Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division and chromosome partitioning];

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500286824  60 GERPYPCP--DCPKAFKNSSSLRRHR-HVHtgerpytcgiCGKSFTQSTNLRQHQRVHTGERPFRCPLCPKTFThSSNLL 136
Cdd:COG5189   346 DGKPYKCPveGCNKKYKNQNGLKYHMlHGH----------QNQKLHENPSPEKMNIFSAKDKPYRCEVCDKRYK-NLNGL 414

                  ....*.
gi 2500286824 137 LHHRTH 142
Cdd:COG5189   415 KYHRKH 420

Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division and chromosome partitioning];

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500286824  60 GERPYPCP--DCPKAFKNSSSLRRHR-HVHtgerpytcgiCGKSFTQSTNLRQHQRVHTGERPFRCPLCPKTFThSSNLL 136
Cdd:COG5189   346 DGKPYKCPveGCNKKYKNQNGLKYHMlHGH----------QNQKLHENPSPEKMNIFSAKDKPYRCEVCDKRYK-NLNGL 414

                  ....*.
gi 2500286824 137 LHHRTH 142
Cdd:COG5189   415 KYHRKH 420

Zinc-finger double domain;

                          10        20
                  ....*....|....*....|....*.
gi 2500286824 106 NLRQHQRVHTGERPFRCPLCPKTFTH 131
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26

N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), Arabidopsis thaliana SUF4 (AtSUF4), and similar proteins; Oryza sativa SUPPRESSOR OF FRI 4 (OsSUF4) is a C2H2-type zinc finger transcription factor which interacts with the major H3K36 methyltransferase SDG725 to promote H3K36me3 (tri-methylation at H3K9) establishment. The transcription factor OsSUF4 recognizes a specific 7-bp DNA element (5'-CGGAAAT-3'), which is contained in the promoter regions of many genes throughout the rice genome. Through interaction with OsSUF4, SDG725 is recruited to the promoters of key florigen genes, RICE FLOWERING LOCUS T1 (RFT1) and Heading date 3a (Hd3a), for H3K36 deposition to promote gene activation and rice plant flowering. OsSUF4 target genes include a number of genes involved in many biological processes. Flowering plant Arabidopsis SUF4 binds to a 15bp DNA element (5'-CCAAATTTTAAGTTT-3') within the promoter of the floral repressor gene FLOWERING LOCUS C (FLC) and recruits the FRI-C transcription activator complex to the FLC promoter. Although the DNA-binding element and target genes of AtSUF4 are different from those of OsSUF4, AtSUF4 is known to interact with the Arabidopsis H3K36 methyltransferase SDG8 (also known as ASHH2/EFS/SET8), and the methylation deposition mechanism mediated by the SUF4 transcription factor and H3K36 methyltransferase may be conserved in Arabidopsis and rice. Proteins in this family have two conserved C2H2-type zinc finger motifs at the N-terminus (included in this model), and a large proline-rich domain at the C-terminus; for OsSUF4, it has been shown that the N-terminal zinc-finger domain is responsible for DNA binding, and that the C-terminal domain interacts with SDG725.

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 2500286824 478 CSVCGKSFAQTSNLRQHQRVHTgerpFRCPLCPKTFTHSSNLLLH-QRTH 526
Cdd:cd20908     4 CYYCDREFDDEKILIQHQKAKH----FKCHICHKKLYTAGGLAVHcLQVH 49

FOG: Zn-finger [General function prediction only];

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500286824 399 KAFKRSSLLAIHQRVHTGLRA-FTCGQCGLTFKWSSHYQYHLR--LHSGE--RPYACTE--CGKAFRNTSCLRRHRHVHT 471
Cdd:COG5048   268 ASSQSSSPNESDSSSEKGFSLpIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCPYslCGKLFSRNDALKRHILLHT 347

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500286824 472 GERPHSC--SVCGKSFAQTSNLRQHQRVH-----TGERPFRCPL--CPKTFTHSSNLLLHQRTHSAERP--FACPICGRG 540
Cdd:COG5048   348 SISPAKEklLNSSSKFSPLLNNEPPQSLQqykdlKNDKKSETLSnsCIRNFKRDSNLSLHIITHLSFRPynCKNPPCSKS 427

                         170
                  ....*....|....*
gi 2500286824 541 FVMAAYLQRHLRTHT 555
Cdd:COG5048   428 FNRHYNLIPHKKIHT 442

FOG: Zn-finger [General function prediction only];

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500286824  45 FKWSSHYQYHLRQHTGER-PYPCPDCPKAFKNSSSLRRHR--HVHTGE--RPYTCGI--CGKSFTQSTNLRQHQRVHTGE 117
Cdd:COG5048   270 SQSSSPNESDSSSEKGFSlPIKSKQCNISFSRSSPLTRHLrsVNHSGEslKPFSCPYslCGKLFSRNDALKRHILLHTSI 349

                          90
                  ....*....|....*...
gi 2500286824 118 RPFRCPLCPKTFTHSSNL 135
Cdd:COG5048   350 SPAKEKLLNSSSKFSPLL 367

Zinc-finger double domain;

                          10        20
                  ....*....|....*....|....*.
gi 2500286824 106 NLRQHQRVHTGERPFRCPLCPKTFTH 131
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26

Zinc-finger double domain;

                          10        20
                  ....*....|....*....|....*.
gi 2500286824  50 HYQYHLRQHTGERPYPCPDCPKAFKN 75
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26

Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two conserved cysteines and histidines co-ordinate a zinc ion. The following pattern describes the zinc finger. #-X-C-X(1-5)-C-X3-#-X5-#-X2-H-X(3-6)-[H/C] Where X can be any amino acid, and numbers in brackets indicate the number of residues. The positions marked # are those that are important for the stable fold of the zinc finger. The final position can be either his or cys. The C2H2 zinc finger is composed of two short beta strands followed by an alpha helix. The amino terminal part of the helix binds the major groove in DNA binding zinc fingers. The accepted consensus binding sequence for Sp1 is usually defined by the asymmetric hexanucleotide core GGGCGG but this sequence does not include, among others, the GAG (=CTC) repeat that constitutes a high-affinity site for Sp1 binding to the wt1 promoter.

                          10        20
                  ....*....|....*....|...
gi 2500286824  92 YTCGICGKSFTQSTNLRQHQRVH 114
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23

Zinc-finger double domain;

                          10        20
                  ....*....|....*....|....*
gi 2500286824 463 LRRHRHVHTGERPHSCSVCGKSFAQ 487
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 26

FOG: Zn-finger [General function prediction only];

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500286824  65 PCPDCPKAFKNSSSLRRHRHVHTGER-------PYTCGICGKSFTQSTNLRQHQR--VHTGE--RPFRCP--LCPKTFTH 131
Cdd:COG5048   256 SASESPRSSLPTASSQSSSPNESDSSsekgfslPIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCPysLCGKLFSR 335

                          90
                  ....*....|.
gi 2500286824 132 SSNLLLHHRTH 142
Cdd:COG5048   336 NDALKRHILLH 346

Zinc-finger double domain;

                          10        20
                  ....*....|....*....|....*.
gi 2500286824 434 HYQYHLRLHSGERPYACTECGKAFRN 459
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26

Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two conserved cysteines and histidines co-ordinate a zinc ion. The following pattern describes the zinc finger. #-X-C-X(1-5)-C-X3-#-X5-#-X2-H-X(3-6)-[H/C] Where X can be any amino acid, and numbers in brackets indicate the number of residues. The positions marked # are those that are important for the stable fold of the zinc finger. The final position can be either his or cys. The C2H2 zinc finger is composed of two short beta strands followed by an alpha helix. The amino terminal part of the helix binds the major groove in DNA binding zinc fingers. The accepted consensus binding sequence for Sp1 is usually defined by the asymmetric hexanucleotide core GGGCGG but this sequence does not include, among others, the GAG (=CTC) repeat that constitutes a high-affinity site for Sp1 binding to the wt1 promoter.

                          10        20
                  ....*....|....*....|...
gi 2500286824 392 YQCGECGKAFKRSSLLAIHQRVH 414
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23

Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two conserved cysteines and histidines co-ordinate a zinc ion. The following pattern describes the zinc finger. #-X-C-X(1-5)-C-X3-#-X5-#-X2-H-X(3-6)-[H/C] Where X can be any amino acid, and numbers in brackets indicate the number of residues. The positions marked # are those that are important for the stable fold of the zinc finger. The final position can be either his or cys. The C2H2 zinc finger is composed of two short beta strands followed by an alpha helix. The amino terminal part of the helix binds the major groove in DNA binding zinc fingers. The accepted consensus binding sequence for Sp1 is usually defined by the asymmetric hexanucleotide core GGGCGG but this sequence does not include, among others, the GAG (=CTC) repeat that constitutes a high-affinity site for Sp1 binding to the wt1 promoter.

                          10        20
                  ....*....|....*....|...
gi 2500286824  64 YPCPDCPKAFKNSSSLRRHRHVH 86
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23

FOG: Zn-finger [General function prediction only];

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500286824  41 CGLAFKWSSHYQYHLRQHTGERPYPC-------------------------------------PDCPKAFKNSSSLRRHR 83
Cdd:COG5048   329 CGKLFSRNDALKRHILLHTSISPAKEkllnssskfspllnneppqslqqykdlkndkksetlsNSCIRNFKRDSNLSLHI 408

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2500286824  84 HVHTGERPY--TCGICGKSFTQSTNLRQHQRVHTGERPFRCplCPKTFTHSSNLLLHH 139
Cdd:COG5048   409 ITHLSFRPYncKNPPCSKSFNRHYNLIPHKKIHTNHAPLLC--SILKSFRRDLDLSNH 464

FOG: Zn-finger [General function prediction only];

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500286824 359 SAERPYKCAECGKAFKGSSGLRYHLRDHTGERPYQCG--ECGKAFKRSSLLAIHQR-VHTGLRAFTCGQCGLTFKWSSHY 435
Cdd:COG5048    29 NAPRPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSysGCDKSFSRPLELSRHLRtHHNNPSDLNSKSLPLSNSKASSS 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500286824 436 QYHLRLHSGERPYACTECGKAFRNTSCLRRHRHVHTGERPHSCSVCGKSFAQTSN-------LRQHQRVHTGERPFRCPL 508
Cdd:COG5048   109 SLSSSSSNSNDNNLLSSHSLPPSSRDPQLPDLLSISNLRNNPLPGNNSSSVNTPQsnslhppLPANSLSKDPSSNLSLLI 188

                         170       180
                  ....*....|....*....|.
gi 2500286824 509 C----PKTFTHSSNLLLHQRT 525
Cdd:COG5048   189 SsnvsTSIPSSSENSPLSSSY 209

Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division and chromosome partitioning];

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2500286824 361 ERPYKCA--ECGKAFKGSSGLRYH-LRDHTG------------------ERPYQCGECGKAFKRSSLLAIHqRVHT 415
Cdd:COG5189   347 GKPYKCPveGCNKKYKNQNGLKYHmLHGHQNqklhenpspekmnifsakDKPYRCEVCDKRYKNLNGLKYH-RKHS 421

Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two conserved cysteines and histidines co-ordinate a zinc ion. The following pattern describes the zinc finger. #-X-C-X(1-5)-C-X3-#-X5-#-X2-H-X(3-6)-[H/C] Where X can be any amino acid, and numbers in brackets indicate the number of residues. The positions marked # are those that are important for the stable fold of the zinc finger. The final position can be either his or cys. The C2H2 zinc finger is composed of two short beta strands followed by an alpha helix. The amino terminal part of the helix binds the major groove in DNA binding zinc fingers. The accepted consensus binding sequence for Sp1 is usually defined by the asymmetric hexanucleotide core GGGCGG but this sequence does not include, among others, the GAG (=CTC) repeat that constitutes a high-affinity site for Sp1 binding to the wt1 promoter.

                          10        20
                  ....*....|....*....|...
gi 2500286824 532 FACPICGRGFVMAAYLQRHLRTH 554
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23

N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), Arabidopsis thaliana SUF4 (AtSUF4), and similar proteins; Oryza sativa SUPPRESSOR OF FRI 4 (OsSUF4) is a C2H2-type zinc finger transcription factor which interacts with the major H3K36 methyltransferase SDG725 to promote H3K36me3 (tri-methylation at H3K9) establishment. The transcription factor OsSUF4 recognizes a specific 7-bp DNA element (5'-CGGAAAT-3'), which is contained in the promoter regions of many genes throughout the rice genome. Through interaction with OsSUF4, SDG725 is recruited to the promoters of key florigen genes, RICE FLOWERING LOCUS T1 (RFT1) and Heading date 3a (Hd3a), for H3K36 deposition to promote gene activation and rice plant flowering. OsSUF4 target genes include a number of genes involved in many biological processes. Flowering plant Arabidopsis SUF4 binds to a 15bp DNA element (5'-CCAAATTTTAAGTTT-3') within the promoter of the floral repressor gene FLOWERING LOCUS C (FLC) and recruits the FRI-C transcription activator complex to the FLC promoter. Although the DNA-binding element and target genes of AtSUF4 are different from those of OsSUF4, AtSUF4 is known to interact with the Arabidopsis H3K36 methyltransferase SDG8 (also known as ASHH2/EFS/SET8), and the methylation deposition mechanism mediated by the SUF4 transcription factor and H3K36 methyltransferase may be conserved in Arabidopsis and rice. Proteins in this family have two conserved C2H2-type zinc finger motifs at the N-terminus (included in this model), and a large proline-rich domain at the C-terminus; for OsSUF4, it has been shown that the N-terminal zinc-finger domain is responsible for DNA binding, and that the C-terminal domain interacts with SDG725.

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 2500286824 478 CSVCGKSFAQTSNLRQHQRVHTgerpFRCPLCPKTFTHSSNLLLH-QRTH 526
Cdd:cd20908     4 CYYCDREFDDEKILIQHQKAKH----FKCHICHKKLYTAGGLAVHcLQVH 49