDIELTRRLKEAGELLGIRLLDHIIIGDGG 112
MPN_DUF2466 cd08071
Mov34/MPN/PAD-1 family; Mov34 DUF2466 (also known as DNA repair protein RadC) domain of ...
 48-160 1.45e-53

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: 165.24  E-value: 1.45e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495291593  48 KQVFSHLQTLLQYHEYEVFALLLLDSKHRVIAFREIFRGTLDAASVYPREVVKIALEHNAAAAILVHNHPSGDPEPSQSD 127
Cdd:cd08071    1 EDVAEYLREELGDLDQEEFVVLLLDTKNRLIAVETISVGTLNSSLVHPREIFKEALRHNAAAIILAHNHPSGDPTPSRED 80

                         90       100       110
                 ....*....|....*....|....*....|...
gi 495291593 128 RTLTTTLKNALNMVGTRILDHVVVGREGSVSLA 160
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 ...
 26-165 3.69e-43

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: 142.58  E-value: 3.69e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495291593   26 ILQMAQQLAMSRLSKGRALTEPKQVFSHLQTLLQYHEYEVFALLLLDSKHRVIAFREIFRGTLDAASVYPREVVKIALEH 105
Cdd:TIGR00608  79 AVELAKRYAKSRMLERPVIRSPEAAAEFLHTDLAHETREHFMVLFLDRKNRLIAKEVVFIGTVNHVPVHPREIFKEALKL 158

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 495291593  106 NAAAAILVHNHPSGDPEPSQSDRTLTTTLKNALNMVGTRILDHVVVGREGSVSLAEMGYL 165
Cdd:TIGR00608 159 SASALILAHNHPSGEPSPSQEDILITERLRKAAELLGIELLDHLIIGKGRYVSFREEGLL 218
MPN_prok_mb cd08059
Mpr1p, Pad1p N-terminal (MPN) domains with catalytic isopeptidase activity (metal-binding); ...
 61-153 2.08e-08

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: 49.48  E-value: 2.08e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495291593  61 HEYEVFALLLLDSKHRVIAFREIFRGTLDAASVYPrevvKIALEHNAAAAILVHNHPSGDPEPSQSDRTLTTTLknalnm 140
Cdd:cd08059   14 HPDEFCGFLSGSKDNVMDELIFLPFVSGSVSAVID----LAALEIGMKVVGLVHSHPSGSCRPSEADLSLFTRF------ 83

                         90
                 ....*....|...
gi 495291593 141 vgtrILDHVVVGR 153
Cdd:cd08059   84 ----GLYHVIVCY 92
 
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