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Conserved domains on  [gi|568981800|ref|XP_006516723|]
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zinc finger and SCAN domain-containing protein 12 isoform X1 [Mus musculus]

Protein Classification

C2H2-type zinc finger protein( domain architecture ID 12210811)

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SCAN smart00431
leucine rich region;
42-148 1.12e-62

leucine rich region;


:

Pssm-ID: 128708 [Multi-domain]  Cd Length: 113  Bit Score: 199.84  E-value: 1.12e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981800    42 RDVFRKYFRQFCYQETSGPREALSRLRELCRQWLRPDLNSKEQILELLVLEQFLTILPGELQAWVQEQNPESVEEVVTVL 121
Cdd:smart00431   1 PEIFRQRFRQFRYQETSGPREALSRLRELCRQWLRPELHTKEQILELLVLEQFLTILPGELQAWVREHHPESGEEAVTLL 80

                           90       100
                   ....*....|....*....|....*..
gi 568981800   122 EDLERELDELGYRASVQTEEQVTFQEV 148
Cdd:smart00431  81 EDLERELDEPGQQVSAHVHGQEVLLEK 107
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
231-437 1.69e-06

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


:

Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 50.46  E-value: 1.69e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981800 231 SSGISHEDSQPLRNENGVNSPANSEYAKHQ------SICPGRKVHGCDECGKSFTQHSRLIEHKR--VHTG--DRPYKC- 299
Cdd:COG5048  246 SSLSSSDSSSSASESPRSSLPTASSQSSSPnesdssSEKGFSLPIKSKQCNISFSRSSPLTRHLRsvNHSGesLKPFSCp 325

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981800 300 -EVCGKTFRWRTVLIRHKVVHTGEKPYKCNecgrafgqwsaLNQHQRLHSGEKhyhcNECgkafcqKAGLFHHLKSHRRN 378
Cdd:COG5048  326 ySLCGKLFSRNDALKRHILLHTSISPAKEK-----------LLNSSSKFSPLL----NNE------PPQSLQQYKDLKND 384

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568981800 379 RPYQCL--QCNKSFNRRSTLSQHQGVHTGAKPYECND--CGKAFVYNSSLATHQETHHKEKPF 437
Cdd:COG5048  385 KKSETLsnSCIRNFKRDSNLSLHIITHLSFRPYNCKNppCSKSFNRHYNLIPHKKIHTNHAPL 447
zf-H2C2_2 pfam13465
Zinc-finger double domain;
446-466 6.92e-03

Zinc-finger double domain;


:

Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 34.27  E-value: 6.92e-03
                          10        20
                  ....*....|....*....|.
gi 568981800  446 QRNHTKEKPYKCSVCGKAFIQ 466
Cdd:pfam13465   6 MRTHTGEKPYKCPECGKSFKS 26
 
Name Accession Description Interval E-value
SCAN smart00431
leucine rich region;
42-148 1.12e-62

leucine rich region;


Pssm-ID: 128708 [Multi-domain]  Cd Length: 113  Bit Score: 199.84  E-value: 1.12e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981800    42 RDVFRKYFRQFCYQETSGPREALSRLRELCRQWLRPDLNSKEQILELLVLEQFLTILPGELQAWVQEQNPESVEEVVTVL 121
Cdd:smart00431   1 PEIFRQRFRQFRYQETSGPREALSRLRELCRQWLRPELHTKEQILELLVLEQFLTILPGELQAWVREHHPESGEEAVTLL 80

                           90       100
                   ....*....|....*....|....*..
gi 568981800   122 EDLERELDELGYRASVQTEEQVTFQEV 148
Cdd:smart00431  81 EDLERELDEPGQQVSAHVHGQEVLLEK 107
SCAN pfam02023
SCAN domain; The SCAN domain (named after SRE-ZBP, CTfin51, AW-1 and Number 18 cDNA) is found ...
 43-130 5.64e-48

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: 160.35  E-value: 5.64e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981800   43 DVFRKYFRQFCYQETSGPREALSRLRELCRQWLRPDLNSKEQILELLVLEQFLTILPGELQAWVQEQNPESVEEVVTVLE 122
Cdd:pfam02023   2 EASRQRFRQFCYQEAEGPREALSQLRELCHQWLRPEKHTKEQILELLVLEQFLTILPEEIQSWVREHHPESGEEAVALAE 81


                  ....*...
gi 568981800  123 DLERELDE 130
Cdd:pfam02023  82 DLLLERGE 89
SCAN cd07936
SCAN oligomerization domain; The SCAN domain (named after SRE-ZBP, CTfin51, AW-1 and Number 18 ...
 43-126 5.25e-39

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: 136.62  E-value: 5.25e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981800  43 DVFRKYFRQFCYQETSGPREALSRLRELCRQWLRPDLNSKEQILELLVLEQFLTILPGELQAWVQEQNPESVEEVVTVLE 122
Cdd:cd07936    2 ETYRQRFRAFQYQEASGPREALQRLRELCRQWLRPEIHTKEQILELLVLEQFLIILPPEVQAWVRERKPESGEEAATLAE 81


                 ....
gi 568981800 123 DLER 126
Cdd:cd07936   82 DLLA 85
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
231-437 1.69e-06

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 50.46  E-value: 1.69e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981800 231 SSGISHEDSQPLRNENGVNSPANSEYAKHQ------SICPGRKVHGCDECGKSFTQHSRLIEHKR--VHTG--DRPYKC- 299
Cdd:COG5048  246 SSLSSSDSSSSASESPRSSLPTASSQSSSPnesdssSEKGFSLPIKSKQCNISFSRSSPLTRHLRsvNHSGesLKPFSCp 325

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981800 300 -EVCGKTFRWRTVLIRHKVVHTGEKPYKCNecgrafgqwsaLNQHQRLHSGEKhyhcNECgkafcqKAGLFHHLKSHRRN 378
Cdd:COG5048  326 ySLCGKLFSRNDALKRHILLHTSISPAKEK-----------LLNSSSKFSPLL----NNE------PPQSLQQYKDLKND 384

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568981800 379 RPYQCL--QCNKSFNRRSTLSQHQGVHTGAKPYECND--CGKAFVYNSSLATHQETHHKEKPF 437
Cdd:COG5048  385 KKSETLsnSCIRNFKRDSNLSLHIITHLSFRPYNCKNppCSKSFNRHYNLIPHKKIHTNHAPL 447
SUF4-like cd20908
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
 379-435 5.80e-05

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: 41.39  E-value: 5.80e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 568981800 379 RPYqCLQCNKSFNRRSTLSQHQGvhtgAKPYECNDCGKAFVYNSSLATHQETHHKEK 435
Cdd:cd20908    1 KPW-CYYCDREFDDEKILIQHQK----AKHFKCHICHKKLYTAGGLAVHCLQVHKET 52
zf-H2C2_2 pfam13465
Zinc-finger double domain;
283-306 4.55e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 37.35  E-value: 4.55e-04
                          10        20
                  ....*....|....*....|....
gi 568981800  283 RLIEHKRVHTGDRPYKCEVCGKTF 306
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSF 24
zf-H2C2_2 pfam13465
Zinc-finger double domain;
446-466 6.92e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 34.27  E-value: 6.92e-03
                          10        20
                  ....*....|....*....|.
gi 568981800  446 QRNHTKEKPYKCSVCGKAFIQ 466
Cdd:pfam13465   6 MRTHTGEKPYKCPECGKSFKS 26
 
Name Accession Description Interval E-value
SCAN smart00431
leucine rich region;
42-148 1.12e-62

leucine rich region;


Pssm-ID: 128708 [Multi-domain]  Cd Length: 113  Bit Score: 199.84  E-value: 1.12e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981800    42 RDVFRKYFRQFCYQETSGPREALSRLRELCRQWLRPDLNSKEQILELLVLEQFLTILPGELQAWVQEQNPESVEEVVTVL 121
Cdd:smart00431   1 PEIFRQRFRQFRYQETSGPREALSRLRELCRQWLRPELHTKEQILELLVLEQFLTILPGELQAWVREHHPESGEEAVTLL 80

                           90       100
                   ....*....|....*....|....*..
gi 568981800   122 EDLERELDELGYRASVQTEEQVTFQEV 148
Cdd:smart00431  81 EDLERELDEPGQQVSAHVHGQEVLLEK 107
SCAN pfam02023
SCAN domain; The SCAN domain (named after SRE-ZBP, CTfin51, AW-1 and Number 18 cDNA) is found ...
 43-130 5.64e-48

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: 160.35  E-value: 5.64e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981800   43 DVFRKYFRQFCYQETSGPREALSRLRELCRQWLRPDLNSKEQILELLVLEQFLTILPGELQAWVQEQNPESVEEVVTVLE 122
Cdd:pfam02023   2 EASRQRFRQFCYQEAEGPREALSQLRELCHQWLRPEKHTKEQILELLVLEQFLTILPEEIQSWVREHHPESGEEAVALAE 81


                  ....*...
gi 568981800  123 DLERELDE 130
Cdd:pfam02023  82 DLLLERGE 89
SCAN cd07936
SCAN oligomerization domain; The SCAN domain (named after SRE-ZBP, CTfin51, AW-1 and Number 18 ...
 43-126 5.25e-39

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: 136.62  E-value: 5.25e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981800  43 DVFRKYFRQFCYQETSGPREALSRLRELCRQWLRPDLNSKEQILELLVLEQFLTILPGELQAWVQEQNPESVEEVVTVLE 122
Cdd:cd07936    2 ETYRQRFRAFQYQEASGPREALQRLRELCRQWLRPEIHTKEQILELLVLEQFLIILPPEVQAWVRERKPESGEEAATLAE 81


                 ....
gi 568981800 123 DLER 126
Cdd:cd07936   82 DLLA 85
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
231-437 1.69e-06

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 50.46  E-value: 1.69e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981800 231 SSGISHEDSQPLRNENGVNSPANSEYAKHQ------SICPGRKVHGCDECGKSFTQHSRLIEHKR--VHTG--DRPYKC- 299
Cdd:COG5048  246 SSLSSSDSSSSASESPRSSLPTASSQSSSPnesdssSEKGFSLPIKSKQCNISFSRSSPLTRHLRsvNHSGesLKPFSCp 325

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981800 300 -EVCGKTFRWRTVLIRHKVVHTGEKPYKCNecgrafgqwsaLNQHQRLHSGEKhyhcNECgkafcqKAGLFHHLKSHRRN 378
Cdd:COG5048  326 ySLCGKLFSRNDALKRHILLHTSISPAKEK-----------LLNSSSKFSPLL----NNE------PPQSLQQYKDLKND 384

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568981800 379 RPYQCL--QCNKSFNRRSTLSQHQGVHTGAKPYECND--CGKAFVYNSSLATHQETHHKEKPF 437
Cdd:COG5048  385 KKSETLsnSCIRNFKRDSNLSLHIITHLSFRPYNCKNppCSKSFNRHYNLIPHKKIHTNHAPL 447
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
378-458 1.89e-05

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 47.00  E-value: 1.89e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981800 378 NRPYQCLQCNKSFNRRSTLSQHQGVHTGAKPYECND--CGKAFVYNSSLATHQETHHKEKPFTQSgpiqQQRNHTKEKPY 455
Cdd:COG5048   31 PRPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYsgCDKSFSRPLELSRHLRTHHNNPSDLNS----KSLPLSNSKAS 106


                 ...
gi 568981800 456 KCS 458
Cdd:COG5048  107 SSS 109
SUF4-like cd20908
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
 379-435 5.80e-05

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: 41.39  E-value: 5.80e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 568981800 379 RPYqCLQCNKSFNRRSTLSQHQGvhtgAKPYECNDCGKAFVYNSSLATHQETHHKEK 435
Cdd:cd20908    1 KPW-CYYCDREFDDEKILIQHQK----AKHFKCHICHKKLYTAGGLAVHCLQVHKET 52
SFP1 COG5189
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ...
 405-464 3.31e-04

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


Pssm-ID: 227516 [Multi-domain]  Cd Length: 423  Bit Score: 43.17  E-value: 3.31e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568981800 405 GAKPYECN--DCGKAFVYNSSLATHQ-ETHHKEKPFTQSGPIQQQRNHTKEKPYKCSVCGKAF 464
Cdd:COG5189  346 DGKPYKCPveGCNKKYKNQNGLKYHMlHGHQNQKLHENPSPEKMNIFSAKDKPYRCEVCDKRY 408
zf-H2C2_2 pfam13465
Zinc-finger double domain;
283-306 4.55e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 37.35  E-value: 4.55e-04
                          10        20
                  ....*....|....*....|....
gi 568981800  283 RLIEHKRVHTGDRPYKCEVCGKTF 306
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSF 24
zf-H2C2_2 pfam13465
Zinc-finger double domain;
339-362 4.88e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 37.35  E-value: 4.88e-04
                          10        20
                  ....*....|....*....|....
gi 568981800  339 ALNQHQRLHSGEKHYHCNECGKAF 362
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSF 24
SUF4-like cd20908
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
 323-378 6.39e-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: 38.69  E-value: 6.39e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 568981800 323 KPYkCNECGRAFGQWSALNQHQRlhsgEKHYHCNECGKAFCQKAGLFHH-LKSHRRN 378
Cdd:cd20908    1 KPW-CYYCDREFDDEKILIQHQK----AKHFKCHICHKKLYTAGGLAVHcLQVHKET 52
zf-H2C2_2 pfam13465
Zinc-finger double domain;
312-334 7.37e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.97  E-value: 7.37e-04
                          10        20
                  ....*....|....*....|...
gi 568981800  312 LIRHKVVHTGEKPYKCNECGRAF 334
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSF 24
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 325-347 2.00e-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: 35.74  E-value: 2.00e-03
                          10        20
                  ....*....|....*....|...
gi 568981800  325 YKCNECGRAFGQWSALNQHQRLH 347
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 409-431 3.40e-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: 3.40e-03
                          10        20
                  ....*....|....*....|...
gi 568981800  409 YECNDCGKAFVYNSSLATHQETH 431
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 353-375 5.44e-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: 5.44e-03
                          10        20
                  ....*....|....*....|...
gi 568981800  353 YHCNECGKAFCQKAGLFHHLKSH 375
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
446-466 6.92e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 34.27  E-value: 6.92e-03
                          10        20
                  ....*....|....*....|.
gi 568981800  446 QRNHTKEKPYKCSVCGKAFIQ 466
Cdd:pfam13465   6 MRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
396-420 6.98e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 34.27  E-value: 6.98e-03
                          10        20
                  ....*....|....*....|....*
gi 568981800  396 LSQHQGVHTGAKPYECNDCGKAFVY 420
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 26
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
323-438 8.14e-03

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 38.52  E-value: 8.14e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981800 323 KPYKCNECGRAFGQWSALNQHQRLHSGEKHYHCNECGKAfcQKAGLFHHLKSHRRNRPYQclqcnksfNRRSTLSQHQGV 402
Cdd:COG5048   32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYSGCD--KSFSRPLELSRHLRTHHNN--------PSDLNSKSLPLS 101

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 568981800 403 HTGAKPYECNDCGKAFVYNSSLATHQETHHKEKPFT 438
Cdd:COG5048  102 NSKASSSSLSSSSSNSNDNNLLSSHSLPPSSRDPQL 137
 
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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