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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530537206  788 SLALFFRKVYYLAGVRLRDLCIKLDISDELRKKIWTCFEFSIIQCTELMMDRHLDQLLMCAIYVMAKVTKEDRSFQNIMR 867
Cdd:cd20606     1 SLSLFFRKVYHLASVRLRDLCAKLDISDELRKKIWTCFEYSLVHCPELMMDRHLDQLLMCAIYVMAKVTKEDKSFQNIMR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530537206  868 CYRTQPQARSQVYRSVLIKG-KRRNSGSSESRSHQNSPTELNTDRASRDSSPVMRSNSTLPVPQPSSAPPTPTRLTGASS 946
Cdd:cd20606    81 CYRTQPQASSSVYRSVLIKGrRRRRSGSSDDSGSQSSSSEENRERTSRDSSPVMRSSSTLPVPQPNSAPPTPTRLTGANS 160

                         170       180
                  ....*....|....*....|....*....
gi 530537206  947 DVEEEERGDLIQFYNNIYRKQIQAFAMKY 975
Cdd:cd20606   161 DMEEEERGDLIQFYNNIYIEQIKEFALKY 189

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.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530537206   101 KGTAEGNYVSLTRILRCSEQSLIEFFNKMKKWEDMANLPPHFRERTERLERNFTVSAVIFKKYEPIFQDIFKYPQEEqpR 180
Cdd:pfam11934    1 DGTVEGNCVSLTRLLRACKLSIIDFFKKMKQWADMANLDWEFRLEIKELERNFSVTTVLFKKYKRIFNELFLSPPPK--E 78

                           90       100       110
                   ....*....|....*....|....*....|
gi 530537206   181 QQRGRKQRRQPCTTSEIFHFCWVLFIYAKG 210
Cdd:pfam11934   79 PKRSKKSRPAPCSYSDLFEFGWLLFLAAKN 108

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530537206   41 QIQQRFEELCSRLNMDEAARAEAWSSYRSMSESYTLEGNDLHWLACA-LYVACRKsvptvskgtaEGNYVSLTRILRCSE 119
Cdd:cd00043     1 KAVDFIRRLCSKLGLPEEVLELAIELLDRFLSKGLLLGRSPELIAAAcLYLACKL----------EELPRTLKEIAKVSG 70

                          90
                  ....*....|..
gi 530537206  120 QSLIEFFNKMKK 131
Cdd:cd00043    71 VSEKELRKAEKE 82

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530537206  788 SLALFFRKVYYLAGVRLRDLCIKLDISDELRKKIWTCFEFSIIQCTELMMDRHLDQLLMCAIYVMAKVTKEDRSFQNIMR 867
Cdd:cd20606     1 SLSLFFRKVYHLASVRLRDLCAKLDISDELRKKIWTCFEYSLVHCPELMMDRHLDQLLMCAIYVMAKVTKEDKSFQNIMR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530537206  868 CYRTQPQARSQVYRSVLIKG-KRRNSGSSESRSHQNSPTELNTDRASRDSSPVMRSNSTLPVPQPSSAPPTPTRLTGASS 946
Cdd:cd20606    81 CYRTQPQASSSVYRSVLIKGrRRRRSGSSDDSGSQSSSSEENRERTSRDSSPVMRSSSTLPVPQPNSAPPTPTRLTGANS 160

                         170       180
                  ....*....|....*....|....*....
gi 530537206  947 DVEEEERGDLIQFYNNIYRKQIQAFAMKY 975
Cdd:cd20606   161 DMEEEERGDLIQFYNNIYIEQIKEFALKY 189

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.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530537206   788 SLALFFRKVYYLAGVRLRDLCIKLDISDELRKKIWTCFEFSIIQCTELMMDRHLDQLLMCAIYVMAKVTKEDRSFQNIMR 867
Cdd:pfam01857    1 SLNLFFRKVYHLAAVRLQDLCSRLDLSSDLREKIWTCFEHSLVHQTDLMKDRHLDQILLCAIYVICKVTKEELTFKEIMK 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530537206   868 CYRTQPQARSQVYRSVLIKGKRRNSGSSESrshqnsptelntdrasrdsspvmrsnstlpvpqpssapptptrltgassd 947
Cdd:pfam01857   81 CYRKQPQASSHVYRSVLIRRRERERNGKNN-------------------------------------------------- 110

                          170       180
                   ....*....|....*....|..
gi 530537206   948 vEEEERGDLIQFYNNIYRKQIQ 969
Cdd:pfam01857  111 -EEEERGDIIKFYNKVFVPAMK 131

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530537206  653 PQPLVNAVPVQNVPGETVS-----VTPVPGQTLVTMATATVTANNGQTV--TI--PVQGIANENGGITFFPVQVNVGGQA 723
Cdd:cd22553   124 VQGQANASNVLQNIAQIASggnavQLPLNNMTQTIPVQVPVSTANGQTVyqTIqvPIQAIQSGNAGGGNQALQAQVIPQL 203

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530537206  724 qAVAGSIQPlsaQALAgSLSSQqvtGTTLQVPGPVA-----IQQISPGGQQQNPGQPLTSSSIRPRKTSS 788
Cdd:cd22553   204 -AQAAQLQP---QQLA-QVSSQ---GYIQQIPANASqqqpqMVQQGPNQSGQIIGQVASASSIQAAAIPL 265

transcriptional regulator ICP4; Provisional

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530537206  887 GKR-RNSGSSESRSHQNSPTELNTDRASRDSSpvMRSNSTLPVPQPSSAPPTPTRLTGASSDVEEeergdliqfynnIYR 965
Cdd:PHA03309 1562 GKRpRSSSSSSSASHDRSPSSSSRRRDGRPSS--RRRPSRRMSARPPSRPPAAVILRASWRYAEE------------VAR 1627

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530537206  966 KQIQAFAMKYSQANAQTDTP-------PLSPYPFVRTgSPRRVQLSQSHPIYISPHNNEAMPSPR 1023
Cdd:PHA03309 1628 EMLDAAASRFDEADGEDPLPpaacggkPIAPETLVAL-CEQRGRGPTSLPRAPTPRSGEALAAPR 1691

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530537206  788 SLALFFRKVYYLAGVRLRDLCIKLDISDELRKKIWTCFEFSIIQCTELMMDRHLDQLLMCAIYVMAKVTKEDRSFQNIMR 867
Cdd:cd20606     1 SLSLFFRKVYHLASVRLRDLCAKLDISDELRKKIWTCFEYSLVHCPELMMDRHLDQLLMCAIYVMAKVTKEDKSFQNIMR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530537206  868 CYRTQPQARSQVYRSVLIKG-KRRNSGSSESRSHQNSPTELNTDRASRDSSPVMRSNSTLPVPQPSSAPPTPTRLTGASS 946
Cdd:cd20606    81 CYRTQPQASSSVYRSVLIKGrRRRRSGSSDDSGSQSSSSEENRERTSRDSSPVMRSSSTLPVPQPNSAPPTPTRLTGANS 160

                         170       180
                  ....*....|....*....|....*....
gi 530537206  947 DVEEEERGDLIQFYNNIYRKQIQAFAMKY 975
Cdd:cd20606   161 DMEEEERGDLIQFYNNIYIEQIKEFALKY 189

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.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530537206   788 SLALFFRKVYYLAGVRLRDLCIKLDISDELRKKIWTCFEFSIIQCTELMMDRHLDQLLMCAIYVMAKVTKEDRSFQNIMR 867
Cdd:pfam01857    1 SLNLFFRKVYHLAAVRLQDLCSRLDLSSDLREKIWTCFEHSLVHQTDLMKDRHLDQILLCAIYVICKVTKEELTFKEIMK 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530537206   868 CYRTQPQARSQVYRSVLIKGKRRNSGSSESrshqnsptelntdrasrdsspvmrsnstlpvpqpssapptptrltgassd 947
Cdd:pfam01857   81 CYRKQPQASSHVYRSVLIRRRERERNGKNN-------------------------------------------------- 110

                          170       180
                   ....*....|....*....|..
gi 530537206   948 vEEEERGDLIQFYNNIYRKQIQ 969
Cdd:pfam01857  111 -EEEERGDIIKFYNKVFVPAMK 131

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530537206  788 SLALFFRKVYYLAGVRLRDLCIKLDISDELRKKIWTCFEFSIIQCTELMMDRHLDQLLMCAIYVMAKVTKEDRSFQNIMR 867
Cdd:cd20600     1 SLGLFFRKVYHLASVRLRDLCEKLEISEELRRKIWTCFEHSLVHHIELMRDRHLDQLLMCAVYVIAKVTKQDKSFQEIMK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530537206  868 CYRTQPQARSqvyrsvlikgkrrnsgssesrshqnsptelntdrasrdsspvmrsnstlpvpqpssapptptrltgassd 947
Cdd:cd20600    81 CYRLQPQAQS---------------------------------------------------------------------- 90

                         170       180
                  ....*....|....*....|....*...
gi 530537206  948 veeeerGDLIQFYNNIYRKQIQAFAMKY 975
Cdd:cd20600    91 ------GDLIQFYNSVYVKKMKEFALKF 112

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530537206  788 SLALFFRKVYYLAGVRLRDLCIKLDISDELRKKIWTCFEFSIIQCTELMMDRHLDQLLMCAIYVMAKVTKEDRSFQNIMR 867
Cdd:cd20599     2 SLSLFYKKVYRLAYLRLNTLCDLLLLHPDLEHRIWTCFEHCLQNRYELLKDRHLDQIMMCSMYGICKVKNKDLRFKTIVT 81

                          90       100
                  ....*....|....*....|....*
gi 530537206  868 CYRTQPQARSQVYRSVLIKGKRRNS 892
Cdd:cd20599    82 AYKDLPHASQEVYKRVLIRGEEYDS 106

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530537206  789 LALFFRKVYYLAGVRLRDLCIKLDISDELRKKIWTCFEFSIIQCTELMMDRHLDQLLMCAIYVMAKVTKEDRSFQNIMRC 868
Cdd:cd20601     1 INVFFQKVLKLAAIRIADLCERLQQPQLVVEQVYRLIEHVLYEQTGLFFNRHIDQIILCCLYGVCKVHKLNVTFREIIYQ 80

                          90       100
                  ....*....|....*....|....*...
gi 530537206  869 YRTQPQARSQVYRSVLIKGKRRNSGSSE 896
Cdd:cd20601    81 YRKQPQCKPDVFRNVVIEQRRPTLGGPD 108

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.

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530537206    802 VRLRDLCIKLDISDELRKKIWTCFEFSIIQCTelMMDRHLDQLLMCAIYVMAKVTKEDRSFQNIMRCYRTQPqaRSQVYR 881
Cdd:smart00385    1 DFLRRVCKALNLDPETLNLAVNLLDRFLSDYK--FLKYSPSLIAAAALYLASKTEETPPWTKELVHYTGYFT--EEEILR 76

                    ....
gi 530537206    882 SVLI 885
Cdd:smart00385   77 MERL 80

N-terminal domain of transcription factor Specificity Protein (SP) 2; 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. SP2 contains the least conserved DNA-binding domain within the SP subfamily of proteins, and its DNA sequence specificity differs from the other SP proteins. It localizes primarily within subnuclear foci associated with the nuclear matrix, and can activate, or in some cases, repress expression from different promoters. The transcription factor SP2 serves as a paradigm for indirect genomic binding. It does not require its DNA-binding domain for genomic DNA binding and occupies target promoters independently of whether they contain a cognate DNA-binding motif. SP2 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. 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 SP2.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530537206  642 PSEGSTSGRIPPQPLVNAVPVQNVPG-ETVSVTPVPGQTLVTMATATVTANNGQTVTIPVqgiANENGgITFFPVQVNVG 720
Cdd:cd22540    90 GSQLSSSAPGGQQVFAIQNPTMIIKGsQTRSSTNQQYQISPQIQAAGQINNSGQIQIIPG---TNQAI-ITPVQVLQQPQ 165

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530537206  721 GQAQAVAgsIQPLSAQALAGSLSSQQVTGTTLQVPG--------PVAIQQISPGG--QQQNPGQPLTSSSIRPRKTSSLA 790
Cdd:cd22540   166 QAHKPVP--IKPAPLQTSNTNSASLQVPGNVIKLQSggnvaltlPVNNLVGTQDGatQLQLAAAPSKPSKKIRKKSAQAA 243