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Conserved domains on  [gi|28893273|ref|NP_796200|]
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zinc finger protein 629 isoform a [Mus musculus]

Protein Classification

C2H2-type zinc finger protein( domain architecture ID 11986654)

Cys2His2 (C2H2)-type zinc finger protein may be involved in transcriptional regulation

CATH:  3.30.160.60
Gene Ontology:  GO:0008270|GO:0003677
PubMed:  22803940|11361095|11179890|12665246|10940247
SCOP:  4003583

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
203-511 1.57e-12

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


:

Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 70.88  E-value: 1.57e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28893273 203 KPYKCPDCGKCFSWSSNLVQHQRTHTGEKPYKCT--ECEKAFTQSTNLIKHQRSHTGEKPYKC--GECRRAFYRSSDLIQ 278
Cdd:COG5048  32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSysGCDKSFSRPLELSRHLRTHHNNPSDLNskSLPLSNSKASSSSLS 111

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28893273 279 HQATHTgEKPYKCPECGKRFGQNHNLLK--HQKIHAGEKPYR-CTECGKSFIQSSEL-------------------TQHQ 336
Cdd:COG5048 112 SSSSNS-NDNNLLSSHSLPPSSRDPQLPdlLSISNLRNNPLPgNNSSSVNTPQSNSLhpplpanslskdpssnlslLISS 190

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28893273 337 RTHTGEKPYECLECGKSFGHSSTLIKHQRTHLREDPFKCPVCGKTFTLSATLLRHQRTHTGERPYKCPECGKSFSVSSNL 416
Cdd:COG5048 191 NVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLSSSDSSSSASESPRSSLPTASS 270

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28893273 417 INHQRIHRGER-------PYICADCGKSFIMSSTLIRHQR--IHTGE--KPYKC--SDCGKSFIRSSHLIQHRRTHTGEK 483
Cdd:COG5048 271 QSSSPNESDSSsekgfslPIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCpySLCGKLFSRNDALKRHILLHTSIS 350

                       330       340
                ....*....|....*....|....*...
gi 28893273 484 PYKCPECGKSFSQSSNLITHVRTHMDEN 511
Cdd:COG5048 351 PAKEKLLNSSSKFSPLLNNEPPQSLQQY 378
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 149-171 2.57e-04

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: 2.57e-04
                          10        20
                  ....*....|....*....|...
gi 28893273   149 YICNECGKSFSQWSKLLRHQRIH 171
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 178-199 7.92e-04

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 28893273   178 TCSECGKSFTQSSHLVQHQRTH 199
Cdd:pfam00096   2 KCPDCGKSFSRKSNLKRHLRTH 23
 
Name Accession Description Interval E-value
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
203-511 1.57e-12

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 70.88  E-value: 1.57e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28893273 203 KPYKCPDCGKCFSWSSNLVQHQRTHTGEKPYKCT--ECEKAFTQSTNLIKHQRSHTGEKPYKC--GECRRAFYRSSDLIQ 278
Cdd:COG5048  32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSysGCDKSFSRPLELSRHLRTHHNNPSDLNskSLPLSNSKASSSSLS 111

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28893273 279 HQATHTgEKPYKCPECGKRFGQNHNLLK--HQKIHAGEKPYR-CTECGKSFIQSSEL-------------------TQHQ 336
Cdd:COG5048 112 SSSSNS-NDNNLLSSHSLPPSSRDPQLPdlLSISNLRNNPLPgNNSSSVNTPQSNSLhpplpanslskdpssnlslLISS 190

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28893273 337 RTHTGEKPYECLECGKSFGHSSTLIKHQRTHLREDPFKCPVCGKTFTLSATLLRHQRTHTGERPYKCPECGKSFSVSSNL 416
Cdd:COG5048 191 NVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLSSSDSSSSASESPRSSLPTASS 270

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28893273 417 INHQRIHRGER-------PYICADCGKSFIMSSTLIRHQR--IHTGE--KPYKC--SDCGKSFIRSSHLIQHRRTHTGEK 483
Cdd:COG5048 271 QSSSPNESDSSsekgfslPIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCpySLCGKLFSRNDALKRHILLHTSIS 350

                       330       340
                ....*....|....*....|....*...
gi 28893273 484 PYKCPECGKSFSQSSNLITHVRTHMDEN 511
Cdd:COG5048 351 PAKEKLLNSSSKFSPLLNNEPPQSLQQY 378
zf-H2C2_2 pfam13465
Zinc-finger double domain;
471-496 3.62e-06

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 43.90  E-value: 3.62e-06
                          10        20
                  ....*....|....*....|....*.
gi 28893273   471 HLIQHRRTHTGEKPYKCPECGKSFSQ 496
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 149-171 2.57e-04

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: 2.57e-04
                          10        20
                  ....*....|....*....|...
gi 28893273   149 YICNECGKSFSQWSKLLRHQRIH 171
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
SUF4-like cd20908
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
 455-506 6.20e-04

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: 6.20e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 28893273 455 KPYkCSDCGKSFIRSSHLIQHRRTHTgekpYKCPECGKSFSQSSNLITHVRT 506
Cdd:cd20908   1 KPW-CYYCDREFDDEKILIQHQKAKH----FKCHICHKKLYTAGGLAVHCLQ 47
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 178-199 7.92e-04

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 28893273   178 TCSECGKSFTQSSHLVQHQRTH 199
Cdd:pfam00096   2 KCPDCGKSFSRKSNLKRHLRTH 23
transpos_IS1 NF033558
IS1 family transposase; Proteins of this family are DDE transposases encoded by the IS1 family ...
 291-327 2.43e-03

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: 2.43e-03
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 28893273  291 CPECgkrfgQNHNLLKHQKIHAGEKPYRCTECGKSFI 327
Cdd:NF033558   1 CPRC-----QSDNVVKNGKSVRGKQRYRCKDCGRQFQ 32
PHA00733 PHA00733
hypothetical protein
 372-419 3.79e-03

hypothetical protein


Pssm-ID: 177301  Cd Length: 128  Bit Score: 38.32  E-value: 3.79e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 28893273  372 PFKCPVCGKTFTLSATLLRHQRthTGERPYKCPECGKSFSVSSNLINH 419
Cdd:PHA00733  73 PYVCPLCLMPFSSSVSLKQHIR--YTEHSKVCPVCGKEFRNTDSTLDH 118
 
Name Accession Description Interval E-value
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
203-511 1.57e-12

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 70.88  E-value: 1.57e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28893273 203 KPYKCPDCGKCFSWSSNLVQHQRTHTGEKPYKCT--ECEKAFTQSTNLIKHQRSHTGEKPYKC--GECRRAFYRSSDLIQ 278
Cdd:COG5048  32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSysGCDKSFSRPLELSRHLRTHHNNPSDLNskSLPLSNSKASSSSLS 111

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28893273 279 HQATHTgEKPYKCPECGKRFGQNHNLLK--HQKIHAGEKPYR-CTECGKSFIQSSEL-------------------TQHQ 336
Cdd:COG5048 112 SSSSNS-NDNNLLSSHSLPPSSRDPQLPdlLSISNLRNNPLPgNNSSSVNTPQSNSLhpplpanslskdpssnlslLISS 190

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28893273 337 RTHTGEKPYECLECGKSFGHSSTLIKHQRTHLREDPFKCPVCGKTFTLSATLLRHQRTHTGERPYKCPECGKSFSVSSNL 416
Cdd:COG5048 191 NVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLSSSDSSSSASESPRSSLPTASS 270

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28893273 417 INHQRIHRGER-------PYICADCGKSFIMSSTLIRHQR--IHTGE--KPYKC--SDCGKSFIRSSHLIQHRRTHTGEK 483
Cdd:COG5048 271 QSSSPNESDSSsekgfslPIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCpySLCGKLFSRNDALKRHILLHTSIS 350

                       330       340
                ....*....|....*....|....*...
gi 28893273 484 PYKCPECGKSFSQSSNLITHVRTHMDEN 511
Cdd:COG5048 351 PAKEKLLNSSSKFSPLLNNEPPQSLQQY 378
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
142-520 1.97e-12

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 70.49  E-value: 1.97e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28893273 142 PSGAEKPYICNECGKSFSQWSKLLRHQRIHTGERPNTCS--ECGKSFTQSSHLVQHQRTHTGEKPYKCPDC--------- 210
Cdd:COG5048  27 LSNAPRPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSysGCDKSFSRPLELSRHLRTHHNNPSDLNSKSlplsnskas 106

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28893273 211 -----GKCFSWSSN-------LVQHQRTHTGEKPYKCTECEKAFTQSTNLIKHQRSHTGEKPYKCG---ECRRAFYRSSD 275
Cdd:COG5048 107 ssslsSSSSNSNDNnllsshsLPPSSRDPQLPDLLSISNLRNNPLPGNNSSSVNTPQSNSLHPPLPansLSKDPSSNLSL 186

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28893273 276 LIQHQATHTGEKPYKCPECGKRFGQNHNLLKHQKIHAgEKPYRCTECgkSFIQSSELTQHQRTHTGeKPYECLECGKSFG 355
Cdd:COG5048 187 LISSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENS-SSSLPLTTN--SQLSPKSLLSQSPSSLS-SSDSSSSASESPR 262

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28893273 356 HSSTLIKHQRTHLRED----------PFKCPVCGKTFTLSATLLRHQRT--HTGE--RPYKCPE--CGKSFSVSSNLINH 419
Cdd:COG5048 263 SSLPTASSQSSSPNESdsssekgfslPIKSKQCNISFSRSSPLTRHLRSvnHSGEslKPFSCPYslCGKLFSRNDALKRH 342

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28893273 420 QRIHRGERPYIC--ADCGKSFIMSST-----LIRHQRIHTGEKPYKCSD--CGKSFIRSSHLIQHRRTHTGEKP--YKCP 488
Cdd:COG5048 343 ILLHTSISPAKEklLNSSSKFSPLLNneppqSLQQYKDLKNDKKSETLSnsCIRNFKRDSNLSLHIITHLSFRPynCKNP 422

                       410       420       430
                ....*....|....*....|....*....|..
gi 28893273 489 ECGKSFSQSSNLITHVRTHMDENLFVCSDCGK 520
Cdd:COG5048 423 PCSKSFNRHYNLIPHKKIHTNHAPLLCSILKS 454
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
152-443 7.58e-10

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 62.02  E-value: 7.58e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28893273 152 NECGKSFSQWSKLLRHQRIHTGERPNTCSECGKSFTQSSHLVQHQRTHTGEKPYKCPDCGKCFSWSSNLVQHQRTHTGEK 231
Cdd:COG5048 174 NSLSKDPSSNLSLLISSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLSSSDS 253

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28893273 232 PYKCTECEKAFTQSTNLIKHQRSHTGE-------KPYKCGECRRAFYRSSDLIQHQAT--HTGE--KPYKCPE--CGKRF 298
Cdd:COG5048 254 SSSASESPRSSLPTASSQSSSPNESDSssekgfsLPIKSKQCNISFSRSSPLTRHLRSvnHSGEslKPFSCPYslCGKLF 333

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28893273 299 GQNHNLLKHQKIHAGEKPYRCTECGKSFIQSSELTQHQRTHTgekpyeclecgksfgHSSTLIKHQRTHLREDPFKCpvc 378
Cdd:COG5048 334 SRNDALKRHILLHTSISPAKEKLLNSSSKFSPLLNNEPPQSL---------------QQYKDLKNDKKSETLSNSCI--- 395

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 28893273 379 gKTFTLSATLLRHQRTHTGERPY--KCPECGKSFSVSSNLINHQRIHRGERPYICADCGKSFIMSST 443
Cdd:COG5048 396 -RNFKRDSNLSLHIITHLSFRPYncKNPPCSKSFNRHYNLIPHKKIHTNHAPLLCSILKSFRRDLDL 461
SFP1 COG5189
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ...
 229-311 1.84e-07

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


Pssm-ID: 227516 [Multi-domain]  Cd Length: 423  Bit Score: 54.34  E-value: 1.84e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28893273 229 GEKPYKC--TECEKAFTqSTNLIKHQRSHtgekpykcGECRRAFYRSSDLIQHQATHTGEKPYKCPECGKRFgQNHNLLK 306
Cdd:COG5189 346 DGKPYKCpvEGCNKKYK-NQNGLKYHMLH--------GHQNQKLHENPSPEKMNIFSAKDKPYRCEVCDKRY-KNLNGLK 415


                ....*
gi 28893273 307 HQKIH 311
Cdd:COG5189 416 YHRKH 420
zf-H2C2_2 pfam13465
Zinc-finger double domain;
471-496 3.62e-06

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 43.90  E-value: 3.62e-06
                          10        20
                  ....*....|....*....|....*.
gi 28893273   471 HLIQHRRTHTGEKPYKCPECGKSFSQ 496
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
219-244 6.78e-06

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 43.13  E-value: 6.78e-06
                          10        20
                  ....*....|....*....|....*.
gi 28893273   219 NLVQHQRTHTGEKPYKCTECEKAFTQ 244
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
388-411 7.62e-06

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 43.13  E-value: 7.62e-06
                          10        20
                  ....*....|....*....|....
gi 28893273   388 LLRHQRTHTGERPYKCPECGKSFS 411
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFK 25
zf-H2C2_2 pfam13465
Zinc-finger double domain;
191-215 1.35e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 42.36  E-value: 1.35e-05
                          10        20
                  ....*....|....*....|....*
gi 28893273   191 HLVQHQRTHTGEKPYKCPDCGKCFS 215
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFK 25
zf-H2C2_2 pfam13465
Zinc-finger double domain;
444-468 2.75e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 41.59  E-value: 2.75e-05
                          10        20
                  ....*....|....*....|....*
gi 28893273   444 LIRHQRIHTGEKPYKCSDCGKSFIR 468
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
275-298 4.28e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 41.20  E-value: 4.28e-05
                          10        20
                  ....*....|....*....|....
gi 28893273   275 DLIQHQATHTGEKPYKCPECGKRF 298
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSF 24
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 485-507 4.90e-05

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: 40.75  E-value: 4.90e-05
                          10        20
                  ....*....|....*....|...
gi 28893273   485 YKCPECGKSFSQSSNLITHVRTH 507
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 457-479 7.04e-05

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: 7.04e-05
                          10        20
                  ....*....|....*....|...
gi 28893273   457 YKCSDCGKSFIRSSHLIQHRRTH 479
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
331-354 8.66e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 40.05  E-value: 8.66e-05
                          10        20
                  ....*....|....*....|....
gi 28893273   331 ELTQHQRTHTGEKPYECLECGKSF 354
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSF 24
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
122-331 1.21e-04

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 45.46  E-value: 1.21e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28893273 122 NSTPVVTASEPSLRELVQGRPSGAEKPYICNECGKSFSQWSKLLRHQR--IHTGERPNTCSE----CGKSFTQSSHLVQH 195
Cdd:COG5048 263 SSLPTASSQSSSPNESDSSSEKGFSLPIKSKQCNISFSRSSPLTRHLRsvNHSGESLKPFSCpyslCGKLFSRNDALKRH 342

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28893273 196 QRTHTGEKPYKCPdcgkcfswssnLVQHQRTHTGEKPYKCTECEKAFTQSTNLIKHQRSHTGekpykcgeCRRAFYRSSD 275
Cdd:COG5048 343 ILLHTSISPAKEK-----------LLNSSSKFSPLLNNEPPQSLQQYKDLKNDKKSETLSNS--------CIRNFKRDSN 403

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 28893273 276 LIQHQATHTGEKP--YKCPECGKRFGQNHNLLKHQKIHAGEKPYRCTECGKSFIQSSE 331
Cdd:COG5048 404 LSLHIITHLSFRPynCKNPPCSKSFNRHYNLIPHKKIHTNHAPLLCSILKSFRRDLDL 461
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 401-423 1.30e-04

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: 1.30e-04
                          10        20
                  ....*....|....*....|...
gi 28893273   401 YKCPECGKSFSVSSNLINHQRIH 423
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 317-339 1.86e-04

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: 1.86e-04
                          10        20
                  ....*....|....*....|...
gi 28893273   317 YRCTECGKSFIQSSELTQHQRTH 339
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
303-328 2.18e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.89  E-value: 2.18e-04
                          10        20
                  ....*....|....*....|....*.
gi 28893273   303 NLLKHQKIHAGEKPYRCTECGKSFIQ 328
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 149-171 2.57e-04

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: 2.57e-04
                          10        20
                  ....*....|....*....|...
gi 28893273   149 YICNECGKSFSQWSKLLRHQRIH 171
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
247-272 6.16e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 37.74  E-value: 6.16e-04
                          10        20
                  ....*....|....*....|....*.
gi 28893273   247 NLIKHQRSHTGEKPYKCGECRRAFYR 272
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
SUF4-like cd20908
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
 455-506 6.20e-04

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: 6.20e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 28893273 455 KPYkCSDCGKSFIRSSHLIQHRRTHTgekpYKCPECGKSFSQSSNLITHVRT 506
Cdd:cd20908   1 KPW-CYYCDREFDDEKILIQHQKAKH----FKCHICHKKLYTAGGLAVHCLQ 47
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 178-199 7.92e-04

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 28893273   178 TCSECGKSFTQSSHLVQHQRTH 199
Cdd:pfam00096   2 KCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 289-311 8.08e-04

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: 8.08e-04
                          10        20
                  ....*....|....*....|...
gi 28893273   289 YKCPECGKRFGQNHNLLKHQKIH 311
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 233-255 8.74e-04

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: 8.74e-04
                          10        20
                  ....*....|....*....|...
gi 28893273   233 YKCTECEKAFTQSTNLIKHQRSH 255
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 345-367 1.17e-03

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: 1.17e-03
                          10        20
                  ....*....|....*....|...
gi 28893273   345 YECLECGKSFGHSSTLIKHQRTH 367
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 373-395 1.43e-03

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: 1.43e-03
                          10        20
                  ....*....|....*....|...
gi 28893273   373 FKCPVCGKTFTLSATLLRHQRTH 395
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
287-594 1.55e-03

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 41.99  E-value: 1.55e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28893273 287 KPYKCPECGKRFGQNHNLLKHQKIHAGEKPYRCT--ECGKSFIQSSELTQHQRTHTGEKPYECLECGKS--FGHSSTLIK 362
Cdd:COG5048  32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSysGCDKSFSRPLELSRHLRTHHNNPSDLNSKSLPLsnSKASSSSLS 111

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28893273 363 HQRTHLReDPFKCPVCGKTFTLSATLLRHQRTHTGERPYKCPECGKSFSVSSNLINHQRIHRGERPyicadcGKSFIMSS 442
Cdd:COG5048 112 SSSSNSN-DNNLLSSHSLPPSSRDPQLPDLLSISNLRNNPLPGNNSSSVNTPQSNSLHPPLPANSL------SKDPSSNL 184

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28893273 443 TLIRHQRIHTGEKPYKCSDCGKSFIRSSHLIQHRRTHTGEKPYKCPECGKSFSQSSNLITHVRTHMDENLFVCSDCGKAF 522
Cdd:COG5048 185 SLLISSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLSSSDSSSSASESPRSS 264

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 28893273 523 LEAQELEQHRVIHergktparraqgdslLGFGDPALMTpppgaKPHKCLVCGKGFNDEGIFMQHQR--IHIGEN 594
Cdd:COG5048 265 LPTASSQSSSPNE---------------SDSSSEKGFS-----LPIKSKQCNISFSRSSPLTRHLRsvNHSGES 318
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 205-227 1.84e-03

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: 1.84e-03
                          10        20
                  ....*....|....*....|...
gi 28893273   205 YKCPDCGKCFSWSSNLVQHQRTH 227
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
SUF4-like cd20908
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
 343-383 2.05e-03

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: 2.05e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|..
gi 28893273 343 KPYeCLECGKSFGHSSTLIKHQR-THlredpFKCPVCGKTFT 383
Cdd:cd20908   1 KPW-CYYCDREFDDEKILIQHQKaKH-----FKCHICHKKLY 36
SUF4-like cd20908
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
 179-223 2.07e-03

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: 2.07e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*
gi 28893273 179 CSECGKSFTQSSHLVQHQRTHTgekpYKCPDCGKCFSWSSNLVQH 223
Cdd:cd20908   4 CYYCDREFDDEKILIQHQKAKH----FKCHICHKKLYTAGGLAVH 44
SUF4-like cd20908
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
 374-424 2.13e-03

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: 2.13e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 28893273 374 KCPVCGKTFTLSATLLRHQRTHTgerpYKCPECGKSFSVSSNLINH-QRIHR 424
Cdd:cd20908   3 WCYYCDREFDDEKILIQHQKAKH----FKCHICHKKLYTAGGLAVHcLQVHK 50
zf-H2C2_2 pfam13465
Zinc-finger double domain;
164-188 2.25e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.20  E-value: 2.25e-03
                          10        20
                  ....*....|....*....|....*
gi 28893273   164 LLRHQRIHTGERPNTCSECGKSFTQ 188
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
360-383 2.41e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.20  E-value: 2.41e-03
                          10        20
                  ....*....|....*....|....
gi 28893273   360 LIKHQRTHLREDPFKCPVCGKTFT 383
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFK 25
transpos_IS1 NF033558
IS1 family transposase; Proteins of this family are DDE transposases encoded by the IS1 family ...
 291-327 2.43e-03

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: 2.43e-03
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 28893273  291 CPECgkrfgQNHNLLKHQKIHAGEKPYRCTECGKSFI 327
Cdd:NF033558   1 CPRC-----QSDNVVKNGKSVRGKQRYRCKDCGRQFQ 32
zf-Di19 pfam05605
Drought induced 19 protein (Di19), zinc-binding; This family consists of several drought ...
 373-425 3.52e-03

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: 3.52e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 28893273   373 FKCPVCGKTFTLsATLLRH-QRTHTGE-RPYKCPECGKsfSVSSNLINHQRIHRG 425
Cdd:pfam05605   3 FTCPFCGEDFDV-VSLCEHvEDEHPVEsKNVVCPVCAA--KVGKDMIGHLTLQHG 54
PHA00733 PHA00733
hypothetical protein
 372-419 3.79e-03

hypothetical protein


Pssm-ID: 177301  Cd Length: 128  Bit Score: 38.32  E-value: 3.79e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 28893273  372 PFKCPVCGKTFTLSATLLRHQRthTGERPYKCPECGKSFSVSSNLINH 419
Cdd:PHA00733  73 PYVCPLCLMPFSSSVSLKQHIR--YTEHSKVCPVCGKEFRNTDSTLDH 118
PHA00733 PHA00733
hypothetical protein
 344-391 4.21e-03

hypothetical protein


Pssm-ID: 177301  Cd Length: 128  Bit Score: 38.32  E-value: 4.21e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 28893273  344 PYECLECGKSFGHSSTLIKHQRthLREDPFKCPVCGKTFTLSATLLRH 391
Cdd:PHA00733  73 PYVCPLCLMPFSSSVSLKQHIR--YTEHSKVCPVCGKEFRNTDSTLDH 118
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 429-451 4.37e-03

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: 4.37e-03
                          10        20
                  ....*....|....*....|...
gi 28893273   429 YICADCGKSFIMSSTLIRHQRIH 451
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
InsA COG3677
Transposase InsA [Mobilome: prophages, transposons];
358-419 4.42e-03

Transposase InsA [Mobilome: prophages, transposons];


Pssm-ID: 442893 [Multi-domain]  Cd Length: 241  Bit Score: 39.85  E-value: 4.42e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 28893273 358 STLIKHQRTHLREDPFKCPVCGktftlSATLLRHQRTHTGERPYKCPECGKSFSVSSNLINH 419
Cdd:COG3677   2 STAEELLEQIRWPNGPVCPHCG-----STRIVKNGKTRNGRQRYRCKDCGRTFTVTTGTIFE 58
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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