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Conserved domains on  [gi|149999358|ref|NP_001092752|]
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zinc finger protein 239 isoform a [Homo sapiens]

Protein Classification

C2H2-type zinc finger protein( domain architecture ID 11473500)

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

CATH:  3.30.160.60
Gene Ontology:  GO:0008270|GO:0003677
PubMed:  11179890|12665246|10940247|11361095|22803940
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];
193-393 2.36e-06

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


:

Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 49.69  E-value: 2.36e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149999358 193 DGHPYEKIHTAEKQYECSQCGKNFSQSSELLLHQRDHT-EEKPYKCEQCGKGFTRSSSLLIHQ--AVHTDE--KPYKCDK 267
Cdd:COG5048  247 SLSSSDSSSSASESPRSSLPTASSQSSSPNESDSSSEKgFSLPIKSKQCNISFSRSSPLTRHLrsVNHSGEslKPFSCPY 326

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149999358 268 --CGKGFTRSSSLLIHHAVHTGEKPYKC--DKCGKGFSQSSKLHIHQRVH-----TGEKPYECE--ECGMSFSQRSNLHI 336
Cdd:COG5048  327 slCGKLFSRNDALKRHILLHTSISPAKEklLNSSSKFSPLLNNEPPQSLQqykdlKNDKKSETLsnSCIRNFKRDSNLSL 406

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 149999358 337 HQRVHTGERP--YKCGECGKGFSQSSNLHIHRCIHTGEKPYQCyeCGKGFSQSSDLRIH 393
Cdd:COG5048  407 HIITHLSFRPynCKNPPCSKSFNRHYNLIPHKKIHTNHAPLLC--SILKSFRRDLDLSN 463
zf-H2C2_2 pfam13465
Zinc-finger double domain;
389-414 1.57e-03

Zinc-finger double domain;


:

Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.81  E-value: 1.57e-03
                          10        20
                  ....*....|....*....|....*.
gi 149999358  389 DLRIHLRVHTGEKPYHCGKCGKGFSQ 414
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 431-453 3.50e-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: 34.97  E-value: 3.50e-03
                          10        20
                  ....*....|....*....|...
gi 149999358  431 YECSKCGKGFSQSSNLHIHQRVH 453
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
418-442 4.40e-03

Zinc-finger double domain;


:

Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 34.65  E-value: 4.40e-03
                          10        20
                  ....*....|....*....|....*
gi 149999358  418 LLIHQRVHTGEKPYECSKCGKGFSQ 442
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 26
 
Name Accession Description Interval E-value
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
193-393 2.36e-06

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 49.69  E-value: 2.36e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149999358 193 DGHPYEKIHTAEKQYECSQCGKNFSQSSELLLHQRDHT-EEKPYKCEQCGKGFTRSSSLLIHQ--AVHTDE--KPYKCDK 267
Cdd:COG5048  247 SLSSSDSSSSASESPRSSLPTASSQSSSPNESDSSSEKgFSLPIKSKQCNISFSRSSPLTRHLrsVNHSGEslKPFSCPY 326

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149999358 268 --CGKGFTRSSSLLIHHAVHTGEKPYKC--DKCGKGFSQSSKLHIHQRVH-----TGEKPYECE--ECGMSFSQRSNLHI 336
Cdd:COG5048  327 slCGKLFSRNDALKRHILLHTSISPAKEklLNSSSKFSPLLNNEPPQSLQqykdlKNDKKSETLsnSCIRNFKRDSNLSL 406

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 149999358 337 HQRVHTGERP--YKCGECGKGFSQSSNLHIHRCIHTGEKPYQCyeCGKGFSQSSDLRIH 393
Cdd:COG5048  407 HIITHLSFRPynCKNPPCSKSFNRHYNLIPHKKIHTNHAPLLC--SILKSFRRDLDLSN 463
zf-H2C2_2 pfam13465
Zinc-finger double domain;
389-414 1.57e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.81  E-value: 1.57e-03
                          10        20
                  ....*....|....*....|....*.
gi 149999358  389 DLRIHLRVHTGEKPYHCGKCGKGFSQ 414
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
309-330 2.19e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.42  E-value: 2.19e-03
                          10        20
                  ....*....|....*....|..
gi 149999358  309 HQRVHTGEKPYECEECGMSFSQ 330
Cdd:pfam13465   5 HMRTHTGEKPYKCPECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 431-453 3.50e-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: 34.97  E-value: 3.50e-03
                          10        20
                  ....*....|....*....|...
gi 149999358  431 YECSKCGKGFSQSSNLHIHQRVH 453
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
418-442 4.40e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 34.65  E-value: 4.40e-03
                          10        20
                  ....*....|....*....|....*
gi 149999358  418 LLIHQRVHTGEKPYECSKCGKGFSQ 442
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 26
SUF4-like cd20908
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
 209-257 8.10e-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: 35.22  E-value: 8.10e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 149999358 209 CSQCGKNFSQSSELLLHQRDHTeekpYKCEQCGKGFTRSSSLLIH-QAVH 257
Cdd:cd20908    4 CYYCDREFDDEKILIQHQKAKH----FKCHICHKKLYTAGGLAVHcLQVH 49
 
Name Accession Description Interval E-value
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
193-393 2.36e-06

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 49.69  E-value: 2.36e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149999358 193 DGHPYEKIHTAEKQYECSQCGKNFSQSSELLLHQRDHT-EEKPYKCEQCGKGFTRSSSLLIHQ--AVHTDE--KPYKCDK 267
Cdd:COG5048  247 SLSSSDSSSSASESPRSSLPTASSQSSSPNESDSSSEKgFSLPIKSKQCNISFSRSSPLTRHLrsVNHSGEslKPFSCPY 326

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149999358 268 --CGKGFTRSSSLLIHHAVHTGEKPYKC--DKCGKGFSQSSKLHIHQRVH-----TGEKPYECE--ECGMSFSQRSNLHI 336
Cdd:COG5048  327 slCGKLFSRNDALKRHILLHTSISPAKEklLNSSSKFSPLLNNEPPQSLQqykdlKNDKKSETLsnSCIRNFKRDSNLSL 406

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 149999358 337 HQRVHTGERP--YKCGECGKGFSQSSNLHIHRCIHTGEKPYQCyeCGKGFSQSSDLRIH 393
Cdd:COG5048  407 HIITHLSFRPynCKNPPCSKSFNRHYNLIPHKKIHTNHAPLLC--SILKSFRRDLDLSN 463
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
178-438 5.93e-05

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 45.46  E-value: 5.93e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149999358 178 PCDHNNCGKILNTSPDGHPYEKIHTAEKQYECSQCGKNFSQSSELLLHQRDHTEEKPYKCEQCGKGFTRSSSLLIHQAVH 257
Cdd:COG5048  170 PLPANSLSKDPSSNLSLLISSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLS 249

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149999358 258 TDEKPYKCDKCG------KGFTRSSSLLIHHAVHTG-EKPYKCDKCGKGFSQSSKLHIHQR--VHTGE--KPYECEE--C 324
Cdd:COG5048  250 SSDSSSSASESPrsslptASSQSSSPNESDSSSEKGfSLPIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCPYslC 329

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149999358 325 GMSFSQRSNLHIHQRVHTGERPYKC--GECGKGFSQSSN-----LHIHRCIHTGEKPYQC--YECGKGFSQSSDLRIHLR 395
Cdd:COG5048  330 GKLFSRNDALKRHILLHTSISPAKEklLNSSSKFSPLLNneppqSLQQYKDLKNDKKSETlsNSCIRNFKRDSNLSLHII 409

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 149999358 396 VHTGEKPYHC--GKCGKGFSQSSKLLIHQRVHTGEKPYECSKCGK 438
Cdd:COG5048  410 THLSFRPYNCknPPCSKSFNRHYNLIPHKKIHTNHAPLLCSILKS 454
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
200-453 8.53e-04

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 41.61  E-value: 8.53e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149999358 200 IHTAEKQYECSQ--CGKNFSQSSELLLHQRDHTEEKPYKCEQCGKG--FTRSSSLLIHQAVHTDeKPYKCDKCGKGFTRS 275
Cdd:COG5048   55 SHTGEKPSQCSYsgCDKSFSRPLELSRHLRTHHNNPSDLNSKSLPLsnSKASSSSLSSSSSNSN-DNNLLSSHSLPPSSR 133

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149999358 276 SSLLIHHAVHTGEKPYKCDKCGKGFSQSSK----------------------LHIHQRVHTGEKPYECEECGMSFSQRSN 333
Cdd:COG5048  134 DPQLPDLLSISNLRNNPLPGNNSSSVNTPQsnslhpplpanslskdpssnlsLLISSNVSTSIPSSSENSPLSSSYSIPS 213

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149999358 334 LHIHQRVHTGERPYKCGECGKGFSQSSNLHIHRCI------HTGEKPYQCYECGKGFSQSSDLRIHLRVHTG-EKPYHCG 406
Cdd:COG5048  214 SSSDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLsssdssSSASESPRSSLPTASSQSSSPNESDSSSEKGfSLPIKSK 293

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 149999358 407 KCGKGFSQSSKLLIHQR--VHTGE--KPYEC--SKCGKGFSQSSNLHIHQRVH 453
Cdd:COG5048  294 QCNISFSRSSPLTRHLRsvNHSGEslKPFSCpySLCGKLFSRNDALKRHILLH 346
zf-H2C2_2 pfam13465
Zinc-finger double domain;
389-414 1.57e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.81  E-value: 1.57e-03
                          10        20
                  ....*....|....*....|....*.
gi 149999358  389 DLRIHLRVHTGEKPYHCGKCGKGFSQ 414
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
309-330 2.19e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.42  E-value: 2.19e-03
                          10        20
                  ....*....|....*....|..
gi 149999358  309 HQRVHTGEKPYECEECGMSFSQ 330
Cdd:pfam13465   5 HMRTHTGEKPYKCPECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 431-453 3.50e-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: 34.97  E-value: 3.50e-03
                          10        20
                  ....*....|....*....|...
gi 149999358  431 YECSKCGKGFSQSSNLHIHQRVH 453
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
221-246 3.84e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 34.65  E-value: 3.84e-03
                          10        20
                  ....*....|....*....|....*.
gi 149999358  221 ELLLHQRDHTEEKPYKCEQCGKGFTR 246
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
289-398 3.91e-03

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 39.68  E-value: 3.91e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149999358 289 KPYKCDKCGKGFSQSSKLHIHQRVHTGEKPYEC--EECGMSFSQRSNLHIHQRVHTGERPYKC-GECGKGFSQSSNLHIH 365
Cdd:COG5048   32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCsySGCDKSFSRPLELSRHLRTHHNNPSDLNsKSLPLSNSKASSSSLS 111

                         90       100       110
                 ....*....|....*....|....*....|...
gi 149999358 366 RCIHTGEKPYQCYECGKGFSQSSDLRIHLRVHT 398
Cdd:COG5048  112 SSSSNSNDNNLLSSHSLPPSSRDPQLPDLLSIS 144
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 319-341 4.39e-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: 34.58  E-value: 4.39e-03
                          10        20
                  ....*....|....*....|...
gi 149999358  319 YECEECGMSFSQRSNLHIHQRVH 341
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
418-442 4.40e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 34.65  E-value: 4.40e-03
                          10        20
                  ....*....|....*....|....*
gi 149999358  418 LLIHQRVHTGEKPYECSKCGKGFSQ 442
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 375-397 5.13e-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: 34.20  E-value: 5.13e-03
                          10        20
                  ....*....|....*....|...
gi 149999358  375 YQCYECGKGFSQSSDLRIHLRVH 397
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
203-451 6.26e-03

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 38.91  E-value: 6.26e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149999358 203 AEKQYECSQCGKNFSQSSELLLHQRDHTEEKPYKC--EQCGKGFTRSSSLLIHQAVHTDEKPYKCDKCGKG--FTRSSSL 278
Cdd:COG5048   30 APRPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCsySGCDKSFSRPLELSRHLRTHHNNPSDLNSKSLPLsnSKASSSS 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149999358 279 LIHHAVHTgEKPYKCDKCGKGFSQSSKLHIHQRVHTGEKPYECEECGMSFSQRSN----------------------LHI 336
Cdd:COG5048  110 LSSSSSNS-NDNNLLSSHSLPPSSRDPQLPDLLSISNLRNNPLPGNNSSSVNTPQsnslhpplpanslskdpssnlsLLI 188

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149999358 337 HQRVHTGERPYKCGECGKGFSQSSNLHIHRCIHTGEKPYQCYECGKGFSQSSDLRIHL------RVHTGEKPYHCGKCGK 410
Cdd:COG5048  189 SSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQSPSslsssdSSSSASESPRSSLPTA 268

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 149999358 411 GFSQSSKLLIHQRVHTG-EKPYECSKCGKGFSQSSNLHIHQR 451
Cdd:COG5048  269 SSQSSSPNESDSSSEKGfSLPIKSKQCNISFSRSSPLTRHLR 310
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 291-313 6.43e-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: 34.20  E-value: 6.43e-03
                          10        20
                  ....*....|....*....|...
gi 149999358  291 YKCDKCGKGFSQSSKLHIHQRVH 313
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
SUF4-like cd20908
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
 209-257 8.10e-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: 35.22  E-value: 8.10e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 149999358 209 CSQCGKNFSQSSELLLHQRDHTeekpYKCEQCGKGFTRSSSLLIH-QAVH 257
Cdd:cd20908    4 CYYCDREFDDEKILIQHQKAKH----FKCHICHKKLYTAGGLAVHcLQVH 49
zf-H2C2_2 pfam13465
Zinc-finger double domain;
337-358 8.51e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 33.88  E-value: 8.51e-03
                          10        20
                  ....*....|....*....|..
gi 149999358  337 HQRVHTGERPYKCGECGKGFSQ 358
Cdd:pfam13465   5 HMRTHTGEKPYKCPECGKSFKS 26
 
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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