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Conserved domains on  [gi|113866022|ref|NP_001038951|]
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zinc finger protein 180 isoform a [Mus musculus]

Protein Classification

C2H2-type zinc finger protein( domain architecture ID 11473154)

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
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
323-585 4.50e-10

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


:

Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 62.41  E-value: 4.50e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113866022 323 CGKSFSWSSHLIaHQRTHTGEKPYKCNLCGKFFTRSSHVVSHQRIHTGEKPYRCNLCGKSFTQRYVLvvHQRTHTGErPY 402
Cdd:COG5048  177 SKDPSSNLSLLI-SSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLS--QSPSSLSS-SD 252
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113866022 403 ECTQCGKSFRQSYKLIAHQRTH----------TGEKPYECTQCGKSFIQSYKLIAHQ--KIHSGE--KPYECSH--CGKS 466
Cdd:COG5048  253 SSSSASESPRSSLPTASSQSSSpnesdsssekGFSLPIKSKQCNISFSRSSPLTRHLrsVNHSGEslKPFSCPYslCGKL 332
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113866022 467 FSQSYKLVAHQRTHTGEKPFEC--NHCGKSFS-----WSSQLVSHQRTHTGEKPYEC--NECGKSFNRSSHLVMHQRTHT 537
Cdd:COG5048  333 FSRNDALKRHILLHTSISPAKEklLNSSSKFSpllnnEPPQSLQQYKDLKNDKKSETlsNSCIRNFKRDSNLSLHIITHL 412
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 113866022 538 GEKPYQCK--QCGKSFSQSYVLVVHQRTHTGEKPYECGQCGKTFRQSSCF 585
Cdd:COG5048  413 SFRPYNCKnpPCSKSFNRHYNLIPHKKIHTNHAPLLCSILKSFRRDLDLS 462
zf-H2C2_2 pfam13465
Zinc-finger double domain;
587-608 3.92e-04

Zinc-finger double domain;


:

Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.12  E-value: 3.92e-04
                          10        20
                  ....*....|....*....|..
gi 113866022  587 QHQRTHTGEKPYECNQCGKTFS 608
Cdd:pfam13465   4 RHMRTHTGEKPYKCPECGKSFK 25
zf-H2C2_2 pfam13465
Zinc-finger double domain;
612-637 4.82e-04

Zinc-finger double domain;


:

Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 37.74  E-value: 4.82e-04
                          10        20
                  ....*....|....*....|....*.
gi 113866022  612 RLIVHQRTHTGEKPYKCGQCGKAFIS 637
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
 
Name Accession Description Interval E-value
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
323-585 4.50e-10

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 62.41  E-value: 4.50e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113866022 323 CGKSFSWSSHLIaHQRTHTGEKPYKCNLCGKFFTRSSHVVSHQRIHTGEKPYRCNLCGKSFTQRYVLvvHQRTHTGErPY 402
Cdd:COG5048  177 SKDPSSNLSLLI-SSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLS--QSPSSLSS-SD 252
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113866022 403 ECTQCGKSFRQSYKLIAHQRTH----------TGEKPYECTQCGKSFIQSYKLIAHQ--KIHSGE--KPYECSH--CGKS 466
Cdd:COG5048  253 SSSSASESPRSSLPTASSQSSSpnesdsssekGFSLPIKSKQCNISFSRSSPLTRHLrsVNHSGEslKPFSCPYslCGKL 332
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113866022 467 FSQSYKLVAHQRTHTGEKPFEC--NHCGKSFS-----WSSQLVSHQRTHTGEKPYEC--NECGKSFNRSSHLVMHQRTHT 537
Cdd:COG5048  333 FSRNDALKRHILLHTSISPAKEklLNSSSKFSpllnnEPPQSLQQYKDLKNDKKSETlsNSCIRNFKRDSNLSLHIITHL 412
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 113866022 538 GEKPYQCK--QCGKSFSQSYVLVVHQRTHTGEKPYECGQCGKTFRQSSCF 585
Cdd:COG5048  413 SFRPYNCKnpPCSKSFNRHYNLIPHKKIHTNHAPLLCSILKSFRRDLDLS 462
zf-H2C2_2 pfam13465
Zinc-finger double domain;
528-553 1.86e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 41.59  E-value: 1.86e-05
                          10        20
                  ....*....|....*....|....*.
gi 113866022  528 HLVMHQRTHTGEKPYQCKQCGKSFSQ 553
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
SUF4-like cd20908
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
320-368 3.48e-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: 42.54  E-value: 3.48e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 113866022 320 CKYCGKSFSWSSHLIAHQRTHTgekpYKCNLCGKFFTRSSHVVSH-QRIH 368
Cdd:cd20908    4 CYYCDREFDDEKILIQHQKAKH----FKCHICHKKLYTAGGLAVHcLQVH 49
zf-H2C2_2 pfam13465
Zinc-finger double domain;
587-608 3.92e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.12  E-value: 3.92e-04
                          10        20
                  ....*....|....*....|..
gi 113866022  587 QHQRTHTGEKPYECNQCGKTFS 608
Cdd:pfam13465   4 RHMRTHTGEKPYKCPECGKSFK 25
zf-H2C2_2 pfam13465
Zinc-finger double domain;
612-637 4.82e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 37.74  E-value: 4.82e-04
                          10        20
                  ....*....|....*....|....*.
gi 113866022  612 RLIVHQRTHTGEKPYKCGQCGKAFIS 637
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
 
Name Accession Description Interval E-value
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
323-585 4.50e-10

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 62.41  E-value: 4.50e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113866022 323 CGKSFSWSSHLIaHQRTHTGEKPYKCNLCGKFFTRSSHVVSHQRIHTGEKPYRCNLCGKSFTQRYVLvvHQRTHTGErPY 402
Cdd:COG5048  177 SKDPSSNLSLLI-SSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLS--QSPSSLSS-SD 252
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113866022 403 ECTQCGKSFRQSYKLIAHQRTH----------TGEKPYECTQCGKSFIQSYKLIAHQ--KIHSGE--KPYECSH--CGKS 466
Cdd:COG5048  253 SSSSASESPRSSLPTASSQSSSpnesdsssekGFSLPIKSKQCNISFSRSSPLTRHLrsVNHSGEslKPFSCPYslCGKL 332
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113866022 467 FSQSYKLVAHQRTHTGEKPFEC--NHCGKSFS-----WSSQLVSHQRTHTGEKPYEC--NECGKSFNRSSHLVMHQRTHT 537
Cdd:COG5048  333 FSRNDALKRHILLHTSISPAKEklLNSSSKFSpllnnEPPQSLQQYKDLKNDKKSETlsNSCIRNFKRDSNLSLHIITHL 412
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 113866022 538 GEKPYQCK--QCGKSFSQSYVLVVHQRTHTGEKPYECGQCGKTFRQSSCF 585
Cdd:COG5048  413 SFRPYNCKnpPCSKSFNRHYNLIPHKKIHTNHAPLLCSILKSFRRDLDLS 462
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
297-650 1.02e-09

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 61.25  E-value: 1.02e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113866022 297 CKTAPSPSLPQSLRNYSEEKR-FECKYCGKSFSWSSHLIAHQRTHTGEKPYKCNLCGKF--FTRSSHVVSHQRIHTGEKP 373
Cdd:COG5048   12 NNSVLSSTPKSTLKSLSNAPRpDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYSGCDksFSRPLELSRHLRTHHNNPS 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113866022 374 YR-----------------------------CNLCGKSFTQRYVLVVHQRTHTGERPYECTQCGKSFRQSYK-------- 416
Cdd:COG5048   92 DLnskslplsnskasssslsssssnsndnnlLSSHSLPPSSRDPQLPDLLSISNLRNNPLPGNNSSSVNTPQsnslhppl 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113866022 417 --------------LIAHQRTHTGEKPYECTQCGKSFIQSYKLIAHQKIHSGEKPYECSHCGKSFSQSYKLVAHQRT--- 479
Cdd:COG5048  172 panslskdpssnlsLLISSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLsss 251
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113866022 480 ---HTGEKPFECNHCGKSFSWSSQLVSHQRTHTG-EKPYECNECGKSFNRSSHLVMHQRT--HTGE--KPYQC--KQCGK 549
Cdd:COG5048  252 dssSSASESPRSSLPTASSQSSSPNESDSSSEKGfSLPIKSKQCNISFSRSSPLTRHLRSvnHSGEslKPFSCpySLCGK 331
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113866022 550 SFSQSYVLVVHQRTHTGEKPYEC--GQCGKTFRQSS-----CFTQHQRTHTGEKPYEC--NQCGKTFSLSARLIVHQRTH 620
Cdd:COG5048  332 LFSRNDALKRHILLHTSISPAKEklLNSSSKFSPLLnneppQSLQQYKDLKNDKKSETlsNSCIRNFKRDSNLSLHIITH 411
                        410       420       430
                 ....*....|....*....|....*....|..
gi 113866022 621 TGEKP--YKCGQCGKAFISSSKRSRHQATHSE 650
Cdd:COG5048  412 LSFRPynCKNPPCSKSFNRHYNLIPHKKIHTN 443
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
391-646 2.60e-08

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 56.63  E-value: 2.60e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113866022 391 VHQRTHTGERPYECTQCGKSFRQSYKLIAHQRTHTGEKPYECTQCGKSFIQSYKLIAHQKIHSgekPYECSHCGKSFSQS 470
Cdd:COG5048  188 ISSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLSS---SDSSSSASESPRSS 264
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113866022 471 YKLVAHQRTH----------TGEKPFECNHCGKSFSWSSQLVSHQRT--HTGE--KPYECNE--CGKSFNRSSHLVMHQR 534
Cdd:COG5048  265 LPTASSQSSSpnesdsssekGFSLPIKSKQCNISFSRSSPLTRHLRSvnHSGEslKPFSCPYslCGKLFSRNDALKRHIL 344
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113866022 535 THTGEKPYQCK--QCGKSFSQ-----SYVLVVHQRTHTGEKPYEC--GQCGKTFRQSSCFTQHQRTHTGEKPYECN--QC 603
Cdd:COG5048  345 LHTSISPAKEKllNSSSKFSPllnnePPQSLQQYKDLKNDKKSETlsNSCIRNFKRDSNLSLHIITHLSFRPYNCKnpPC 424
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 113866022 604 GKTFSLSARLIVHQRTHTGEKPYKCGQCGKAFISSSKRSRHQA 646
Cdd:COG5048  425 SKSFNRHYNLIPHKKIHTNHAPLLCSILKSFRRDLDLSNHGKD 467
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
302-532 6.77e-08

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 55.47  E-value: 6.77e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113866022 302 SPSLPQSLRNYSEEKRFECkyCGKSFSWSSHLIAHQRTHtgekpYKCNLCGKFFTRSSHVVSHQRIHTG-EKPYRCNLCG 380
Cdd:COG5048  224 SSSLPLTTNSQLSPKSLLS--QSPSSLSSSDSSSSASES-----PRSSLPTASSQSSSPNESDSSSEKGfSLPIKSKQCN 296
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113866022 381 KSFTQRYVLVVHQRT--HTGE--RPYECT--QCGKSFRQSYKLIAHQRTHTGEKPYEC--TQCGKSFIQ-----SYKLIA 447
Cdd:COG5048  297 ISFSRSSPLTRHLRSvnHSGEslKPFSCPysLCGKLFSRNDALKRHILLHTSISPAKEklLNSSSKFSPllnnePPQSLQ 376
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113866022 448 HQKIHSGEKPYECSH--CGKSFSQSYKLVAHQRTHTGEKP--FECNHCGKSFSWSSQLVSHQRTHTGEKPYECNECgKSF 523
Cdd:COG5048  377 QYKDLKNDKKSETLSnsCIRNFKRDSNLSLHIITHLSFRPynCKNPPCSKSFNRHYNLIPHKKIHTNHAPLLCSIL-KSF 455

                 ....*....
gi 113866022 524 NRSSHLVMH 532
Cdd:COG5048  456 RRDLDLSNH 464
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
298-504 1.49e-07

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 54.32  E-value: 1.49e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113866022 298 KTAPSPSLPQSLRNYSEEKRFECKYCGKSFSWSSHLIAHQRT--HTGE--KPYKC--NLCGKFFTRSSHVVSHQRIHTGE 371
Cdd:COG5048  270 SQSSSPNESDSSSEKGFSLPIKSKQCNISFSRSSPLTRHLRSvnHSGEslKPFSCpySLCGKLFSRNDALKRHILLHTSI 349
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113866022 372 KPYRCNL--CGKSFTQ-----RYVLVVHQRTHTGERPYECT--QCGKSFRQSYKLIAHQRTHTGEKPYECTqcgksfiqs 442
Cdd:COG5048  350 SPAKEKLlnSSSKFSPllnnePPQSLQQYKDLKNDKKSETLsnSCIRNFKRDSNLSLHIITHLSFRPYNCK--------- 420
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 113866022 443 ykliahqkihsgekpyeCSHCGKSFSQSYKLVAHQRTHTGEKPFECNHCGKSFSwSSQLVSH 504
Cdd:COG5048  421 -----------------NPPCSKSFNRHYNLIPHKKIHTNHAPLLCSILKSFRR-DLDLSNH 464
zf-H2C2_2 pfam13465
Zinc-finger double domain;
528-553 1.86e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 41.59  E-value: 1.86e-05
                          10        20
                  ....*....|....*....|....*.
gi 113866022  528 HLVMHQRTHTGEKPYQCKQCGKSFSQ 553
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
SUF4-like cd20908
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
320-368 3.48e-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: 42.54  E-value: 3.48e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 113866022 320 CKYCGKSFSWSSHLIAHQRTHTgekpYKCNLCGKFFTRSSHVVSH-QRIH 368
Cdd:cd20908    4 CYYCDREFDDEKILIQHQKAKH----FKCHICHKKLYTAGGLAVHcLQVH 49
zf-H2C2_2 pfam13465
Zinc-finger double domain;
501-525 4.44e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 40.82  E-value: 4.44e-05
                          10        20
                  ....*....|....*....|....*
gi 113866022  501 LVSHQRTHTGEKPYECNECGKSFNR 525
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
360-385 2.03e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.89  E-value: 2.03e-04
                          10        20
                  ....*....|....*....|....*.
gi 113866022  360 HVVSHQRIHTGEKPYRCNLCGKSFTQ 385
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
389-413 2.42e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.51  E-value: 2.42e-04
                          10        20
                  ....*....|....*....|....*
gi 113866022  389 LVVHQRTHTGERPYECTQCGKSFRQ 413
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
420-441 2.78e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.51  E-value: 2.78e-04
                          10        20
                  ....*....|....*....|..
gi 113866022  420 HQRTHTGEKPYECTQCGKSFIQ 441
Cdd:pfam13465   5 HMRTHTGEKPYKCPECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
514-536 3.12e-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: 38.05  E-value: 3.12e-04
                          10        20
                  ....*....|....*....|...
gi 113866022  514 YECNECGKSFNRSSHLVMHQRTH 536
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
332-357 3.59e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.12  E-value: 3.59e-04
                          10        20
                  ....*....|....*....|....*.
gi 113866022  332 HLIAHQRTHTGEKPYKCNLCGKFFTR 357
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
587-608 3.92e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.12  E-value: 3.92e-04
                          10        20
                  ....*....|....*....|..
gi 113866022  587 QHQRTHTGEKPYECNQCGKTFS 608
Cdd:pfam13465   4 RHMRTHTGEKPYKCPECGKSFK 25
SUF4-like cd20908
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
484-532 4.45e-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: 4.45e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 113866022 484 KPFeCNHCGKSFSWSSQLVSHQRTHTgekpYECNECGKSFNRSSHLVMH 532
Cdd:cd20908    1 KPW-CYYCDREFDDEKILIQHQKAKH----FKCHICHKKLYTAGGLAVH 44
zf-H2C2_2 pfam13465
Zinc-finger double domain;
612-637 4.82e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 37.74  E-value: 4.82e-04
                          10        20
                  ....*....|....*....|....*.
gi 113866022  612 RLIVHQRTHTGEKPYKCGQCGKAFIS 637
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
473-496 5.06e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 37.74  E-value: 5.06e-04
                          10        20
                  ....*....|....*....|....
gi 113866022  473 LVAHQRTHTGEKPFECNHCGKSFS 496
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFK 25
zf-H2C2_2 pfam13465
Zinc-finger double domain;
557-581 5.75e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 37.35  E-value: 5.75e-04
                          10        20
                  ....*....|....*....|....*
gi 113866022  557 LVVHQRTHTGEKPYECGQCGKTFRQ 581
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
458-480 6.77e-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: 6.77e-04
                          10        20
                  ....*....|....*....|...
gi 113866022  458 YECSHCGKSFSQSYKLVAHQRTH 480
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
402-424 1.03e-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: 1.03e-03
                          10        20
                  ....*....|....*....|...
gi 113866022  402 YECTQCGKSFRQSYKLIAHQRTH 424
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
448-469 1.18e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.58  E-value: 1.18e-03
                          10        20
                  ....*....|....*....|..
gi 113866022  448 HQKIHSGEKPYECSHCGKSFSQ 469
Cdd:pfam13465   5 HMRTHTGEKPYKCPECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
318-340 3.66e-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: 3.66e-03
                          10        20
                  ....*....|....*....|...
gi 113866022  318 FECKYCGKSFSWSSHLIAHQRTH 340
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
570-592 3.88e-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: 3.88e-03
                          10        20
                  ....*....|....*....|...
gi 113866022  570 YECGQCGKTFRQSSCFTQHQRTH 592
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
542-564 4.72e-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: 4.72e-03
                          10        20
                  ....*....|....*....|...
gi 113866022  542 YQCKQCGKSFSQSYVLVVHQRTH 564
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
346-368 5.37e-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: 34.58  E-value: 5.37e-03
                          10        20
                  ....*....|....*....|...
gi 113866022  346 YKCNLCGKFFTRSSHVVSHQRIH 368
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
374-396 7.07e-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: 7.07e-03
                          10        20
                  ....*....|....*....|...
gi 113866022  374 YRCNLCGKSFTQRYVLVVHQRTH 396
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
430-452 7.49e-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: 7.49e-03
                          10        20
                  ....*....|....*....|...
gi 113866022  430 YECTQCGKSFIQSYKLIAHQKIH 452
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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