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Conserved domains on  [gi|116812597|ref|NP_060122|]
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zinc finger protein 586 isoform a [Homo sapiens]

Protein Classification

KRAB domain-containing zinc finger protein( domain architecture ID 12016931)

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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
14-55 7.56e-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: 84.83  E-value: 7.56e-21
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 116812597   14 SVTFEDVAVNFSLEEWSLLNEAQRCLYRDVMLETLTLISSLG 55
Cdd:pfam01352   1 SVTFEDVAVDFTQEEWALLDPAQRNLYRDVMLENYRNLVSLG 42
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
104-366 3.15e-09

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


:

Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 58.55  E-value: 3.15e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812597 104 TEPRRDHKHRNVRTGERPYECSKYGKLFHQKPTLHIHERFHTGQKTYECSECGKSFHQSSSLLQRQTLHTRERPYECIEC 183
Cdd:COG5048  181 SSNLSLLISSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLSSSDSSSSASES 260
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812597 184 GKAFAEKSSLINHRKVHSGA-------KRYECNECGKSFAYTSSLIKHRR--IHTGE--RPYECSE--CGRSFAENSSLI 250
Cdd:COG5048  261 PRSSLPTASSQSSSPNESDSssekgfsLPIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCPYslCGKLFSRNDALK 340
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812597 251 KHLRVHTGERPYECV--ECGKSFRRSSSLLQHQRVHTR-----ERPYEC--SECGKSFSLRSNLIHHQRVHTGERHE--- 318
Cdd:COG5048  341 RHILLHTSISPAKEKllNSSSKFSPLLNNEPPQSLQQYkdlknDKKSETlsNSCIRNFKRDSNLSLHIITHLSFRPYnck 420
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 116812597 319 CGQCGKSFSRKSSLIIHLRVHTGERPYECSDCgKSFAENSSLIKHLRV 366
Cdd:COG5048  421 NPPCSKSFNRHYNLIPHKKIHTNHAPLLCSIL-KSFRRDLDLSNHGKD 467
zf-H2C2_2 pfam13465
Zinc-finger double domain;
359-384 2.75e-03

Zinc-finger double domain;


:

Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.04  E-value: 2.75e-03
                          10        20
                  ....*....|....*....|....*.
gi 116812597  359 SLIKHLRVHTGERPYECIDCGKSFRH 384
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
 
Name Accession Description Interval E-value
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
14-55 7.56e-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: 84.83  E-value: 7.56e-21
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 116812597   14 SVTFEDVAVNFSLEEWSLLNEAQRCLYRDVMLETLTLISSLG 55
Cdd:pfam01352   1 SVTFEDVAVDFTQEEWALLDPAQRNLYRDVMLENYRNLVSLG 42
KRAB smart00349
krueppel associated box;
15-56 1.99e-16

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 73.01  E-value: 1.99e-16
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 116812597    15 VTFEDVAVNFSLEEWSLLNEAQRCLYRDVMLETLTLISSLGC 56
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGF 42
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
15-52 1.04e-14

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: 67.57  E-value: 1.04e-14
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 116812597  15 VTFEDVAVNFSLEEWSLLNEAQRCLYRDVMLET-LTLIS 52
Cdd:cd07765    1 VTFEDVAVYFSQEEWELLDPAQRDLYRDVMLENyENLVS 39
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
104-366 3.15e-09

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 58.55  E-value: 3.15e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812597 104 TEPRRDHKHRNVRTGERPYECSKYGKLFHQKPTLHIHERFHTGQKTYECSECGKSFHQSSSLLQRQTLHTRERPYECIEC 183
Cdd:COG5048  181 SSNLSLLISSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLSSSDSSSSASES 260
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812597 184 GKAFAEKSSLINHRKVHSGA-------KRYECNECGKSFAYTSSLIKHRR--IHTGE--RPYECSE--CGRSFAENSSLI 250
Cdd:COG5048  261 PRSSLPTASSQSSSPNESDSssekgfsLPIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCPYslCGKLFSRNDALK 340
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812597 251 KHLRVHTGERPYECV--ECGKSFRRSSSLLQHQRVHTR-----ERPYEC--SECGKSFSLRSNLIHHQRVHTGERHE--- 318
Cdd:COG5048  341 RHILLHTSISPAKEKllNSSSKFSPLLNNEPPQSLQQYkdlknDKKSETlsNSCIRNFKRDSNLSLHIITHLSFRPYnck 420
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 116812597 319 CGQCGKSFSRKSSLIIHLRVHTGERPYECSDCgKSFAENSSLIKHLRV 366
Cdd:COG5048  421 NPPCSKSFNRHYNLIPHKKIHTNHAPLLCSIL-KSFRRDLDLSNHGKD 467
zf-H2C2_2 pfam13465
Zinc-finger double domain;
359-384 2.75e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.04  E-value: 2.75e-03
                          10        20
                  ....*....|....*....|....*.
gi 116812597  359 SLIKHLRVHTGERPYECIDCGKSFRH 384
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
SUF4-like cd20908
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
288-339 5.84e-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: 35.61  E-value: 5.84e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 116812597 288 RPYeCSECGKSFSLRSNLIHHQRvhtgERH-ECGQCGKSFSRKSSLIIH-LRVH 339
Cdd:cd20908    1 KPW-CYYCDREFDDEKILIQHQK----AKHfKCHICHKKLYTAGGLAVHcLQVH 49
zf-H2C2_2 pfam13465
Zinc-finger double domain;
220-244 6.15e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 33.88  E-value: 6.15e-03
                          10        20
                  ....*....|....*....|....*
gi 116812597  220 SLIKHRRIHTGERPYECSECGRSFA 244
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFK 25
 
Name Accession Description Interval E-value
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
14-55 7.56e-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: 84.83  E-value: 7.56e-21
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 116812597   14 SVTFEDVAVNFSLEEWSLLNEAQRCLYRDVMLETLTLISSLG 55
Cdd:pfam01352   1 SVTFEDVAVDFTQEEWALLDPAQRNLYRDVMLENYRNLVSLG 42
KRAB smart00349
krueppel associated box;
15-56 1.99e-16

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 73.01  E-value: 1.99e-16
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 116812597    15 VTFEDVAVNFSLEEWSLLNEAQRCLYRDVMLETLTLISSLGC 56
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGF 42
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
15-52 1.04e-14

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: 67.57  E-value: 1.04e-14
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 116812597  15 VTFEDVAVNFSLEEWSLLNEAQRCLYRDVMLET-LTLIS 52
Cdd:cd07765    1 VTFEDVAVYFSQEEWELLDPAQRDLYRDVMLENyENLVS 39
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
104-366 3.15e-09

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 58.55  E-value: 3.15e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812597 104 TEPRRDHKHRNVRTGERPYECSKYGKLFHQKPTLHIHERFHTGQKTYECSECGKSFHQSSSLLQRQTLHTRERPYECIEC 183
Cdd:COG5048  181 SSNLSLLISSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLSSSDSSSSASES 260
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812597 184 GKAFAEKSSLINHRKVHSGA-------KRYECNECGKSFAYTSSLIKHRR--IHTGE--RPYECSE--CGRSFAENSSLI 250
Cdd:COG5048  261 PRSSLPTASSQSSSPNESDSssekgfsLPIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCPYslCGKLFSRNDALK 340
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812597 251 KHLRVHTGERPYECV--ECGKSFRRSSSLLQHQRVHTR-----ERPYEC--SECGKSFSLRSNLIHHQRVHTGERHE--- 318
Cdd:COG5048  341 RHILLHTSISPAKEKllNSSSKFSPLLNNEPPQSLQQYkdlknDKKSETlsNSCIRNFKRDSNLSLHIITHLSFRPYnck 420
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 116812597 319 CGQCGKSFSRKSSLIIHLRVHTGERPYECSDCgKSFAENSSLIKHLRV 366
Cdd:COG5048  421 NPPCSKSFNRHYNLIPHKKIHTNHAPLLCSIL-KSFRRDLDLSNHGKD 467
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
132-396 2.97e-06

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 49.31  E-value: 2.97e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812597 132 HQKPTLHIHERFHTGQKTYECSECGKSFHQSSSLLQRQTLHTRERPYECIECGKAFAEKSSLINHRKVHSGAKRYECNEC 211
Cdd:COG5048  181 SSNLSLLISSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLSSSDSSSSASES 260
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812597 212 GKSFAYTSSLIKHRRIHTGER-------PYECSECGRSFAENSSLIKHLR--VHTGE--RPYECVE--CGKSFRRSSSLL 278
Cdd:COG5048  261 PRSSLPTASSQSSSPNESDSSsekgfslPIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCPYslCGKLFSRNDALK 340
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812597 279 QHQRVHTRERPYEC--SECGKSFSLRSNLIHHQRVHTgerhecgQCGKSFSRKSsliihlrvhtgERPYecSDCGKSFAE 356
Cdd:COG5048  341 RHILLHTSISPAKEklLNSSSKFSPLLNNEPPQSLQQ-------YKDLKNDKKS-----------ETLS--NSCIRNFKR 400
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 116812597 357 NSSLIKHLRVHTGERPYECID--CGKSFRHSSSFRRHQRVHT 396
Cdd:COG5048  401 DSNLSLHIITHLSFRPYNCKNppCSKSFNRHYNLIPHKKIHT 442
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
120-402 3.02e-06

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 48.92  E-value: 3.02e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812597 120 RPYECSKYGKLFHQKPTLHIHERFHTGQKTYECS--ECGKSFHQSSSLLQRQTLHTRERPYEC-IECGKAFAEKSSLINH 196
Cdd:COG5048   32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSysGCDKSFSRPLELSRHLRTHHNNPSDLNsKSLPLSNSKASSSSLS 111
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812597 197 RKVHSGAKRYECNECGKSFAYTSSLIKHRRIHTGERPYECSECGRSFAE----------------------NSSLIKHLR 254
Cdd:COG5048  112 SSSSNSNDNNLLSSHSLPPSSRDPQLPDLLSISNLRNNPLPGNNSSSVNtpqsnslhpplpanslskdpssNLSLLISSN 191
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812597 255 VHTGERPYECVECGKSFRRSSSLLQHQRVHTRERPYECSECGKSFSLRSNL-------IHHQRVHTGERHECGQCGKSFS 327
Cdd:COG5048  192 VSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLSqspsslsSSDSSSSASESPRSSLPTASSQ 271
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812597 328 RKSSLIIHLRVHTGER-PYECSDCGKSFAENSSLIKHLR--VHTGE--RPYEC--IDCGKSFRHSSSFRRHQRVHTGMRP 400
Cdd:COG5048  272 SSSPNESDSSSEKGFSlPIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCpySLCGKLFSRNDALKRHILLHTSISP 351

                 ..
gi 116812597 401 YK 402
Cdd:COG5048  352 AK 353
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
82-395 2.18e-05

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 46.23  E-value: 2.18e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812597  82 HSGERPYECGEY--RKLFKNKSCLTEPRRDHkHRNVRTGERPYECSKYGKLFHQKPTLHIHERFhtgqktYECSECGKSF 159
Cdd:COG5048   56 HTGEKPSQCSYSgcDKSFSRPLELSRHLRTH-HNNPSDLNSKSLPLSNSKASSSSLSSSSSNSN------DNNLLSSHSL 128
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812597 160 HQSSSLLQRQTLHTRERPYECiecgKAFAEKSSLINHRKVHSGAKRYECNECGKSFAYTSSLIKHRRIHTGERPYECSEC 239
Cdd:COG5048  129 PPSSRDPQLPDLLSISNLRNN----PLPGNNSSSVNTPQSNSLHPPLPANSLSKDPSSNLSLLISSNVSTSIPSSSENSP 204
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812597 240 GRSFAENSSLIKHLRVHTGERPYECVECGKSFRRSSSLLQHQRVHTRERPYECSEC-----GKSFSLRSNLIHH---QRV 311
Cdd:COG5048  205 LSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLSSSDSSSSASESprsslPTASSQSSSPNESdssSEK 284
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812597 312 HTGERHECGQCGKSFSRKSSLIIHLR--VHTGE--RPYEC--SDCGKSFAENSSLIKHLRVHTGERPYECI--DCGKSFR 383
Cdd:COG5048  285 GFSLPIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCpySLCGKLFSRNDALKRHILLHTSISPAKEKllNSSSKFS 364
                        330
                 ....*....|..
gi 116812597 384 HSSSFRRHQRVH 395
Cdd:COG5048  365 PLLNNEPPQSLQ 376
zf-H2C2_2 pfam13465
Zinc-finger double domain;
359-384 2.75e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.04  E-value: 2.75e-03
                          10        20
                  ....*....|....*....|....*.
gi 116812597  359 SLIKHLRVHTGERPYECIDCGKSFRH 384
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
SUF4-like cd20908
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
288-339 5.84e-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: 35.61  E-value: 5.84e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 116812597 288 RPYeCSECGKSFSLRSNLIHHQRvhtgERH-ECGQCGKSFSRKSSLIIH-LRVH 339
Cdd:cd20908    1 KPW-CYYCDREFDDEKILIQHQK----AKHfKCHICHKKLYTAGGLAVHcLQVH 49
zf-H2C2_2 pfam13465
Zinc-finger double domain;
220-244 6.15e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 33.88  E-value: 6.15e-03
                          10        20
                  ....*....|....*....|....*
gi 116812597  220 SLIKHRRIHTGERPYECSECGRSFA 244
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFK 25
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
290-312 7.68e-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: 33.81  E-value: 7.68e-03
                          10        20
                  ....*....|....*....|...
gi 116812597  290 YECSECGKSFSLRSNLIHHQRVH 312
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
276-300 8.60e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 33.50  E-value: 8.60e-03
                          10        20
                  ....*....|....*....|....*
gi 116812597  276 SLLQHQRVHTRERPYECSECGKSFS 300
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFK 25
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
262-284 8.82e-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: 33.43  E-value: 8.82e-03
                          10        20
                  ....*....|....*....|...
gi 116812597  262 YECVECGKSFRRSSSLLQHQRVH 284
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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