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Conserved domains on  [gi|2462495459|ref|XP_054187289|]
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zinc finger protein 311 isoform X5 [Homo sapiens]

Protein Classification

KRAB domain-containing zinc finger protein( domain architecture ID 12204378)

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 smart00349
krueppel associated box;
72-132 3.88e-29

krueppel associated box;


:

Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 109.99  E-value: 3.88e-29
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462495459   72 VTFEDVAVNFTNREWQCLTYAQRHLYKDVMLENYGNMVSLGFPFPKPPLISHLEREVDPCV 132
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQVPKPDLISQLEQGEEPWI 61
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
281-608 5.18e-09

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


:

Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 58.94  E-value: 5.18e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495459 281 KPHVCNECGKAFKTRNQLSMHRIIHTGEKPFNCTQ--CGKAFNSRSALCRHKKTHSGEKPHECRDCGKAFKTRNRLCMHQ 358
Cdd:COG5048    32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYsgCDKSFSRPLELSRHLRTHHNNPSDLNSKSLPLSNSKASSSSLS 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495459 359 LIHTGE-KPYKCNCCGKAFQFKHSLTIHGRIHTGEKPYECEEC-GKAFSGSSDLTKHIRIHTGerpyecSKCGRAFSRSS 436
Cdd:COG5048   112 SSSSNSnDNNLLSSHSLPPSSRDPQLPDLLSISNLRNNPLPGNnSSSVNTPQSNSLHPPLPAN------SLSKDPSSNLS 185
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495459 437 DLSKHKRIHTREKHYGCPQCGKDFSIKAELTKHRRIHTEEkRYRCEECGKAFRHNCKRRAHEREHTGEKPYQCRDCGKTF 516
Cdd:COG5048   186 LLISSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSS-SLPLTTNSQLSPKSLLSQSPSSLSSSDSSSSASESPRSS 264
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495459 517 Q--DQHCLTIHQRIHTGE-----KPYKCLECGKAFSGKSNLTNHRR--IHTGE--KPHKC--EVCGMAFHHSSVLRQHKR 583
Cdd:COG5048   265 LptASSQSSSPNESDSSSekgfsLPIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCpySLCGKLFSRNDALKRHIL 344
                         330       340
                  ....*....|....*....|....*
gi 2462495459 584 IHTGEKPYTCSECGTSFRQGSALIG 608
Cdd:COG5048   345 LHTSISPAKEKLLNSSSKFSPLLNN 369
zf-H2C2_2 pfam13465
Zinc-finger double domain;
609-628 2.36e-03

Zinc-finger double domain;


:

Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.81  E-value: 2.36e-03
                          10        20
                  ....*....|....*....|
gi 2462495459 609 HKRVHTGEKPYECEECGKAF 628
Cdd:pfam13465   5 HMRTHTGEKPYKCPECGKSF 24
 
Name Accession Description Interval E-value
KRAB smart00349
krueppel associated box;
72-132 3.88e-29

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 109.99  E-value: 3.88e-29
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462495459   72 VTFEDVAVNFTNREWQCLTYAQRHLYKDVMLENYGNMVSLGFPFPKPPLISHLEREVDPCV 132
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQVPKPDLISQLEQGEEPWI 61
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
71-112 3.25e-22

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: 89.45  E-value: 3.25e-22
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 2462495459  71 SVTFEDVAVNFTNREWQCLTYAQRHLYKDVMLENYGNMVSLG 112
Cdd:pfam01352   1 SVTFEDVAVDFTQEEWALLDPAQRNLYRDVMLENYRNLVSLG 42
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
72-111 2.83e-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: 81.06  E-value: 2.83e-19
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 2462495459  72 VTFEDVAVNFTNREWQCLTYAQRHLYKDVMLENYGNMVSL 111
Cdd:cd07765     1 VTFEDVAVYFSQEEWELLDPAQRDLYRDVMLENYENLVSL 40
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
281-608 5.18e-09

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 58.94  E-value: 5.18e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495459 281 KPHVCNECGKAFKTRNQLSMHRIIHTGEKPFNCTQ--CGKAFNSRSALCRHKKTHSGEKPHECRDCGKAFKTRNRLCMHQ 358
Cdd:COG5048    32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYsgCDKSFSRPLELSRHLRTHHNNPSDLNSKSLPLSNSKASSSSLS 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495459 359 LIHTGE-KPYKCNCCGKAFQFKHSLTIHGRIHTGEKPYECEEC-GKAFSGSSDLTKHIRIHTGerpyecSKCGRAFSRSS 436
Cdd:COG5048   112 SSSSNSnDNNLLSSHSLPPSSRDPQLPDLLSISNLRNNPLPGNnSSSVNTPQSNSLHPPLPAN------SLSKDPSSNLS 185
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495459 437 DLSKHKRIHTREKHYGCPQCGKDFSIKAELTKHRRIHTEEkRYRCEECGKAFRHNCKRRAHEREHTGEKPYQCRDCGKTF 516
Cdd:COG5048   186 LLISSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSS-SLPLTTNSQLSPKSLLSQSPSSLSSSDSSSSASESPRSS 264
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495459 517 Q--DQHCLTIHQRIHTGE-----KPYKCLECGKAFSGKSNLTNHRR--IHTGE--KPHKC--EVCGMAFHHSSVLRQHKR 583
Cdd:COG5048   265 LptASSQSSSPNESDSSSekgfsLPIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCpySLCGKLFSRNDALKRHIL 344
                         330       340
                  ....*....|....*....|....*
gi 2462495459 584 IHTGEKPYTCSECGTSFRQGSALIG 608
Cdd:COG5048   345 LHTSISPAKEKLLNSSSKFSPLLNN 369
SUF4-like cd20908
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
505-553 5.80e-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: 39.08  E-value: 5.80e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 2462495459 505 KPYqCRDCGKTFQDQHCLTIHQRIHTgekpYKCLECGKAFSGKSNLTNH 553
Cdd:cd20908     1 KPW-CYYCDREFDDEKILIQHQKAKH----FKCHICHKKLYTAGGLAVH 44
zf-H2C2_2 pfam13465
Zinc-finger double domain;
328-350 6.99e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 37.35  E-value: 6.99e-04
                          10        20
                  ....*....|....*....|...
gi 2462495459 328 RHKKTHSGEKPHECRDCGKAFKT 350
Cdd:pfam13465   4 RHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
609-628 2.36e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.81  E-value: 2.36e-03
                          10        20
                  ....*....|....*....|
gi 2462495459 609 HKRVHTGEKPYECEECGKAF 628
Cdd:pfam13465   5 HMRTHTGEKPYKCPECGKSF 24
 
Name Accession Description Interval E-value
KRAB smart00349
krueppel associated box;
72-132 3.88e-29

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 109.99  E-value: 3.88e-29
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462495459   72 VTFEDVAVNFTNREWQCLTYAQRHLYKDVMLENYGNMVSLGFPFPKPPLISHLEREVDPCV 132
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQVPKPDLISQLEQGEEPWI 61
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
71-112 3.25e-22

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: 89.45  E-value: 3.25e-22
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 2462495459  71 SVTFEDVAVNFTNREWQCLTYAQRHLYKDVMLENYGNMVSLG 112
Cdd:pfam01352   1 SVTFEDVAVDFTQEEWALLDPAQRNLYRDVMLENYRNLVSLG 42
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
72-111 2.83e-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: 81.06  E-value: 2.83e-19
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 2462495459  72 VTFEDVAVNFTNREWQCLTYAQRHLYKDVMLENYGNMVSL 111
Cdd:cd07765     1 VTFEDVAVYFSQEEWELLDPAQRDLYRDVMLENYENLVSL 40
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
281-608 5.18e-09

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 58.94  E-value: 5.18e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495459 281 KPHVCNECGKAFKTRNQLSMHRIIHTGEKPFNCTQ--CGKAFNSRSALCRHKKTHSGEKPHECRDCGKAFKTRNRLCMHQ 358
Cdd:COG5048    32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYsgCDKSFSRPLELSRHLRTHHNNPSDLNSKSLPLSNSKASSSSLS 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495459 359 LIHTGE-KPYKCNCCGKAFQFKHSLTIHGRIHTGEKPYECEEC-GKAFSGSSDLTKHIRIHTGerpyecSKCGRAFSRSS 436
Cdd:COG5048   112 SSSSNSnDNNLLSSHSLPPSSRDPQLPDLLSISNLRNNPLPGNnSSSVNTPQSNSLHPPLPAN------SLSKDPSSNLS 185
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495459 437 DLSKHKRIHTREKHYGCPQCGKDFSIKAELTKHRRIHTEEkRYRCEECGKAFRHNCKRRAHEREHTGEKPYQCRDCGKTF 516
Cdd:COG5048   186 LLISSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSS-SLPLTTNSQLSPKSLLSQSPSSLSSSDSSSSASESPRSS 264
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495459 517 Q--DQHCLTIHQRIHTGE-----KPYKCLECGKAFSGKSNLTNHRR--IHTGE--KPHKC--EVCGMAFHHSSVLRQHKR 583
Cdd:COG5048   265 LptASSQSSSPNESDSSSekgfsLPIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCpySLCGKLFSRNDALKRHIL 344
                         330       340
                  ....*....|....*....|....*
gi 2462495459 584 IHTGEKPYTCSECGTSFRQGSALIG 608
Cdd:COG5048   345 LHTSISPAKEKLLNSSSKFSPLLNN 369
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
231-553 2.34e-07

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 53.93  E-value: 2.34e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495459 231 VLSKNLNPNSKHSQCNKVLIAQKLHECAR--------CGKNFSWHSDLILHEQIHSGEKPHVCNECGKAFKTRNQLSMHR 302
Cdd:COG5048   140 LLSISNLRNNPLPGNNSSSVNTPQSNSLHpplpanslSKDPSSNLSLLISSNVSTSIPSSSENSPLSSSYSIPSSSSDQN 219
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495459 303 IIHTgEKPFNCTQCGKAFNSRSALCRHKKTHSGEKPHECRDCGKAFKTRNRLCMHQLIHTGE-------KPYKCNCCGKA 375
Cdd:COG5048   220 LENS-SSSLPLTTNSQLSPKSLLSQSPSSLSSSDSSSSASESPRSSLPTASSQSSSPNESDSssekgfsLPIKSKQCNIS 298
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495459 376 FQFKHSLTIH--GRIHTGE--KPYECEE--CGKAFSGSSDLTKHIRIHTGERPYEC--SKCGRAFSRSSDLSKHKRIHtr 447
Cdd:COG5048   299 FSRSSPLTRHlrSVNHSGEslKPFSCPYslCGKLFSRNDALKRHILLHTSISPAKEklLNSSSKFSPLLNNEPPQSLQ-- 376
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495459 448 ekhygcPQCGKDFSIKAELTKHRRIHTEEKRYrceecgkafrhncKRRAHEREHTGEKPYQCRD--CGKTFQDQHCLTIH 525
Cdd:COG5048   377 ------QYKDLKNDKKSETLSNSCIRNFKRDS-------------NLSLHIITHLSFRPYNCKNppCSKSFNRHYNLIPH 437
                         330       340
                  ....*....|....*....|....*...
gi 2462495459 526 QRIHTgEKPYKCLECGKAFSGKSNLTNH 553
Cdd:COG5048   438 KKIHT-NHAPLLCSILKSFRRDLDLSNH 464
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
206-443 1.11e-06

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 51.62  E-value: 1.11e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495459 206 SIREKLREEKEGSEEVTCKKGKNQK--VLSKNLNPNSKHSQCNkvliAQKLHECARCGKNFSWHSDLILHEQIHSG-EKP 282
Cdd:COG5048   214 SSSDQNLENSSSSLPLTTNSQLSPKslLSQSPSSLSSSDSSSS----ASESPRSSLPTASSQSSSPNESDSSSEKGfSLP 289
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495459 283 HVCNECGKAFKTRNQLSMHR--IIHTGE--KPFNCT--QCGKAFNSRSALCRHKKTHSGEKPHECRDC------GKAFKT 350
Cdd:COG5048   290 IKSKQCNISFSRSSPLTRHLrsVNHSGEslKPFSCPysLCGKLFSRNDALKRHILLHTSISPAKEKLLnssskfSPLLNN 369
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495459 351 RNRLCMHQliHTGEKPYKCNCCGKAFQFKHSLTIHGRI-----HTGEKPYECE--ECGKAFSGSSDLTKHIRIHTGERPY 423
Cdd:COG5048   370 EPPQSLQQ--YKDLKNDKKSETLSNSCIRNFKRDSNLSlhiitHLSFRPYNCKnpPCSKSFNRHYNLIPHKKIHTNHAPL 447
                         250       260
                  ....*....|....*....|
gi 2462495459 424 ECSKCGRaFSRSSDLSKHKR 443
Cdd:COG5048   448 LCSILKS-FRRDLDLSNHGK 466
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
365-648 3.22e-05

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 47.00  E-value: 3.22e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495459 365 KPYKCNCCGKAFQFKHSLTIHGRIHTGEKPYEC--EECGKAFSGSSDLTKHIRIHTGERPYECSKCGR---AFSRSSDLS 439
Cdd:COG5048    32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCsySGCDKSFSRPLELSRHLRTHHNNPSDLNSKSLPlsnSKASSSSLS 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495459 440 KHkrIHTREKHYGCPQCGKDFSIKAELTKHRRIHTEEKRYRCEECGKAFRH----NCKRRAHEREHTGEKPYQCRD---- 511
Cdd:COG5048   112 SS--SSNSNDNNLLSSHSLPPSSRDPQLPDLLSISNLRNNPLPGNNSSSVNtpqsNSLHPPLPANSLSKDPSSNLSllis 189
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495459 512 --------CGKTFQDQH-------------------CLTIHQRIHTGEKPYK---------------CLECGKAFSGKSN 549
Cdd:COG5048   190 snvstsipSSSENSPLSssysipssssdqnlensssSLPLTTNSQLSPKSLLsqspsslsssdssssASESPRSSLPTAS 269
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495459 550 LTNHRRIHTGE-------KPHKCEVCGMAFHHSSVLRQHKR--IHTGE--KPYTCSE--CGTSFRQGSALIGHKRVHTGE 616
Cdd:COG5048   270 SQSSSPNESDSssekgfsLPIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCPYslCGKLFSRNDALKRHILLHTSI 349
                         330       340       350
                  ....*....|....*....|....*....|....
gi 2462495459 617 KPYEC--EECGKAFRVSSNLTGHKKRKHQVWSTH 648
Cdd:COG5048   350 SPAKEklLNSSSKFSPLLNNEPPQSLQQYKDLKN 383
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
408-604 8.94e-05

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 45.46  E-value: 8.94e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495459 408 SDLTKHIRIHTgerPYECSKCGRAFSRSSDLSKHKR--IHTRE--KHYGCP--QCGKDFSIKAELTKHRRIHTeekryrc 481
Cdd:COG5048   278 SDSSSEKGFSL---PIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCPysLCGKLFSRNDALKRHILLHT------- 347
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495459 482 eecgKAFRHNCKRRAHEREHTGEKPYqcrdCGKTFQDQHCLTIHQRIHTGEKPykclECGKAFSGKSNLTNHRRIHTGEK 561
Cdd:COG5048   348 ----SISPAKEKLLNSSSKFSPLLNN----EPPQSLQQYKDLKNDKKSETLSN----SCIRNFKRDSNLSLHIITHLSFR 415
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 2462495459 562 PH--KCEVCGMAFHHSSVLRQHKRIHTGEKPYTCSECGTSFRQGS 604
Cdd:COG5048   416 PYncKNPPCSKSFNRHYNLIPHKKIHTNHAPLLCSILKSFRRDLD 460
SUF4-like cd20908
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
505-553 5.80e-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: 39.08  E-value: 5.80e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 2462495459 505 KPYqCRDCGKTFQDQHCLTIHQRIHTgekpYKCLECGKAFSGKSNLTNH 553
Cdd:cd20908     1 KPW-CYYCDREFDDEKILIQHQKAKH----FKCHICHKKLYTAGGLAVH 44
zf-H2C2_2 pfam13465
Zinc-finger double domain;
328-350 6.99e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 37.35  E-value: 6.99e-04
                          10        20
                  ....*....|....*....|...
gi 2462495459 328 RHKKTHSGEKPHECRDCGKAFKT 350
Cdd:pfam13465   4 RHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
549-572 9.85e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.97  E-value: 9.85e-04
                          10        20
                  ....*....|....*....|....
gi 2462495459 549 NLTNHRRIHTGEKPHKCEVCGMAF 572
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSF 24
zf-H2C2_2 pfam13465
Zinc-finger double domain;
409-434 1.03e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.97  E-value: 1.03e-03
                          10        20
                  ....*....|....*....|....*.
gi 2462495459 409 DLTKHIRIHTGERPYECSKCGRAFSR 434
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
SFP1 COG5189
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ...
263-385 1.50e-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: 1.50e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495459 263 NFSWHSDLILHEQIHSGEKPHVCNECGKAFKTRNQL----SMHRIIHTGEKPFNC--TQCGKAFNSRSALCRHKKT-HSG 335
Cdd:COG5189   298 NKEIRGGISTGEMIDVRKLPCTNSSSNGKLAHGGERnidtPSRMLKVKDGKPYKCpvEGCNKKYKNQNGLKYHMLHgHQN 377
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2462495459 336 EKPHECRDCGKafktrnrlcmHQLIHTGEKPYKCNCCGKAFQFKHSLTIH 385
Cdd:COG5189   378 QKLHENPSPEK----------MNIFSAKDKPYRCEVCDKRYKNLNGLKYH 417
zf-H2C2_2 pfam13465
Zinc-finger double domain;
522-545 1.53e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.20  E-value: 1.53e-03
                          10        20
                  ....*....|....*....|....
gi 2462495459 522 LTIHQRIHTGEKPYKCLECGKAFS 545
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFK 25
SFP1 COG5189
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ...
554-642 1.85e-03

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


Pssm-ID: 227516 [Multi-domain]  Cd Length: 423  Bit Score: 41.24  E-value: 1.85e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495459 554 RRIHT-GEKPHKCEV--CGMAFHHSSVLRQHkRIHtgekpytcSECGTSFRQGSALIGHKRVHTGEKPYECEECGKAFRV 630
Cdd:COG5189   340 RMLKVkDGKPYKCPVegCNKKYKNQNGLKYH-MLH--------GHQNQKLHENPSPEKMNIFSAKDKPYRCEVCDKRYKN 410
                          90
                  ....*....|..
gi 2462495459 631 SSNLTGHKKRKH 642
Cdd:COG5189   411 LNGLKYHRKHSH 422
zf-H2C2_2 pfam13465
Zinc-finger double domain;
578-602 1.86e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.20  E-value: 1.86e-03
                          10        20
                  ....*....|....*....|....*
gi 2462495459 578 LRQHKRIHTGEKPYTCSECGTSFRQ 602
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
609-628 2.36e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.81  E-value: 2.36e-03
                          10        20
                  ....*....|....*....|
gi 2462495459 609 HKRVHTGEKPYECEECGKAF 628
Cdd:pfam13465   5 HMRTHTGEKPYKCPECGKSF 24
zf-H2C2_2 pfam13465
Zinc-finger double domain;
298-322 3.26e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.42  E-value: 3.26e-03
                          10        20
                  ....*....|....*....|....*
gi 2462495459 298 LSMHRIIHTGEKPFNCTQCGKAFNS 322
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
465-490 3.30e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.42  E-value: 3.30e-03
                          10        20
                  ....*....|....*....|....*.
gi 2462495459 465 ELTKHRRIHTEEKRYRCEECGKAFRH 490
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
395-417 3.84e-03

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


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 35.35  E-value: 3.84e-03
                          10        20
                  ....*....|....*....|...
gi 2462495459 395 YECEECGKAFSGSSDLTKHIRIH 417
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
535-557 6.85e-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: 6.85e-03
                          10        20
                  ....*....|....*....|...
gi 2462495459 535 YKCLECGKAFSGKSNLTNHRRIH 557
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
423-445 6.92e-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: 6.92e-03
                          10        20
                  ....*....|....*....|...
gi 2462495459 423 YECSKCGRAFSRSSDLSKHKRIH 445
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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