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Conserved domains on  [gi|31982552|ref|NP_766382|]
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zinc finger protein 454 isoform 1 [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;
14-67 6.15e-25

krueppel associated box;


:

Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 97.66  E-value: 6.15e-25
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 31982552     14 VTFKDVAVLFTQEEWGQLSSAQRALYQDVMLENYSNLVSLaGLLGSQPDMFFPL 67
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSL-GFQVPKPDLISQL 53
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
197-532 4.34e-12

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


:

Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 68.18  E-value: 4.34e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982552 197 GKAFSKSSTLKKHQKLHTEKLNPSQKSPmkekrYKCRECGKAFHQSTHLIHHQRVHTGEKPYQCKD--CGKAFSVSSSLS 274
Cdd:COG5048   6 SQSSSSNNSVLSSTPKSTLKSLSNAPRP-----DSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYsgCDKSFSRPLELS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982552 275 YHQKIHTGEKPFEC----------------NVCGKAFIRNIHLSHHHRMHTGEKPFQCNLcdkafvcrahltkHQHIHSG 338
Cdd:COG5048  81 RHLRTHHNNPSDLNskslplsnskasssslSSSSSNSNDNNLLSSHSLPPSSRDPQLPDL-------------LSISNLR 147

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982552 339 KKPYK-CNECGKAFNQSTSFLQ-------------------HQRIHTGEKPFECNECGKAFRVNSSLTEHQRIHTGEKPY 398
Cdd:COG5048 148 NNPLPgNNSSSVNTPQSNSLHPplpanslskdpssnlslliSSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSL 227

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982552 399 QCIECGKAFRDNSSFARHRKIHTGEKPYRCGLCEKAFR--DQSALAQHQRTHTGE-----KPYTCNICEKAFSDHSALTQ 471
Cdd:COG5048 228 PLTTNSQLSPKSLLSQSPSSLSSSDSSSSASESPRSSLptASSQSSSPNESDSSSekgfsLPIKSKQCNISFSRSSPLTR 307

                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 31982552 472 HKR--IHTRE--KPYKC--KTCGKAFIRSTHLIQHQRIHTGEKPYKC--NTCGKAFNQTANLAQHQRHH 532
Cdd:COG5048 308 HLRsvNHSGEslKPFSCpySLCGKLFSRNDALKRHILLHTSISPAKEklLNSSSKFSPLLNNEPPQSLQ 376
 
Name Accession Description Interval E-value
KRAB smart00349
krueppel associated box;
14-67 6.15e-25

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 97.66  E-value: 6.15e-25
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 31982552     14 VTFKDVAVLFTQEEWGQLSSAQRALYQDVMLENYSNLVSLaGLLGSQPDMFFPL 67
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSL-GFQVPKPDLISQL 53
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
 13-53 8.75e-23

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: 90.99  E-value: 8.75e-23
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 31982552    13 LVTFKDVAVLFTQEEWGQLSSAQRALYQDVMLENYSNLVSL 53
Cdd:pfam01352   1 SVTFEDVAVDFTQEEWALLDPAQRNLYRDVMLENYRNLVSL 41
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
 14-53 1.46e-20

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: 84.52  E-value: 1.46e-20
                        10        20        30        40
                ....*....|....*....|....*....|....*....|
gi 31982552  14 VTFKDVAVLFTQEEWGQLSSAQRALYQDVMLENYSNLVSL 53
Cdd:cd07765   1 VTFEDVAVYFSQEEWELLDPAQRDLYRDVMLENYENLVSL 40
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
197-532 4.34e-12

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 68.18  E-value: 4.34e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982552 197 GKAFSKSSTLKKHQKLHTEKLNPSQKSPmkekrYKCRECGKAFHQSTHLIHHQRVHTGEKPYQCKD--CGKAFSVSSSLS 274
Cdd:COG5048   6 SQSSSSNNSVLSSTPKSTLKSLSNAPRP-----DSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYsgCDKSFSRPLELS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982552 275 YHQKIHTGEKPFEC----------------NVCGKAFIRNIHLSHHHRMHTGEKPFQCNLcdkafvcrahltkHQHIHSG 338
Cdd:COG5048  81 RHLRTHHNNPSDLNskslplsnskasssslSSSSSNSNDNNLLSSHSLPPSSRDPQLPDL-------------LSISNLR 147

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982552 339 KKPYK-CNECGKAFNQSTSFLQ-------------------HQRIHTGEKPFECNECGKAFRVNSSLTEHQRIHTGEKPY 398
Cdd:COG5048 148 NNPLPgNNSSSVNTPQSNSLHPplpanslskdpssnlslliSSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSL 227

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982552 399 QCIECGKAFRDNSSFARHRKIHTGEKPYRCGLCEKAFR--DQSALAQHQRTHTGE-----KPYTCNICEKAFSDHSALTQ 471
Cdd:COG5048 228 PLTTNSQLSPKSLLSQSPSSLSSSDSSSSASESPRSSLptASSQSSSPNESDSSSekgfsLPIKSKQCNISFSRSSPLTR 307

                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 31982552 472 HKR--IHTRE--KPYKC--KTCGKAFIRSTHLIQHQRIHTGEKPYKC--NTCGKAFNQTANLAQHQRHH 532
Cdd:COG5048 308 HLRsvNHSGEslKPFSCpySLCGKLFSRNDALKRHILLHTSISPAKEklLNSSSKFSPLLNNEPPQSLQ 376
zf-H2C2_2 pfam13465
Zinc-finger double domain;
496-521 8.49e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 39.66  E-value: 8.49e-05
                          10        20
                  ....*....|....*....|....*.
gi 31982552   496 HLIQHQRIHTGEKPYKCNTCGKAFNQ 521
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
SUF4-like cd20908
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
 480-533 2.81e-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: 39.85  E-value: 2.81e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 31982552 480 KPYkCKTCGKAFIRSTHLIQHQRIHTgekpYKCNTCGKAFNQTANLAQH--QRHHT 533
Cdd:cd20908   1 KPW-CYYCDREFDDEKILIQHQKAKH----FKCHICHKKLYTAGGLAVHclQVHKE 51
PHA00733 PHA00733
hypothetical protein
 453-500 4.03e-03

hypothetical protein


Pssm-ID: 177301  Cd Length: 128  Bit Score: 37.55  E-value: 4.03e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 31982552  453 PYTCNICEKAFSDHSALTQHKRIHTREKpyKCKTCGKAFIRSTHLIQH 500
Cdd:PHA00733  73 PYVCPLCLMPFSSSVSLKQHIRYTEHSK--VCPVCGKEFRNTDSTLDH 118
 
Name Accession Description Interval E-value
KRAB smart00349
krueppel associated box;
14-67 6.15e-25

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 97.66  E-value: 6.15e-25
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 31982552     14 VTFKDVAVLFTQEEWGQLSSAQRALYQDVMLENYSNLVSLaGLLGSQPDMFFPL 67
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSL-GFQVPKPDLISQL 53
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
 13-53 8.75e-23

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: 90.99  E-value: 8.75e-23
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 31982552    13 LVTFKDVAVLFTQEEWGQLSSAQRALYQDVMLENYSNLVSL 53
Cdd:pfam01352   1 SVTFEDVAVDFTQEEWALLDPAQRNLYRDVMLENYRNLVSL 41
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
 14-53 1.46e-20

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: 84.52  E-value: 1.46e-20
                        10        20        30        40
                ....*....|....*....|....*....|....*....|
gi 31982552  14 VTFKDVAVLFTQEEWGQLSSAQRALYQDVMLENYSNLVSL 53
Cdd:cd07765   1 VTFEDVAVYFSQEEWELLDPAQRDLYRDVMLENYENLVSL 40
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
197-532 4.34e-12

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 68.18  E-value: 4.34e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982552 197 GKAFSKSSTLKKHQKLHTEKLNPSQKSPmkekrYKCRECGKAFHQSTHLIHHQRVHTGEKPYQCKD--CGKAFSVSSSLS 274
Cdd:COG5048   6 SQSSSSNNSVLSSTPKSTLKSLSNAPRP-----DSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYsgCDKSFSRPLELS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982552 275 YHQKIHTGEKPFEC----------------NVCGKAFIRNIHLSHHHRMHTGEKPFQCNLcdkafvcrahltkHQHIHSG 338
Cdd:COG5048  81 RHLRTHHNNPSDLNskslplsnskasssslSSSSSNSNDNNLLSSHSLPPSSRDPQLPDL-------------LSISNLR 147

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982552 339 KKPYK-CNECGKAFNQSTSFLQ-------------------HQRIHTGEKPFECNECGKAFRVNSSLTEHQRIHTGEKPY 398
Cdd:COG5048 148 NNPLPgNNSSSVNTPQSNSLHPplpanslskdpssnlslliSSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSL 227

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982552 399 QCIECGKAFRDNSSFARHRKIHTGEKPYRCGLCEKAFR--DQSALAQHQRTHTGE-----KPYTCNICEKAFSDHSALTQ 471
Cdd:COG5048 228 PLTTNSQLSPKSLLSQSPSSLSSSDSSSSASESPRSSLptASSQSSSPNESDSSSekgfsLPIKSKQCNISFSRSSPLTR 307

                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 31982552 472 HKR--IHTRE--KPYKC--KTCGKAFIRSTHLIQHQRIHTGEKPYKC--NTCGKAFNQTANLAQHQRHH 532
Cdd:COG5048 308 HLRsvNHSGEslKPFSCpySLCGKLFSRNDALKRHILLHTSISPAKEklLNSSSKFSPLLNNEPPQSLQ 376
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
161-528 7.79e-09

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 58.17  E-value: 7.79e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982552 161 NTPSKLSEQRVRAESSSPIQSQRSQASKTAFECSECgKAFSKSSTLKKHQKLHTEKLNPSQKSPMKEKRYKCRECGKAFH 240
Cdd:COG5048  73 FSRPLELSRHLRTHHNNPSDLNSKSLPLSNSKASSS-SLSSSSSNSNDNNLLSSHSLPPSSRDPQLPDLLSISNLRNNPL 151

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982552 241 QSTHLIHHQRVHTGEKPYQC--KDCGKAFSVSSSLSYHQKIHTGEKPFECNVCGKAFIRNIHLSHHHRMHTGEKPFQCNL 318
Cdd:COG5048 152 PGNNSSSVNTPQSNSLHPPLpaNSLSKDPSSNLSLLISSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTT 231

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982552 319 CdkAFVCRAHLTKHQHIhSGKKPYKCNECGKAFNQSTSFLQHQRIH----------TGEKPFECNECGKAFRVNSSLTEH 388
Cdd:COG5048 232 N--SQLSPKSLLSQSPS-SLSSSDSSSSASESPRSSLPTASSQSSSpnesdsssekGFSLPIKSKQCNISFSRSSPLTRH 308

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982552 389 QR--IHTGE--KPYQCIE--CGKAFRDNSSFARHRKIHTGEKPYRCGLC-------EKAFRDQSALAQHQRTHTGEKPYT 455
Cdd:COG5048 309 LRsvNHSGEslKPFSCPYslCGKLFSRNDALKRHILLHTSISPAKEKLLnssskfsPLLNNEPPQSLQQYKDLKNDKKSE 388

                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 31982552 456 C--NICEKAFSDHSALTQHKRIHTREKP--YKCKTCGKAFIRSTHLIQHQRIHTGEKPYKCNTCGKaFNQTANLAQH 528
Cdd:COG5048 389 TlsNSCIRNFKRDSNLSLHIITHLSFRPynCKNPPCSKSFNRHYNLIPHKKIHTNHAPLLCSILKS-FRRDLDLSNH 464
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
156-417 9.45e-09

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 57.78  E-value: 9.45e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982552 156 VLTQQNTPSKLSEQRVRAESSSPIQSQRSQASKTAfecSECGKAFSKSSTLKKHQKLHTEKLNPSQKSPMKEKRYKCREC 235
Cdd:COG5048 219 NLENSSSSLPLTTNSQLSPKSLLSQSPSSLSSSDS---SSSASESPRSSLPTASSQSSSPNESDSSSEKGFSLPIKSKQC 295

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982552 236 GKAFHQSTHLIHHQR--VHTGE--KPYQC--KDCGKAFSVSSSLSYHQKIHTGEKPFEC--NVCGKAFIRNIH-----LS 302
Cdd:COG5048 296 NISFSRSSPLTRHLRsvNHSGEslKPFSCpySLCGKLFSRNDALKRHILLHTSISPAKEklLNSSSKFSPLLNneppqSL 375

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982552 303 HHHRMHTGEKPFQC--NLCDKAFVCRAHLTKHQHIHSGKKPYKCNecgkafnqstsflqhqrihtgekpfeCNECGKAFR 380
Cdd:COG5048 376 QQYKDLKNDKKSETlsNSCIRNFKRDSNLSLHIITHLSFRPYNCK--------------------------NPPCSKSFN 429

                       250       260       270
                ....*....|....*....|....*....|....*..
gi 31982552 381 VNSSLTEHQRIHTGEKPYQCIECGKAFRDNSSFARHR 417
Cdd:COG5048 430 RHYNLIPHKKIHTNHAPLLCSILKSFRRDLDLSNHGK 466
SFP1 COG5189
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ...
 450-533 6.72e-05

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


Pssm-ID: 227516 [Multi-domain]  Cd Length: 423  Bit Score: 45.48  E-value: 6.72e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982552 450 GEKPYTCNI--CEKAFSDHSALTQHkRIHTREKPYKCKTCGKafirsthlIQHQRIHTGEKPYKCNTCGKAFNQTANLAQ 527
Cdd:COG5189 346 DGKPYKCPVegCNKKYKNQNGLKYH-MLHGHQNQKLHENPSP--------EKMNIFSAKDKPYRCEVCDKRYKNLNGLKY 416


                ....*.
gi 31982552 528 HQRHHT 533
Cdd:COG5189 417 HRKHSH 422
zf-H2C2_2 pfam13465
Zinc-finger double domain;
496-521 8.49e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 39.66  E-value: 8.49e-05
                          10        20
                  ....*....|....*....|....*.
gi 31982552   496 HLIQHQRIHTGEKPYKCNTCGKAFNQ 521
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
384-407 2.67e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.12  E-value: 2.67e-04
                          10        20
                  ....*....|....*....|....
gi 31982552   384 SLTEHQRIHTGEKPYQCIECGKAF 407
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSF 24
SUF4-like cd20908
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
 480-533 2.81e-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: 39.85  E-value: 2.81e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 31982552 480 KPYkCKTCGKAFIRSTHLIQHQRIHTgekpYKCNTCGKAFNQTANLAQH--QRHHT 533
Cdd:cd20908   1 KPW-CYYCDREFDDEKILIQHQKAKH----FKCHICHKKLYTAGGLAVHclQVHKE 51
zf-H2C2_2 pfam13465
Zinc-finger double domain;
468-493 4.08e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 37.74  E-value: 4.08e-04
                          10        20
                  ....*....|....*....|....*.
gi 31982552   468 ALTQHKRIHTREKPYKCKTCGKAFIR 493
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
272-297 4.86e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 37.35  E-value: 4.86e-04
                          10        20
                  ....*....|....*....|....*.
gi 31982552   272 SLSYHQKIHTGEKPFECNVCGKAFIR 297
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
480-536 5.57e-04

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 42.38  E-value: 5.57e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 31982552 480 KPYKCKTCGKAFIRSTHLIQHQRIHTGEKPYKCN--TCGKAFNQTANLAQHQRHHTGGK 536
Cdd:COG5048  32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSysGCDKSFSRPLELSRHLRTHHNNP 90
zf-H2C2_2 pfam13465
Zinc-finger double domain;
440-464 5.92e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 37.35  E-value: 5.92e-04
                          10        20
                  ....*....|....*....|....*
gi 31982552   440 ALAQHQRTHTGEKPYTCNICEKAFS 464
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFK 25
zf-H2C2_2 pfam13465
Zinc-finger double domain;
359-379 9.03e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.58  E-value: 9.03e-04
                          10        20
                  ....*....|....*....|.
gi 31982552   359 QHQRIHTGEKPFECNECGKAF 379
Cdd:pfam13465   4 RHMRTHTGEKPYKCPECGKSF 24
zf-H2C2_2 pfam13465
Zinc-finger double domain;
328-353 1.30e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.20  E-value: 1.30e-03
                          10        20
                  ....*....|....*....|....*.
gi 31982552   328 HLTKHQHIHSGKKPYKCNECGKAFNQ 353
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
SFP1 COG5189
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ...
 338-418 2.06e-03

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


Pssm-ID: 227516 [Multi-domain]  Cd Length: 423  Bit Score: 40.47  E-value: 2.06e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982552 338 GKKPYKCN--ECGKAFNQSTSfLQHQRIHtgekpfecNECGKAFRVNSSLTEHQRIHTGEKPYQCIECGKAFRDNSSFAR 415
Cdd:COG5189 346 DGKPYKCPveGCNKKYKNQNG-LKYHMLH--------GHQNQKLHENPSPEKMNIFSAKDKPYRCEVCDKRYKNLNGLKY 416


                ...
gi 31982552 416 HRK 418
Cdd:COG5189 417 HRK 419
zf-H2C2_2 pfam13465
Zinc-finger double domain;
248-268 2.74e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.42  E-value: 2.74e-03
                          10        20
                  ....*....|....*....|.
gi 31982552   248 HQRVHTGEKPYQCKDCGKAFS 268
Cdd:pfam13465   5 HMRTHTGEKPYKCPECGKSFK 25
zf-H2C2_2 pfam13465
Zinc-finger double domain;
304-325 2.79e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.42  E-value: 2.79e-03
                          10        20
                  ....*....|....*....|..
gi 31982552   304 HHRMHTGEKPFQCNLCDKAFVC 325
Cdd:pfam13465   5 HMRTHTGEKPYKCPECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 482-504 3.39e-03

Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two conserved cysteines and histidines co-ordinate a zinc ion. The following pattern describes the zinc finger. #-X-C-X(1-5)-C-X3-#-X5-#-X2-H-X(3-6)-[H/C] Where X can be any amino acid, and numbers in brackets indicate the number of residues. The positions marked # are those that are important for the stable fold of the zinc finger. The final position can be either his or cys. The C2H2 zinc finger is composed of two short beta strands followed by an alpha helix. The amino terminal part of the helix binds the major groove in DNA binding zinc fingers. The accepted consensus binding sequence for Sp1 is usually defined by the asymmetric hexanucleotide core GGGCGG but this sequence does not include, among others, the GAG (=CTC) repeat that constitutes a high-affinity site for Sp1 binding to the wt1 promoter.


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 34.97  E-value: 3.39e-03
                          10        20
                  ....*....|....*....|...
gi 31982552   482 YKCKTCGKAFIRSTHLIQHQRIH 504
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
PHA00733 PHA00733
hypothetical protein
 453-500 4.03e-03

hypothetical protein


Pssm-ID: 177301  Cd Length: 128  Bit Score: 37.55  E-value: 4.03e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 31982552  453 PYTCNICEKAFSDHSALTQHKRIHTREKpyKCKTCGKAFIRSTHLIQH 500
Cdd:PHA00733  73 PYVCPLCLMPFSSSVSLKQHIRYTEHSK--VCPVCGKEFRNTDSTLDH 118
SFP1 COG5189
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ...
 394-473 5.94e-03

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


Pssm-ID: 227516 [Multi-domain]  Cd Length: 423  Bit Score: 39.32  E-value: 5.94e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982552 394 GEKPYQC--IECGKAFRDNSSFARHRKiHtgekpyrcGLCEKAFRDQSALAQHQRTHTGEKPYTCNICEKAFSDHSALTQ 471
Cdd:COG5189 346 DGKPYKCpvEGCNKKYKNQNGLKYHML-H--------GHQNQKLHENPSPEKMNIFSAKDKPYRCEVCDKRYKNLNGLKY 416


                ..
gi 31982552 472 HK 473
Cdd:COG5189 417 HR 418
zf-H2C2_2 pfam13465
Zinc-finger double domain;
412-435 6.13e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 34.27  E-value: 6.13e-03
                          10        20
                  ....*....|....*....|....
gi 31982552   412 SFARHRKIHTGEKPYRCGLCEKAF 435
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSF 24
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 191-213 6.73e-03

Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two conserved cysteines and histidines co-ordinate a zinc ion. The following pattern describes the zinc finger. #-X-C-X(1-5)-C-X3-#-X5-#-X2-H-X(3-6)-[H/C] Where X can be any amino acid, and numbers in brackets indicate the number of residues. The positions marked # are those that are important for the stable fold of the zinc finger. The final position can be either his or cys. The C2H2 zinc finger is composed of two short beta strands followed by an alpha helix. The amino terminal part of the helix binds the major groove in DNA binding zinc fingers. The accepted consensus binding sequence for Sp1 is usually defined by the asymmetric hexanucleotide core GGGCGG but this sequence does not include, among others, the GAG (=CTC) repeat that constitutes a high-affinity site for Sp1 binding to the wt1 promoter.


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 34.20  E-value: 6.73e-03
                          10        20
                  ....*....|....*....|...
gi 31982552   191 FECSECGKAFSKSSTLKKHQKLH 213
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
SFP1 COG5189
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ...
 366-449 7.07e-03

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


Pssm-ID: 227516 [Multi-domain]  Cd Length: 423  Bit Score: 38.93  E-value: 7.07e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982552 366 GEKPFECN--ECGKAFRVNSSLTEHqRIHTgekpyqciECGKAFRDNSSFARHRKIHTGEKPYRCGLCEKAFRDQSALAQ 443
Cdd:COG5189 346 DGKPYKCPveGCNKKYKNQNGLKYH-MLHG--------HQNQKLHENPSPEKMNIFSAKDKPYRCEVCDKRYKNLNGLKY 416


                ....*.
gi 31982552 444 HqRTHT 449
Cdd:COG5189 417 H-RKHS 421
 
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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