NCBI Conserved Domain Search

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

Pssm-ID: 227381 [Multi-domain] Cd Length: 467 Bit Score: 71.65 E-value: 7.06e-13

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331007 202 KPYKCPDCGKCFSWSSNLVQHQRTHTGEKPYKCT--ECEKAFTQSTNLIKHQRSHTGEKPYKC--GECRRAFYRSSDLIQ 277
Cdd:COG5048   32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSysGCDKSFSRPLELSRHLRTHHNNPSDLNskSLPLSNSKASSSSLS 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331007 278 HQATHTgEKPYKCPECGKRFGQNHNLLK--HQKIHAGEKPYR-CTECGKSFIQSSEL-------------------TQHQ 335
Cdd:COG5048  112 SSSSNS-NDNNLLSSHSLPPSSRDPQLPdlLSISNLRNNPLPgNNSSSVNTPQSNSLhpplpanslskdpssnlslLISS 190

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331007 336 RTHTGEKPYECLECGKSFGHSSTLIKHQRTHLREDPFKCPVCGKTFTLSATLLRHQRTHTGERPYKCPECGKSFSVSSNL 415
Cdd:COG5048  191 NVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLSSSDSSSSASESPRSSLPTASS 270

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331007 416 INHQRIHRGER-------PYICADCGKSFIMSSTLIRHQR--IHTGE--KPYKC--SDCGKSFIRSSHLIQHRRTHTGEK 482
Cdd:COG5048  271 QSSSPNESDSSsekgfslPIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCpySLCGKLFSRNDALKRHILLHTSIS 350

                        330       340
                 ....*....|....*....|....*...
gi 564331007 483 PYKCPECGKSFSQSSNLITHVRTHMDEN 510
Cdd:COG5048  351 PAKEKLLNSSSKFSPLLNNEPPQSLQQY 378

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

Pssm-ID: 227381 [Multi-domain] Cd Length: 467 Bit Score: 71.65 E-value: 7.25e-13

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331007 141 PSGAEKPYICNECGKSFSQWSKLLRHQRIHTGERPNTCS--ECGKSFTQSSHLVQHQRTHTGEKPYKCPDC--------- 209
Cdd:COG5048   27 LSNAPRPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSysGCDKSFSRPLELSRHLRTHHNNPSDLNSKSlplsnskas 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331007 210 -----GKCFSWSSN-------LVQHQRTHTGEKPYKCTECEKAFTQSTNLIKHQRSHTGEKPYKCG---ECRRAFYRSSD 274
Cdd:COG5048  107 ssslsSSSSNSNDNnllsshsLPPSSRDPQLPDLLSISNLRNNPLPGNNSSSVNTPQSNSLHPPLPansLSKDPSSNLSL 186

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331007 275 LIQHQATHTGEKPYKCPECGKRFGQNHNLLKHQKIHAgEKPYRCTECgkSFIQSSELTQHQRTHTGeKPYECLECGKSFG 354
Cdd:COG5048  187 LISSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENS-SSSLPLTTN--SQLSPKSLLSQSPSSLS-SSDSSSSASESPR 262

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331007 355 HSSTLIKHQRTHLRED----------PFKCPVCGKTFTLSATLLRHQRT--HTGE--RPYKCPE--CGKSFSVSSNLINH 418
Cdd:COG5048  263 SSLPTASSQSSSPNESdsssekgfslPIKSKQCNISFSRSSPLTRHLRSvnHSGEslKPFSCPYslCGKLFSRNDALKRH 342

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331007 419 QRIHRGERPYIC--ADCGKSFIMSST-----LIRHQRIHTGEKPYKCSD--CGKSFIRSSHLIQHRRTHTGEKP--YKCP 487
Cdd:COG5048  343 ILLHTSISPAKEklLNSSSKFSPLLNneppqSLQQYKDLKNDKKSETLSnsCIRNFKRDSNLSLHIITHLSFRPynCKNP 422

                        410       420       430
                 ....*....|....*....|....*....|..
gi 564331007 488 ECGKSFSQSSNLITHVRTHMDENLFVCSDCGK 519
Cdd:COG5048  423 PCSKSFNRHYNLIPHKKIHTNHAPLLCSILKS 454

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

Pssm-ID: 227381 [Multi-domain] Cd Length: 467 Bit Score: 63.18 E-value: 4.08e-10

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331007 151 NECGKSFSQWSKLLRHQRIHTGERPNTCSECGKSFTQSSHLVQHQRTHTGEKPYKCPDCGKCFSWSSNLVQHQRTHTGEK 230
Cdd:COG5048  174 NSLSKDPSSNLSLLISSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLSSSDS 253

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331007 231 PYKCTECEKAFTQSTNLIKHQRSHTGE-------KPYKCGECRRAFYRSSDLIQHQAT--HTGE--KPYKCPE--CGKRF 297
Cdd:COG5048  254 SSSASESPRSSLPTASSQSSSPNESDSssekgfsLPIKSKQCNISFSRSSPLTRHLRSvnHSGEslKPFSCPYslCGKLF 333

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331007 298 GQNHNLLKHQKIHAGEKPYRCTECGKSFIQSSELTQHQRTHTgekpyeclecgksfgHSSTLIKHQRTHLREDPFKCpvc 377
Cdd:COG5048  334 SRNDALKRHILLHTSISPAKEKLLNSSSKFSPLLNNEPPQSL---------------QQYKDLKNDKKSETLSNSCI--- 395

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564331007 378 gKTFTLSATLLRHQRTHTGERP--YKCPECGKSFSVSSNLINHQRIHRGERPYICADCGKSFIMSST 442
Cdd:COG5048  396 -RNFKRDSNLSLHIITHLSFRPynCKNPPCSKSFNRHYNLIPHKKIHTNHAPLLCSILKSFRRDLDL 461

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

Pssm-ID: 227516 [Multi-domain] Cd Length: 423 Bit Score: 54.72 E-value: 1.41e-07

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331007 228 GEKPYKC--TECEKAFTQSTNLiKHQRSHtgekpykcGECRRAFYRSSDLIQHQATHTGEKPYKCPECGKRFgQNHNLLK 305
Cdd:COG5189  346 DGKPYKCpvEGCNKKYKNQNGL-KYHMLH--------GHQNQKLHENPSPEKMNIFSAKDKPYRCEVCDKRY-KNLNGLK 415


                 ....*
gi 564331007 306 HQKIH 310
Cdd:COG5189  416 YHRKH 420

Zinc-finger double domain;

Pssm-ID: 463886 [Multi-domain] Cd Length: 26 Bit Score: 44.28 E-value: 3.09e-06

                          10        20
                  ....*....|....*....|....*.
gi 564331007  470 HLIQHRRTHTGEKPYKCPECGKSFSQ 495
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26

Zinc-finger double domain;

Pssm-ID: 463886 [Multi-domain] Cd Length: 26 Bit Score: 43.51 E-value: 5.96e-06

                          10        20
                  ....*....|....*....|....*.
gi 564331007  218 NLVQHQRTHTGEKPYKCTECEKAFTQ 243
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26

Zinc-finger double domain;

Pssm-ID: 463886 [Multi-domain] Cd Length: 26 Bit Score: 43.51 E-value: 6.57e-06

                          10        20
                  ....*....|....*....|....
gi 564331007  387 LLRHQRTHTGERPYKCPECGKSFS 410
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFK 25

Zinc-finger double domain;

Pssm-ID: 463886 [Multi-domain] Cd Length: 26 Bit Score: 42.74 E-value: 1.17e-05

                          10        20
                  ....*....|....*....|....*
gi 564331007  190 HLVQHQRTHTGEKPYKCPDCGKCFS 214
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFK 25

Zinc-finger double domain;

Pssm-ID: 463886 [Multi-domain] Cd Length: 26 Bit Score: 41.59 E-value: 2.37e-05

                          10        20
                  ....*....|....*....|....*
gi 564331007  443 LIRHQRIHTGEKPYKCSDCGKSFIR 467
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 26

Zinc-finger double domain;

Pssm-ID: 463886 [Multi-domain] Cd Length: 26 Bit Score: 41.20 E-value: 3.72e-05

                          10        20
                  ....*....|....*....|....
gi 564331007  274 DLIQHQATHTGEKPYKCPECGKRF 297
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSF 24

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.

Pssm-ID: 395048 [Multi-domain] Cd Length: 23 Bit Score: 41.13 E-value: 4.44e-05

                          10        20
                  ....*....|....*....|...
gi 564331007  484 YKCPECGKSFSQSSNLITHVRTH 506
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.

Pssm-ID: 395048 [Multi-domain] Cd Length: 23 Bit Score: 40.36 E-value: 6.44e-05

                          10        20
                  ....*....|....*....|...
gi 564331007  456 YKCSDCGKSFIRSSHLIQHRRTH 478
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23

Zinc-finger double domain;

Pssm-ID: 463886 [Multi-domain] Cd Length: 26 Bit Score: 40.43 E-value: 7.62e-05

                          10        20
                  ....*....|....*....|....
gi 564331007  330 ELTQHQRTHTGEKPYECLECGKSF 353
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSF 24

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.

Pssm-ID: 395048 [Multi-domain] Cd Length: 23 Bit Score: 39.59 E-value: 1.21e-04

                          10        20
                  ....*....|....*....|...
gi 564331007  400 YKCPECGKSFSVSSNLINHQRIH 422
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.

Pssm-ID: 395048 [Multi-domain] Cd Length: 23 Bit Score: 39.21 E-value: 1.65e-04

                          10        20
                  ....*....|....*....|...
gi 564331007  316 YRCTECGKSFIQSSELTQHQRTH 338
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23

Zinc-finger double domain;

Pssm-ID: 463886 [Multi-domain] Cd Length: 26 Bit Score: 39.28 E-value: 1.95e-04

                          10        20
                  ....*....|....*....|....*.
gi 564331007  302 NLLKHQKIHAGEKPYRCTECGKSFIQ 327
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.

Pssm-ID: 395048 [Multi-domain] Cd Length: 23 Bit Score: 38.82 E-value: 2.32e-04

                          10        20
                  ....*....|....*....|...
gi 564331007  148 YICNECGKSFSQWSKLLRHQRIH 170
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23

Zinc-finger double domain;

Pssm-ID: 463886 [Multi-domain] Cd Length: 26 Bit Score: 37.74 E-value: 5.47e-04

                          10        20
                  ....*....|....*....|....*.
gi 564331007  246 NLIKHQRSHTGEKPYKCGECRRAFYR 271
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.

Pssm-ID: 411020 [Multi-domain] Cd Length: 82 Bit Score: 39.46 E-value: 5.61e-04

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 564331007 454 KPYkCSDCGKSFIRSSHLIQHRRTHTgekpYKCPECGKSFSQSSNLITHVRT 505
Cdd:cd20908    1 KPW-CYYCDREFDDEKILIQHQKAKH----FKCHICHKKLYTAGGLAVHCLQ 47

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.

Pssm-ID: 395048 [Multi-domain] Cd Length: 23 Bit Score: 37.66 E-value: 7.18e-04

                          10        20
                  ....*....|....*....|..
gi 564331007  177 TCSECGKSFTQSSHLVQHQRTH 198
Cdd:pfam00096   2 KCPDCGKSFSRKSNLKRHLRTH 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.

Pssm-ID: 395048 [Multi-domain] Cd Length: 23 Bit Score: 37.66 E-value: 7.46e-04

                          10        20
                  ....*....|....*....|...
gi 564331007  288 YKCPECGKRFGQNHNLLKHQKIH 310
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.

Pssm-ID: 395048 [Multi-domain] Cd Length: 23 Bit Score: 37.28 E-value: 7.92e-04

                          10        20
                  ....*....|....*....|...
gi 564331007  232 YKCTECEKAFTQSTNLIKHQRSH 254
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.

Pssm-ID: 395048 [Multi-domain] Cd Length: 23 Bit Score: 36.89 E-value: 1.05e-03

                          10        20
                  ....*....|....*....|...
gi 564331007  344 YECLECGKSFGHSSTLIKHQRTH 366
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23

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

Pssm-ID: 227381 [Multi-domain] Cd Length: 467 Bit Score: 42.38 E-value: 1.09e-03

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331007 286 KPYKCPECGKRFGQNHNLLKHQKIHAGEKPYRCT--ECGKSFIQSSELTQHQRTHTGEKPYECLECGKS--FGHSSTLIK 361
Cdd:COG5048   32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSysGCDKSFSRPLELSRHLRTHHNNPSDLNSKSLPLsnSKASSSSLS 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331007 362 HQRTHLReDPFKCPVCGKTFTLSATLLRHQRTHTGERPYKCPECGKSFSVSSNLINHQRIHRGERPyicadcGKSFIMSS 441
Cdd:COG5048  112 SSSSNSN-DNNLLSSHSLPPSSRDPQLPDLLSISNLRNNPLPGNNSSSVNTPQSNSLHPPLPANSL------SKDPSSNL 184

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331007 442 TLIRHQRIHTGEKPYKCSDCGKSFIRSSHLIQHRRTHTGEKPYKCPECGKSFSQSSNLITHVRTHMDENLFVCSDCGKAF 521
Cdd:COG5048  185 SLLISSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLSSSDSSSSASESPRSS 264

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564331007 522 LEAQELEQHRVIHeRGKTPARRAQgdgllglgdpalmtpppgaKPHKCLVCGKGFNDEGIFMQHQR--IHVGEN 593
Cdd:COG5048  265 LPTASSQSSSPNE-SDSSSEKGFS-------------------LPIKSKQCNISFSRSSPLTRHLRsvNHSGES 318

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.

Pssm-ID: 395048 [Multi-domain] Cd Length: 23 Bit Score: 36.89 E-value: 1.31e-03

                          10        20
                  ....*....|....*....|...
gi 564331007  372 FKCPVCGKTFTLSATLLRHQRTH 394
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.

Pssm-ID: 395048 [Multi-domain] Cd Length: 23 Bit Score: 36.51 E-value: 1.72e-03

                          10        20
                  ....*....|....*....|...
gi 564331007  204 YKCPDCGKCFSWSSNLVQHQRTH 226
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.

Pssm-ID: 411020 [Multi-domain] Cd Length: 82 Bit Score: 37.92 E-value: 1.82e-03

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 564331007 342 KPYeCLECGKSFGHSSTLIKHQR-THlredpFKCPVCGKTFT 382
Cdd:cd20908    1 KPW-CYYCDREFDDEKILIQHQKaKH-----FKCHICHKKLY 36

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.

Pssm-ID: 411020 [Multi-domain] Cd Length: 82 Bit Score: 37.92 E-value: 1.89e-03

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 564331007 178 CSECGKSFTQSSHLVQHQRTHTgekpYKCPDCGKCFSWSSNLVQH 222
Cdd:cd20908    4 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.

Pssm-ID: 411020 [Multi-domain] Cd Length: 82 Bit Score: 37.92 E-value: 1.97e-03

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 564331007 373 KCPVCGKTFTLSATLLRHQRTHTgerpYKCPECGKSFSVSSNLINH-QRIHR 423
Cdd:cd20908    3 WCYYCDREFDDEKILIQHQKAKH----FKCHICHKKLYTAGGLAVHcLQVHK 50

Zinc-finger double domain;

Pssm-ID: 463886 [Multi-domain] Cd Length: 26 Bit Score: 36.20 E-value: 2.02e-03

                          10        20
                  ....*....|....*....|....*
gi 564331007  163 LLRHQRIHTGERPNTCSECGKSFTQ 187
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 26

Zinc-finger double domain;

Pssm-ID: 463886 [Multi-domain] Cd Length: 26 Bit Score: 36.20 E-value: 2.21e-03

                          10        20
                  ....*....|....*....|....
gi 564331007  359 LIKHQRTHLREDPFKCPVCGKTFT 382
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFK 25

IS1 family transposase; Proteins of this family are DDE transposases encoded by the IS1 family elements usually through a translational frameshift mechanism.

Pssm-ID: 468085 [Multi-domain] Cd Length: 199 Bit Score: 39.95 E-value: 2.49e-03

                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 564331007 290 CPECgkrfgQNHNLLKHQKIHAGEKPYRCTECGKSFI 326
Cdd:NF033558   1 CPRC-----QSDNVVKNGKSVRGKQRYRCKDCGRQFQ 32

Drought induced 19 protein (Di19), zinc-binding; This family consists of several drought induced 19 (Di19) like proteins. Di19 has been found to be strongly expressed in both the roots and leaves of Arabidopsis thaliana during progressive drought. This domain is a zinc-binding domain.

Pssm-ID: 428539 Cd Length: 54 Bit Score: 36.51 E-value: 2.75e-03

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 564331007  372 FKCPVCGKTFTLsATLLRH-QRTHTGE-RPYKCPECGKsfSVSSNLINHQRIHRG 424
Cdd:pfam05605   3 FTCPFCGEDFDV-VSLCEHvEDEHPVEsKNVVCPVCAA--KVGKDMIGHLTLQHG 54

hypothetical protein

Pssm-ID: 177301 Cd Length: 128 Bit Score: 38.32 E-value: 3.71e-03

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 564331007 371 PFKCPVCGKTFTLSATLLRHQRthTGERPYKCPECGKSFSVSSNLINH 418
Cdd:PHA00733  73 PYVCPLCLMPFSSSVSLKQHIR--YTEHSKVCPVCGKEFRNTDSTLDH 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.

Pssm-ID: 395048 [Multi-domain] Cd Length: 23 Bit Score: 35.35 E-value: 4.03e-03

                          10        20
                  ....*....|....*....|...
gi 564331007  428 YICADCGKSFIMSSTLIRHQRIH 450
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23

hypothetical protein

Pssm-ID: 177301 Cd Length: 128 Bit Score: 38.32 E-value: 4.12e-03

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 564331007 343 PYECLECGKSFGHSSTLIKHQRthLREDPFKCPVCGKTFTLSATLLRH 390
Cdd:PHA00733  73 PYVCPLCLMPFSSSVSLKQHIR--YTEHSKVCPVCGKEFRNTDSTLDH 118

Transposase InsA [Mobilome: prophages, transposons];

Pssm-ID: 442893 [Multi-domain] Cd Length: 241 Bit Score: 39.47 E-value: 4.92e-03

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564331007 357 STLIKHQRTHLREDPFKCPVCGktftlSATLLRHQRTHTGERPYKCPECGKSFSVSSNLINH 418
Cdd:COG3677    2 STAEELLEQIRWPNGPVCPHCG-----STRIVKNGKTRNGRQRYRCKDCGRTFTVTTGTIFE 58

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

Pssm-ID: 227516 [Multi-domain] Cd Length: 423 Bit Score: 39.32 E-value: 9.35e-03

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331007 284 GEKPYKCP--ECGKRFgQNHNLLKHQKIHAgekpyrctecgksfiqsseltqHQRTHTGEKPYEclecgksfghsstlIK 361
Cdd:COG5189  346 DGKPYKCPveGCNKKY-KNQNGLKYHMLHG----------------------HQNQKLHENPSP--------------EK 388

                         90       100       110
                 ....*....|....*....|....*....|....
gi 564331007 362 HQRTHLREDPFKCPVCGKTFTlSATLLRHQRTHT 395
Cdd:COG5189  389 MNIFSAKDKPYRCEVCDKRYK-NLNGLKYHRKHS 421