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Conserved domains on  [gi|1552040536|ref|NP_001354981|]
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cell cycle checkpoint control protein RAD9B isoform f [Homo sapiens]

Protein Classification

cell cycle checkpoint control RAD9 family protein( domain architecture ID 12050602)

cell cycle checkpoint control RAD9 family protein, similar to RAD9 which is a component of the 9-1-1 cell-cycle checkpoint response complex that plays a major role in DNA repair; may be partial

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Rad9 pfam04139
Rad9; Rad9 is required for transient cell-cycle arrests and transcriptional induction of DNA ...
17-276 3.09e-121

Rad9; Rad9 is required for transient cell-cycle arrests and transcriptional induction of DNA repair in response to DNA damage. It contains a Bcl-2 homology domain 3 (BH3).


:

Pssm-ID: 427739  Cd Length: 253  Bit Score: 352.05  E-value: 3.09e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552040536  17 FGKAVQALSRISDEFWLDPSKKGLALRCVNSSRSAYGCVLFSPVFFQHYQwsalvkmsENELDTTLHLKCKLGMKSILPI 96
Cdd:pfam04139   1 FSRALQCLSRIGDELYIEISEDGLALTTVNSSRSAYGVVTFSKDFFDKYQ--------MLSTDVPPQINCKILVKSILSI 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552040536  97 FRCLNSLERNIEKCRIFTRSDKCKVVIQFFYRHGIKRTHNICFQESQPLQVIFDKNVCTNTLMIQPRLLADAIVLFTSSQ 176
Cdd:pfam04139  73 FRSLSALEVTVEKCKIQIDGDKSKVIFQFLCKHGVIKTHKIHYEQSQPLHAVFDKNTCPSTLVINPRVLSDLLVHFTSST 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552040536 177 EEVTLAVTPLNFCLKSSNEESMDLSNAVHSEMFVGSDEFDFFQIGMDTEITFCFKELKGILTFSEATHAPISIYFDFPGK 256
Cdd:pfam04139 153 EEITIQLTPDRVLIKSYTDEVNDLTSSLYTELSIDPEEFDQYQLNGDVEITFCFKEFKAILAFAEVLHAPIAMYFSFPGK 232
                         250       260
                  ....*....|....*....|.
gi 1552040536 257 PLALSIDD-MLVEANFILATL 276
Cdd:pfam04139 233 PLLLTFKKsSLIEANFILATL 253
 
Name Accession Description Interval E-value
Rad9 pfam04139
Rad9; Rad9 is required for transient cell-cycle arrests and transcriptional induction of DNA ...
17-276 3.09e-121

Rad9; Rad9 is required for transient cell-cycle arrests and transcriptional induction of DNA repair in response to DNA damage. It contains a Bcl-2 homology domain 3 (BH3).


Pssm-ID: 427739  Cd Length: 253  Bit Score: 352.05  E-value: 3.09e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552040536  17 FGKAVQALSRISDEFWLDPSKKGLALRCVNSSRSAYGCVLFSPVFFQHYQwsalvkmsENELDTTLHLKCKLGMKSILPI 96
Cdd:pfam04139   1 FSRALQCLSRIGDELYIEISEDGLALTTVNSSRSAYGVVTFSKDFFDKYQ--------MLSTDVPPQINCKILVKSILSI 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552040536  97 FRCLNSLERNIEKCRIFTRSDKCKVVIQFFYRHGIKRTHNICFQESQPLQVIFDKNVCTNTLMIQPRLLADAIVLFTSSQ 176
Cdd:pfam04139  73 FRSLSALEVTVEKCKIQIDGDKSKVIFQFLCKHGVIKTHKIHYEQSQPLHAVFDKNTCPSTLVINPRVLSDLLVHFTSST 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552040536 177 EEVTLAVTPLNFCLKSSNEESMDLSNAVHSEMFVGSDEFDFFQIGMDTEITFCFKELKGILTFSEATHAPISIYFDFPGK 256
Cdd:pfam04139 153 EEITIQLTPDRVLIKSYTDEVNDLTSSLYTELSIDPEEFDQYQLNGDVEITFCFKEFKAILAFAEVLHAPIAMYFSFPGK 232
                         250       260
                  ....*....|....*....|.
gi 1552040536 257 PLALSIDD-MLVEANFILATL 276
Cdd:pfam04139 233 PLLLTFKKsSLIEANFILATL 253
PCNA cd00577
Proliferating Cell Nuclear Antigen (PCNA) domain found in eukaryotes and archaea. These ...
9-278 2.89e-46

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: 159.33  E-value: 2.89e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552040536   9 MSGSQVKVFGKAVQALSRISDEFWLDPSKKGLALRCVNSSRSAYGCVLFSPVFFQHYQWsalvkmseneldtTLHLKCKL 88
Cdd:cd00577     1 ATLSNAKLLKKIVDALSKLVDEANFDITEDGISLQAMDSSHVALVSLFLPKELFEEYRC-------------DEEISLGV 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552040536  89 GMKSILPIFRCLNSlerniEKCRIFTRSDKCKVVIQFFYRH-GIKRTHNICFQESQPLQVIFDKNVCTNTLMIQPRLLAD 167
Cdd:cd00577    68 NLKSLLKILKCAGN-----EDCVTLRADDEDPLKILFESSKgDVTSEFSLKLMDIDSEQLPIPELEYDATVTLPSDELKD 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552040536 168 AIVLFTSSQEEVTLAVTPLNFCLKSSNeesmDLSNAVHSEMFVGSDEFDFFQIGMDTEITFCFKELKGILTFSEAtHAPI 247
Cdd:cd00577   143 IVRDLESISDSVTISASKDGFKFSAEG----ELGGASVTLLPKDSDLLVTIECSEPVSSTYSLKYLKDFTKAAPL-SDKV 217
                         250       260       270
                  ....*....|....*....|....*....|..
gi 1552040536 248 SIYFDFPGkPLALSIDDM-LVEANFILATLAD 278
Cdd:cd00577   218 TLSFGSDG-PLSLEFKIAdGGHLTFYLAPKIE 248
 
Name Accession Description Interval E-value
Rad9 pfam04139
Rad9; Rad9 is required for transient cell-cycle arrests and transcriptional induction of DNA ...
17-276 3.09e-121

Rad9; Rad9 is required for transient cell-cycle arrests and transcriptional induction of DNA repair in response to DNA damage. It contains a Bcl-2 homology domain 3 (BH3).


Pssm-ID: 427739  Cd Length: 253  Bit Score: 352.05  E-value: 3.09e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552040536  17 FGKAVQALSRISDEFWLDPSKKGLALRCVNSSRSAYGCVLFSPVFFQHYQwsalvkmsENELDTTLHLKCKLGMKSILPI 96
Cdd:pfam04139   1 FSRALQCLSRIGDELYIEISEDGLALTTVNSSRSAYGVVTFSKDFFDKYQ--------MLSTDVPPQINCKILVKSILSI 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552040536  97 FRCLNSLERNIEKCRIFTRSDKCKVVIQFFYRHGIKRTHNICFQESQPLQVIFDKNVCTNTLMIQPRLLADAIVLFTSSQ 176
Cdd:pfam04139  73 FRSLSALEVTVEKCKIQIDGDKSKVIFQFLCKHGVIKTHKIHYEQSQPLHAVFDKNTCPSTLVINPRVLSDLLVHFTSST 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552040536 177 EEVTLAVTPLNFCLKSSNEESMDLSNAVHSEMFVGSDEFDFFQIGMDTEITFCFKELKGILTFSEATHAPISIYFDFPGK 256
Cdd:pfam04139 153 EEITIQLTPDRVLIKSYTDEVNDLTSSLYTELSIDPEEFDQYQLNGDVEITFCFKEFKAILAFAEVLHAPIAMYFSFPGK 232
                         250       260
                  ....*....|....*....|.
gi 1552040536 257 PLALSIDD-MLVEANFILATL 276
Cdd:pfam04139 233 PLLLTFKKsSLIEANFILATL 253
PCNA cd00577
Proliferating Cell Nuclear Antigen (PCNA) domain found in eukaryotes and archaea. These ...
9-278 2.89e-46

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: 159.33  E-value: 2.89e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552040536   9 MSGSQVKVFGKAVQALSRISDEFWLDPSKKGLALRCVNSSRSAYGCVLFSPVFFQHYQWsalvkmseneldtTLHLKCKL 88
Cdd:cd00577     1 ATLSNAKLLKKIVDALSKLVDEANFDITEDGISLQAMDSSHVALVSLFLPKELFEEYRC-------------DEEISLGV 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552040536  89 GMKSILPIFRCLNSlerniEKCRIFTRSDKCKVVIQFFYRH-GIKRTHNICFQESQPLQVIFDKNVCTNTLMIQPRLLAD 167
Cdd:cd00577    68 NLKSLLKILKCAGN-----EDCVTLRADDEDPLKILFESSKgDVTSEFSLKLMDIDSEQLPIPELEYDATVTLPSDELKD 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552040536 168 AIVLFTSSQEEVTLAVTPLNFCLKSSNeesmDLSNAVHSEMFVGSDEFDFFQIGMDTEITFCFKELKGILTFSEAtHAPI 247
Cdd:cd00577   143 IVRDLESISDSVTISASKDGFKFSAEG----ELGGASVTLLPKDSDLLVTIECSEPVSSTYSLKYLKDFTKAAPL-SDKV 217
                         250       260       270
                  ....*....|....*....|....*....|..
gi 1552040536 248 SIYFDFPGkPLALSIDDM-LVEANFILATLAD 278
Cdd:cd00577   218 TLSFGSDG-PLSLEFKIAdGGHLTFYLAPKIE 248
 
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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