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

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196536405  446 PYKCAECGKAFKGSSGLRYHLR--DHTGE--RPYQCGE--CGKAFKRSSLLAIHQRVHTGLRAFTC---------GQCGL 510
Cdd:COG5048    289 PIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCPYslCGKLFSRNDALKRHILLHTSISPAKEkllnssskfSPLLN 368

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196536405  511 TFKWSSHYQYHLRLHSgeRPYACT--ECGKAFRNTSCLRRHRHVHTGERPHSCsvcgksfaqtsnlrqhqrvhtgerpfR 588
Cdd:COG5048    369 NEPPQSLQQYKDLKND--KKSETLsnSCIRNFKRDSNLSLHIITHLSFRPYNC--------------------------K 420

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 2196536405  589 CPLCPKTFTHSSNLLLHQRTHSAERPFACPICGRgFVMAAYLQRHLR 635
Cdd:COG5048    421 NPPCSKSFNRHYNLIPHKKIHTNHAPLLCSILKS-FRRDLDLSNHGK 466

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

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196536405  446 PYKCAECGKAFKGSSGLRYHLR--DHTGE--RPYQCGE--CGKAFKRSSLLAIHQRVHTGLRAFTC---------GQCGL 510
Cdd:COG5048    289 PIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCPYslCGKLFSRNDALKRHILLHTSISPAKEkllnssskfSPLLN 368

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196536405  511 TFKWSSHYQYHLRLHSgeRPYACT--ECGKAFRNTSCLRRHRHVHTGERPHSCsvcgksfaqtsnlrqhqrvhtgerpfR 588
Cdd:COG5048    369 NEPPQSLQQYKDLKND--KKSETLsnSCIRNFKRDSNLSLHIITHLSFRPYNC--------------------------K 420

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 2196536405  589 CPLCPKTFTHSSNLLLHQRTHSAERPFACPICGRgFVMAAYLQRHLR 635
Cdd:COG5048    421 NPPCSKSFNRHYNLIPHKKIHTNHAPLLCSILKS-FRRDLDLSNHGK 466

Zinc-finger double domain;

                           10        20
                   ....*....|....*....|....*.
gi 2196536405  573 NLRQHQRVHTGERPFRCPLCPKTFTH 598
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
                   ....*....|....*....|....*....|....*....|....*....
gi 2196536405  172 RPYsCSICGKSFTQSTNLRQHQRVHTgerpFRCPLCPKTFTHSSNLLLH 220
Cdd:cd20908      1 KPW-CYYCDREFDDEKILIQHQKAKH----FKCHICHKKLYTAGGLAVH 44

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

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196536405  446 PYKCAECGKAFKGSSGLRYHLR--DHTGE--RPYQCGE--CGKAFKRSSLLAIHQRVHTGLRAFTC---------GQCGL 510
Cdd:COG5048    289 PIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCPYslCGKLFSRNDALKRHILLHTSISPAKEkllnssskfSPLLN 368

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196536405  511 TFKWSSHYQYHLRLHSgeRPYACT--ECGKAFRNTSCLRRHRHVHTGERPHSCsvcgksfaqtsnlrqhqrvhtgerpfR 588
Cdd:COG5048    369 NEPPQSLQQYKDLKND--KKSETLsnSCIRNFKRDSNLSLHIITHLSFRPYNC--------------------------K 420

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 2196536405  589 CPLCPKTFTHSSNLLLHQRTHSAERPFACPICGRgFVMAAYLQRHLR 635
Cdd:COG5048    421 NPPCSKSFNRHYNLIPHKKIHTNHAPLLCSILKS-FRRDLDLSNHGK 466

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

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196536405  142 GERPYPCP--DCPKAFKNSSSLRRHR-HVHtgerpyscsiCGKSFTQSTNLRQHQRVHTGERPFRCPLCPKTFThSSNLL 218
Cdd:COG5189    346 DGKPYKCPveGCNKKYKNQNGLKYHMlHGH----------QNQKLHENPSPEKMNIFSAKDKPYRCEVCDKRYK-NLNGL 414

                   ....*.
gi 2196536405  219 LHHRTH 224
Cdd:COG5189    415 KYHRKH 420

Zinc-finger double domain;

                           10        20
                   ....*....|....*....|....*.
gi 2196536405  573 NLRQHQRVHTGERPFRCPLCPKTFTH 598
Cdd:pfam13465    1 NLKRHMRTHTGEKPYKCPECGKSFKS 26

Zinc-finger double domain;

                           10        20
                   ....*....|....*....|....*.
gi 2196536405  132 HYQYHLRQHTGERPYPCPDCPKAFKN 157
Cdd:pfam13465    1 NLKRHMRTHTGEKPYKCPECGKSFKS 26

Zinc-finger double domain;

                           10        20
                   ....*....|....*....|.
gi 2196536405   52 HQRTHTGERPYKCPDCPKAFK 72
Cdd:pfam13465    5 HMRTHTGEKPYKCPECGKSFK 25

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 2196536405  174 YSCSICGKSFTQSTNLRQHQRVH 196
Cdd:pfam00096    1 YKCPDCGKSFSRKSNLKRHLRTH 23

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

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196536405  527 GERPYAC--TECGKAFRNTSCLRRHR-HVHTGERPHscsvcgksfaQTSNLRQHQRVHTGERPFRCPLCPKTFTHSSNLL 603
Cdd:COG5189    346 DGKPYKCpvEGCNKKYKNQNGLKYHMlHGHQNQKLH----------ENPSPEKMNIFSAKDKPYRCEVCDKRYKNLNGLK 415

                   ....*..
gi 2196536405  604 LHqRTHS 610
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 2196536405  587 FRCPLCPKTFTHSSNLLLHQRTH 609
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 2196536405  202 FRCPLCPKTFTHSSNLLLHHRTH 224
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 2196536405  475 YQCGECGKAFKRSSLLAIHQRVH 497
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 2196536405  146 YPCPDCPKAFKNSSSLRRHRHVH 168
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 2196536405   90 YQCPDCPKAFKRSSLLQIHRSVH 112
Cdd:pfam00096    1 YKCPDCGKSFSRKSNLKRHLRTH 23

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

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2196536405  585 RPFRCPLCPKTFTHSSNLLLHQRTHSAERPFACPICGRG--FVMAAYLQRHLRTH 637
Cdd:COG5048     32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYSGCDksFSRPLELSRHLRTH 86

hypothetical protein

                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2196536405  131 SHYQYHLRQHTGERPYPCPDCPKAFKNSSSLRrhRHVHTGERPYSCSICGKSFTQSTNLRQH 192
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 2196536405  531 YACTECGKAFRNTSCLRRHRHVH 553
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 2196536405   62 YKCPDCPKAFKGSSALLYHQRGH 84
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 2196536405  447 YKCAECGKAFKGSSGLRYHLRDH 469
Cdd:pfam00096    1 YKCPDCGKSFSRKSNLKRHLRTH 23