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Conserved domains on  [gi|1942964707|ref|XP_038015371|]
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retinoblastoma-like protein 1 isoform X6 [Motacilla alba alba]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
RB_A pfam01858
Retinoblastoma-associated protein A domain; This domain has the cyclin fold as predicted.
 318-511 4.27e-103

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


:

Pssm-ID: 460364  Cd Length: 195  Bit Score: 319.91  E-value: 4.27e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942964707 318 TPVASATQSVSRLQSMVAGLKNAPSEQLTAIFESCARSPLESIMSRVKEIGETFCCCYIQSTDEQPGSHIDFAMNRLKLA 397
Cdd:pfam01858   1 TPVSSAMQTVSWLQTLLSGLSDEPSEKLLRIFKSCSRDPTETILKRVKELGEIFCQKYTEASGEHPSFCIEIAEQRFRLA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942964707 398 EILYYKILETIMVQETRRLHGKDLTALLEQDLFHRSLLACCLEIVLFAYSSPR-TFPWIIEVLDLRPFYFYKVIEVLIRS 476
Cdd:pfam01858  81 EKLYYKVLESILKSEKKRLPGNDLSSLLSNDIFHRSLLACCLEIVLFAYNSERlSFPWILEVFGLPPFDFYKVIESFIRA 160

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1942964707 477 EEGLSRDMVKHLNSIEEQILESLAWTRNSALWNAL 511
Cdd:pfam01858 161 EDGLPRELVKHLNSIEEQILESLAWKSDSPLWELL 195
CYCLIN_RBL1 cd20605
cyclin box found in retinoblastoma-like protein 1 (RBL1) and similar proteins; RBL1, also ...
 704-874 9.15e-82

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: 260.59  E-value: 9.15e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942964707 704 KPKRTGSLALFYRKVYHLASVRLRDLCLKLDVSNDLRRKIWTCFEFTLVHCADLMKDRHLDQLLLCAFYIMAKVTKEERT 783
Cdd:cd20605     1 KPKKTGSLALFYRKVYHLASVRLRDLCLKLDVSNELRRKIWTCFEFSLVHCTDLMKDRHLDQLLLCAFYIMAKVTKEERT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942964707 784 FQDIMKSYRNQPQANSHVYRSVLLRntydvpldknanpememaedssvktgsslgrsaentsesetEERGDLIKFYNAVY 863
Cdd:cd20605    81 FQDIMKCYRNQPQANSHVYRSVLLK-----------------------------------------EERGDLIKFYNTIY 119

                         170
                  ....*....|.
gi 1942964707 864 VGRVKSFALKY 874
Cdd:cd20605   120 VGRVKSFALKY 130
DUF3452 pfam11934
Domain of unknown function (DUF3452); This presumed domain is functionally uncharacterized. ...
 1-108 1.30e-48

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: 168.93  E-value: 1.30e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942964707   1 MKKWMDMSNLPQEFRERVERLERNFEVSTVIFKKFEPIFFDIFQNPyeESSKPHRSRKQRRVPCSVKDLFNFCWTLFVYT 80
Cdd:pfam11934  29 MKQWADMANLDWEFRLEIKELERNFSVTTVLFKKYKRIFNELFLSP--PPKEPKRSKKSRPAPCSYSDLFEFGWLLFLAA 106

                          90       100
                  ....*....|....*....|....*...
gi 1942964707  81 KGNFRMIGDDLVNSYHLLLCCLDVIFAN 108
Cdd:pfam11934 107 KNEFPSISKDLVTSYHLLLCCLDLVYVN 134
Rb_C super family cl07508
Rb C-terminal domain; The Rb C-terminal domain is required for high-affinity binding to E2F-DP ...
 886-971 6.04e-08

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.


The actual alignment was detected with superfamily member pfam08934:

Pssm-ID: 462639  Cd Length: 152  Bit Score: 53.05  E-value: 6.04e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942964707 886 PPLSPFPSIRQQPV----SPRRISQQHSVYVSPHKNG----ACLTPRTALLYKFNGS--PSKSLKDINNMIKQGEhRSKK 955
Cdd:pfam08934  10 PTLSPIPHIPRSPYkfpnSPLRVPGSNNVYISPLKSPrlspGMMTPRSRILVSIGESfgTSEKFQKINQMVSSSD-RSLK 88

                          90
                  ....*....|....*.
gi 1942964707 956 RAITIDSdTESPSKRL 971
Cdd:pfam08934  89 RSLDGGS-TPKPLKRL 103
 
Name Accession Description Interval E-value
RB_A pfam01858
Retinoblastoma-associated protein A domain; This domain has the cyclin fold as predicted.
 318-511 4.27e-103

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


Pssm-ID: 460364  Cd Length: 195  Bit Score: 319.91  E-value: 4.27e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942964707 318 TPVASATQSVSRLQSMVAGLKNAPSEQLTAIFESCARSPLESIMSRVKEIGETFCCCYIQSTDEQPGSHIDFAMNRLKLA 397
Cdd:pfam01858   1 TPVSSAMQTVSWLQTLLSGLSDEPSEKLLRIFKSCSRDPTETILKRVKELGEIFCQKYTEASGEHPSFCIEIAEQRFRLA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942964707 398 EILYYKILETIMVQETRRLHGKDLTALLEQDLFHRSLLACCLEIVLFAYSSPR-TFPWIIEVLDLRPFYFYKVIEVLIRS 476
Cdd:pfam01858  81 EKLYYKVLESILKSEKKRLPGNDLSSLLSNDIFHRSLLACCLEIVLFAYNSERlSFPWILEVFGLPPFDFYKVIESFIRA 160

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1942964707 477 EEGLSRDMVKHLNSIEEQILESLAWTRNSALWNAL 511
Cdd:pfam01858 161 EDGLPRELVKHLNSIEEQILESLAWKSDSPLWELL 195
CYCLIN_RBL1 cd20605
cyclin box found in retinoblastoma-like protein 1 (RBL1) and similar proteins; RBL1, also ...
 704-874 9.15e-82

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: 260.59  E-value: 9.15e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942964707 704 KPKRTGSLALFYRKVYHLASVRLRDLCLKLDVSNDLRRKIWTCFEFTLVHCADLMKDRHLDQLLLCAFYIMAKVTKEERT 783
Cdd:cd20605     1 KPKKTGSLALFYRKVYHLASVRLRDLCLKLDVSNELRRKIWTCFEFSLVHCTDLMKDRHLDQLLLCAFYIMAKVTKEERT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942964707 784 FQDIMKSYRNQPQANSHVYRSVLLRntydvpldknanpememaedssvktgsslgrsaentsesetEERGDLIKFYNAVY 863
Cdd:cd20605    81 FQDIMKCYRNQPQANSHVYRSVLLK-----------------------------------------EERGDLIKFYNTIY 119

                         170
                  ....*....|.
gi 1942964707 864 VGRVKSFALKY 874
Cdd:cd20605   120 VGRVKSFALKY 130
RB_B pfam01857
Retinoblastoma-associated protein B domain; The crystal structure of the Rb pocket bound to a ...
 710-868 1.12e-70

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: 230.53  E-value: 1.12e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942964707 710 SLALFYRKVYHLASVRLRDLCLKLDVSNDLRRKIWTCFEFTLVHCADLMKDRHLDQLLLCAFYIMAKVTKEERTFQDIMK 789
Cdd:pfam01857   1 SLNLFFRKVYHLAAVRLQDLCSRLDLSSDLREKIWTCFEHSLVHQTDLMKDRHLDQILLCAIYVICKVTKEELTFKEIMK 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1942964707 790 SYRNQPQANSHVYRSVLLRNTYDVPLDKNANPEmemaedssvktgsslgrsaentseseteERGDLIKFYNAVYVGRVK 868
Cdd:pfam01857  81 CYRKQPQASSHVYRSVLIRRRERERNGKNNEEE----------------------------ERGDIIKFYNKVFVPAMK 131
DUF3452 pfam11934
Domain of unknown function (DUF3452); This presumed domain is functionally uncharacterized. ...
 1-108 1.30e-48

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: 168.93  E-value: 1.30e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942964707   1 MKKWMDMSNLPQEFRERVERLERNFEVSTVIFKKFEPIFFDIFQNPyeESSKPHRSRKQRRVPCSVKDLFNFCWTLFVYT 80
Cdd:pfam11934  29 MKQWADMANLDWEFRLEIKELERNFSVTTVLFKKYKRIFNELFLSP--PPKEPKRSKKSRPAPCSYSDLFEFGWLLFLAA 106

                          90       100
                  ....*....|....*....|....*...
gi 1942964707  81 KGNFRMIGDDLVNSYHLLLCCLDVIFAN 108
Cdd:pfam11934 107 KNEFPSISKDLVTSYHLLLCCLDLVYVN 134
Rb_C pfam08934
Rb C-terminal domain; The Rb C-terminal domain is required for high-affinity binding to E2F-DP ...
 886-971 6.04e-08

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: 53.05  E-value: 6.04e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942964707 886 PPLSPFPSIRQQPV----SPRRISQQHSVYVSPHKNG----ACLTPRTALLYKFNGS--PSKSLKDINNMIKQGEhRSKK 955
Cdd:pfam08934  10 PTLSPIPHIPRSPYkfpnSPLRVPGSNNVYISPLKSPrlspGMMTPRSRILVSIGESfgTSEKFQKINQMVSSSD-RSLK 88

                          90
                  ....*....|....*.
gi 1942964707 956 RAITIDSdTESPSKRL 971
Cdd:pfam08934  89 RSLDGGS-TPKPLKRL 103
CYCLIN smart00385
domain present in cyclins, TFIIB and Retinoblastoma; A helical domain present in cyclins and ...
 724-794 1.19e-04

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: 41.42  E-value: 1.19e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1942964707  724 VRLRDLCLKLDVSNDLRRKIWTCFEFTLVHCaDLMKdRHLDQLLLCAFYIMAKVTKEERTFQDIMKSYRNQ 794
Cdd:smart00385   1 DFLRRVCKALNLDPETLNLAVNLLDRFLSDY-KFLK-YSPSLIAAAALYLASKTEETPPWTKELVHYTGYF 69
 
Name Accession Description Interval E-value
RB_A pfam01858
Retinoblastoma-associated protein A domain; This domain has the cyclin fold as predicted.
 318-511 4.27e-103

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


Pssm-ID: 460364  Cd Length: 195  Bit Score: 319.91  E-value: 4.27e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942964707 318 TPVASATQSVSRLQSMVAGLKNAPSEQLTAIFESCARSPLESIMSRVKEIGETFCCCYIQSTDEQPGSHIDFAMNRLKLA 397
Cdd:pfam01858   1 TPVSSAMQTVSWLQTLLSGLSDEPSEKLLRIFKSCSRDPTETILKRVKELGEIFCQKYTEASGEHPSFCIEIAEQRFRLA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942964707 398 EILYYKILETIMVQETRRLHGKDLTALLEQDLFHRSLLACCLEIVLFAYSSPR-TFPWIIEVLDLRPFYFYKVIEVLIRS 476
Cdd:pfam01858  81 EKLYYKVLESILKSEKKRLPGNDLSSLLSNDIFHRSLLACCLEIVLFAYNSERlSFPWILEVFGLPPFDFYKVIESFIRA 160

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1942964707 477 EEGLSRDMVKHLNSIEEQILESLAWTRNSALWNAL 511
Cdd:pfam01858 161 EDGLPRELVKHLNSIEEQILESLAWKSDSPLWELL 195
CYCLIN_RBL1 cd20605
cyclin box found in retinoblastoma-like protein 1 (RBL1) and similar proteins; RBL1, also ...
 704-874 9.15e-82

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: 260.59  E-value: 9.15e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942964707 704 KPKRTGSLALFYRKVYHLASVRLRDLCLKLDVSNDLRRKIWTCFEFTLVHCADLMKDRHLDQLLLCAFYIMAKVTKEERT 783
Cdd:cd20605     1 KPKKTGSLALFYRKVYHLASVRLRDLCLKLDVSNELRRKIWTCFEFSLVHCTDLMKDRHLDQLLLCAFYIMAKVTKEERT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942964707 784 FQDIMKSYRNQPQANSHVYRSVLLRntydvpldknanpememaedssvktgsslgrsaentsesetEERGDLIKFYNAVY 863
Cdd:cd20605    81 FQDIMKCYRNQPQANSHVYRSVLLK-----------------------------------------EERGDLIKFYNTIY 119

                         170
                  ....*....|.
gi 1942964707 864 VGRVKSFALKY 874
Cdd:cd20605   120 VGRVKSFALKY 130
RB_B pfam01857
Retinoblastoma-associated protein B domain; The crystal structure of the Rb pocket bound to a ...
 710-868 1.12e-70

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: 230.53  E-value: 1.12e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942964707 710 SLALFYRKVYHLASVRLRDLCLKLDVSNDLRRKIWTCFEFTLVHCADLMKDRHLDQLLLCAFYIMAKVTKEERTFQDIMK 789
Cdd:pfam01857   1 SLNLFFRKVYHLAAVRLQDLCSRLDLSSDLREKIWTCFEHSLVHQTDLMKDRHLDQILLCAIYVICKVTKEELTFKEIMK 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1942964707 790 SYRNQPQANSHVYRSVLLRNTYDVPLDKNANPEmemaedssvktgsslgrsaentseseteERGDLIKFYNAVYVGRVK 868
Cdd:pfam01857  81 CYRKQPQASSHVYRSVLIRRRERERNGKNNEEE----------------------------ERGDIIKFYNKVFVPAMK 131
CYCLIN_RBL2 cd20606
cyclin box found in retinoblastoma-like protein 2 (RBL2) and similar proteins; RBL2, also ...
 710-874 1.67e-66

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: 221.31  E-value: 1.67e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942964707 710 SLALFYRKVYHLASVRLRDLCLKLDVSNDLRRKIWTCFEFTLVHCADLMKDRHLDQLLLCAFYIMAKVTKEERTFQDIMK 789
Cdd:cd20606     1 SLSLFFRKVYHLASVRLRDLCAKLDISDELRKKIWTCFEYSLVHCPELMMDRHLDQLLMCAIYVMAKVTKEDKSFQNIMR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942964707 790 SYRNQPQANSHVYRSVLLR------------NTYDVPLDKNaNPEMEMAEDSSVKTGSSL-------------GRSAENT 844
Cdd:cd20606    81 CYRTQPQASSSVYRSVLIKgrrrrrsgssddSGSQSSSSEE-NRERTSRDSSPVMRSSSTlpvpqpnsapptpTRLTGAN 159

                         170       180       190
                  ....*....|....*....|....*....|
gi 1942964707 845 SESETEERGDLIKFYNAVYVGRVKSFALKY 874
Cdd:cd20606   160 SDMEEEERGDLIQFYNNIYIEQIKEFALKY 189
CYCLIN_RBL cd20600
cyclin box found in retinoblastoma-like protein (RBL) subfamily; The RBL subfamily includes ...
 710-874 9.79e-64

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: 210.34  E-value: 9.79e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942964707 710 SLALFYRKVYHLASVRLRDLCLKLDVSNDLRRKIWTCFEFTLVHCADLMKDRHLDQLLLCAFYIMAKVTKEERTFQDIMK 789
Cdd:cd20600     1 SLGLFFRKVYHLASVRLRDLCEKLEISEELRRKIWTCFEHSLVHHIELMRDRHLDQLLMCAVYVIAKVTKQDKSFQEIMK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942964707 790 SYRNQPQANShvyrsvllrntydvpldknanpememaedssvktgsslgrsaentseseteerGDLIKFYNAVYVGRVKS 869
Cdd:cd20600    81 CYRLQPQAQS-----------------------------------------------------GDLIQFYNSVYVKKMKE 107


                  ....*
gi 1942964707 870 FALKY 874
Cdd:cd20600   108 FALKF 112
DUF3452 pfam11934
Domain of unknown function (DUF3452); This presumed domain is functionally uncharacterized. ...
 1-108 1.30e-48

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: 168.93  E-value: 1.30e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942964707   1 MKKWMDMSNLPQEFRERVERLERNFEVSTVIFKKFEPIFFDIFQNPyeESSKPHRSRKQRRVPCSVKDLFNFCWTLFVYT 80
Cdd:pfam11934  29 MKQWADMANLDWEFRLEIKELERNFSVTTVLFKKYKRIFNELFLSP--PPKEPKRSKKSRPAPCSYSDLFEFGWLLFLAA 106

                          90       100
                  ....*....|....*....|....*...
gi 1942964707  81 KGNFRMIGDDLVNSYHLLLCCLDVIFAN 108
Cdd:pfam11934 107 KNEFPSISKDLVTSYHLLLCCLDLVYVN 134
CYCLIN_RB-like cd20548
cyclin box found in retinoblastoma-associated protein (RB) family; The RB family includes ...
 711-863 6.59e-40

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: 143.60  E-value: 6.59e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942964707 711 LALFYRKVYHLASVRLRDLCLKLD-VSNDLRRKIWTCFEFTLVHCADLMKDRHLDQLLLCAFYIMAKVTKEERTFQDIMK 789
Cdd:cd20548     1 LQLFFRKLYRLAAARLQDLCKRLDlLSPPLRERIWTVFKHILSEETELLFDRHLDQIILCSIYAVCKVNNENLTFKEILD 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1942964707 790 SYRNQPQANSHVYRSVlLRNTYDVPLDKNANpememaedssvktgsslgrsaentseseteeRGDLIKFYNAVY 863
Cdd:cd20548    81 AYRKQPQAESEVYRSV-LPLFRSVGSDDEGE-------------------------------SGDIIKFYNQVF 122
CYCLIN_RB cd20599
cyclin box found in retinoblastoma-associated protein (RB) and similar proteins; RB, also ...
 710-874 1.08e-35

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: 131.64  E-value: 1.08e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942964707 710 SLALFYRKVYHLASVRLRDLCLKLDVSNDLRRKIWTCFEFTLVHCADLMKDRHLDQLLLCAFYIMAKVTKEERTFQDIMK 789
Cdd:cd20599     2 SLSLFYKKVYRLAYLRLNTLCDLLLLHPDLEHRIWTCFEHCLQNRYELLKDRHLDQIMMCSMYGICKVKNKDLRFKTIVT 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942964707 790 SYRNQPQANSHVYRSVLLRntydvpldknanpemEMAEDSsvktgsslgrsaentseseteergdLIKFYNAVYVGRVKS 869
Cdd:cd20599    82 AYKDLPHASQEVYKRVLIR---------------GEEYDS-------------------------IIGFYNRVFMQALKT 121


                  ....*
gi 1942964707 870 FALKY 874
Cdd:cd20599   122 NILQF 126
CYCLIN_AtRBR_like cd20601
cyclin box found in Arabidopsis thaliana retinoblastoma-related protein 1 (AtRBR1) and similar ...
 711-872 2.06e-30

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: 116.72  E-value: 2.06e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942964707 711 LALFYRKVYHLASVRLRDLCLKLDVSNDLRRKIWTCFEFTLVHCADLMKDRHLDQLLLCAFYIMAKVTKEERTFQDIMKS 790
Cdd:cd20601     1 INVFFQKVLKLAAIRIADLCERLQQPQLVVEQVYRLIEHVLYEQTGLFFNRHIDQIILCCLYGVCKVHKLNVTFREIIYQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942964707 791 YRNQPQANSHVYRSVLLRNTydvpldknaNPEMEMAEdssvktgsslgrsaentseseteeRGDLIKFYNAVYVGRVKSF 870
Cdd:cd20601    81 YRKQPQCKPDVFRNVVIEQR---------RPTLGGPD------------------------HGDIIAFYNEVFVPATKPF 127


                  ..
gi 1942964707 871 AL 872
Cdd:cd20601   128 LL 129
Rb_C pfam08934
Rb C-terminal domain; The Rb C-terminal domain is required for high-affinity binding to E2F-DP ...
 886-971 6.04e-08

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: 53.05  E-value: 6.04e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942964707 886 PPLSPFPSIRQQPV----SPRRISQQHSVYVSPHKNG----ACLTPRTALLYKFNGS--PSKSLKDINNMIKQGEhRSKK 955
Cdd:pfam08934  10 PTLSPIPHIPRSPYkfpnSPLRVPGSNNVYISPLKSPrlspGMMTPRSRILVSIGESfgTSEKFQKINQMVSSSD-RSLK 88

                          90
                  ....*....|....*.
gi 1942964707 956 RAITIDSdTESPSKRL 971
Cdd:pfam08934  89 RSLDGGS-TPKPLKRL 103
CYCLIN smart00385
domain present in cyclins, TFIIB and Retinoblastoma; A helical domain present in cyclins and ...
 724-794 1.19e-04

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: 41.42  E-value: 1.19e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1942964707  724 VRLRDLCLKLDVSNDLRRKIWTCFEFTLVHCaDLMKdRHLDQLLLCAFYIMAKVTKEERTFQDIMKSYRNQ 794
Cdd:smart00385   1 DFLRRVCKALNLDPETLNLAVNLLDRFLSDY-KFLK-YSPSLIAAAALYLASKTEETPPWTKELVHYTGYF 69
CYCLIN_SF cd00043
Cyclin box fold superfamily; The cyclin box is a protein binding domain that functions in ...
 725-796 3.29e-03

Cyclin box fold superfamily; The cyclin box is a protein binding domain that functions in cell-cycle and transcriptional control. It is about 100 amino acids in length, composed of five helices, and is present in cyclins, transcription initiation factor IIB (TFIIB), and retinoblastoma tumour suppressor protein (Rb). Cyclins consist of 8 classes of cell cycle regulators that function as regulatory subunits of cyclin-dependent kinases (CDKs), which are serine/threonine kinases. The catalytic activities of CDKs are modulated not only by their interactions with cyclins but also by CDK inhibitors (CKIs). CDKs, cyclins and CKIs play key roles in transcription, epigenetic regulation, metabolism, stem cell self-renewal, neuronal functions, and spermatogenesis. TFIIB is a transcription factor that binds the TATA box. Members in this superfamily contain one or two copies of the cyclin box.


Pssm-ID: 410207 [Multi-domain]  Cd Length: 82  Bit Score: 37.39  E-value: 3.29e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1942964707 725 RLRDLCLKLDVSNDLRRKIWTCFEftLVHCADLMKDRHLDQLLLCAFYIMAKVTKEERTFQDIMKSYRNQPQ 796
Cdd:cd00043     5 FIRRLCSKLGLPEEVLELAIELLD--RFLSKGLLLGRSPELIAAACLYLACKLEELPRTLKEIAKVSGVSEK 74
 
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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