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Conserved domains on  [gi|7305545|ref|NP_038772|]
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zinc finger protein 354B [Mus musculus]

Protein Classification

KRAB domain-containing zinc finger protein( domain architecture ID 12204268)

KRAB (Kruppel-associated box) domain-containing zinc finger protein (KRAB-ZFP) plays important roles in cell differentiation and organ development, and in regulating viral replication and transcription

CATH:  3.30.160.60
Gene Ontology:  GO:0003700|GO:0046872
PubMed:  22803940
SCOP:  4003583

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
KRAB smart00349
krueppel associated box;
14-73 1.24e-32

krueppel associated box;


:

Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 119.62  E-value: 1.24e-32
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305545      14 VTFEDVAVLFTRDEWKKLVPSQRSLYREVMLENYSNLASLGFPFTKPKMISVLQQGEEPW 73
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQVPKPDLISQLEQGEEPW 60
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
182-585 5.06e-10

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


:

Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 62.02  E-value: 5.06e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305545  182 TQRNSLEENSTLLSQPKLKTVekrYKCSTCEKAFIHNSSLRKHLKNHTGERLFQCKD--CLKAFSQSSALIQHQRTHTGE 259
Cdd:COG5048  13 NSVLSSTPKSTLKSLSNAPRP---DSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYsgCDKSFSRPLELSRHLRTHHNN 89

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305545  260 KPYICKECGKAFSHSASLCKHLRTHTLE-KSYTCKECGKSFSRRSGL--FLHQKIHARENPHKYNPGRKASTSLS----- 331
Cdd:COG5048  90 PSDLNSKSLPLSNSKASSSSLSSSSSNSnDNNLLSSHSLPPSSRDPQlpDLLSISNLRNNPLPGNNSSSVNTPQSnslhp 169

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305545  332 --------------GCQRIHSRKKTYL----CNECGNTFKSSSSLRYHQRIHTGEKPFKCSECGRAFSQSASLIQHERIH 393
Cdd:COG5048 170 plpanslskdpssnLSLLISSNVSTSIpsssENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLS 249

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305545  394 TGEKPYRCSECGKGFTSISRLNRHRIIHTGE-------KFYNCNECGKALSSHSTLIIHER--IHTGE--KPCKCKV--C 460
Cdd:COG5048 250 SSDSSSSASESPRSSLPTASSQSSSPNESDSssekgfsLPIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCPYslC 329

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305545  461 GKAFRQSSALIQHQRMHTGERPYKCNEC-------GKTFRCNSSLSNHQRTHTGEKPYRC--QECGMSFGQSAALIQHRR 531
Cdd:COG5048 330 GKLFSRNDALKRHILLHTSISPAKEKLLnssskfsPLLNNEPPQSLQQYKDLKNDKKSETlsNSCIRNFKRDSNLSLHII 409

                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 7305545  532 IHTGEKP--FKCNTCGKSFRQSSSLIAHQRIHTGEKPYECSACGKlFSQRSSLTNH 585
Cdd:COG5048 410 THLSFRPynCKNPPCSKSFNRHYNLIPHKKIHTNHAPLLCSILKS-FRRDLDLSNH 464
 
Name Accession Description Interval E-value
KRAB smart00349
krueppel associated box;
14-73 1.24e-32

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 119.62  E-value: 1.24e-32
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305545      14 VTFEDVAVLFTRDEWKKLVPSQRSLYREVMLENYSNLASLGFPFTKPKMISVLQQGEEPW 73
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQVPKPDLISQLEQGEEPW 60
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
 13-54 1.59e-21

KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc finger proteins containing C2H2 fingers. The KRAB domain is found to be involved in protein-protein interactions. The KRAB domain is generally encoded by two exons. The regions coded by the two exons are known as KRAB-A and KRAB-B. The A box plays an important role in repression by binding to corepressors, while the B box is thought to enhance this repression brought about by the A box. KRAB-containing proteins are thought to have critical functions in cell proliferation and differentiation, apoptosis and neoplastic transformation.


Pssm-ID: 460171  Cd Length: 42  Bit Score: 87.53  E-value: 1.59e-21
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 7305545     13 SVTFEDVAVLFTRDEWKKLVPSQRSLYREVMLENYSNLASLG 54
Cdd:pfam01352   1 SVTFEDVAVDFTQEEWALLDPAQRNLYRDVMLENYRNLVSLG 42
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
 14-53 1.87e-19

KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression module, found in a subgroup of the zinc finger proteins (ZFPs) of the C2H2 family, KRAB-ZFPs. KRAB-ZFPs comprise the largest group of transcriptional regulators in mammals, and are only found in tetrapods. These proteins have been shown to play important roles in cell differentiation and organ development, and in regulating viral replication and transcription. A KRAB domain may consist of an A-box, or of an A-box plus either a B-box, a divergent B-box (b), or a C-box. Only the A-box is included in this model. The A-box is needed for repression, the B- and C- boxes are not. KRAB-ZFPs have one or two KRAB domains at their amino-terminal end, and multiple C2H2 zinc finger motifs at their C-termini. Some KRAB-ZFPs also contain a SCAN domain which mediates homo- and hetero-oligomerization. The KRAB domain is a protein-protein interaction module which represses transcription through recruiting corepressors. A key mechanism appears to be the following: KRAB-AFPs tethered to DNA recruit, via their KRAB domain, the repressor KAP1 (KRAB-associated protein-1, also known as transcription intermediary factor 1 beta , KRAB-A interacting protein , and tripartite motif protein 28). The KAP1/ KRAB-AFP complex in turn recruits the heterochromatin protein 1 (HP1) family, and other chromatin modulating proteins, leading to transcriptional repression through heterochromatin formation.


Pssm-ID: 143639  Cd Length: 40  Bit Score: 81.44  E-value: 1.87e-19
                        10        20        30        40
                ....*....|....*....|....*....|....*....|
gi 7305545   14 VTFEDVAVLFTRDEWKKLVPSQRSLYREVMLENYSNLASL 53
Cdd:cd07765   1 VTFEDVAVYFSQEEWELLDPAQRDLYRDVMLENYENLVSL 40
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
182-585 5.06e-10

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 62.02  E-value: 5.06e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305545  182 TQRNSLEENSTLLSQPKLKTVekrYKCSTCEKAFIHNSSLRKHLKNHTGERLFQCKD--CLKAFSQSSALIQHQRTHTGE 259
Cdd:COG5048  13 NSVLSSTPKSTLKSLSNAPRP---DSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYsgCDKSFSRPLELSRHLRTHHNN 89

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305545  260 KPYICKECGKAFSHSASLCKHLRTHTLE-KSYTCKECGKSFSRRSGL--FLHQKIHARENPHKYNPGRKASTSLS----- 331
Cdd:COG5048  90 PSDLNSKSLPLSNSKASSSSLSSSSSNSnDNNLLSSHSLPPSSRDPQlpDLLSISNLRNNPLPGNNSSSVNTPQSnslhp 169

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305545  332 --------------GCQRIHSRKKTYL----CNECGNTFKSSSSLRYHQRIHTGEKPFKCSECGRAFSQSASLIQHERIH 393
Cdd:COG5048 170 plpanslskdpssnLSLLISSNVSTSIpsssENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLS 249

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305545  394 TGEKPYRCSECGKGFTSISRLNRHRIIHTGE-------KFYNCNECGKALSSHSTLIIHER--IHTGE--KPCKCKV--C 460
Cdd:COG5048 250 SSDSSSSASESPRSSLPTASSQSSSPNESDSssekgfsLPIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCPYslC 329

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305545  461 GKAFRQSSALIQHQRMHTGERPYKCNEC-------GKTFRCNSSLSNHQRTHTGEKPYRC--QECGMSFGQSAALIQHRR 531
Cdd:COG5048 330 GKLFSRNDALKRHILLHTSISPAKEKLLnssskfsPLLNNEPPQSLQQYKDLKNDKKSETlsNSCIRNFKRDSNLSLHII 409

                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 7305545  532 IHTGEKP--FKCNTCGKSFRQSSSLIAHQRIHTGEKPYECSACGKlFSQRSSLTNH 585
Cdd:COG5048 410 THLSFRPynCKNPPCSKSFNRHYNLIPHKKIHTNHAPLLCSILKS-FRRDLDLSNH 464
SUF4-like cd20908
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
 453-501 1.08e-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: 41.00  E-value: 1.08e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*....
gi 7305545  453 KPcKCKVCGKAFRQSSALIQHQRMHTgerpYKCNECGKTFRCNSSLSNH 501
Cdd:cd20908   1 KP-WCYYCDREFDDEKILIQHQKAKH----FKCHICHKKLYTAGGLAVH 44
zf-H2C2_2 pfam13465
Zinc-finger double domain;
357-382 1.17e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 39.28  E-value: 1.17e-04
                          10        20
                  ....*....|....*....|....*.
gi 7305545    357 SLRYHQRIHTGEKPFKCSECGRAFSQ 382
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
PHA00733 PHA00733
hypothetical protein
 510-557 8.97e-04

hypothetical protein


Pssm-ID: 177301  Cd Length: 128  Bit Score: 39.47  E-value: 8.97e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 7305545   510 PYRCQECGMSFGQSAALIQHRRIHTGEKpfKCNTCGKSFRQSSSLIAH 557
Cdd:PHA00733  73 PYVCPLCLMPFSSSVSLKQHIRYTEHSK--VCPVCGKEFRNTDSTLDH 118
 
Name Accession Description Interval E-value
KRAB smart00349
krueppel associated box;
14-73 1.24e-32

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 119.62  E-value: 1.24e-32
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305545      14 VTFEDVAVLFTRDEWKKLVPSQRSLYREVMLENYSNLASLGFPFTKPKMISVLQQGEEPW 73
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQVPKPDLISQLEQGEEPW 60
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
 13-54 1.59e-21

KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc finger proteins containing C2H2 fingers. The KRAB domain is found to be involved in protein-protein interactions. The KRAB domain is generally encoded by two exons. The regions coded by the two exons are known as KRAB-A and KRAB-B. The A box plays an important role in repression by binding to corepressors, while the B box is thought to enhance this repression brought about by the A box. KRAB-containing proteins are thought to have critical functions in cell proliferation and differentiation, apoptosis and neoplastic transformation.


Pssm-ID: 460171  Cd Length: 42  Bit Score: 87.53  E-value: 1.59e-21
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 7305545     13 SVTFEDVAVLFTRDEWKKLVPSQRSLYREVMLENYSNLASLG 54
Cdd:pfam01352   1 SVTFEDVAVDFTQEEWALLDPAQRNLYRDVMLENYRNLVSLG 42
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
 14-53 1.87e-19

KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression module, found in a subgroup of the zinc finger proteins (ZFPs) of the C2H2 family, KRAB-ZFPs. KRAB-ZFPs comprise the largest group of transcriptional regulators in mammals, and are only found in tetrapods. These proteins have been shown to play important roles in cell differentiation and organ development, and in regulating viral replication and transcription. A KRAB domain may consist of an A-box, or of an A-box plus either a B-box, a divergent B-box (b), or a C-box. Only the A-box is included in this model. The A-box is needed for repression, the B- and C- boxes are not. KRAB-ZFPs have one or two KRAB domains at their amino-terminal end, and multiple C2H2 zinc finger motifs at their C-termini. Some KRAB-ZFPs also contain a SCAN domain which mediates homo- and hetero-oligomerization. The KRAB domain is a protein-protein interaction module which represses transcription through recruiting corepressors. A key mechanism appears to be the following: KRAB-AFPs tethered to DNA recruit, via their KRAB domain, the repressor KAP1 (KRAB-associated protein-1, also known as transcription intermediary factor 1 beta , KRAB-A interacting protein , and tripartite motif protein 28). The KAP1/ KRAB-AFP complex in turn recruits the heterochromatin protein 1 (HP1) family, and other chromatin modulating proteins, leading to transcriptional repression through heterochromatin formation.


Pssm-ID: 143639  Cd Length: 40  Bit Score: 81.44  E-value: 1.87e-19
                        10        20        30        40
                ....*....|....*....|....*....|....*....|
gi 7305545   14 VTFEDVAVLFTRDEWKKLVPSQRSLYREVMLENYSNLASL 53
Cdd:cd07765   1 VTFEDVAVYFSQEEWELLDPAQRDLYRDVMLENYENLVSL 40
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
182-585 5.06e-10

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 62.02  E-value: 5.06e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305545  182 TQRNSLEENSTLLSQPKLKTVekrYKCSTCEKAFIHNSSLRKHLKNHTGERLFQCKD--CLKAFSQSSALIQHQRTHTGE 259
Cdd:COG5048  13 NSVLSSTPKSTLKSLSNAPRP---DSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYsgCDKSFSRPLELSRHLRTHHNN 89

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305545  260 KPYICKECGKAFSHSASLCKHLRTHTLE-KSYTCKECGKSFSRRSGL--FLHQKIHARENPHKYNPGRKASTSLS----- 331
Cdd:COG5048  90 PSDLNSKSLPLSNSKASSSSLSSSSSNSnDNNLLSSHSLPPSSRDPQlpDLLSISNLRNNPLPGNNSSSVNTPQSnslhp 169

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305545  332 --------------GCQRIHSRKKTYL----CNECGNTFKSSSSLRYHQRIHTGEKPFKCSECGRAFSQSASLIQHERIH 393
Cdd:COG5048 170 plpanslskdpssnLSLLISSNVSTSIpsssENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLS 249

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305545  394 TGEKPYRCSECGKGFTSISRLNRHRIIHTGE-------KFYNCNECGKALSSHSTLIIHER--IHTGE--KPCKCKV--C 460
Cdd:COG5048 250 SSDSSSSASESPRSSLPTASSQSSSPNESDSssekgfsLPIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCPYslC 329

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305545  461 GKAFRQSSALIQHQRMHTGERPYKCNEC-------GKTFRCNSSLSNHQRTHTGEKPYRC--QECGMSFGQSAALIQHRR 531
Cdd:COG5048 330 GKLFSRNDALKRHILLHTSISPAKEKLLnssskfsPLLNNEPPQSLQQYKDLKNDKKSETlsNSCIRNFKRDSNLSLHII 409

                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 7305545  532 IHTGEKP--FKCNTCGKSFRQSSSLIAHQRIHTGEKPYECSACGKlFSQRSSLTNH 585
Cdd:COG5048 410 THLSFRPynCKNPPCSKSFNRHYNLIPHKKIHTNHAPLLCSILKS-FRRDLDLSNH 464
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
244-590 9.79e-09

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 57.78  E-value: 9.79e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305545  244 SQSSALIQHQRTHTGE----KPYICKECGKAFSHSASLCKHLRTHTLEKSYTC--KECGKSFSRRSGLFLHQKIHarenp 317
Cdd:COG5048  12 NNSVLSSTPKSTLKSLsnapRPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCsySGCDKSFSRPLELSRHLRTH----- 86

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305545  318 hkynpgrkaSTSLSGCQRIHSRKKTYLCNECGNTFKSSSSLryhqrihtgeKPFKCSECGRAFSQSASLIQHERIHTGEK 397
Cdd:COG5048  87 ---------HNNPSDLNSKSLPLSNSKASSSSLSSSSSNSN----------DNNLLSSHSLPPSSRDPQLPDLLSISNLR 147

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305545  398 PYRCSECGKGFTSISRLNRHRIIHTGekfyncNECGKALSSHSTLIIHERIHTGEKPCKCKVCGKAFRQSSALIQHQRMH 477
Cdd:COG5048 148 NNPLPGNNSSSVNTPQSNSLHPPLPA------NSLSKDPSSNLSLLISSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLE 221

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305545  478 TGERPYKCNECGKTFRCNSSLSNHQRTHTGEKPYRCQECGMSFGQSAALIQHRRIHTGE-------KPFKCNTCGKSFRQ 550
Cdd:COG5048 222 NSSSSLPLTTNSQLSPKSLLSQSPSSLSSSDSSSSASESPRSSLPTASSQSSSPNESDSssekgfsLPIKSKQCNISFSR 301

                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*.
gi 7305545  551 SSSLIAHQR--IHTGE--KPYEC--SACGKLFSQRSSLTNHYRIHI 590
Cdd:COG5048 302 SSPLTRHLRsvNHSGEslKPFSCpySLCGKLFSRNDALKRHILLHT 347
SUF4-like cd20908
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
 453-501 1.08e-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: 41.00  E-value: 1.08e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*....
gi 7305545  453 KPcKCKVCGKAFRQSSALIQHQRMHTgerpYKCNECGKTFRCNSSLSNH 501
Cdd:cd20908   1 KP-WCYYCDREFDDEKILIQHQKAKH----FKCHICHKKLYTAGGLAVH 44
zf-H2C2_2 pfam13465
Zinc-finger double domain;
357-382 1.17e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 39.28  E-value: 1.17e-04
                          10        20
                  ....*....|....*....|....*.
gi 7305545    357 SLRYHQRIHTGEKPFKCSECGRAFSQ 382
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
469-494 3.46e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.12  E-value: 3.46e-04
                          10        20
                  ....*....|....*....|....*.
gi 7305545    469 ALIQHQRMHTGERPYKCNECGKTFRC 494
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
525-550 3.94e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 37.74  E-value: 3.94e-04
                          10        20
                  ....*....|....*....|....*.
gi 7305545    525 ALIQHRRIHTGEKPFKCNTCGKSFRQ 550
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
385-410 4.22e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 37.74  E-value: 4.22e-04
                          10        20
                  ....*....|....*....|....*.
gi 7305545    385 SLIQHERIHTGEKPYRCSECGKGFTS 410
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
PHA00733 PHA00733
hypothetical protein
 510-557 8.97e-04

hypothetical protein


Pssm-ID: 177301  Cd Length: 128  Bit Score: 39.47  E-value: 8.97e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 7305545   510 PYRCQECGMSFGQSAALIQHRRIHTGEKpfKCNTCGKSFRQSSSLIAH 557
Cdd:PHA00733  73 PYVCPLCLMPFSSSVSLKQHIRYTEHSK--VCPVCGKEFRNTDSTLDH 118
zf-H2C2_2 pfam13465
Zinc-finger double domain;
497-520 9.07e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.97  E-value: 9.07e-04
                          10        20
                  ....*....|....*....|....
gi 7305545    497 SLSNHQRTHTGEKPYRCQECGMSF 520
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSF 24
SFP1 COG5189
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ...
 341-418 1.26e-03

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


Pssm-ID: 227516 [Multi-domain]  Cd Length: 423  Bit Score: 41.63  E-value: 1.26e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305545  341 KTYLCN--ECGNTFKSSSSLRYHqRIHtgekpfkcSECGRAFSQSASLIQHERIHTGEKPYRCSECGKGFTSISRLNRHR 418
Cdd:COG5189 348 KPYKCPveGCNKKYKNQNGLKYH-MLH--------GHQNQKLHENPSPEKMNIFSAKDKPYRCEVCDKRYKNLNGLKYHR 418
SUF4-like cd20908
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
 369-417 1.33e-03

N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), Arabidopsis thaliana SUF4 (AtSUF4), and similar proteins; Oryza sativa SUPPRESSOR OF FRI 4 (OsSUF4) is a C2H2-type zinc finger transcription factor which interacts with the major H3K36 methyltransferase SDG725 to promote H3K36me3 (tri-methylation at H3K9) establishment. The transcription factor OsSUF4 recognizes a specific 7-bp DNA element (5'-CGGAAAT-3'), which is contained in the promoter regions of many genes throughout the rice genome. Through interaction with OsSUF4, SDG725 is recruited to the promoters of key florigen genes, RICE FLOWERING LOCUS T1 (RFT1) and Heading date 3a (Hd3a), for H3K36 deposition to promote gene activation and rice plant flowering. OsSUF4 target genes include a number of genes involved in many biological processes. Flowering plant Arabidopsis SUF4 binds to a 15bp DNA element (5'-CCAAATTTTAAGTTT-3') within the promoter of the floral repressor gene FLOWERING LOCUS C (FLC) and recruits the FRI-C transcription activator complex to the FLC promoter. Although the DNA-binding element and target genes of AtSUF4 are different from those of OsSUF4, AtSUF4 is known to interact with the Arabidopsis H3K36 methyltransferase SDG8 (also known as ASHH2/EFS/SET8), and the methylation deposition mechanism mediated by the SUF4 transcription factor and H3K36 methyltransferase may be conserved in Arabidopsis and rice. Proteins in this family have two conserved C2H2-type zinc finger motifs at the N-terminus (included in this model), and a large proline-rich domain at the C-terminus; for OsSUF4, it has been shown that the N-terminal zinc-finger domain is responsible for DNA binding, and that the C-terminal domain interacts with SDG725.


Pssm-ID: 411020 [Multi-domain]  Cd Length: 82  Bit Score: 37.92  E-value: 1.33e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*....
gi 7305545  369 KPFkCSECGRAFSQSASLIQHERIHTgekpYRCSECGKGFTSISRLNRH 417
Cdd:cd20908   1 KPW-CYYCDREFDDEKILIQHQKAKH----FKCHICHKKLYTAGGLAVH 44
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 539-561 1.53e-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: 36.12  E-value: 1.53e-03
                          10        20
                  ....*....|....*....|...
gi 7305545    539 FKCNTCGKSFRQSSSLIAHQRIH 561
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
248-273 1.82e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.81  E-value: 1.82e-03
                          10        20
                  ....*....|....*....|....*.
gi 7305545    248 ALIQHQRTHTGEKPYICKECGKAFSH 273
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 262-284 3.71e-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: 3.71e-03
                          10        20
                  ....*....|....*....|...
gi 7305545    262 YICKECGKAFSHSASLCKHLRTH 284
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 290-312 5.03e-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: 34.58  E-value: 5.03e-03
                          10        20
                  ....*....|....*....|...
gi 7305545    290 YTCKECGKSFSRRSGLFLHQKIH 312
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
553-578 5.92e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 34.65  E-value: 5.92e-03
                          10        20
                  ....*....|....*....|....*.
gi 7305545    553 SLIAHQRIHTGEKPYECSACGKLFSQ 578
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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