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Conserved domains on  [gi|535739718|gb|EQY73983|]
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phage DNA repair protein [Escherichia coli UMEA 3264-1]

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, ...
 28-158 2.91e-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: 196.05  E-value: 2.91e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535739718  28 RHLHEP---GVAFTSTRAAREWLILNMAGLEREEFRVLYLNNQNQLIAGETLFTGTINRTEVHPREVIKRALYHNAAAVV 104
Cdd:COG2003   91 RLLREEleeRPVISSPEDVADYLRARLAHLPREVFRVLFLDTKNRLIADEELSIGTLNHTPVYPREVFKRALRLNAAAII 170

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 535739718 105 LAHNHPSGEVTPSKADRLITERLVQALGLVDIRVPDHLIVGGSQVFSFAEHGLL 158
Cdd:COG2003  171 LAHNHPSGDPEPSRADIELTRRLKEAGELLGIRLLDHIIIGDGGYVSFAEEGLL 224
 
Name Accession Description Interval E-value
RadC COG2003
DNA repair protein RadC, contains a helix-hairpin-helix DNA-binding motif [Replication, ...
 28-158 2.91e-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: 196.05  E-value: 2.91e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535739718  28 RHLHEP---GVAFTSTRAAREWLILNMAGLEREEFRVLYLNNQNQLIAGETLFTGTINRTEVHPREVIKRALYHNAAAVV 104
Cdd:COG2003   91 RLLREEleeRPVISSPEDVADYLRARLAHLPREVFRVLFLDTKNRLIADEELSIGTLNHTPVYPREVFKRALRLNAAAII 170

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 535739718 105 LAHNHPSGEVTPSKADRLITERLVQALGLVDIRVPDHLIVGGSQVFSFAEHGLL 158
Cdd:COG2003  171 LAHNHPSGDPEPSRADIELTRRLKEAGELLGIRLLDHIIIGDGGYVSFAEEGLL 224
PRK00024 PRK00024
DNA repair protein RadC;
28-158 4.91e-64

DNA repair protein RadC;


Pssm-ID: 178801 [Multi-domain]  Cd Length: 224  Bit Score: 195.29  E-value: 4.91e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535739718  28 RHLHE---PGVAFTSTRAAREWLILNMAGLEREEFRVLYLNNQNQLIAGETLFTGTINRTEVHPREVIKRALYHNAAAVV 104
Cdd:PRK00024  91 RILAErlrEREVLLSPEDVADYLMAELRDEEQEHFVVLFLDTKNRVIADEELFIGTLNSSIVHPREIVKRALKLNAAALI 170

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 535739718 105 LAHNHPSGEVTPSKADRLITERLVQALGLVDIRVPDHLIVGGSQVFSFAEHGLL 158
Cdd:PRK00024 171 LAHNHPSGDPEPSQADILITKRLKEAGELLGIRLLDHIIIGDGEYVSFAERGLL 224
MPN_DUF2466 cd08071
Mov34/MPN/PAD-1 family; Mov34 DUF2466 (also known as DNA repair protein RadC) domain of ...
 41-153 1.79e-58

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: 177.57  E-value: 1.79e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535739718  41 RAAREWLILNMAGLEREEFRVLYLNNQNQLIAGETLFTGTINRTEVHPREVIKRALYHNAAAVVLAHNHPSGEVTPSKAD 120
Cdd:cd08071    1 EDVAEYLREELGDLDQEEFVVLLLDTKNRLIAVETISVGTLNSSLVHPREIFKEALRHNAAAIILAHNHPSGDPTPSRED 80

                         90       100       110
                 ....*....|....*....|....*....|...
gi 535739718 121 RLITERLVQALGLVDIRVPDHLIVGGSQVFSFA 153
Cdd:cd08071   81 IELTKRLKEAGELLGIRLLDHIIVGDGGYFSFR 113
RadC pfam04002
RadC-like JAB domain; A family of proteins present widely across the bacteria. This family was ...
 37-146 3.05e-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: 169.12  E-value: 3.05e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535739718   37 FTSTRAAREWLILNMAGLEREEFRVLYLNNQNQLIAGETLFTGTINRTEVHPREVIKRALYHNAAAVVLAHNHPSGEVTP 116
Cdd:pfam04002   1 ITSPEDVAEYLMEELRDLDQEVFRVLFLDTKNRLIADEELSEGTLNSTLVHPREIFKRALRLNAAAVILAHNHPSGDPEP 80

                          90       100       110
                  ....*....|....*....|....*....|
gi 535739718  117 SKADRLITERLVQALGLVDIRVPDHLIVGG 146
Cdd:pfam04002  81 SREDIELTRRLKEAGELLGIRLLDHIIIGD 110
radc TIGR00608
DNA repair protein radc; The genes in this family for which the functions are known have an as ...
 39-158 1.40e-47

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: 153.36  E-value: 1.40e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535739718   39 STRAAREWLILNMAGLEREEFRVLYLNNQNQLIAGETLFTGTINRTEVHPREVIKRALYHNAAAVVLAHNHPSGEVTPSK 118
Cdd:TIGR00608  99 SPEAAAEFLHTDLAHETREHFMVLFLDRKNRLIAKEVVFIGTVNHVPVHPREIFKEALKLSASALILAHNHPSGEPSPSQ 178

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 535739718  119 ADRLITERLVQALGLVDIRVPDHLIVGGSQVFSFAEHGLL 158
Cdd:TIGR00608 179 EDILITERLRKAAELLGIELLDHLIIGKGRYVSFREEGLL 218
 
Name Accession Description Interval E-value
RadC COG2003
DNA repair protein RadC, contains a helix-hairpin-helix DNA-binding motif [Replication, ...
 28-158 2.91e-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: 196.05  E-value: 2.91e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535739718  28 RHLHEP---GVAFTSTRAAREWLILNMAGLEREEFRVLYLNNQNQLIAGETLFTGTINRTEVHPREVIKRALYHNAAAVV 104
Cdd:COG2003   91 RLLREEleeRPVISSPEDVADYLRARLAHLPREVFRVLFLDTKNRLIADEELSIGTLNHTPVYPREVFKRALRLNAAAII 170

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 535739718 105 LAHNHPSGEVTPSKADRLITERLVQALGLVDIRVPDHLIVGGSQVFSFAEHGLL 158
Cdd:COG2003  171 LAHNHPSGDPEPSRADIELTRRLKEAGELLGIRLLDHIIIGDGGYVSFAEEGLL 224
PRK00024 PRK00024
DNA repair protein RadC;
28-158 4.91e-64

DNA repair protein RadC;


Pssm-ID: 178801 [Multi-domain]  Cd Length: 224  Bit Score: 195.29  E-value: 4.91e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535739718  28 RHLHE---PGVAFTSTRAAREWLILNMAGLEREEFRVLYLNNQNQLIAGETLFTGTINRTEVHPREVIKRALYHNAAAVV 104
Cdd:PRK00024  91 RILAErlrEREVLLSPEDVADYLMAELRDEEQEHFVVLFLDTKNRVIADEELFIGTLNSSIVHPREIVKRALKLNAAALI 170

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 535739718 105 LAHNHPSGEVTPSKADRLITERLVQALGLVDIRVPDHLIVGGSQVFSFAEHGLL 158
Cdd:PRK00024 171 LAHNHPSGDPEPSQADILITKRLKEAGELLGIRLLDHIIIGDGEYVSFAERGLL 224
MPN_DUF2466 cd08071
Mov34/MPN/PAD-1 family; Mov34 DUF2466 (also known as DNA repair protein RadC) domain of ...
 41-153 1.79e-58

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: 177.57  E-value: 1.79e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535739718  41 RAAREWLILNMAGLEREEFRVLYLNNQNQLIAGETLFTGTINRTEVHPREVIKRALYHNAAAVVLAHNHPSGEVTPSKAD 120
Cdd:cd08071    1 EDVAEYLREELGDLDQEEFVVLLLDTKNRLIAVETISVGTLNSSLVHPREIFKEALRHNAAAIILAHNHPSGDPTPSRED 80

                         90       100       110
                 ....*....|....*....|....*....|...
gi 535739718 121 RLITERLVQALGLVDIRVPDHLIVGGSQVFSFA 153
Cdd:cd08071   81 IELTKRLKEAGELLGIRLLDHIIVGDGGYFSFR 113
RadC pfam04002
RadC-like JAB domain; A family of proteins present widely across the bacteria. This family was ...
 37-146 3.05e-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: 169.12  E-value: 3.05e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535739718   37 FTSTRAAREWLILNMAGLEREEFRVLYLNNQNQLIAGETLFTGTINRTEVHPREVIKRALYHNAAAVVLAHNHPSGEVTP 116
Cdd:pfam04002   1 ITSPEDVAEYLMEELRDLDQEVFRVLFLDTKNRLIADEELSEGTLNSTLVHPREIFKRALRLNAAAVILAHNHPSGDPEP 80

                          90       100       110
                  ....*....|....*....|....*....|
gi 535739718  117 SKADRLITERLVQALGLVDIRVPDHLIVGG 146
Cdd:pfam04002  81 SREDIELTRRLKEAGELLGIRLLDHIIIGD 110
radc TIGR00608
DNA repair protein radc; The genes in this family for which the functions are known have an as ...
 39-158 1.40e-47

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: 153.36  E-value: 1.40e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535739718   39 STRAAREWLILNMAGLEREEFRVLYLNNQNQLIAGETLFTGTINRTEVHPREVIKRALYHNAAAVVLAHNHPSGEVTPSK 118
Cdd:TIGR00608  99 SPEAAAEFLHTDLAHETREHFMVLFLDRKNRLIAKEVVFIGTVNHVPVHPREIFKEALKLSASALILAHNHPSGEPSPSQ 178

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 535739718  119 ADRLITERLVQALGLVDIRVPDHLIVGGSQVFSFAEHGLL 158
Cdd:TIGR00608 179 EDILITERLRKAAELLGIELLDHLIIGKGRYVSFREEGLL 218
MPN_prok_mb cd08059
Mpr1p, Pad1p N-terminal (MPN) domains with catalytic isopeptidase activity (metal-binding); ...
 61-145 2.24e-03

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: 35.62  E-value: 2.24e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535739718  61 VLYLNNQNQLIAGETLftgTINRTEVHPReVIKRALYHNAAAVVLAHNHPSGEVTPSKADRLITERlvqaLGLvdirvpD 140
Cdd:cd08059   21 FLSGSKDNVMDELIFL---PFVSGSVSAV-IDLAALEIGMKVVGLVHSHPSGSCRPSEADLSLFTR----FGL------Y 86


                 ....*
gi 535739718 141 HLIVG 145
Cdd:cd08059   87 HVIVC 91
 
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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