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Conserved domains on  [gi|1239899541|ref|XP_022273643|]
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cell cycle checkpoint protein RAD1 isoform X4 [Canis lupus familiaris]

Protein Classification

Rad1/Rec1/Rad17 family repair protein( domain architecture ID 12031406)

Rad1/Rec1/Rad17 family repair protein similar to Homo sapiens cell cycle checkpoint protein RAD1, Saccharomyces cerevisiae DNA damage checkpoint control protein RAD17 and Ustilago maydis DNA repair exonuclease REC1

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Rad1 pfam02144
Repair protein Rad1/Rec1/Rad17;
16-256 1.34e-118

Repair protein Rad1/Rec1/Rad17;


:

Pssm-ID: 396631  Cd Length: 257  Bit Score: 340.02  E-value: 1.34e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239899541  16 LVASLDNVRHLSTILKAIHFRDHATCFATKNGIKVTVENAKCVQANAFIQAGIFQEFIV-----------QEESVTFRIN 84
Cdd:pfam02144   1 FSATTSNVRHLYTLLKCIGFVDKALVQISSDGLKFTVEDNRVIQAQAFLDKALFSSYNFnpptaqdddddEEDSPSFCLN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239899541  85 LTILLDCLSIFGSSPMPGTLTALRMCYQGYGYPLMLFLEEGGVVTVCKINTQEPEETLDFDFCSTNVINKIILQSEGLRE 164
Cdd:pfam02144  81 LSALLDCLNIFGGNDDSSVKTSCRMSYKGEGSPLVLILEEDGVTTTCELSTYEPEDDLDLDLDRDEVVFKVILKSDWLHN 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239899541 165 AFSELDMTSEVLQITMSP-NKPYFRLSTFGNAGSSHLDYPKDSDLMESFQC----NQTQVNRYKISLLKPSTKALVLSCK 239
Cdd:pfam02144 161 ALRELDETSEELYISASPtDAPHFALSSFGELGSSKVEFPNESSVLETFECydlgDEIVISRYKFSLLKKARKALALASK 240

                         250
                  ....*....|....*..
gi 1239899541 240 VSIRTDNRGFLSLQYMI 256
Cdd:pfam02144 241 VSIRMDVRGLLSLQFMI 257
 
Name Accession Description Interval E-value
Rad1 pfam02144
Repair protein Rad1/Rec1/Rad17;
16-256 1.34e-118

Repair protein Rad1/Rec1/Rad17;


Pssm-ID: 396631  Cd Length: 257  Bit Score: 340.02  E-value: 1.34e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239899541  16 LVASLDNVRHLSTILKAIHFRDHATCFATKNGIKVTVENAKCVQANAFIQAGIFQEFIV-----------QEESVTFRIN 84
Cdd:pfam02144   1 FSATTSNVRHLYTLLKCIGFVDKALVQISSDGLKFTVEDNRVIQAQAFLDKALFSSYNFnpptaqdddddEEDSPSFCLN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239899541  85 LTILLDCLSIFGSSPMPGTLTALRMCYQGYGYPLMLFLEEGGVVTVCKINTQEPEETLDFDFCSTNVINKIILQSEGLRE 164
Cdd:pfam02144  81 LSALLDCLNIFGGNDDSSVKTSCRMSYKGEGSPLVLILEEDGVTTTCELSTYEPEDDLDLDLDRDEVVFKVILKSDWLHN 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239899541 165 AFSELDMTSEVLQITMSP-NKPYFRLSTFGNAGSSHLDYPKDSDLMESFQC----NQTQVNRYKISLLKPSTKALVLSCK 239
Cdd:pfam02144 161 ALRELDETSEELYISASPtDAPHFALSSFGELGSSKVEFPNESSVLETFECydlgDEIVISRYKFSLLKKARKALALASK 240

                         250
                  ....*....|....*..
gi 1239899541 240 VSIRTDNRGFLSLQYMI 256
Cdd:pfam02144 241 VSIRMDVRGLLSLQFMI 257
PCNA cd00577
Proliferating Cell Nuclear Antigen (PCNA) domain found in eukaryotes and archaea. These ...
 18-275 9.50e-60

Proliferating Cell Nuclear Antigen (PCNA) domain found in eukaryotes and archaea. These polymerase processivity factors play a role in DNA replication and repair. PCNA encircles duplex DNA in its central cavity, providing a DNA-bound platform for the attachment of the polymerase. The trimeric PCNA ring is structurally similar to the dimeric ring formed by the DNA polymerase processivity factors in bacteria (beta subunit DNA polymerase III holoenzyme) and in bacteriophages (catalytic subunits in T4 and RB69). This structural correspondence further substantiates the mechanistic connection between eukaryotic and prokaryotic DNA replication that has been suggested on biochemical grounds. PCNA is also involved with proteins involved in cell cycle processes such as DNA repair and apoptosis. Many of these proteins contain a highly conserved motif known as the PIP-box (PCNA interacting protein box) which contains the sequence Qxx[LIM]xxF[FY].


Pssm-ID: 238322 [Multi-domain]  Cd Length: 248  Bit Score: 190.15  E-value: 9.50e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239899541  18 ASLDNVRHLSTILKAIHFRDHATCF-ATKNGIKVTVENAKCV-QANAFIQAGIFQEFIVQEEsVTFRINLTILLDCLSIF 95
Cdd:cd00577     1 ATLSNAKLLKKIVDALSKLVDEANFdITEDGISLQAMDSSHVaLVSLFLPKELFEEYRCDEE-ISLGVNLKSLLKILKCA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239899541  96 GSSpmpgtlTALRMCYQGyGYPLMLFLEE--GGVVTVCKINTQEPEETLDfDFCSTNVINKIILQSEGLREAFSELDMTS 173
Cdd:cd00577    80 GNE------DCVTLRADD-EDPLKILFESskGDVTSEFSLKLMDIDSEQL-PIPELEYDATVTLPSDELKDIVRDLESIS 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239899541 174 EVLQITMSPNKpyFRLSTFGN-AGSSHLDYPKDSDLMESFQCNQTQVNRYKISLLKPSTKALVLSCKVSIRTDNRGFLSL 252
Cdd:cd00577   152 DSVTISASKDG--FKFSAEGElGGASVTLLPKDSDLLVTIECSEPVSSTYSLKYLKDFTKAAPLSDKVTLSFGSDGPLSL 229

                         250       260
                  ....*....|....*....|...
gi 1239899541 253 QYMIRNEdgqiCFVEYYCCPDEE 275
Cdd:cd00577   230 EFKIADG----GHLTFYLAPKIE 248
PRK01115 PRK01115
DNA polymerase sliding clamp; Validated
 18-265 3.26e-04

DNA polymerase sliding clamp; Validated


Pssm-ID: 234903 [Multi-domain]  Cd Length: 247  Bit Score: 41.35  E-value: 3.26e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239899541  18 ASLDNVRHLSTILKAI-HFRDHATCFATKNGIKV-TVENAKCVQANAFIQAGIFQEFIVQEEsVTFRINLTILLDCLSIF 95
Cdd:PRK01115    4 AVYPDAKDFKYIIDAIsKLVDEAKFKFTEDGIRLrALDPAKVAMVDLELPKEAFEEYEVDEE-EKIGVDLEDLKKILKRA 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239899541  96 GSSpmpgtlTALRMCYQGYGYPLMLFLEEGGV----VTVCKINTQEPEE-TLDFDFcstnvinKIILQSEGLREAFSELD 170
Cdd:PRK01115   83 KKG------DKLELELDEEENKLKITFGGEKTrefsLPLLDVSSEEPPEpNLELPV-------KAVILGDDLKDAIKDAE 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239899541 171 MTSEVLQITMSPNKpyFRLSTFGNaGSSHLDYPKDSDLMESFQCNQTQVNRYKISLLKPSTKALVLSCKVSIRTDNRGFL 250
Cdd:PRK01115  150 LVSDHIELEADEDK--FYIEAEGE-GEDEVELSLDSGPLIELSVEEPAKSSYSLDYLKDMVKATSASDEVTIEFGSDMPL 226

                         250
                  ....*....|....*
gi 1239899541 251 SLQYMIRNEdGQICF 265
Cdd:PRK01115  227 KLEFEIAGG-GKVTY 240
 
Name Accession Description Interval E-value
Rad1 pfam02144
Repair protein Rad1/Rec1/Rad17;
16-256 1.34e-118

Repair protein Rad1/Rec1/Rad17;


Pssm-ID: 396631  Cd Length: 257  Bit Score: 340.02  E-value: 1.34e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239899541  16 LVASLDNVRHLSTILKAIHFRDHATCFATKNGIKVTVENAKCVQANAFIQAGIFQEFIV-----------QEESVTFRIN 84
Cdd:pfam02144   1 FSATTSNVRHLYTLLKCIGFVDKALVQISSDGLKFTVEDNRVIQAQAFLDKALFSSYNFnpptaqdddddEEDSPSFCLN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239899541  85 LTILLDCLSIFGSSPMPGTLTALRMCYQGYGYPLMLFLEEGGVVTVCKINTQEPEETLDFDFCSTNVINKIILQSEGLRE 164
Cdd:pfam02144  81 LSALLDCLNIFGGNDDSSVKTSCRMSYKGEGSPLVLILEEDGVTTTCELSTYEPEDDLDLDLDRDEVVFKVILKSDWLHN 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239899541 165 AFSELDMTSEVLQITMSP-NKPYFRLSTFGNAGSSHLDYPKDSDLMESFQC----NQTQVNRYKISLLKPSTKALVLSCK 239
Cdd:pfam02144 161 ALRELDETSEELYISASPtDAPHFALSSFGELGSSKVEFPNESSVLETFECydlgDEIVISRYKFSLLKKARKALALASK 240

                         250
                  ....*....|....*..
gi 1239899541 240 VSIRTDNRGFLSLQYMI 256
Cdd:pfam02144 241 VSIRMDVRGLLSLQFMI 257
PCNA cd00577
Proliferating Cell Nuclear Antigen (PCNA) domain found in eukaryotes and archaea. These ...
 18-275 9.50e-60

Proliferating Cell Nuclear Antigen (PCNA) domain found in eukaryotes and archaea. These polymerase processivity factors play a role in DNA replication and repair. PCNA encircles duplex DNA in its central cavity, providing a DNA-bound platform for the attachment of the polymerase. The trimeric PCNA ring is structurally similar to the dimeric ring formed by the DNA polymerase processivity factors in bacteria (beta subunit DNA polymerase III holoenzyme) and in bacteriophages (catalytic subunits in T4 and RB69). This structural correspondence further substantiates the mechanistic connection between eukaryotic and prokaryotic DNA replication that has been suggested on biochemical grounds. PCNA is also involved with proteins involved in cell cycle processes such as DNA repair and apoptosis. Many of these proteins contain a highly conserved motif known as the PIP-box (PCNA interacting protein box) which contains the sequence Qxx[LIM]xxF[FY].


Pssm-ID: 238322 [Multi-domain]  Cd Length: 248  Bit Score: 190.15  E-value: 9.50e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239899541  18 ASLDNVRHLSTILKAIHFRDHATCF-ATKNGIKVTVENAKCV-QANAFIQAGIFQEFIVQEEsVTFRINLTILLDCLSIF 95
Cdd:cd00577     1 ATLSNAKLLKKIVDALSKLVDEANFdITEDGISLQAMDSSHVaLVSLFLPKELFEEYRCDEE-ISLGVNLKSLLKILKCA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239899541  96 GSSpmpgtlTALRMCYQGyGYPLMLFLEE--GGVVTVCKINTQEPEETLDfDFCSTNVINKIILQSEGLREAFSELDMTS 173
Cdd:cd00577    80 GNE------DCVTLRADD-EDPLKILFESskGDVTSEFSLKLMDIDSEQL-PIPELEYDATVTLPSDELKDIVRDLESIS 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239899541 174 EVLQITMSPNKpyFRLSTFGN-AGSSHLDYPKDSDLMESFQCNQTQVNRYKISLLKPSTKALVLSCKVSIRTDNRGFLSL 252
Cdd:cd00577   152 DSVTISASKDG--FKFSAEGElGGASVTLLPKDSDLLVTIECSEPVSSTYSLKYLKDFTKAAPLSDKVTLSFGSDGPLSL 229

                         250       260
                  ....*....|....*....|...
gi 1239899541 253 QYMIRNEdgqiCFVEYYCCPDEE 275
Cdd:cd00577   230 EFKIADG----GHLTFYLAPKIE 248
PRK01115 PRK01115
DNA polymerase sliding clamp; Validated
 18-265 3.26e-04

DNA polymerase sliding clamp; Validated


Pssm-ID: 234903 [Multi-domain]  Cd Length: 247  Bit Score: 41.35  E-value: 3.26e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239899541  18 ASLDNVRHLSTILKAI-HFRDHATCFATKNGIKV-TVENAKCVQANAFIQAGIFQEFIVQEEsVTFRINLTILLDCLSIF 95
Cdd:PRK01115    4 AVYPDAKDFKYIIDAIsKLVDEAKFKFTEDGIRLrALDPAKVAMVDLELPKEAFEEYEVDEE-EKIGVDLEDLKKILKRA 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239899541  96 GSSpmpgtlTALRMCYQGYGYPLMLFLEEGGV----VTVCKINTQEPEE-TLDFDFcstnvinKIILQSEGLREAFSELD 170
Cdd:PRK01115   83 KKG------DKLELELDEEENKLKITFGGEKTrefsLPLLDVSSEEPPEpNLELPV-------KAVILGDDLKDAIKDAE 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239899541 171 MTSEVLQITMSPNKpyFRLSTFGNaGSSHLDYPKDSDLMESFQCNQTQVNRYKISLLKPSTKALVLSCKVSIRTDNRGFL 250
Cdd:PRK01115  150 LVSDHIELEADEDK--FYIEAEGE-GEDEVELSLDSGPLIELSVEEPAKSSYSLDYLKDMVKATSASDEVTIEFGSDMPL 226

                         250
                  ....*....|....*
gi 1239899541 251 SLQYMIRNEdGQICF 265
Cdd:PRK01115  227 KLEFEIAGG-GKVTY 240
 
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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