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Conserved domains on  [gi|2117983372|ref|XP_044283681|]
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retinoblastoma-like protein 2 isoform X2 [Varanus komodoensis]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CYCLIN_RBL2 cd20606
cyclin box found in retinoblastoma-like protein 2 (RBL2) and similar proteins; RBL2, also ...
 858-1046 3.29e-120

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: 368.46  E-value: 3.29e-120
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117983372  858 SLALFFRKVFHLASVRLRDLCLKLDIPAELRKKIWTCFEFSLAQCSELMMGRHLDQLLMCAIYVISKVTEEDTSFQNIMR 937
Cdd:cd20606      1 SLSLFFRKVYHLASVRLRDLCAKLDISDELRKKIWTCFEYSLVHCPELMMDRHLDQLLMCAIYVMAKVTKEDKSFQNIMR 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117983372  938 CYRTQPQAKSHVYRSVLIKGRRRRHSGSGNSNQQRNSPTDRNRDRTSRDSSPVMRSSSTLPVPQPSSAPPTPTRLAGANS 1017
Cdd:cd20606     81 CYRTQPQASSSVYRSVLIKGRRRRRSGSSDDSGSQSSSSEENRERTSRDSSPVMRSSSTLPVPQPNSAPPTPTRLTGANS 160

                          170       180
                   ....*....|....*....|....*....
gi 2117983372 1018 DIEEEERGDLIQFYNNVYTDRIKDFALKY 1046
Cdd:cd20606    161 DMEEEERGDLIQFYNNIYIEQIKEFALKY 189
RB_A pfam01858
Retinoblastoma-associated protein A domain; This domain has the cyclin fold as predicted.
 445-636 1.99e-97

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


:

Pssm-ID: 460364  Cd Length: 195  Bit Score: 307.59  E-value: 1.99e-97
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117983372  445 SPISIATYSLTRLHTMLTGLKNAPSENLEQILRSCSRDPSVSIASRVKEMYEIYCKK--TQSDGEPGSVKDIAGKHFRLA 522
Cdd:pfam01858    1 TPVSSAMQTVSWLQTLLSGLSDEPSEKLLRIFKSCSRDPTETILKRVKELGEIFCQKytEASGEHPSFCIEIAEQRFRLA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117983372  523 EVLYYKVLESVIEQEKRRLGDADLSAVLEHDVFHRSLLACCLEIIIYSYTAV-DSFPFITDLFDVPAFHFYKVIEILIRA 601
Cdd:pfam01858   81 EKLYYKVLESILKSEKKRLPGNDLSSLLSNDIFHRSLLACCLEIVLFAYNSErLSFPWILEVFGLPPFDFYKVIESFIRA 160

                          170       180       190
                   ....*....|....*....|....*....|....*
gi 2117983372  602 EDGLCREVVKHLNHIEEQILESLAWKEDSPLWDKI 636
Cdd:pfam01858  161 EDGLPRELVKHLNSIEEQILESLAWKSDSPLWELL 195
DUF3452 pfam11934
Domain of unknown function (DUF3452); This presumed domain is functionally uncharacterized. ...
 133-266 1.46e-55

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: 188.96  E-value: 1.46e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117983372  133 GTVEGNYVSLIRILRCSGQSLIEFFNKMKKWEDMANLPSQFRERTTRLERNFTVSAVIFKKYEPIFQDIFKYPQDDqpRQ 212
Cdd:pfam11934    2 GTVEGNCVSLTRLLRACKLSIIDFFKKMKQWADMANLDWEFRLEIKELERNFSVTTVLFKKYKRIFNELFLSPPPK--EP 79

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2117983372  213 QRGRKQRRQPCTVSEVFQFCWVLFVYAKGNFPMISDDLVNAYHLLLCVLDLVFA 266
Cdd:pfam11934   80 KRSKKSRPAPCSYSDLFEFGWLLFLAAKNEFPSISKDLVTSYHLLLCCLDLVYV 133
SP1-4_N super family cl41773
N-terminal domain of transcription factor Specificity Proteins (SP) 1-4; Specificity Proteins ...
 730-846 5.55e-05

N-terminal domain of transcription factor Specificity Proteins (SP) 1-4; Specificity Proteins (SPs) are transcription factors that are involved in many cellular processes, including cell differentiation, cell growth, apoptosis, immune responses, response to DNA damage, and chromatin remodeling. There are many SPs in vertebrates (9 SPs in humans and mice, 7 SPs in chicken, and 11 SPs in teleost fish), but arthropods only have 3 SPs. SPs belong to a family of proteins, called the SP/Kruppel or Krueppel-like Factor (KLF) family, characterized by a C-terminal DNA-binding domain of 81 amino acids consisting of three Kruppel-like C2H2 zinc fingers. These factors bind to a loose consensus motif, namely NNRCRCCYY (where N is any nucleotide; R is A/G, and Y is C/T), such as the recurring motifs in GC and GT boxes (5'-GGGGCGGGG-3' and 5-GGTGTGGGG-3') that are present in promoters and more distal regulatory elements of mammalian genes. SP factors preferentially bind GC boxes, while KLFs bind CACCC boxes. Another characteristic hallmark of SP factors is the presence of the Buttonhead (BTD) box CXCPXC, just N-terminal to the zinc fingers. The function of the BTD box is unknown, but it is thought to play an important physiological role. Another feature of most SP factors is the presence of a conserved amino acid stretch, the so-called SP box, located close to the N-terminus. SP factors may be separated into three groups based on their domain architecture and the similarity of their N-terminal transactivation domains: SP1-4, SP5, and SP6-9. The transactivation domains between the three groups are not homologous to one another. SP1-4 have similar N-terminal transactivation domains characterized by glutamine-rich regions, which, in most cases, have adjacent serine/threonine-rich regions. This model represents the N-terminal domain of SP1-4.


The actual alignment was detected with superfamily member cd22553:

Pssm-ID: 425404 [Multi-domain]  Cd Length: 384  Bit Score: 46.94  E-value: 5.55e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117983372  730 QPVISPMPVQNVS-PETIPVTPVPGQTLVtvatatvtanngQTVTIPVQGIANENGGITFIPVQVNVSGQ-AQPlsTSIQ 807
Cdd:cd22553    145 NAVQLPLNNMTQTiPVQVPVSTANGQTVY------------QTIQVPIQAIQSGNAGGGNQALQAQVIPQlAQA--AQLQ 210

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 2117983372  808 PlsaQSLAgalsspQVAGtalqlQGQFQQIALPGEQQRQ 846
Cdd:cd22553    211 P---QQLA------QVSS-----QGYIQQIPANASQQQP 235
 
Name Accession Description Interval E-value
CYCLIN_RBL2 cd20606
cyclin box found in retinoblastoma-like protein 2 (RBL2) and similar proteins; RBL2, also ...
 858-1046 3.29e-120

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: 368.46  E-value: 3.29e-120
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117983372  858 SLALFFRKVFHLASVRLRDLCLKLDIPAELRKKIWTCFEFSLAQCSELMMGRHLDQLLMCAIYVISKVTEEDTSFQNIMR 937
Cdd:cd20606      1 SLSLFFRKVYHLASVRLRDLCAKLDISDELRKKIWTCFEYSLVHCPELMMDRHLDQLLMCAIYVMAKVTKEDKSFQNIMR 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117983372  938 CYRTQPQAKSHVYRSVLIKGRRRRHSGSGNSNQQRNSPTDRNRDRTSRDSSPVMRSSSTLPVPQPSSAPPTPTRLAGANS 1017
Cdd:cd20606     81 CYRTQPQASSSVYRSVLIKGRRRRRSGSSDDSGSQSSSSEENRERTSRDSSPVMRSSSTLPVPQPNSAPPTPTRLTGANS 160

                          170       180
                   ....*....|....*....|....*....
gi 2117983372 1018 DIEEEERGDLIQFYNNVYTDRIKDFALKY 1046
Cdd:cd20606    161 DMEEEERGDLIQFYNNIYIEQIKEFALKY 189
RB_A pfam01858
Retinoblastoma-associated protein A domain; This domain has the cyclin fold as predicted.
 445-636 1.99e-97

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


Pssm-ID: 460364  Cd Length: 195  Bit Score: 307.59  E-value: 1.99e-97
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117983372  445 SPISIATYSLTRLHTMLTGLKNAPSENLEQILRSCSRDPSVSIASRVKEMYEIYCKK--TQSDGEPGSVKDIAGKHFRLA 522
Cdd:pfam01858    1 TPVSSAMQTVSWLQTLLSGLSDEPSEKLLRIFKSCSRDPTETILKRVKELGEIFCQKytEASGEHPSFCIEIAEQRFRLA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117983372  523 EVLYYKVLESVIEQEKRRLGDADLSAVLEHDVFHRSLLACCLEIIIYSYTAV-DSFPFITDLFDVPAFHFYKVIEILIRA 601
Cdd:pfam01858   81 EKLYYKVLESILKSEKKRLPGNDLSSLLSNDIFHRSLLACCLEIVLFAYNSErLSFPWILEVFGLPPFDFYKVIESFIRA 160

                          170       180       190
                   ....*....|....*....|....*....|....*
gi 2117983372  602 EDGLCREVVKHLNHIEEQILESLAWKEDSPLWDKI 636
Cdd:pfam01858  161 EDGLPRELVKHLNSIEEQILESLAWKSDSPLWELL 195
RB_B pfam01857
Retinoblastoma-associated protein B domain; The crystal structure of the Rb pocket bound to a ...
 858-1040 1.27e-69

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: 228.60  E-value: 1.27e-69
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117983372  858 SLALFFRKVFHLASVRLRDLCLKLDIPAELRKKIWTCFEFSLAQCSELMMGRHLDQLLMCAIYVISKVTEEDTSFQNIMR 937
Cdd:pfam01857    1 SLNLFFRKVYHLAAVRLQDLCSRLDLSSDLREKIWTCFEHSLVHQTDLMKDRHLDQILLCAIYVICKVTKEELTFKEIMK 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117983372  938 CYRTQPQAKSHVYRSVLIKGRRRRHSGSGNsnqqrnsptdrnrdrtsrdsspvmrssstlpvpqpssapptptrlagans 1017
Cdd:pfam01857   81 CYRKQPQASSHVYRSVLIRRRERERNGKNN-------------------------------------------------- 110

                          170       180
                   ....*....|....*....|...
gi 2117983372 1018 diEEEERGDLIQFYNNVYTDRIK 1040
Cdd:pfam01857  111 --EEEERGDIIKFYNKVFVPAMK 131
DUF3452 pfam11934
Domain of unknown function (DUF3452); This presumed domain is functionally uncharacterized. ...
 133-266 1.46e-55

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: 188.96  E-value: 1.46e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117983372  133 GTVEGNYVSLIRILRCSGQSLIEFFNKMKKWEDMANLPSQFRERTTRLERNFTVSAVIFKKYEPIFQDIFKYPQDDqpRQ 212
Cdd:pfam11934    2 GTVEGNCVSLTRLLRACKLSIIDFFKKMKQWADMANLDWEFRLEIKELERNFSVTTVLFKKYKRIFNELFLSPPPK--EP 79

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2117983372  213 QRGRKQRRQPCTVSEVFQFCWVLFVYAKGNFPMISDDLVNAYHLLLCVLDLVFA 266
Cdd:pfam11934   80 KRSKKSRPAPCSYSDLFEFGWLLFLAAKNEFPSISKDLVTSYHLLLCCLDLVYV 133
CYCLIN smart00385
domain present in cyclins, TFIIB and Retinoblastoma; A helical domain present in cyclins and ...
 872-940 6.34e-06

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: 45.28  E-value: 6.34e-06
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2117983372   872 VRLRDLCLKLDIPAELRKKIWTCFEFSLAQCSelMMGRHLDQLLMCAIYVISKVTEEDTSFQNIMRCYR 940
Cdd:smart00385    1 DFLRRVCKALNLDPETLNLAVNLLDRFLSDYK--FLKYSPSLIAAAALYLASKTEETPPWTKELVHYTG 67
SP1-4_arthropods_N cd22553
N-terminal domain of transcription factor Specificity Protein (SP) 1-4 from arthropods; ...
 730-846 5.55e-05

N-terminal domain of transcription factor Specificity Protein (SP) 1-4 from arthropods; Specificity Proteins (SPs) are transcription factors that are involved in many cellular processes, including cell differentiation, cell growth, apoptosis, immune responses, response to DNA damage, and chromatin remodeling. There are many SPs in vertebrates (9 SPs in humans and mice, 7 SPs in the chicken, and 11 SPs in teleost fish), but arthropods only have 3 SPs. One SP is clade SP1-4, which is expressed ubiquitously throughout development. SP1-4 belongs to a family of proteins, called the SP/Kruppel or Krueppel-like Factor (KLF) family, characterized by a C-terminal DNA-binding domain of 81 amino acids consisting of three Kruppel-like C2H2 zinc fingers. These factors bind to a loose consensus motif, namely NNRCRCCYY (where N is any nucleotide; R is A/G, and Y is C/T), such as the recurring motifs in GC and GT boxes (5'-GGGGCGGGG-3' and 5-GGTGTGGGG-3') that are present in promoters and more distal regulatory elements of mammalian genes. SP factors preferentially bind GC boxes, while KLFs bind CACCC boxes. Another characteristic hallmark of SP factors is the presence of the Buttonhead (BTD) box CXCPXC, just N-terminal to the zinc fingers. The function of the BTD box is unknown, but it is thought to play an important physiological role. Another feature of most SP factors is the presence of a conserved amino acid stretch, the so-called SP box, located close to the N-terminus. This model represents the N-terminal domain of SP1-4 from arthropods.


Pssm-ID: 411778 [Multi-domain]  Cd Length: 384  Bit Score: 46.94  E-value: 5.55e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117983372  730 QPVISPMPVQNVS-PETIPVTPVPGQTLVtvatatvtanngQTVTIPVQGIANENGGITFIPVQVNVSGQ-AQPlsTSIQ 807
Cdd:cd22553    145 NAVQLPLNNMTQTiPVQVPVSTANGQTVY------------QTIQVPIQAIQSGNAGGGNQALQAQVIPQlAQA--AQLQ 210

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 2117983372  808 PlsaQSLAgalsspQVAGtalqlQGQFQQIALPGEQQRQ 846
Cdd:cd22553    211 P---QQLA------QVSS-----QGYIQQIPANASQQQP 235
PHA03253 PHA03253
UL35; Provisional
 977-1107 9.67e-03

UL35; Provisional


Pssm-ID: 223025  Cd Length: 609  Bit Score: 39.93  E-value: 9.67e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117983372  977 DRNRDRTSRDSSPVmRSSSTLPVPQPSSAPPTPTRLAGANSDIEEEERGDLIQFYN-----NVYTD--RIKDFALKYSST 1049
Cdd:PHA03253   460 NVNEGRSSSRASPS-HSTSTIPYSPPQSGRSTPTSILRQRTPIRSNSRSSSVSFSQgdsnrSHYSDetNISDYSYPMADL 538

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2117983372 1050 NGAEAPPLSPYPFvrsgSPRRIqlSQNHSvyISPHKNESTLSPREKIFYYFSSSPSKR 1107
Cdd:PHA03253   539 DLEDEEPMEDHPH----SPQSI--SSNNS--MSRTSRALQNSQRRRPPTMFPSSSERQ 588
 
Name Accession Description Interval E-value
CYCLIN_RBL2 cd20606
cyclin box found in retinoblastoma-like protein 2 (RBL2) and similar proteins; RBL2, also ...
 858-1046 3.29e-120

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: 368.46  E-value: 3.29e-120
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117983372  858 SLALFFRKVFHLASVRLRDLCLKLDIPAELRKKIWTCFEFSLAQCSELMMGRHLDQLLMCAIYVISKVTEEDTSFQNIMR 937
Cdd:cd20606      1 SLSLFFRKVYHLASVRLRDLCAKLDISDELRKKIWTCFEYSLVHCPELMMDRHLDQLLMCAIYVMAKVTKEDKSFQNIMR 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117983372  938 CYRTQPQAKSHVYRSVLIKGRRRRHSGSGNSNQQRNSPTDRNRDRTSRDSSPVMRSSSTLPVPQPSSAPPTPTRLAGANS 1017
Cdd:cd20606     81 CYRTQPQASSSVYRSVLIKGRRRRRSGSSDDSGSQSSSSEENRERTSRDSSPVMRSSSTLPVPQPNSAPPTPTRLTGANS 160

                          170       180
                   ....*....|....*....|....*....
gi 2117983372 1018 DIEEEERGDLIQFYNNVYTDRIKDFALKY 1046
Cdd:cd20606    161 DMEEEERGDLIQFYNNIYIEQIKEFALKY 189
RB_A pfam01858
Retinoblastoma-associated protein A domain; This domain has the cyclin fold as predicted.
 445-636 1.99e-97

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


Pssm-ID: 460364  Cd Length: 195  Bit Score: 307.59  E-value: 1.99e-97
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117983372  445 SPISIATYSLTRLHTMLTGLKNAPSENLEQILRSCSRDPSVSIASRVKEMYEIYCKK--TQSDGEPGSVKDIAGKHFRLA 522
Cdd:pfam01858    1 TPVSSAMQTVSWLQTLLSGLSDEPSEKLLRIFKSCSRDPTETILKRVKELGEIFCQKytEASGEHPSFCIEIAEQRFRLA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117983372  523 EVLYYKVLESVIEQEKRRLGDADLSAVLEHDVFHRSLLACCLEIIIYSYTAV-DSFPFITDLFDVPAFHFYKVIEILIRA 601
Cdd:pfam01858   81 EKLYYKVLESILKSEKKRLPGNDLSSLLSNDIFHRSLLACCLEIVLFAYNSErLSFPWILEVFGLPPFDFYKVIESFIRA 160

                          170       180       190
                   ....*....|....*....|....*....|....*
gi 2117983372  602 EDGLCREVVKHLNHIEEQILESLAWKEDSPLWDKI 636
Cdd:pfam01858  161 EDGLPRELVKHLNSIEEQILESLAWKSDSPLWELL 195
RB_B pfam01857
Retinoblastoma-associated protein B domain; The crystal structure of the Rb pocket bound to a ...
 858-1040 1.27e-69

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: 228.60  E-value: 1.27e-69
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117983372  858 SLALFFRKVFHLASVRLRDLCLKLDIPAELRKKIWTCFEFSLAQCSELMMGRHLDQLLMCAIYVISKVTEEDTSFQNIMR 937
Cdd:pfam01857    1 SLNLFFRKVYHLAAVRLQDLCSRLDLSSDLREKIWTCFEHSLVHQTDLMKDRHLDQILLCAIYVICKVTKEELTFKEIMK 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117983372  938 CYRTQPQAKSHVYRSVLIKGRRRRHSGSGNsnqqrnsptdrnrdrtsrdsspvmrssstlpvpqpssapptptrlagans 1017
Cdd:pfam01857   81 CYRKQPQASSHVYRSVLIRRRERERNGKNN-------------------------------------------------- 110

                          170       180
                   ....*....|....*....|...
gi 2117983372 1018 diEEEERGDLIQFYNNVYTDRIK 1040
Cdd:pfam01857  111 --EEEERGDIIKFYNKVFVPAMK 131
CYCLIN_RBL1 cd20605
cyclin box found in retinoblastoma-like protein 1 (RBL1) and similar proteins; RBL1, also ...
 852-1046 6.48e-65

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: 215.52  E-value: 6.48e-65
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117983372  852 RPRRAGSLALFFRKVFHLASVRLRDLCLKLDIPAELRKKIWTCFEFSLAQCSELMMGRHLDQLLMCAIYVISKVTEEDTS 931
Cdd:cd20605      1 KPKKTGSLALFYRKVYHLASVRLRDLCLKLDVSNELRRKIWTCFEFSLVHCTDLMKDRHLDQLLLCAFYIMAKVTKEERT 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117983372  932 FQNIMRCYRTQPQAKSHVYRSVLIKgrrrrhsgsgnsnqqrnsptdrnrdrtsrdsspvmrssstlpvpqpssapptptr 1011
Cdd:cd20605     81 FQDIMKCYRNQPQANSHVYRSVLLK------------------------------------------------------- 105

                          170       180       190
                   ....*....|....*....|....*....|....*
gi 2117983372 1012 lagansdieeEERGDLIQFYNNVYTDRIKDFALKY 1046
Cdd:cd20605    106 ----------EERGDLIKFYNTIYVGRVKSFALKY 130
CYCLIN_RBL cd20600
cyclin box found in retinoblastoma-like protein (RBL) subfamily; The RBL subfamily includes ...
 858-1046 5.96e-61

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: 203.40  E-value: 5.96e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117983372  858 SLALFFRKVFHLASVRLRDLCLKLDIPAELRKKIWTCFEFSLAQCSELMMGRHLDQLLMCAIYVISKVTEEDTSFQNIMR 937
Cdd:cd20600      1 SLGLFFRKVYHLASVRLRDLCEKLEISEELRRKIWTCFEHSLVHHIELMRDRHLDQLLMCAVYVIAKVTKQDKSFQEIMK 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117983372  938 CYRTQPQAKShvyrsvlikgrrrrhsgsgnsnqqrnsptdrnrdrtsrdsspvmrssstlpvpqpssapptptrlagans 1017
Cdd:cd20600     81 CYRLQPQAQS---------------------------------------------------------------------- 90

                          170       180
                   ....*....|....*....|....*....
gi 2117983372 1018 dieeeerGDLIQFYNNVYTDRIKDFALKY 1046
Cdd:cd20600     91 -------GDLIQFYNSVYVKKMKEFALKF 112
DUF3452 pfam11934
Domain of unknown function (DUF3452); This presumed domain is functionally uncharacterized. ...
 133-266 1.46e-55

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: 188.96  E-value: 1.46e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117983372  133 GTVEGNYVSLIRILRCSGQSLIEFFNKMKKWEDMANLPSQFRERTTRLERNFTVSAVIFKKYEPIFQDIFKYPQDDqpRQ 212
Cdd:pfam11934    2 GTVEGNCVSLTRLLRACKLSIIDFFKKMKQWADMANLDWEFRLEIKELERNFSVTTVLFKKYKRIFNELFLSPPPK--EP 79

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2117983372  213 QRGRKQRRQPCTVSEVFQFCWVLFVYAKGNFPMISDDLVNAYHLLLCVLDLVFA 266
Cdd:pfam11934   80 KRSKKSRPAPCSYSDLFEFGWLLFLAAKNEFPSISKDLVTSYHLLLCCLDLVYV 133
CYCLIN_RB cd20599
cyclin box found in retinoblastoma-associated protein (RB) and similar proteins; RB, also ...
 858-957 1.51e-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: 131.26  E-value: 1.51e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117983372  858 SLALFFRKVFHLASVRLRDLCLKLDIPAELRKKIWTCFEFSLAQCSELMMGRHLDQLLMCAIYVISKVTEEDTSFQNIMR 937
Cdd:cd20599      2 SLSLFYKKVYRLAYLRLNTLCDLLLLHPDLEHRIWTCFEHCLQNRYELLKDRHLDQIMMCSMYGICKVKNKDLRFKTIVT 81

                           90       100
                   ....*....|....*....|
gi 2117983372  938 CYRTQPQAKSHVYRSVLIKG 957
Cdd:cd20599     82 AYKDLPHASQEVYKRVLIRG 101
CYCLIN_RB-like cd20548
cyclin box found in retinoblastoma-associated protein (RB) family; The RB family includes ...
 859-1035 3.99e-35

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: 130.12  E-value: 3.99e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117983372  859 LALFFRKVFHLASVRLRDLCLKLD-IPAELRKKIWTCFEFSLAQCSELMMGRHLDQLLMCAIYVISKVTEEDTSFQNIMR 937
Cdd:cd20548      1 LQLFFRKLYRLAAARLQDLCKRLDlLSPPLRERIWTVFKHILSEETELLFDRHLDQIILCSIYAVCKVNNENLTFKEILD 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117983372  938 CYRTQPQAKSHVYRSVLIKGrrrrhsgsgnsnqqrnsptdrnRDRTSRDsspvmrssstlpvpqpssapptptrlagans 1017
Cdd:cd20548     81 AYRKQPQAESEVYRSVLPLF----------------------RSVGSDD------------------------------- 107

                          170
                   ....*....|....*...
gi 2117983372 1018 dieEEERGDLIQFYNNVY 1035
Cdd:cd20548    108 ---EGESGDIIKFYNQVF 122
CYCLIN_AtRBR_like cd20601
cyclin box found in Arabidopsis thaliana retinoblastoma-related protein 1 (AtRBR1) and similar ...
 859-1044 2.88e-28

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: 110.56  E-value: 2.88e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117983372  859 LALFFRKVFHLASVRLRDLCLKLDIPAELRKKIWTCFEFSLAQCSELMMGRHLDQLLMCAIYVISKVTEEDTSFQNIMRC 938
Cdd:cd20601      1 INVFFQKVLKLAAIRIADLCERLQQPQLVVEQVYRLIEHVLYEQTGLFFNRHIDQIILCCLYGVCKVHKLNVTFREIIYQ 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117983372  939 YRTQPQAKSHVYRSVLIKGRRRRHSGSgnsnqqrnsptdrnrdrtsrdsspvmrssstlpvpqpssapptptrlagansd 1018
Cdd:cd20601     81 YRKQPQCKPDVFRNVVIEQRRPTLGGP----------------------------------------------------- 107

                          170       180
                   ....*....|....*....|....*.
gi 2117983372 1019 ieeeERGDLIQFYNNVYTDRIKDFAL 1044
Cdd:cd20601    108 ----DHGDIIAFYNEVFVPATKPFLL 129
CYCLIN smart00385
domain present in cyclins, TFIIB and Retinoblastoma; A helical domain present in cyclins and ...
 872-940 6.34e-06

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: 45.28  E-value: 6.34e-06
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2117983372   872 VRLRDLCLKLDIPAELRKKIWTCFEFSLAQCSelMMGRHLDQLLMCAIYVISKVTEEDTSFQNIMRCYR 940
Cdd:smart00385    1 DFLRRVCKALNLDPETLNLAVNLLDRFLSDYK--FLKYSPSLIAAAALYLASKTEETPPWTKELVHYTG 67
SP1-4_arthropods_N cd22553
N-terminal domain of transcription factor Specificity Protein (SP) 1-4 from arthropods; ...
 730-846 5.55e-05

N-terminal domain of transcription factor Specificity Protein (SP) 1-4 from arthropods; Specificity Proteins (SPs) are transcription factors that are involved in many cellular processes, including cell differentiation, cell growth, apoptosis, immune responses, response to DNA damage, and chromatin remodeling. There are many SPs in vertebrates (9 SPs in humans and mice, 7 SPs in the chicken, and 11 SPs in teleost fish), but arthropods only have 3 SPs. One SP is clade SP1-4, which is expressed ubiquitously throughout development. SP1-4 belongs to a family of proteins, called the SP/Kruppel or Krueppel-like Factor (KLF) family, characterized by a C-terminal DNA-binding domain of 81 amino acids consisting of three Kruppel-like C2H2 zinc fingers. These factors bind to a loose consensus motif, namely NNRCRCCYY (where N is any nucleotide; R is A/G, and Y is C/T), such as the recurring motifs in GC and GT boxes (5'-GGGGCGGGG-3' and 5-GGTGTGGGG-3') that are present in promoters and more distal regulatory elements of mammalian genes. SP factors preferentially bind GC boxes, while KLFs bind CACCC boxes. Another characteristic hallmark of SP factors is the presence of the Buttonhead (BTD) box CXCPXC, just N-terminal to the zinc fingers. The function of the BTD box is unknown, but it is thought to play an important physiological role. Another feature of most SP factors is the presence of a conserved amino acid stretch, the so-called SP box, located close to the N-terminus. This model represents the N-terminal domain of SP1-4 from arthropods.


Pssm-ID: 411778 [Multi-domain]  Cd Length: 384  Bit Score: 46.94  E-value: 5.55e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117983372  730 QPVISPMPVQNVS-PETIPVTPVPGQTLVtvatatvtanngQTVTIPVQGIANENGGITFIPVQVNVSGQ-AQPlsTSIQ 807
Cdd:cd22553    145 NAVQLPLNNMTQTiPVQVPVSTANGQTVY------------QTIQVPIQAIQSGNAGGGNQALQAQVIPQlAQA--AQLQ 210

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 2117983372  808 PlsaQSLAgalsspQVAGtalqlQGQFQQIALPGEQQRQ 846
Cdd:cd22553    211 P---QQLA------QVSS-----QGYIQQIPANASQQQP 235
CYCLIN_SF cd00043
Cyclin box fold superfamily; The cyclin box is a protein binding domain that functions in ...
 873-944 4.19e-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: 4.19e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2117983372  873 RLRDLCLKLDIPAELRKKIWTCFEfsLAQCSELMMGRHLDQLLMCAIYVISKVTEEDTSFQNIMRCYRTQPQ 944
Cdd:cd00043      5 FIRRLCSKLGLPEEVLELAIELLD--RFLSKGLLLGRSPELIAAACLYLACKLEELPRTLKEIAKVSGVSEK 74
PHA03253 PHA03253
UL35; Provisional
 977-1107 9.67e-03

UL35; Provisional


Pssm-ID: 223025  Cd Length: 609  Bit Score: 39.93  E-value: 9.67e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117983372  977 DRNRDRTSRDSSPVmRSSSTLPVPQPSSAPPTPTRLAGANSDIEEEERGDLIQFYN-----NVYTD--RIKDFALKYSST 1049
Cdd:PHA03253   460 NVNEGRSSSRASPS-HSTSTIPYSPPQSGRSTPTSILRQRTPIRSNSRSSSVSFSQgdsnrSHYSDetNISDYSYPMADL 538

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2117983372 1050 NGAEAPPLSPYPFvrsgSPRRIqlSQNHSvyISPHKNESTLSPREKIFYYFSSSPSKR 1107
Cdd:PHA03253   539 DLEDEEPMEDHPH----SPQSI--SSNNS--MSRTSRALQNSQRRRPPTMFPSSSERQ 588
 
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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