NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|188528630|ref|NP_033055|]
View 

retinoblastoma-associated protein [Mus musculus]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
Rb_C pfam08934
Rb C-terminal domain; The Rb C-terminal domain is required for high-affinity binding to E2F-DP ...
 761-918 5.56e-94

Rb C-terminal domain; The Rb C-terminal domain is required for high-affinity binding to E2F-DP complexes and for maximal repression of E2F-responsive promoters, thereby acting as a growth suppressor by blocking the G1-S transition of the cell cycle. This domain has a strand-loop-helix structure, which directly interacts with both E2F1 and DP1, followed by a tail segment that lacks regular secondary structure.


:

Pssm-ID: 462639  Cd Length: 152  Bit Score: 293.03  E-value: 5.56e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188528630  761 ILQYASTRPPTLSPIPHIPRSPYKFSSSPLRIPGG-NIYISPLKSPYkiseglPTPTKMTPRSRILVSIGESFGTSEKFQ 839
Cdd:pfam08934   1 ILQYASPRPPTLSPIPHIPRSPYKFPNSPLRVPGSnNVYISPLKSPR------LSPGMMTPRSRILVSIGESFGTSEKFQ 74

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 188528630  840 KINQMVCNSDRVLKRSAEGGNPPKPLKKLRFDIEGADEADGSKHlPAESKFQQKLAEMTSTRTRMQKQRMNESKDVSNK 918
Cdd:pfam08934  75 KINQMVSSSDRSLKRSLDGGSTPKPLKRLRFDVDGQDEADGSKS-GGESKFIQKLAEMTSTRSRMQEQKMKENAETSNK 152
RB_A pfam01858
Retinoblastoma-associated protein A domain; This domain has the cyclin fold as predicted.
 367-567 1.64e-87

Retinoblastoma-associated protein A domain; This domain has the cyclin fold as predicted.


:

Pssm-ID: 460364  Cd Length: 195  Bit Score: 277.16  E-value: 1.64e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188528630  367 TPVRTVMNTIQQLMVILNSASDQPSENLISYFNNCTVNPKENILKRVKDVGHIFKEKFANAVGQG---CVDIGVQRYKLG 443
Cdd:pfam01858   1 TPVSSAMQTVSWLQTLLSGLSDEPSEKLLRIFKSCSRDPTETILKRVKELGEIFCQKYTEASGEHpsfCIEIAEQRFRLA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188528630  444 VRLYYRVMESMLKSEEERLSIQNFSKLLNDNIFHMSLLACALEVVMATYSRSTLqhldsgtdlSFPWILNVLNLKAFDFY 523
Cdd:pfam01858  81 EKLYYKVLESILKSEKKRLPGNDLSSLLSNDIFHRSLLACCLEIVLFAYNSERL---------SFPWILEVFGLPPFDFY 151

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 188528630  524 KVIESFIKVEANLTREMIKHLERCEHRIMESLAWLSDSPLFDLI 567
Cdd:pfam01858 152 KVIESFIRAEDGLPRELVKHLNSIEEQILESLAWKSDSPLWELL 195
CYCLIN_RB cd20599
cyclin box found in retinoblastoma-associated protein (RB) and similar proteins; RB, also ...
 638-764 1.00e-74

cyclin box found in retinoblastoma-associated protein (RB) and similar proteins; RB, also called p105-Rb, pRb, or pp110, is a key regulator of entry into cell division and also acts as a tumor suppressor. It promotes G0-G1 transition when phosphorylated by CDK3/cyclin-C. It also acts as a transcription repressor of E2F1 target genes. RB is directly involved in heterochromatin formation by maintaining overall chromatin structure, especially that of constitutive heterochromatin by stabilizing histone methylation. It recruits and targets histone methyltransferases SUV39H1, KMT5B and KMT5C, leading to epigenetic transcriptional repression. It controls histone H4 'Lys-20' trimethylation. RB contains one cyclin box. The cyclin box is a protein binding domain.


:

Pssm-ID: 410302  Cd Length: 126  Bit Score: 240.27  E-value: 1.00e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188528630 638 TSLALFYKKVYRLAYLRLNTLCARLLSdHPELEHIIWTLFQHTLQNEYELMRDRHLDQIMMCSMYGICKVKNIDLKFKII 717
Cdd:cd20599    1 TSLSLFYKKVYRLAYLRLNTLCDLLLL-HPDLEHRIWTCFEHCLQNRYELLKDRHLDQIMMCSMYGICKVKNKDLRFKTI 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 188528630 718 VTAYKDLPHAAQETFKRVLIREEEFDSIIVFYNSVFMQRLKTNILQY 764
Cdd:cd20599   80 VTAYKDLPHASQEVYKRVLIRGEEYDSIIGFYNRVFMQALKTNILQF 126
DUF3452 super family cl13385
Domain of unknown function (DUF3452); This presumed domain is functionally uncharacterized. ...
 112-221 1.25e-08

Domain of unknown function (DUF3452); This presumed domain is functionally uncharacterized. This domain is found in bacteria and eukaryotes. This domain is typically between 124 to 150 amino acids in length. This domain is found associated with pfam01858, pfam01857. This domain has a single completely conserved residue W that may be functionally important.


The actual alignment was detected with superfamily member pfam11934:

Pssm-ID: 463402  Cd Length: 134  Bit Score: 54.14  E-value: 1.25e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188528630  112 TELQKSIETSVYKFFDLLKE----IDTSTKVDNAMSRLLKKYNVLCALYSKLERTCELIYLTQPSSALSTEINSM----- 182
Cdd:pfam11934  12 TRLLRACKLSIIDFFKKMKQwadmANLDWEFRLEIKELERNFSVTTVLFKKYKRIFNELFLSPPPKEPKRSKKSRpapcs 91

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 188528630  183 --LVLKISWITFLLAKGEVLQMEDDLVISFQLMLCVVDYFI 221
Cdd:pfam11934  92 ysDLFEFGWLLFLAAKNEFPSISKDLVTSYHLLLCCLDLVY 132
 
Name Accession Description Interval E-value
Rb_C pfam08934
Rb C-terminal domain; The Rb C-terminal domain is required for high-affinity binding to E2F-DP ...
 761-918 5.56e-94

Rb C-terminal domain; The Rb C-terminal domain is required for high-affinity binding to E2F-DP complexes and for maximal repression of E2F-responsive promoters, thereby acting as a growth suppressor by blocking the G1-S transition of the cell cycle. This domain has a strand-loop-helix structure, which directly interacts with both E2F1 and DP1, followed by a tail segment that lacks regular secondary structure.


Pssm-ID: 462639  Cd Length: 152  Bit Score: 293.03  E-value: 5.56e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188528630  761 ILQYASTRPPTLSPIPHIPRSPYKFSSSPLRIPGG-NIYISPLKSPYkiseglPTPTKMTPRSRILVSIGESFGTSEKFQ 839
Cdd:pfam08934   1 ILQYASPRPPTLSPIPHIPRSPYKFPNSPLRVPGSnNVYISPLKSPR------LSPGMMTPRSRILVSIGESFGTSEKFQ 74

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 188528630  840 KINQMVCNSDRVLKRSAEGGNPPKPLKKLRFDIEGADEADGSKHlPAESKFQQKLAEMTSTRTRMQKQRMNESKDVSNK 918
Cdd:pfam08934  75 KINQMVSSSDRSLKRSLDGGSTPKPLKRLRFDVDGQDEADGSKS-GGESKFIQKLAEMTSTRSRMQEQKMKENAETSNK 152
RB_A pfam01858
Retinoblastoma-associated protein A domain; This domain has the cyclin fold as predicted.
 367-567 1.64e-87

Retinoblastoma-associated protein A domain; This domain has the cyclin fold as predicted.


Pssm-ID: 460364  Cd Length: 195  Bit Score: 277.16  E-value: 1.64e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188528630  367 TPVRTVMNTIQQLMVILNSASDQPSENLISYFNNCTVNPKENILKRVKDVGHIFKEKFANAVGQG---CVDIGVQRYKLG 443
Cdd:pfam01858   1 TPVSSAMQTVSWLQTLLSGLSDEPSEKLLRIFKSCSRDPTETILKRVKELGEIFCQKYTEASGEHpsfCIEIAEQRFRLA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188528630  444 VRLYYRVMESMLKSEEERLSIQNFSKLLNDNIFHMSLLACALEVVMATYSRSTLqhldsgtdlSFPWILNVLNLKAFDFY 523
Cdd:pfam01858  81 EKLYYKVLESILKSEKKRLPGNDLSSLLSNDIFHRSLLACCLEIVLFAYNSERL---------SFPWILEVFGLPPFDFY 151

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 188528630  524 KVIESFIKVEANLTREMIKHLERCEHRIMESLAWLSDSPLFDLI 567
Cdd:pfam01858 152 KVIESFIRAEDGLPRELVKHLNSIEEQILESLAWKSDSPLWELL 195
CYCLIN_RB cd20599
cyclin box found in retinoblastoma-associated protein (RB) and similar proteins; RB, also ...
 638-764 1.00e-74

cyclin box found in retinoblastoma-associated protein (RB) and similar proteins; RB, also called p105-Rb, pRb, or pp110, is a key regulator of entry into cell division and also acts as a tumor suppressor. It promotes G0-G1 transition when phosphorylated by CDK3/cyclin-C. It also acts as a transcription repressor of E2F1 target genes. RB is directly involved in heterochromatin formation by maintaining overall chromatin structure, especially that of constitutive heterochromatin by stabilizing histone methylation. It recruits and targets histone methyltransferases SUV39H1, KMT5B and KMT5C, leading to epigenetic transcriptional repression. It controls histone H4 'Lys-20' trimethylation. RB contains one cyclin box. The cyclin box is a protein binding domain.


Pssm-ID: 410302  Cd Length: 126  Bit Score: 240.27  E-value: 1.00e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188528630 638 TSLALFYKKVYRLAYLRLNTLCARLLSdHPELEHIIWTLFQHTLQNEYELMRDRHLDQIMMCSMYGICKVKNIDLKFKII 717
Cdd:cd20599    1 TSLSLFYKKVYRLAYLRLNTLCDLLLL-HPDLEHRIWTCFEHCLQNRYELLKDRHLDQIMMCSMYGICKVKNKDLRFKTI 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 188528630 718 VTAYKDLPHAAQETFKRVLIREEEFDSIIVFYNSVFMQRLKTNILQY 764
Cdd:cd20599   80 VTAYKDLPHASQEVYKRVLIRGEEYDSIIGFYNRVFMQALKTNILQF 126
RB_B pfam01857
Retinoblastoma-associated protein B domain; The crystal structure of the Rb pocket bound to a ...
 639-758 1.75e-44

Retinoblastoma-associated protein B domain; The crystal structure of the Rb pocket bound to a nine-residue E7 peptide containing the LxCxE motif, shared by other Rb-binding viral and cellular proteins, shows that the LxCxE peptide binds a highly conserved groove on the B domain. The B domain has a cyclin fold.


Pssm-ID: 460363  Cd Length: 131  Bit Score: 156.57  E-value: 1.75e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188528630  639 SLALFYKKVYRLAYLRLNTLCARLLSDhPELEHIIWTLFQHTLQNEYELMRDRHLDQIMMCSMYGICKVKNIDLKFKIIV 718
Cdd:pfam01857   1 SLNLFFRKVYHLAAVRLQDLCSRLDLS-SDLREKIWTCFEHSLVHQTDLMKDRHLDQILLCAIYVICKVTKEELTFKEIM 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 188528630  719 TAYKDLPHAAQETFKRVLIR------------EEEFDSIIVFYNSVFMQRLK 758
Cdd:pfam01857  80 KCYRKQPQASSHVYRSVLIRrrererngknneEEERGDIIKFYNKVFVPAMK 131
DUF3452 pfam11934
Domain of unknown function (DUF3452); This presumed domain is functionally uncharacterized. ...
 112-221 1.25e-08

Domain of unknown function (DUF3452); This presumed domain is functionally uncharacterized. This domain is found in bacteria and eukaryotes. This domain is typically between 124 to 150 amino acids in length. This domain is found associated with pfam01858, pfam01857. This domain has a single completely conserved residue W that may be functionally important.


Pssm-ID: 463402  Cd Length: 134  Bit Score: 54.14  E-value: 1.25e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188528630  112 TELQKSIETSVYKFFDLLKE----IDTSTKVDNAMSRLLKKYNVLCALYSKLERTCELIYLTQPSSALSTEINSM----- 182
Cdd:pfam11934  12 TRLLRACKLSIIDFFKKMKQwadmANLDWEFRLEIKELERNFSVTTVLFKKYKRIFNELFLSPPPKEPKRSKKSRpapcs 91

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 188528630  183 --LVLKISWITFLLAKGEVLQMEDDLVISFQLMLCVVDYFI 221
Cdd:pfam11934  92 ysDLFEFGWLLFLAAKNEFPSISKDLVTSYHLLLCCLDLVY 132
CYCLIN smart00385
domain present in cyclins, TFIIB and Retinoblastoma; A helical domain present in cyclins and ...
 654-723 1.30e-03

domain present in cyclins, TFIIB and Retinoblastoma; A helical domain present in cyclins and TFIIB (twice) and Retinoblastoma (once). A protein recognition domain functioning in cell-cycle and transcription control.


Pssm-ID: 214641 [Multi-domain]  Cd Length: 83  Bit Score: 38.34  E-value: 1.30e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188528630   654 RLNTLCARLLSDhPELEHIIWTLFQHTLQnEYELMRdRHLDQIMMCSMYGICKVKNIDLKFKIIVTAYKD 723
Cdd:smart00385   2 FLRRVCKALNLD-PETLNLAVNLLDRFLS-DYKFLK-YSPSLIAAAALYLASKTEETPPWTKELVHYTGY 68
 
Name Accession Description Interval E-value
Rb_C pfam08934
Rb C-terminal domain; The Rb C-terminal domain is required for high-affinity binding to E2F-DP ...
 761-918 5.56e-94

Rb C-terminal domain; The Rb C-terminal domain is required for high-affinity binding to E2F-DP complexes and for maximal repression of E2F-responsive promoters, thereby acting as a growth suppressor by blocking the G1-S transition of the cell cycle. This domain has a strand-loop-helix structure, which directly interacts with both E2F1 and DP1, followed by a tail segment that lacks regular secondary structure.


Pssm-ID: 462639  Cd Length: 152  Bit Score: 293.03  E-value: 5.56e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188528630  761 ILQYASTRPPTLSPIPHIPRSPYKFSSSPLRIPGG-NIYISPLKSPYkiseglPTPTKMTPRSRILVSIGESFGTSEKFQ 839
Cdd:pfam08934   1 ILQYASPRPPTLSPIPHIPRSPYKFPNSPLRVPGSnNVYISPLKSPR------LSPGMMTPRSRILVSIGESFGTSEKFQ 74

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 188528630  840 KINQMVCNSDRVLKRSAEGGNPPKPLKKLRFDIEGADEADGSKHlPAESKFQQKLAEMTSTRTRMQKQRMNESKDVSNK 918
Cdd:pfam08934  75 KINQMVSSSDRSLKRSLDGGSTPKPLKRLRFDVDGQDEADGSKS-GGESKFIQKLAEMTSTRSRMQEQKMKENAETSNK 152
RB_A pfam01858
Retinoblastoma-associated protein A domain; This domain has the cyclin fold as predicted.
 367-567 1.64e-87

Retinoblastoma-associated protein A domain; This domain has the cyclin fold as predicted.


Pssm-ID: 460364  Cd Length: 195  Bit Score: 277.16  E-value: 1.64e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188528630  367 TPVRTVMNTIQQLMVILNSASDQPSENLISYFNNCTVNPKENILKRVKDVGHIFKEKFANAVGQG---CVDIGVQRYKLG 443
Cdd:pfam01858   1 TPVSSAMQTVSWLQTLLSGLSDEPSEKLLRIFKSCSRDPTETILKRVKELGEIFCQKYTEASGEHpsfCIEIAEQRFRLA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188528630  444 VRLYYRVMESMLKSEEERLSIQNFSKLLNDNIFHMSLLACALEVVMATYSRSTLqhldsgtdlSFPWILNVLNLKAFDFY 523
Cdd:pfam01858  81 EKLYYKVLESILKSEKKRLPGNDLSSLLSNDIFHRSLLACCLEIVLFAYNSERL---------SFPWILEVFGLPPFDFY 151

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 188528630  524 KVIESFIKVEANLTREMIKHLERCEHRIMESLAWLSDSPLFDLI 567
Cdd:pfam01858 152 KVIESFIRAEDGLPRELVKHLNSIEEQILESLAWKSDSPLWELL 195
CYCLIN_RB cd20599
cyclin box found in retinoblastoma-associated protein (RB) and similar proteins; RB, also ...
 638-764 1.00e-74

cyclin box found in retinoblastoma-associated protein (RB) and similar proteins; RB, also called p105-Rb, pRb, or pp110, is a key regulator of entry into cell division and also acts as a tumor suppressor. It promotes G0-G1 transition when phosphorylated by CDK3/cyclin-C. It also acts as a transcription repressor of E2F1 target genes. RB is directly involved in heterochromatin formation by maintaining overall chromatin structure, especially that of constitutive heterochromatin by stabilizing histone methylation. It recruits and targets histone methyltransferases SUV39H1, KMT5B and KMT5C, leading to epigenetic transcriptional repression. It controls histone H4 'Lys-20' trimethylation. RB contains one cyclin box. The cyclin box is a protein binding domain.


Pssm-ID: 410302  Cd Length: 126  Bit Score: 240.27  E-value: 1.00e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188528630 638 TSLALFYKKVYRLAYLRLNTLCARLLSdHPELEHIIWTLFQHTLQNEYELMRDRHLDQIMMCSMYGICKVKNIDLKFKII 717
Cdd:cd20599    1 TSLSLFYKKVYRLAYLRLNTLCDLLLL-HPDLEHRIWTCFEHCLQNRYELLKDRHLDQIMMCSMYGICKVKNKDLRFKTI 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 188528630 718 VTAYKDLPHAAQETFKRVLIREEEFDSIIVFYNSVFMQRLKTNILQY 764
Cdd:cd20599   80 VTAYKDLPHASQEVYKRVLIRGEEYDSIIGFYNRVFMQALKTNILQF 126
RB_B pfam01857
Retinoblastoma-associated protein B domain; The crystal structure of the Rb pocket bound to a ...
 639-758 1.75e-44

Retinoblastoma-associated protein B domain; The crystal structure of the Rb pocket bound to a nine-residue E7 peptide containing the LxCxE motif, shared by other Rb-binding viral and cellular proteins, shows that the LxCxE peptide binds a highly conserved groove on the B domain. The B domain has a cyclin fold.


Pssm-ID: 460363  Cd Length: 131  Bit Score: 156.57  E-value: 1.75e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188528630  639 SLALFYKKVYRLAYLRLNTLCARLLSDhPELEHIIWTLFQHTLQNEYELMRDRHLDQIMMCSMYGICKVKNIDLKFKIIV 718
Cdd:pfam01857   1 SLNLFFRKVYHLAAVRLQDLCSRLDLS-SDLREKIWTCFEHSLVHQTDLMKDRHLDQILLCAIYVICKVTKEELTFKEIM 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 188528630  719 TAYKDLPHAAQETFKRVLIR------------EEEFDSIIVFYNSVFMQRLK 758
Cdd:pfam01857  80 KCYRKQPQASSHVYRSVLIRrrererngknneEEERGDIIKFYNKVFVPAMK 131
CYCLIN_RB-like cd20548
cyclin box found in retinoblastoma-associated protein (RB) family; The RB family includes ...
 640-753 1.74e-41

cyclin box found in retinoblastoma-associated protein (RB) family; The RB family includes retinoblastoma-associated protein (RB), and two retinoblastoma-like proteins, RBL1 and RBL2. RB, also called p105-Rb, pRb, or pp110, is a key regulator of entry into cell division, and also acts as a tumor suppressor. It promotes G0-G1 transition when phosphorylated by CDK3/cyclin-C. It also acts as a transcription repressor of E2F1 target genes. RB is directly involved in heterochromatin formation by maintaining overall chromatin structure. It recruits and targets histone methyltransferases SUV39H1, KMT5B and KMT5C, leading to epigenetic transcriptional repression. RBL1 and RBL2 are also key regulators of entry into cell division. RBL1 and RBL2 recruit and target histone methyltransferases KMT5B and KMT5C, leading to epigenetic transcriptional repression. They control histone H4 'Lys-20' trimethylation and probably act as transcription repressors by recruiting chromatin-modifying enzymes to promoters. They may also act as tumor suppressors. Members of this family contain one cyclin box. The cyclin box is a protein binding domain.


Pssm-ID: 410251  Cd Length: 122  Bit Score: 147.84  E-value: 1.74e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188528630 640 LALFYKKVYRLAYLRLNTLCARLLSDHPELEHIIWTLFQHTLQNEYELMRDRHLDQIMMCSMYGICKVKNIDLKFKIIVT 719
Cdd:cd20548    1 LQLFFRKLYRLAAARLQDLCKRLDLLSPPLRERIWTVFKHILSEETELLFDRHLDQIILCSIYAVCKVNNENLTFKEILD 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 188528630 720 AYKDLPHAAQETFKRVLIR--------EEEFDSIIVFYNSVF 753
Cdd:cd20548   81 AYRKQPQAESEVYRSVLPLfrsvgsddEGESGDIIKFYNQVF 122
CYCLIN_RBL cd20600
cyclin box found in retinoblastoma-like protein (RBL) subfamily; The RBL subfamily includes ...
 639-764 1.32e-32

cyclin box found in retinoblastoma-like protein (RBL) subfamily; The RBL subfamily includes two retinoblastoma-like proteins, RBL1 and RBL2. They are key regulators of entry into cell division and are directly involved in heterochromatin formation by maintaining overall chromatin structure. RBL1 and RBL2 recruit and target histone methyltransferases KMT5B and KMT5C, leading to epigenetic transcriptional repression. They control histone H4 'Lys-20' trimethylation and probably act as transcription repressors by recruiting chromatin-modifying enzymes to promoters. They may also act as tumor suppressors. Members of this family contain one cyclin box. The cyclin box is a protein binding domain.


Pssm-ID: 410303  Cd Length: 112  Bit Score: 122.13  E-value: 1.32e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188528630 639 SLALFYKKVYRLAYLRLNTLCARLLSDhPELEHIIWTLFQHTLQNEYELMRDRHLDQIMMCSMYGICKVKNIDLKFKIIV 718
Cdd:cd20600    1 SLGLFFRKVYHLASVRLRDLCEKLEIS-EELRRKIWTCFEHSLVHHIELMRDRHLDQLLMCAVYVIAKVTKQDKSFQEIM 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 188528630 719 TAYKDLPHAAQetfkrvlireeefDSIIVFYNSVFMQRLKTNILQY 764
Cdd:cd20600   80 KCYRLQPQAQS-------------GDLIQFYNSVYVKKMKEFALKF 112
CYCLIN_RBL1 cd20605
cyclin box found in retinoblastoma-like protein 1 (RBL1) and similar proteins; RBL1, also ...
 633-764 7.83e-31

cyclin box found in retinoblastoma-like protein 1 (RBL1) and similar proteins; RBL1, also called 107 kDa retinoblastoma-associated protein (p107), retinoblastoma-related protein 1 (RBR-1), or pRb1, is a key regulator of entry into cell division. It is directly involved in heterochromatin formation by maintaining overall chromatin structure, especially that of constitutive heterochromatin by stabilizing histone methylation. RBL1 recruits and targets histone methyltransferases KMT5B and KMT5C, leading to epigenetic transcriptional repression. It controls histone H4 'Lys-20' trimethylation. RBL1 probably acts as a transcription repressor by recruiting chromatin-modifying enzymes to promoters. It may also act as a tumor suppressor. RBL1 contains one cyclin box. The cyclin box is a protein binding domain.


Pssm-ID: 410308  Cd Length: 130  Bit Score: 117.68  E-value: 7.83e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188528630 633 KPLKSTSLALFYKKVYRLAYLRLNTLCARLlSDHPELEHIIWTLFQHTLQNEYELMRDRHLDQIMMCSMYGICKVKNIDL 712
Cdd:cd20605    1 KPKKTGSLALFYRKVYHLASVRLRDLCLKL-DVSNELRRKIWTCFEFSLVHCTDLMKDRHLDQLLLCAFYIMAKVTKEER 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 188528630 713 KFKIIVTAYKDLPHAAQETFKRVLIREEEFDsIIVFYNSVFMQRLKTNILQY 764
Cdd:cd20605   80 TFQDIMKCYRNQPQANSHVYRSVLLKEERGD-LIKFYNTIYVGRVKSFALKY 130
CYCLIN_AtRBR_like cd20601
cyclin box found in Arabidopsis thaliana retinoblastoma-related protein 1 (AtRBR1) and similar ...
 640-762 2.44e-27

cyclin box found in Arabidopsis thaliana retinoblastoma-related protein 1 (AtRBR1) and similar proteins; AtRBR1 is a key regulator of entry into cell division. It acts as a transcription repressor of E2F target genes, whose activity is required for progress from the G1 to the S phase of the cell cycle. AtRBR1 plays a central role in the mechanism controlling meristem cell differentiation, cell fate establishment and cell fate maintenance during organogenesis and gametogenesis. AtRBR1 contains one cyclin box. The cyclin box is a protein binding domain.


Pssm-ID: 410304  Cd Length: 129  Bit Score: 107.86  E-value: 2.44e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188528630 640 LALFYKKVYRLAYLRLNTLCARLlSDHPELEHIIWTLFQHTLQNEYELMRDRHLDQIMMCSMYGICKVKNIDLKFKIIVT 719
Cdd:cd20601    1 INVFFQKVLKLAAIRIADLCERL-QQPQLVVEQVYRLIEHVLYEQTGLFFNRHIDQIILCCLYGVCKVHKLNVTFREIIY 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 188528630 720 AYKDLPHAAQETFKRVLIREEEFD-------SIIVFYNSVFMQRLKTNIL 762
Cdd:cd20601   80 QYRKQPQCKPDVFRNVVIEQRRPTlggpdhgDIIAFYNEVFVPATKPFLL 129
CYCLIN_RBL2 cd20606
cyclin box found in retinoblastoma-like protein 2 (RBL2) and similar proteins; RBL2, also ...
 639-738 9.15e-24

cyclin box found in retinoblastoma-like protein 2 (RBL2) and similar proteins; RBL2, also called 130 kDa retinoblastoma-associated protein (p130), retinoblastoma-related protein 2 (RBR-2), or pRb2, is a key regulator of entry into cell division. It is directly involved in heterochromatin formation by maintaining overall chromatin structure, especially that of constitutive heterochromatin by stabilizing histone methylation. RBL2 recruits and targets histone methyltransferases KMT5B and KMT5C, leading to epigenetic transcriptional repression. It controls histone H4 'Lys-20' trimethylation. It probably acts as a transcription repressor by recruiting chromatin-modifying enzymes to promoters. It may also act as a tumor suppressor. RBL2 contains one cyclin box. The cyclin box is a protein binding domain.


Pssm-ID: 410309  Cd Length: 189  Bit Score: 99.59  E-value: 9.15e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188528630 639 SLALFYKKVYRLAYLRLNTLCARL-LSDhpELEHIIWTLFQHTLQNEYELMRDRHLDQIMMCSMYGICKVKNIDLKFKII 717
Cdd:cd20606    1 SLSLFFRKVYHLASVRLRDLCAKLdISD--ELRKKIWTCFEYSLVHCPELMMDRHLDQLLMCAIYVMAKVTKEDKSFQNI 78

                         90       100
                 ....*....|....*....|.
gi 188528630 718 VTAYKDLPHAAQETFKRVLIR 738
Cdd:cd20606   79 MRCYRTQPQASSSVYRSVLIK 99
DUF3452 pfam11934
Domain of unknown function (DUF3452); This presumed domain is functionally uncharacterized. ...
 112-221 1.25e-08

Domain of unknown function (DUF3452); This presumed domain is functionally uncharacterized. This domain is found in bacteria and eukaryotes. This domain is typically between 124 to 150 amino acids in length. This domain is found associated with pfam01858, pfam01857. This domain has a single completely conserved residue W that may be functionally important.


Pssm-ID: 463402  Cd Length: 134  Bit Score: 54.14  E-value: 1.25e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188528630  112 TELQKSIETSVYKFFDLLKE----IDTSTKVDNAMSRLLKKYNVLCALYSKLERTCELIYLTQPSSALSTEINSM----- 182
Cdd:pfam11934  12 TRLLRACKLSIIDFFKKMKQwadmANLDWEFRLEIKELERNFSVTTVLFKKYKRIFNELFLSPPPKEPKRSKKSRpapcs 91

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 188528630  183 --LVLKISWITFLLAKGEVLQMEDDLVISFQLMLCVVDYFI 221
Cdd:pfam11934  92 ysDLFEFGWLLFLAAKNEFPSISKDLVTSYHLLLCCLDLVY 132
CYCLIN smart00385
domain present in cyclins, TFIIB and Retinoblastoma; A helical domain present in cyclins and ...
 654-723 1.30e-03

domain present in cyclins, TFIIB and Retinoblastoma; A helical domain present in cyclins and TFIIB (twice) and Retinoblastoma (once). A protein recognition domain functioning in cell-cycle and transcription control.


Pssm-ID: 214641 [Multi-domain]  Cd Length: 83  Bit Score: 38.34  E-value: 1.30e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188528630   654 RLNTLCARLLSDhPELEHIIWTLFQHTLQnEYELMRdRHLDQIMMCSMYGICKVKNIDLKFKIIVTAYKD 723
Cdd:smart00385   2 FLRRVCKALNLD-PETLNLAVNLLDRFLS-DYKFLK-YSPSLIAAAALYLASKTEETPPWTKELVHYTGY 68
 
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