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Conserved domains on  [gi|767940688|ref|XP_011513180|]
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zinc finger and SCAN domain-containing protein 9 isoform X4 [Homo sapiens]

Protein Classification

SCAN and COG5048 domain-containing protein( domain architecture ID 12210801)

SCAN and COG5048 domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SCAN smart00431
leucine rich region;
180-292 5.78e-66

leucine rich region;


:

Pssm-ID: 128708 [Multi-domain]  Cd Length: 113  Bit Score: 209.08  E-value: 5.78e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940688   180 REIFRRHFRQLCYQETPGPREALTRLQELCYQWLRPHVSTKEQILDLLVLEQFLSILPKELQGWVREHCPESGEEAVILL 259
Cdd:smart00431   1 PEIFRQRFRQFRYQETSGPREALSRLRELCRQWLRPELHTKEQILELLVLEQFLTILPGELQAWVREHHPESGEEAVTLL 80

                           90       100       110
                   ....*....|....*....|....*....|...
gi 767940688   260 EDLERELDEPQHEMVAHRHRQEVLCKEMVPLAE 292
Cdd:smart00431  81 EDLERELDEPGQQVSAHVHGQEVLLEKMVPLGA 113
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
385-521 1.36e-11

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


:

Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 66.64  E-value: 1.36e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940688 385 QHKCDECGKSFTQSSGLIRHQR--IHTGE--RPYECNE--CGKAFSRSSGLFNHRGIHNIQKRYHCK--ECGKVFSQ--- 453
Cdd:COG5048  289 PIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCPYslCGKLFSRNDALKRHILLHTSISPAKEKllNSSSKFSPlln 368

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767940688 454 --SAGLIQHQRIHKGEKPYQC--SQCSKSYSRRSFLIEHQRSHTGERPHQC--IECGKSFNRHCNLIRHQKIHT 521
Cdd:COG5048  369 nePPQSLQQYKDLKNDKKSETlsNSCIRNFKRDSNLSLHIITHLSFRPYNCknPPCSKSFNRHYNLIPHKKIHT 442
 
Name Accession Description Interval E-value
SCAN smart00431
leucine rich region;
180-292 5.78e-66

leucine rich region;


Pssm-ID: 128708 [Multi-domain]  Cd Length: 113  Bit Score: 209.08  E-value: 5.78e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940688   180 REIFRRHFRQLCYQETPGPREALTRLQELCYQWLRPHVSTKEQILDLLVLEQFLSILPKELQGWVREHCPESGEEAVILL 259
Cdd:smart00431   1 PEIFRQRFRQFRYQETSGPREALSRLRELCRQWLRPELHTKEQILELLVLEQFLTILPGELQAWVREHHPESGEEAVTLL 80

                           90       100       110
                   ....*....|....*....|....*....|...
gi 767940688   260 EDLERELDEPQHEMVAHRHRQEVLCKEMVPLAE 292
Cdd:smart00431  81 EDLERELDEPGQQVSAHVHGQEVLLEKMVPLGA 113
SCAN pfam02023
SCAN domain; The SCAN domain (named after SRE-ZBP, CTfin51, AW-1 and Number 18 cDNA) is found ...
 181-268 1.49e-47

SCAN domain; The SCAN domain (named after SRE-ZBP, CTfin51, AW-1 and Number 18 cDNA) is found in several pfam00096 proteins. The domain has been shown to be able to mediate homo- and hetero-oligomerization.


Pssm-ID: 460417 [Multi-domain]  Cd Length: 89  Bit Score: 159.96  E-value: 1.49e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940688  181 EIFRRHFRQLCYQETPGPREALTRLQELCYQWLRPHVSTKEQILDLLVLEQFLSILPKELQGWVREHCPESGEEAVILLE 260
Cdd:pfam02023   2 EASRQRFRQFCYQEAEGPREALSQLRELCHQWLRPEKHTKEQILELLVLEQFLTILPEEIQSWVREHHPESGEEAVALAE 81


                  ....*...
gi 767940688  261 DLERELDE 268
Cdd:pfam02023  82 DLLLERGE 89
SCAN cd07936
SCAN oligomerization domain; The SCAN domain (named after SRE-ZBP, CTfin51, AW-1 and Number 18 ...
 181-264 1.75e-36

SCAN oligomerization domain; The SCAN domain (named after SRE-ZBP, CTfin51, AW-1 and Number 18 cDNA) is found in several vertebrate proteins that contain C2H2 zinc finger motifs, many of which may be transcription factors playing roles in cell survival and differentiation. This protein-interaction domain is able to mediate homo- and hetero-oligomerization of SCAN-containing proteins. Some SCAN-containing proteins, including those of lower vertebrates, do not contain zinc finger motifs. It has been noted that the SCAN domain resembles a domain-swapped version of the C-terminal domain of the HIV capsid protein. This domain model features elements common to the three general groups of SCAN domains (SCAN-A1, SCAN-A2, and SCAN-B). The SCAND1 protein is truncated at the C-terminus with respect to this model, the SCAND2 protein appears to have a truncated central helix.


Pssm-ID: 153421  Cd Length: 85  Bit Score: 130.07  E-value: 1.75e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940688 181 EIFRRHFRQLCYQETPGPREALTRLQELCYQWLRPHVSTKEQILDLLVLEQFLSILPKELQGWVREHCPESGEEAVILLE 260
Cdd:cd07936    2 ETYRQRFRAFQYQEASGPREALQRLRELCRQWLRPEIHTKEQILELLVLEQFLIILPPEVQAWVRERKPESGEEAATLAE 81


                 ....
gi 767940688 261 DLER 264
Cdd:cd07936   82 DLLA 85
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
385-521 1.36e-11

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 66.64  E-value: 1.36e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940688 385 QHKCDECGKSFTQSSGLIRHQR--IHTGE--RPYECNE--CGKAFSRSSGLFNHRGIHNIQKRYHCK--ECGKVFSQ--- 453
Cdd:COG5048  289 PIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCPYslCGKLFSRNDALKRHILLHTSISPAKEKllNSSSKFSPlln 368

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767940688 454 --SAGLIQHQRIHKGEKPYQC--SQCSKSYSRRSFLIEHQRSHTGERPHQC--IECGKSFNRHCNLIRHQKIHT 521
Cdd:COG5048  369 nePPQSLQQYKDLKNDKKSETlsNSCIRNFKRDSNLSLHIITHLSFRPYNCknPPCSKSFNRHYNLIPHKKIHT 442
zf-H2C2_2 pfam13465
Zinc-finger double domain;
401-425 9.84e-06

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 42.36  E-value: 9.84e-06
                          10        20
                  ....*....|....*....|....*
gi 767940688  401 LIRHQRIHTGERPYECNECGKAFSR 425
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 26
SUF4-like cd20908
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
 386-432 3.70e-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: 36.38  E-value: 3.70e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 767940688 386 HKCDECGKSFTQSSGLIRHQRIHTgerpYECNECGKAFSRSSGLFNH 432
Cdd:cd20908    2 PWCYYCDREFDDEKILIQHQKAKH----FKCHICHKKLYTAGGLAVH 44
 
Name Accession Description Interval E-value
SCAN smart00431
leucine rich region;
180-292 5.78e-66

leucine rich region;


Pssm-ID: 128708 [Multi-domain]  Cd Length: 113  Bit Score: 209.08  E-value: 5.78e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940688   180 REIFRRHFRQLCYQETPGPREALTRLQELCYQWLRPHVSTKEQILDLLVLEQFLSILPKELQGWVREHCPESGEEAVILL 259
Cdd:smart00431   1 PEIFRQRFRQFRYQETSGPREALSRLRELCRQWLRPELHTKEQILELLVLEQFLTILPGELQAWVREHHPESGEEAVTLL 80

                           90       100       110
                   ....*....|....*....|....*....|...
gi 767940688   260 EDLERELDEPQHEMVAHRHRQEVLCKEMVPLAE 292
Cdd:smart00431  81 EDLERELDEPGQQVSAHVHGQEVLLEKMVPLGA 113
SCAN pfam02023
SCAN domain; The SCAN domain (named after SRE-ZBP, CTfin51, AW-1 and Number 18 cDNA) is found ...
 181-268 1.49e-47

SCAN domain; The SCAN domain (named after SRE-ZBP, CTfin51, AW-1 and Number 18 cDNA) is found in several pfam00096 proteins. The domain has been shown to be able to mediate homo- and hetero-oligomerization.


Pssm-ID: 460417 [Multi-domain]  Cd Length: 89  Bit Score: 159.96  E-value: 1.49e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940688  181 EIFRRHFRQLCYQETPGPREALTRLQELCYQWLRPHVSTKEQILDLLVLEQFLSILPKELQGWVREHCPESGEEAVILLE 260
Cdd:pfam02023   2 EASRQRFRQFCYQEAEGPREALSQLRELCHQWLRPEKHTKEQILELLVLEQFLTILPEEIQSWVREHHPESGEEAVALAE 81


                  ....*...
gi 767940688  261 DLERELDE 268
Cdd:pfam02023  82 DLLLERGE 89
SCAN cd07936
SCAN oligomerization domain; The SCAN domain (named after SRE-ZBP, CTfin51, AW-1 and Number 18 ...
 181-264 1.75e-36

SCAN oligomerization domain; The SCAN domain (named after SRE-ZBP, CTfin51, AW-1 and Number 18 cDNA) is found in several vertebrate proteins that contain C2H2 zinc finger motifs, many of which may be transcription factors playing roles in cell survival and differentiation. This protein-interaction domain is able to mediate homo- and hetero-oligomerization of SCAN-containing proteins. Some SCAN-containing proteins, including those of lower vertebrates, do not contain zinc finger motifs. It has been noted that the SCAN domain resembles a domain-swapped version of the C-terminal domain of the HIV capsid protein. This domain model features elements common to the three general groups of SCAN domains (SCAN-A1, SCAN-A2, and SCAN-B). The SCAND1 protein is truncated at the C-terminus with respect to this model, the SCAND2 protein appears to have a truncated central helix.


Pssm-ID: 153421  Cd Length: 85  Bit Score: 130.07  E-value: 1.75e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940688 181 EIFRRHFRQLCYQETPGPREALTRLQELCYQWLRPHVSTKEQILDLLVLEQFLSILPKELQGWVREHCPESGEEAVILLE 260
Cdd:cd07936    2 ETYRQRFRAFQYQEASGPREALQRLRELCRQWLRPEIHTKEQILELLVLEQFLIILPPEVQAWVRERKPESGEEAATLAE 81


                 ....
gi 767940688 261 DLER 264
Cdd:cd07936   82 DLLA 85
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
385-521 1.36e-11

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 66.64  E-value: 1.36e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940688 385 QHKCDECGKSFTQSSGLIRHQR--IHTGE--RPYECNE--CGKAFSRSSGLFNHRGIHNIQKRYHCK--ECGKVFSQ--- 453
Cdd:COG5048  289 PIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCPYslCGKLFSRNDALKRHILLHTSISPAKEKllNSSSKFSPlln 368

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767940688 454 --SAGLIQHQRIHKGEKPYQC--SQCSKSYSRRSFLIEHQRSHTGERPHQC--IECGKSFNRHCNLIRHQKIHT 521
Cdd:COG5048  369 nePPQSLQQYKDLKNDKKSETlsNSCIRNFKRDSNLSLHIITHLSFRPYNCknPPCSKSFNRHYNLIPHKKIHT 442
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
385-520 3.27e-06

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 49.69  E-value: 3.27e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940688 385 QHKCDECGKSFTQSSGLIRHQRIHTGERPYECNECGKAFSRSSGLFNHRG---IHNIQKRYHCKECGKVFSQSAGLIQHQ 461
Cdd:COG5048   33 PDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYSGCDKSFSRPLELSRHlrtHHNNPSDLNSKSLPLSNSKASSSSLSS 112

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767940688 462 RIHKGEKPYQCSQCSKSYSRRSFLIEHQRSHTGERPHQCIECGKSFNRH--CNLIRHQKIH 520
Cdd:COG5048  113 SSSNSNDNNLLSSHSLPPSSRDPQLPDLLSISNLRNNPLPGNNSSSVNTpqSNSLHPPLPA 173
zf-H2C2_2 pfam13465
Zinc-finger double domain;
401-425 9.84e-06

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 42.36  E-value: 9.84e-06
                          10        20
                  ....*....|....*....|....*
gi 767940688  401 LIRHQRIHTGERPYECNECGKAFSR 425
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
485-509 3.84e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 40.43  E-value: 3.84e-05
                          10        20
                  ....*....|....*....|....*
gi 767940688  485 LIEHQRSHTGERPHQCIECGKSFNR 509
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 386-408 9.18e-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: 39.59  E-value: 9.18e-05
                          10        20
                  ....*....|....*....|...
gi 767940688  386 HKCDECGKSFTQSSGLIRHQRIH 408
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
376-521 1.09e-04

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 44.69  E-value: 1.09e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940688 376 QWGNLLGEGQHKCDECGKSFTQSSGLIRHQRIHTGERPYECNECGKAFSRSSGLFNHRGIHNIQKRYHCKECGKVFSQSA 455
Cdd:COG5048  189 SSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLSSSDSSSSASESPRSSLPTA 268

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767940688 456 GLIQHQRIHKGE-------KPYQCSQCSKSYSRRSFLIEHQRS--HTGE--RPHQCIE--CGKSFNRHCNLIRHQKIHT 521
Cdd:COG5048  269 SSQSSSPNESDSssekgfsLPIKSKQCNISFSRSSPLTRHLRSvnHSGEslKPFSCPYslCGKLFSRNDALKRHILLHT 347
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
437-498 1.25e-04

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 44.69  E-value: 1.25e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767940688 437 NIQKRYHCKECGKVFSQSAGLIQHQRIHKGEKPYQCSQ--CSKSYSRRSFLIEHQRSHTGERPH 498
Cdd:COG5048   29 NAPRPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYsgCDKSFSRPLELSRHLRTHHNNPSD 92
SFP1 COG5189
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ...
 410-493 1.42e-04

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


Pssm-ID: 227516 [Multi-domain]  Cd Length: 423  Bit Score: 44.32  E-value: 1.42e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940688 410 GERPYECN--ECGKAFSRSSGLfnhrgihniqkRYHCKE--CGKVFSQSAGLIQHQRIHKGEKPYQCSQCSKSYSRRSFL 485
Cdd:COG5189  346 DGKPYKCPveGCNKKYKNQNGL-----------KYHMLHghQNQKLHENPSPEKMNIFSAKDKPYRCEVCDKRYKNLNGL 414


                 ....*...
gi 767940688 486 IEHqRSHT 493
Cdd:COG5189  415 KYH-RKHS 421
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
452-521 1.55e-04

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 44.30  E-value: 1.55e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767940688 452 SQSAGLIQHQRIHKGE----KPYQCSQCSKSYSRRSFLIEHQRSHTGERPHQC--IECGKSFNRHCNLIRHQKIHT 521
Cdd:COG5048   12 NNSVLSSTPKSTLKSLsnapRPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCsySGCDKSFSRPLELSRHLRTHH 87
zf-H2C2_2 pfam13465
Zinc-finger double domain;
457-481 3.04e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.12  E-value: 3.04e-04
                          10        20
                  ....*....|....*....|....*
gi 767940688  457 LIQHQRIHKGEKPYQCSQCSKSYSR 481
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 442-464 9.85e-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: 36.51  E-value: 9.85e-04
                          10        20
                  ....*....|....*....|...
gi 767940688  442 YHCKECGKVFSQSAGLIQHQRIH 464
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
396-492 1.58e-03

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 41.22  E-value: 1.58e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940688 396 TQSSGLIRHQRIHTGE----RPYECNECGKAFSRSSGLFNHRGIHNIQKRYHC--KECGKVFSQSAGLIQHQRIHKGEKP 469
Cdd:COG5048   12 NNSVLSSTPKSTLKSLsnapRPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCsySGCDKSFSRPLELSRHLRTHHNNPS 91

                         90       100
                 ....*....|....*....|....*
gi 767940688 470 YQCSQCSKS--YSRRSFLIEHQRSH 492
Cdd:COG5048   92 DLNSKSLPLsnSKASSSSLSSSSSN 116
SUF4-like cd20908
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
 386-432 3.70e-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: 36.38  E-value: 3.70e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 767940688 386 HKCDECGKSFTQSSGLIRHQRIHTgerpYECNECGKAFSRSSGLFNH 432
Cdd:cd20908    2 PWCYYCDREFDDEKILIQHQKAKH----FKCHICHKKLYTAGGLAVH 44
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 414-436 4.83e-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: 4.83e-03
                          10        20
                  ....*....|....*....|...
gi 767940688  414 YECNECGKAFSRSSGLFNHRGIH 436
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 470-492 6.17e-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: 34.20  E-value: 6.17e-03
                          10        20
                  ....*....|....*....|...
gi 767940688  470 YQCSQCSKSYSRRSFLIEHQRSH 492
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
 
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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