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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958652573 364 PYKCAECGKAFKGSSGLRYHLR--DHTGE--RPYQCGE--CGKAFKRSSLLAIHQRVHTGLRAFTC---------GQCGL 428
Cdd:COG5048   289 PIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCPYslCGKLFSRNDALKRHILLHTSISPAKEkllnssskfSPLLN 368

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958652573 429 TFKWSSHYQYHLRLHSgeRPYACT--ECGKAFRNTSCLRRHRHVHTGERPHSCsvcgksfaqtsnlrqhqrvhtgerpfR 506
Cdd:COG5048   369 NEPPQSLQQYKDLKND--KKSETLsnSCIRNFKRDSNLSLHIITHLSFRPYNC--------------------------K 420

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1958652573 507 CPLCPKTFTHSSNLLLHQRTHSAERPFACPICGRgFVMAAYLQRHLR 553
Cdd:COG5048   421 NPPCSKSFNRHYNLIPHKKIHTNHAPLLCSILKS-FRRDLDLSNHGK 466

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958652573 364 PYKCAECGKAFKGSSGLRYHLR--DHTGE--RPYQCGE--CGKAFKRSSLLAIHQRVHTGLRAFTC---------GQCGL 428
Cdd:COG5048   289 PIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCPYslCGKLFSRNDALKRHILLHTSISPAKEkllnssskfSPLLN 368

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958652573 429 TFKWSSHYQYHLRLHSgeRPYACT--ECGKAFRNTSCLRRHRHVHTGERPHSCsvcgksfaqtsnlrqhqrvhtgerpfR 506
Cdd:COG5048   369 NEPPQSLQQYKDLKND--KKSETLsnSCIRNFKRDSNLSLHIITHLSFRPYNC--------------------------K 420

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1958652573 507 CPLCPKTFTHSSNLLLHQRTHSAERPFACPICGRgFVMAAYLQRHLR 553
Cdd:COG5048   421 NPPCSKSFNRHYNLIPHKKIHTNHAPLLCSILKS-FRRDLDLSNHGK 466

Zinc-finger double domain;

                          10        20
                  ....*....|....*....|....*.
gi 1958652573 106 NLRQHQRVHTGERPFRCPLCPKTFTH 131
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26

hypothetical protein

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1958652573  91 PYSCSICGKSFTQSTNLRQHQRVhtGERPFRCPLCPKTFTHSSNLLLH 138
Cdd:PHA00733   73 PYVCPLCLMPFSSSVSLKQHIRY--TEHSKVCPVCGKEFRNTDSTLDH 118

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 1958652573 479 CSVCGKSFAQTSNLRQHQRVHTgerpFRCPLCPKTFTHSSNLLLH-QRTH 527
Cdd:cd20908     4 CYYCDREFDDEKILIQHQKAKH----FKCHICHKKLYTAGGLAVHcLQVH 49

zinc finger;

                           10        20
                   ....*....|....*....|...
gi 1958652573  505 FRCPLCPKTFTHSSNLLLHQRTH 527
Cdd:smart00355   1 YRCPECGKVFKSKSALREHMRTH 23

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958652573 364 PYKCAECGKAFKGSSGLRYHLR--DHTGE--RPYQCGE--CGKAFKRSSLLAIHQRVHTGLRAFTC---------GQCGL 428
Cdd:COG5048   289 PIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCPYslCGKLFSRNDALKRHILLHTSISPAKEkllnssskfSPLLN 368

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958652573 429 TFKWSSHYQYHLRLHSgeRPYACT--ECGKAFRNTSCLRRHRHVHTGERPHSCsvcgksfaqtsnlrqhqrvhtgerpfR 506
Cdd:COG5048   369 NEPPQSLQQYKDLKND--KKSETLsnSCIRNFKRDSNLSLHIITHLSFRPYNC--------------------------K 420

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1958652573 507 CPLCPKTFTHSSNLLLHQRTHSAERPFACPICGRgFVMAAYLQRHLR 553
Cdd:COG5048   421 NPPCSKSFNRHYNLIPHKKIHTNHAPLLCSILKS-FRRDLDLSNHGK 466

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958652573  45 FKWSSHYQYHLRQHTGER-PYPCPDCPKAFKNSSSLRRHR--HVHTGE--RPYSC--SICGKSFTQSTNLRQHQRVHTGE 117
Cdd:COG5048   270 SQSSSPNESDSSSEKGFSlPIKSKQCNISFSRSSPLTRHLrsVNHSGEslKPFSCpySLCGKLFSRNDALKRHILLHTSI 349

                          90
                  ....*....|....*...
gi 1958652573 118 RPFRCPLCPKTFTHSSNL 135
Cdd:COG5048   350 SPAKEKLLNSSSKFSPLL 367

Zinc-finger double domain;

                          10        20
                  ....*....|....*....|....*.
gi 1958652573 106 NLRQHQRVHTGERPFRCPLCPKTFTH 131
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26

Zinc-finger double domain;

                          10        20
                  ....*....|....*....|....*
gi 1958652573 380 LRYHLRDHTGERPYQCGECGKAFKR 404
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 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 1958652573  92 YSCSICGKSFTQSTNLRQHQRVH 114
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958652573  65 PCPDCPKAFKNSSSLRRHRHVHTGER-------PYSCSICGKSFTQSTNLRQHQR--VHTGE--RPFRCP--LCPKTFTH 131
Cdd:COG5048   256 SASESPRSSLPTASSQSSSPNESDSSsekgfslPIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCPysLCGKLFSR 335

                          90
                  ....*....|.
gi 1958652573 132 SSNLLLHHRTH 142
Cdd:COG5048   336 NDALKRHILLH 346

Zinc-finger double domain;

                          10        20
                  ....*....|....*....|....*
gi 1958652573 464 LRRHRHVHTGERPHSCSVCGKSFAQ 488
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 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 1958652573 120 FRCPLCPKTFTHSSNLLLHHRTH 142
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958652573  40 LCGLAFKWSSHYQYHLRQHTGERPYPC-------------------------------------PDCPKAFKNSSSLRRH 82
Cdd:COG5048   328 LCGKLFSRNDALKRHILLHTSISPAKEkllnssskfspllnneppqslqqykdlkndkksetlsNSCIRNFKRDSNLSLH 407

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1958652573  83 RHVHTGERPYSC--SICGKSFTQSTNLRQHQRVHTGERPFRCplCPKTFTHSSNLLLHH 139
Cdd:COG5048   408 IITHLSFRPYNCknPPCSKSFNRHYNLIPHKKIHTNHAPLLC--SILKSFRRDLDLSNH 464

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 1958652573  64 YPCPDCPKAFKNSSSLRRHRHVH 86
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 1958652573 477 HSCSVCGKSFAQTSNLRQHQRVH 499
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23

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

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1958652573 503 RPFRCPLCPKTFTHSSNLLLHQRTHSAERPFACPICGRG--FVMAAYLQRHLRTH 555
Cdd:COG5048    32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYSGCDksFSRPLELSRHLRTH 86

hypothetical protein

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958652573  49 SHYQYHLRQHTGERPYPCPDCPKAFKNSSSLRrhRHVHTGERPYSCSICGKSFTQSTNLRQH 110
Cdd:PHA00733   59 SSYLYKLLTSKAVSPYVCPLCLMPFSSSVSLK--QHIRYTEHSKVCPVCGKEFRNTDSTLDH 118

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 1958652573 449 YACTECGKAFRNTSCLRRHRHVH 471
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
                  ....*....|....*....|....*....|....*....|....*....
gi 1958652573  90 RPYsCSICGKSFTQSTNLRQHQRVHTgerpFRCPLCPKTFTHSSNLLLH 138
Cdd:cd20908     1 KPW-CYYCDREFDDEKILIQHQKAKH----FKCHICHKKLYTAGGLAVH 44

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 1958652573 479 CSVCGKSFAQTSNLRQHQRVHTgerpFRCPLCPKTFTHSSNLLLH-QRTH 527
Cdd:cd20908     4 CYYCDREFDDEKILIQHQKAKH----FKCHICHKKLYTAGGLAVHcLQVH 49

zinc finger;

                           10        20
                   ....*....|....*....|...
gi 1958652573   92 YSCSICGKSFTQSTNLRQHQRVH 114
Cdd:smart00355   1 YRCPECGKVFKSKSALREHMRTH 23