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Conserved domains on  [gi|19115721|ref|NP_594809|]
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checkpoint clamp complex protein Rad1 [Schizosaccharomyces pombe]

Protein Classification

RAD1 family protein( domain architecture ID 708224)

RAD1 family protein such as DNA damage checkpoint control protein RAD1 that is involved both in DNA damage checkpoint control and DNA repair

Gene Ontology:  GO:0000077|GO:0006281

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Rad1 super family cl27458
Repair protein Rad1/Rec1/Rad17;
2-262 8.53e-64

Repair protein Rad1/Rec1/Rad17;


The actual alignment was detected with superfamily member pfam02144:

Pssm-ID: 396631  Cd Length: 257  Bit Score: 202.51  E-value: 8.53e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115721     2 FQAETVCLKQIQSTLRCIDFSKECTIEITSRGLRFAVEESQSLQAHAFLDKSLFQTFNF------QGDSDGDTYM-FQTM 74
Cdd:pfam02144   1 FSATTSNVRHLYTLLKCIGFVDKALVQISSDGLKFTVEDNRVIQAQAFLDKALFSSYNFnpptaqDDDDDEEDSPsFCLN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115721    75 ISPLLQSLSIYTDGKERISTSAwdqptvnimhkrgviCKVQYNGPGCPFIWEVEEmAGYATACELLTMECEDDVDINRLA 154
Cdd:pfam02144  81 LSALLDCLNIFGGNDDSSVKTS---------------CRMSYKGEGSPLVLILEE-DGVTTTCELSTYEPEDDLDLDLDR 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115721   155 STLCTKIIMKSNWLYDALVELDNNMGENLIIHTSSQKSTFLLRCVGALSTTEIEYPNEKSVLESFETDSEN----TYSYR 230
Cdd:pfam02144 145 DEVVFKVILKSDWLHNALRELDETSEELYISASPTDAPHFALSSFGELGSSKVEFPNESSVLETFECYDLGdeivISRYK 224
                         250       260       270
                  ....*....|....*....|....*....|..
gi 19115721   231 FSLIRHALKALQVGSKVNLRIDENGTLSIQIM 262
Cdd:pfam02144 225 FSLLKKARKALALASKVSIRMDVRGLLSLQFM 256
 
Name Accession Description Interval E-value
Rad1 pfam02144
Repair protein Rad1/Rec1/Rad17;
2-262 8.53e-64

Repair protein Rad1/Rec1/Rad17;


Pssm-ID: 396631  Cd Length: 257  Bit Score: 202.51  E-value: 8.53e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115721     2 FQAETVCLKQIQSTLRCIDFSKECTIEITSRGLRFAVEESQSLQAHAFLDKSLFQTFNF------QGDSDGDTYM-FQTM 74
Cdd:pfam02144   1 FSATTSNVRHLYTLLKCIGFVDKALVQISSDGLKFTVEDNRVIQAQAFLDKALFSSYNFnpptaqDDDDDEEDSPsFCLN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115721    75 ISPLLQSLSIYTDGKERISTSAwdqptvnimhkrgviCKVQYNGPGCPFIWEVEEmAGYATACELLTMECEDDVDINRLA 154
Cdd:pfam02144  81 LSALLDCLNIFGGNDDSSVKTS---------------CRMSYKGEGSPLVLILEE-DGVTTTCELSTYEPEDDLDLDLDR 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115721   155 STLCTKIIMKSNWLYDALVELDNNMGENLIIHTSSQKSTFLLRCVGALSTTEIEYPNEKSVLESFETDSEN----TYSYR 230
Cdd:pfam02144 145 DEVVFKVILKSDWLHNALRELDETSEELYISASPTDAPHFALSSFGELGSSKVEFPNESSVLETFECYDLGdeivISRYK 224
                         250       260       270
                  ....*....|....*....|....*....|..
gi 19115721   231 FSLIRHALKALQVGSKVNLRIDENGTLSIQIM 262
Cdd:pfam02144 225 FSLLKKARKALALASKVSIRMDVRGLLSLQFM 256
PCNA cd00577
Proliferating Cell Nuclear Antigen (PCNA) domain found in eukaryotes and archaea. These ...
8-281 1.32e-15

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: 74.97  E-value: 1.32e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115721   8 CLKQIQSTLrcIDFSKECTIEITSRGLRF-AVEESQSLQAHAFLDKSLFQTFNFQGDsdgdtymfqtmispllQSLSIYT 86
Cdd:cd00577   8 LLKKIVDAL--SKLVDEANFDITEDGISLqAMDSSHVALVSLFLPKELFEEYRCDEE----------------ISLGVNL 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115721  87 DGKERISTSAwdqptvnimhKRGVICKVQYNGpGCPF-IWEVEEMAGYATACELLTMECE-DDVDINRLASTLctKIIMK 164
Cdd:cd00577  70 KSLLKILKCA----------GNEDCVTLRADD-EDPLkILFESSKGDVTSEFSLKLMDIDsEQLPIPELEYDA--TVTLP 136
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115721 165 SNWLYDALVELDNnMGENLIIhtSSQKSTFLLRCVGALSTT-EIEYPNEKSVLESFETDSENTYSYRFSLIRHALKALQV 243
Cdd:cd00577 137 SDELKDIVRDLES-ISDSVTI--SASKDGFKFSAEGELGGAsVTLLPKDSDLLVTIECSEPVSSTYSLKYLKDFTKAAPL 213
                       250       260       270
                ....*....|....*....|....*....|....*...
gi 19115721 244 GSKVNLRIDENGTLSIQIMLVGQEglctFVDFCIVPLD 281
Cdd:cd00577 214 SDKVTLSFGSDGPLSLEFKIADGG----HLTFYLAPKI 247
 
Name Accession Description Interval E-value
Rad1 pfam02144
Repair protein Rad1/Rec1/Rad17;
2-262 8.53e-64

Repair protein Rad1/Rec1/Rad17;


Pssm-ID: 396631  Cd Length: 257  Bit Score: 202.51  E-value: 8.53e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115721     2 FQAETVCLKQIQSTLRCIDFSKECTIEITSRGLRFAVEESQSLQAHAFLDKSLFQTFNF------QGDSDGDTYM-FQTM 74
Cdd:pfam02144   1 FSATTSNVRHLYTLLKCIGFVDKALVQISSDGLKFTVEDNRVIQAQAFLDKALFSSYNFnpptaqDDDDDEEDSPsFCLN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115721    75 ISPLLQSLSIYTDGKERISTSAwdqptvnimhkrgviCKVQYNGPGCPFIWEVEEmAGYATACELLTMECEDDVDINRLA 154
Cdd:pfam02144  81 LSALLDCLNIFGGNDDSSVKTS---------------CRMSYKGEGSPLVLILEE-DGVTTTCELSTYEPEDDLDLDLDR 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115721   155 STLCTKIIMKSNWLYDALVELDNNMGENLIIHTSSQKSTFLLRCVGALSTTEIEYPNEKSVLESFETDSEN----TYSYR 230
Cdd:pfam02144 145 DEVVFKVILKSDWLHNALRELDETSEELYISASPTDAPHFALSSFGELGSSKVEFPNESSVLETFECYDLGdeivISRYK 224
                         250       260       270
                  ....*....|....*....|....*....|..
gi 19115721   231 FSLIRHALKALQVGSKVNLRIDENGTLSIQIM 262
Cdd:pfam02144 225 FSLLKKARKALALASKVSIRMDVRGLLSLQFM 256
PCNA cd00577
Proliferating Cell Nuclear Antigen (PCNA) domain found in eukaryotes and archaea. These ...
8-281 1.32e-15

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: 74.97  E-value: 1.32e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115721   8 CLKQIQSTLrcIDFSKECTIEITSRGLRF-AVEESQSLQAHAFLDKSLFQTFNFQGDsdgdtymfqtmispllQSLSIYT 86
Cdd:cd00577   8 LLKKIVDAL--SKLVDEANFDITEDGISLqAMDSSHVALVSLFLPKELFEEYRCDEE----------------ISLGVNL 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115721  87 DGKERISTSAwdqptvnimhKRGVICKVQYNGpGCPF-IWEVEEMAGYATACELLTMECE-DDVDINRLASTLctKIIMK 164
Cdd:cd00577  70 KSLLKILKCA----------GNEDCVTLRADD-EDPLkILFESSKGDVTSEFSLKLMDIDsEQLPIPELEYDA--TVTLP 136
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115721 165 SNWLYDALVELDNnMGENLIIhtSSQKSTFLLRCVGALSTT-EIEYPNEKSVLESFETDSENTYSYRFSLIRHALKALQV 243
Cdd:cd00577 137 SDELKDIVRDLES-ISDSVTI--SASKDGFKFSAEGELGGAsVTLLPKDSDLLVTIECSEPVSSTYSLKYLKDFTKAAPL 213
                       250       260       270
                ....*....|....*....|....*....|....*...
gi 19115721 244 GSKVNLRIDENGTLSIQIMLVGQEglctFVDFCIVPLD 281
Cdd:cd00577 214 SDKVTLSFGSDGPLSLEFKIADGG----HLTFYLAPKI 247
 
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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