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 1910909669  734 YTCRYCGKIFPRSANLTRHLRTH 756
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 1910909669  189 FICEVCHKSYTQFSNLCRHKRMH 211
Cdd:pfam00096    1 YKCPDCGKSFSRKSNLKRHLRTH 23

hypothetical protein

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910909669  690 EKLESFSALKPEASELLQSVPSMFNFRapPNALPEN------LLRKGKERYTCRYCGKIFPRSANLTRHLRThtGEQPYR 763
Cdd:PHA00733    26 EELKRYHSLTPEQKRLIRAVVKTLIYN--PQLLDESsylyklLTSKAVSPYVCPLCLMPFSSSVSLKQHIRY--TEHSKV 101

                           90       100
                   ....*....|....*....|...
gi 1910909669  764 CKYCDRSFSISSNLQRHVRNIHN 786
Cdd:PHA00733   102 CPVCGKEFRNTDSTLDHVCKKHN 124

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 1910909669  734 YTCRYCGKIFPRSANLTRHLRTH 756
Cdd:pfam00096    1 YKCPDCGKSFSRKSNLKRHLRTH 23

Transposase InsA [Mobilome: prophages, transposons];

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 1910909669  728 RKGKERYTCRYCGkifprSANLTRHLRTHTGEQPYRCKYCDRSFSI 773
Cdd:COG3677     11 IRWPNGPVCPHCG-----STRIVKNGKTRNGRQRYRCKDCGRTFTV 51

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 1910909669  791 FKCHLCDRCFGQQTNLDRHLKKH 813
Cdd:pfam00096    1 YKCPDCGKSFSRKSNLKRHLRTH 23

Domain of unknown function (DUF4045); This presumed domain is functionally uncharacterized. This domain family is found in bacteria and eukaryotes, and is typically between 384 and 430 amino acids in length.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910909669  524 PDRDLRSLPLKMEPQSPSEVKKLQKGSSESPFDLTTKRKDEKPLTPVPSKPPATPATSQDQPLDLSMGSRSR---ASGTK 600
Cdd:pfam13254  277 PSKSAEASTEKKEPDTESSPETSSEKSAPSLLSPVSKASIDKPLSSPDRDPLSPKPKPQSPPKDFRANLRSRevpKDKSK 356

                           90
                   ....*....|.
gi 1910909669  601 LTEPRKNHVFG 611
Cdd:pfam13254  357 KDEPEFKNVFG 367

zinc finger;

                            10        20
                    ....*....|....*....|...
gi 1910909669   734 YTCRYCGKIFPRSANLTRHLRTH 756
Cdd:smart00355    1 YRCPECGKVFKSKSALREHMRTH 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 1910909669  734 YTCRYCGKIFPRSANLTRHLRTH 756
Cdd:pfam00096    1 YKCPDCGKSFSRKSNLKRHLRTH 23

Transposase InsA [Mobilome: prophages, transposons];

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 1910909669  728 RKGKERYTCRYCGkifprSANLTRHLRTHTGEQPYRCKYCDRSFSI 773
Cdd:COG3677     11 IRWPNGPVCPHCG-----STRIVKNGKTRNGRQRYRCKDCGRTFTV 51

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 1910909669  791 FKCHLCDRCFGQQTNLDRHLKKH 813
Cdd:pfam00096    1 YKCPDCGKSFSRKSNLKRHLRTH 23

Domain of unknown function (DUF4045); This presumed domain is functionally uncharacterized. This domain family is found in bacteria and eukaryotes, and is typically between 384 and 430 amino acids in length.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910909669  524 PDRDLRSLPLKMEPQSPSEVKKLQKGSSESPFDLTTKRKDEKPLTPVPSKPPATPATSQDQPLDLSMGSRSR---ASGTK 600
Cdd:pfam13254  277 PSKSAEASTEKKEPDTESSPETSSEKSAPSLLSPVSKASIDKPLSSPDRDPLSPKPKPQSPPKDFRANLRSRevpKDKSK 356

                           90
                   ....*....|.
gi 1910909669  601 LTEPRKNHVFG 611
Cdd:pfam13254  357 KDEPEFKNVFG 367

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 1910909669  762 YRCKYCDRSFSISSNLQRHVR 782
Cdd:pfam00096    1 YKCPDCGKSFSRKSNLKRHLR 21

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 1910909669  736 CRYCGKIFPRSANLTRHLRTHTgeqpYRCKYCDRSFSISSNLQRHVRNIHnKEK 789
Cdd:cd20908      4 CYYCDREFDDEKILIQHQKAKH----FKCHICHKKLYTAGGLAVHCLQVH-KET 52