Zinc-finger double domain;

                          10        20
                  ....*....|....*....|....*
gi 1907152597 231 LKTHVRTHTGERPYKCELCDKGFAQ 255
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 26

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152597 240 GERPYKCEL--CDKGFAQKCQLVFHsrMHHGEekpykcdvCNLQFATSSNLKIHARKHSGEKPYVCDRCGQRFAQASTLT 317
Cdd:COG5189   346 DGKPYKCPVegCNKKYKNQNGLKYH--MLHGH--------QNQKLHENPSPEKMNIFSAKDKPYRCEVCDKRYKNLNGLK 415

                  ....*..
gi 1907152597 318 YHvRRHT 324
Cdd:COG5189   416 YH-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 1907152597 357 YICGICGKSFISSGELNKHFRSH 379
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23

Zinc-finger double domain;

                          10        20
                  ....*....|....*....|....*
gi 1907152597 231 LKTHVRTHTGERPYKCELCDKGFAQ 255
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 26

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152597 240 GERPYKCEL--CDKGFAQKCQLVFHsrMHHGEekpykcdvCNLQFATSSNLKIHARKHSGEKPYVCDRCGQRFAQASTLT 317
Cdd:COG5189   346 DGKPYKCPVegCNKKYKNQNGLKYH--MLHGH--------QNQKLHENPSPEKMNIFSAKDKPYRCEVCDKRYKNLNGLK 415

                  ....*..
gi 1907152597 318 YHvRRHT 324
Cdd:COG5189   416 YH-RKHS 421

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 1907152597 242 RPYkCELCDKGFAQKCQLVFHSRMHHgeekpYKCDVCNLQFATSSNLKIHA 292
Cdd:cd20908     1 KPW-CYYCDREFDDEKILIQHQKAKH-----FKCHICHKKLYTAGGLAVHC 45

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152597 177 EELDARFSKAKPMCNTCGKVFSEASSLRRHMR--IH--KGVKPYVC--HLCGKAFTQCNQLKTHVRTHTGERPYKCELCd 250
Cdd:COG5048   279 DSSSEKGFSLPIKSKQCNISFSRSSPLTRHLRsvNHsgESLKPFSCpySLCGKLFSRNDALKRHILLHTSISPAKEKLL- 357

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152597 251 kgfaqkcqlvfHSRMHHGEEKPYKCDVCNLQFATSSNLKIHARKHSGEKPYvcdrcgqrFAQASTLTYHVRRHTGEKPYV 330
Cdd:COG5048   358 -----------NSSSKFSPLLNNEPPQSLQQYKDLKNDKKSETLSNSCIRN--------FKRDSNLSLHIITHLSFRPYN 418

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1907152597 331 CD--TCGKAFAVSSSLITHSRKHTGEKPYICGICGKSFISSGELNKHF 376
Cdd:COG5048   419 CKnpPCSKSFNRHYNLIPHKKIHTNHAPLLCSILKSFRRDLDLSNHGK 466

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152597 325 GEKPYVCDT--CGKAFAVSSSLITHsRKHtgekpyicGICGKSFISSGELNKHFRSHTGERPFICELCGNSYTDIKNLKK 402
Cdd:COG5189   346 DGKPYKCPVegCNKKYKNQNGLKYH-MLH--------GHQNQKLHENPSPEKMNIFSAKDKPYRCEVCDKRYKNLNGLKY 416

                  ....*.
gi 1907152597 403 HKTKVH 408
Cdd:COG5189   417 HRKHSH 422

Zinc-finger double domain;

                          10        20
                  ....*....|....*....|....*
gi 1907152597 231 LKTHVRTHTGERPYKCELCDKGFAQ 255
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 26

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152597 240 GERPYKCEL--CDKGFAQKCQLVFHsrMHHGEekpykcdvCNLQFATSSNLKIHARKHSGEKPYVCDRCGQRFAQASTLT 317
Cdd:COG5189   346 DGKPYKCPVegCNKKYKNQNGLKYH--MLHGH--------QNQKLHENPSPEKMNIFSAKDKPYRCEVCDKRYKNLNGLK 415

                  ....*..
gi 1907152597 318 YHvRRHT 324
Cdd:COG5189   416 YH-RKHS 421

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 1907152597 242 RPYkCELCDKGFAQKCQLVFHSRMHHgeekpYKCDVCNLQFATSSNLKIHA 292
Cdd:cd20908     1 KPW-CYYCDREFDDEKILIQHQKAKH-----FKCHICHKKLYTAGGLAVHC 45

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 1907152597 190 CNTCGKVFSEASSLRRHMRIH 210
Cdd:pfam00096   3 CPDCGKSFSRKSNLKRHLRTH 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 1907152597 357 YICGICGKSFISSGELNKHFRSH 379
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23

Zinc-finger double domain;

                          10        20
                  ....*....|....*....|....*.
gi 1907152597 343 SLITHSRKHTGEKPYICGICGKSFIS 368
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 1907152597 273 YKCDVCNLQFATSSNLKIHARKH 295
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23