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Conserved domains on  [gi|2462489642|ref|XP_054184447|]
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zinc finger protein 311 isoform X1 [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;
97-157 4.08e-29

krueppel associated box;


:

Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 109.99  E-value: 4.08e-29
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462489642   97 VTFEDVAVNFTNREWQCLTYAQRHLYKDVMLENYGNMVSLGFPFPKPPLISHLEREVDPCV 157
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQVPKPDLISQLEQGEEPWI 61
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
306-633 7.75e-09

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


:

Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 58.55  E-value: 7.75e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462489642 306 KPHVCNECGKAFKTRNQLSMHRIIHTGEKPFNCTQ--CGKAFNSRSALCRHKKTHSGEKPHECRDCGKAFKTRNRLCMHQ 383
Cdd:COG5048    32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYsgCDKSFSRPLELSRHLRTHHNNPSDLNSKSLPLSNSKASSSSLS 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462489642 384 LIHTGE-KPYKCNCCGKAFQFKHSLTIHGRIHTGEKPYECEEC-GKAFSGSSDLTKHIRIHTGerpyecSKCGRAFSRSS 461
Cdd:COG5048   112 SSSSNSnDNNLLSSHSLPPSSRDPQLPDLLSISNLRNNPLPGNnSSSVNTPQSNSLHPPLPAN------SLSKDPSSNLS 185
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462489642 462 DLSKHKRIHTREKHYGCPQCGKDFSIKAELTKHRRIHTEEkRYRCEECGKAFRHNCKRRAHEREHTGEKPYQCRDCGKTF 541
Cdd:COG5048   186 LLISSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSS-SLPLTTNSQLSPKSLLSQSPSSLSSSDSSSSASESPRSS 264
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462489642 542 QDK--HCLTIHQRIHTGE-----KPYKCLECGKAFSGKSNLTNHRR--IHTGE--KPHKC--EVCGMAFHHSSVLRQHKR 608
Cdd:COG5048   265 LPTasSQSSSPNESDSSSekgfsLPIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCpySLCGKLFSRNDALKRHIL 344
                         330       340
                  ....*....|....*....|....*
gi 2462489642 609 IHTGEKPYTCSECGTSFRQGSALIG 633
Cdd:COG5048   345 LHTSISPAKEKLLNSSSKFSPLLNN 369
zf-H2C2_2 pfam13465
Zinc-finger double domain;
634-653 2.45e-03

Zinc-finger double domain;


:

Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.81  E-value: 2.45e-03
                          10        20
                  ....*....|....*....|
gi 2462489642 634 HKRVHTGEKPYECEECGKAF 653
Cdd:pfam13465   5 HMRTHTGEKPYKCPECGKSF 24
 
Name Accession Description Interval E-value
KRAB smart00349
krueppel associated box;
97-157 4.08e-29

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 109.99  E-value: 4.08e-29
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462489642   97 VTFEDVAVNFTNREWQCLTYAQRHLYKDVMLENYGNMVSLGFPFPKPPLISHLEREVDPCV 157
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQVPKPDLISQLEQGEEPWI 61
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
96-137 3.37e-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: 3.37e-22
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 2462489642  96 SVTFEDVAVNFTNREWQCLTYAQRHLYKDVMLENYGNMVSLG 137
Cdd:pfam01352   1 SVTFEDVAVDFTQEEWALLDPAQRNLYRDVMLENYRNLVSLG 42
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
97-136 2.94e-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: 2.94e-19
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 2462489642  97 VTFEDVAVNFTNREWQCLTYAQRHLYKDVMLENYGNMVSL 136
Cdd:cd07765     1 VTFEDVAVYFSQEEWELLDPAQRDLYRDVMLENYENLVSL 40
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
306-633 7.75e-09

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 58.55  E-value: 7.75e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462489642 306 KPHVCNECGKAFKTRNQLSMHRIIHTGEKPFNCTQ--CGKAFNSRSALCRHKKTHSGEKPHECRDCGKAFKTRNRLCMHQ 383
Cdd:COG5048    32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYsgCDKSFSRPLELSRHLRTHHNNPSDLNSKSLPLSNSKASSSSLS 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462489642 384 LIHTGE-KPYKCNCCGKAFQFKHSLTIHGRIHTGEKPYECEEC-GKAFSGSSDLTKHIRIHTGerpyecSKCGRAFSRSS 461
Cdd:COG5048   112 SSSSNSnDNNLLSSHSLPPSSRDPQLPDLLSISNLRNNPLPGNnSSSVNTPQSNSLHPPLPAN------SLSKDPSSNLS 185
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462489642 462 DLSKHKRIHTREKHYGCPQCGKDFSIKAELTKHRRIHTEEkRYRCEECGKAFRHNCKRRAHEREHTGEKPYQCRDCGKTF 541
Cdd:COG5048   186 LLISSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSS-SLPLTTNSQLSPKSLLSQSPSSLSSSDSSSSASESPRSS 264
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462489642 542 QDK--HCLTIHQRIHTGE-----KPYKCLECGKAFSGKSNLTNHRR--IHTGE--KPHKC--EVCGMAFHHSSVLRQHKR 608
Cdd:COG5048   265 LPTasSQSSSPNESDSSSekgfsLPIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCpySLCGKLFSRNDALKRHIL 344
                         330       340
                  ....*....|....*....|....*
gi 2462489642 609 IHTGEKPYTCSECGTSFRQGSALIG 633
Cdd:COG5048   345 LHTSISPAKEKLLNSSSKFSPLLNN 369
zf-H2C2_2 pfam13465
Zinc-finger double domain;
353-375 7.24e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 37.35  E-value: 7.24e-04
                          10        20
                  ....*....|....*....|...
gi 2462489642 353 RHKKTHSGEKPHECRDCGKAFKT 375
Cdd:pfam13465   4 RHMRTHTGEKPYKCPECGKSFKS 26
SUF4-like cd20908
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
530-578 1.56e-03

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


Pssm-ID: 411020 [Multi-domain]  Cd Length: 82  Bit Score: 37.92  E-value: 1.56e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 2462489642 530 KPYqCRDCGKTFQDKHCLTIHQRIHTgekpYKCLECGKAFSGKSNLTNH 578
Cdd:cd20908     1 KPW-CYYCDREFDDEKILIQHQKAKH----FKCHICHKKLYTAGGLAVH 44
zf-H2C2_2 pfam13465
Zinc-finger double domain;
634-653 2.45e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.81  E-value: 2.45e-03
                          10        20
                  ....*....|....*....|
gi 2462489642 634 HKRVHTGEKPYECEECGKAF 653
Cdd:pfam13465   5 HMRTHTGEKPYKCPECGKSF 24
 
Name Accession Description Interval E-value
KRAB smart00349
krueppel associated box;
97-157 4.08e-29

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 109.99  E-value: 4.08e-29
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462489642   97 VTFEDVAVNFTNREWQCLTYAQRHLYKDVMLENYGNMVSLGFPFPKPPLISHLEREVDPCV 157
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQVPKPDLISQLEQGEEPWI 61
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
96-137 3.37e-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: 3.37e-22
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 2462489642  96 SVTFEDVAVNFTNREWQCLTYAQRHLYKDVMLENYGNMVSLG 137
Cdd:pfam01352   1 SVTFEDVAVDFTQEEWALLDPAQRNLYRDVMLENYRNLVSLG 42
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
97-136 2.94e-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: 2.94e-19
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 2462489642  97 VTFEDVAVNFTNREWQCLTYAQRHLYKDVMLENYGNMVSL 136
Cdd:cd07765     1 VTFEDVAVYFSQEEWELLDPAQRDLYRDVMLENYENLVSL 40
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
306-633 7.75e-09

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 58.55  E-value: 7.75e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462489642 306 KPHVCNECGKAFKTRNQLSMHRIIHTGEKPFNCTQ--CGKAFNSRSALCRHKKTHSGEKPHECRDCGKAFKTRNRLCMHQ 383
Cdd:COG5048    32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYsgCDKSFSRPLELSRHLRTHHNNPSDLNSKSLPLSNSKASSSSLS 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462489642 384 LIHTGE-KPYKCNCCGKAFQFKHSLTIHGRIHTGEKPYECEEC-GKAFSGSSDLTKHIRIHTGerpyecSKCGRAFSRSS 461
Cdd:COG5048   112 SSSSNSnDNNLLSSHSLPPSSRDPQLPDLLSISNLRNNPLPGNnSSSVNTPQSNSLHPPLPAN------SLSKDPSSNLS 185
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462489642 462 DLSKHKRIHTREKHYGCPQCGKDFSIKAELTKHRRIHTEEkRYRCEECGKAFRHNCKRRAHEREHTGEKPYQCRDCGKTF 541
Cdd:COG5048   186 LLISSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSS-SLPLTTNSQLSPKSLLSQSPSSLSSSDSSSSASESPRSS 264
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462489642 542 QDK--HCLTIHQRIHTGE-----KPYKCLECGKAFSGKSNLTNHRR--IHTGE--KPHKC--EVCGMAFHHSSVLRQHKR 608
Cdd:COG5048   265 LPTasSQSSSPNESDSSSekgfsLPIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCpySLCGKLFSRNDALKRHIL 344
                         330       340
                  ....*....|....*....|....*
gi 2462489642 609 IHTGEKPYTCSECGTSFRQGSALIG 633
Cdd:COG5048   345 LHTSISPAKEKLLNSSSKFSPLLNN 369
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
231-468 1.01e-06

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 51.62  E-value: 1.01e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462489642 231 SIREKLREEKEGSEEVTCKKGKNQK--VLSKNLNPNSKHSQCNkvliAQKLHECARCGKNFSWHSDLILHEQIHSG-EKP 307
Cdd:COG5048   214 SSSDQNLENSSSSLPLTTNSQLSPKslLSQSPSSLSSSDSSSS----ASESPRSSLPTASSQSSSPNESDSSSEKGfSLP 289
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462489642 308 HVCNECGKAFKTRNQLSMHR--IIHTGE--KPFNCT--QCGKAFNSRSALCRHKKTHSGEKPHECRDC------GKAFKT 375
Cdd:COG5048   290 IKSKQCNISFSRSSPLTRHLrsVNHSGEslKPFSCPysLCGKLFSRNDALKRHILLHTSISPAKEKLLnssskfSPLLNN 369
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462489642 376 RNRLCMHQliHTGEKPYKCNCCGKAFQFKHSLTIHGRI-----HTGEKPYECE--ECGKAFSGSSDLTKHIRIHTGERPY 448
Cdd:COG5048   370 EPPQSLQQ--YKDLKNDKKSETLSNSCIRNFKRDSNLSlhiitHLSFRPYNCKnpPCSKSFNRHYNLIPHKKIHTNHAPL 447
                         250       260
                  ....*....|....*....|
gi 2462489642 449 ECSKCGRaFSRSSDLSKHKR 468
Cdd:COG5048   448 LCSILKS-FRRDLDLSNHGK 466
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
256-578 3.18e-06

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 50.08  E-value: 3.18e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462489642 256 VLSKNLNPNSKHSQCNKVLIAQKLHECAR--------CGKNFSWHSDLILHEQIHSGEKPHVCNECGKAFKTRNQLSMHR 327
Cdd:COG5048   140 LLSISNLRNNPLPGNNSSSVNTPQSNSLHpplpanslSKDPSSNLSLLISSNVSTSIPSSSENSPLSSSYSIPSSSSDQN 219
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462489642 328 IIHTgEKPFNCTQCGKAFNSRSALCRHKKTHSGEKPHECRDCGKAFKTRNRLCMHQLIHtgekpykcnccgkafqfkHSL 407
Cdd:COG5048   220 LENS-SSSLPLTTNSQLSPKSLLSQSPSSLSSSDSSSSASESPRSSLPTASSQSSSPNE------------------SDS 280
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462489642 408 TIHGRIHTgekPYECEECGKAFSGSSDLTKHIR--IHTGE--RPYEC--SKCGRAFSRSSDLSKHKRIHTREKHYGCP-- 479
Cdd:COG5048   281 SSEKGFSL---PIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCpySLCGKLFSRNDALKRHILLHTSISPAKEKll 357
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462489642 480 QCGKDFSIK-----AELTKHRRIHTEEKRYRCEECGKAFrhNCKRRAHEREHT------GEKPYQCRDCGKTFQDKHCLT 548
Cdd:COG5048   358 NSSSKFSPLlnnepPQSLQQYKDLKNDKKSETLSNSCIR--NFKRDSNLSLHIithlsfRPYNCKNPPCSKSFNRHYNLI 435
                         330       340       350
                  ....*....|....*....|....*....|
gi 2462489642 549 IHQRIHTgEKPYKCLECGKAFSGKSNLTNH 578
Cdd:COG5048   436 PHKKIHT-NHAPLLCSILKSFRRDLDLSNH 464
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
390-667 3.75e-05

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 46.61  E-value: 3.75e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462489642 390 KPYKCNCCGKAFQFKHSLTIHGRIHTGEKPYEC--EECGKAFSGSSDLTKHIRIHTGERPYECSKCGR---AFSRSSDLS 464
Cdd:COG5048    32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCsySGCDKSFSRPLELSRHLRTHHNNPSDLNSKSLPlsnSKASSSSLS 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462489642 465 KHkrIHTREKHYGCPQCGKDFSIKAELTKHRRIHTEEKRYRCEECGKAFRH----NCKRRAHEREHTGEKPYQCRDcgkt 540
Cdd:COG5048   112 SS--SSNSNDNNLLSSHSLPPSSRDPQLPDLLSISNLRNNPLPGNNSSSVNtpqsNSLHPPLPANSLSKDPSSNLS---- 185
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462489642 541 fqdkhcLTIHQRIHTGEKPYKCLECGKAFSGKSNLTNHRRIHTGEKPHKCEVCGMAFHHSSVLRQHKRIHTGEKPYTCSE 620
Cdd:COG5048   186 ------LLISSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLSSSDSSSSASE 259
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2462489642 621 CGTSFRQGSALIGHKRVHTGE-------KPYECEECGKAFRVSSNLTGHKKRKH 667
Cdd:COG5048   260 SPRSSLPTASSQSSSPNESDSssekgfsLPIKSKQCNISFSRSSPLTRHLRSVN 313
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
433-629 1.21e-04

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 45.07  E-value: 1.21e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462489642 433 SDLTKHIRIHTgerPYECSKCGRAFSRSSDLSKHKR--IHTRE--KHYGCP--QCGKDFSIKAELTKHRRIHTeekryrc 506
Cdd:COG5048   278 SDSSSEKGFSL---PIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCPysLCGKLFSRNDALKRHILLHT------- 347
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462489642 507 eecgKAFRHNCKRRAHEREHTGEKPYqcrdCGKTFQDKHCLTIHQRIHTGEKPykclECGKAFSGKSNLTNHRRIHTGEK 586
Cdd:COG5048   348 ----SISPAKEKLLNSSSKFSPLLNN----EPPQSLQQYKDLKNDKKSETLSN----SCIRNFKRDSNLSLHIITHLSFR 415
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 2462489642 587 PH--KCEVCGMAFHHSSVLRQHKRIHTGEKPYTCSECGTSFRQGS 629
Cdd:COG5048   416 PYncKNPPCSKSFNRHYNLIPHKKIHTNHAPLLCSILKSFRRDLD 460
zf-H2C2_2 pfam13465
Zinc-finger double domain;
353-375 7.24e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 37.35  E-value: 7.24e-04
                          10        20
                  ....*....|....*....|...
gi 2462489642 353 RHKKTHSGEKPHECRDCGKAFKT 375
Cdd:pfam13465   4 RHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
574-597 1.02e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.97  E-value: 1.02e-03
                          10        20
                  ....*....|....*....|....
gi 2462489642 574 NLTNHRRIHTGEKPHKCEVCGMAF 597
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSF 24
zf-H2C2_2 pfam13465
Zinc-finger double domain;
434-459 1.07e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.97  E-value: 1.07e-03
                          10        20
                  ....*....|....*....|....*.
gi 2462489642 434 DLTKHIRIHTGERPYECSKCGRAFSR 459
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
SUF4-like cd20908
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
530-578 1.56e-03

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


Pssm-ID: 411020 [Multi-domain]  Cd Length: 82  Bit Score: 37.92  E-value: 1.56e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 2462489642 530 KPYqCRDCGKTFQDKHCLTIHQRIHTgekpYKCLECGKAFSGKSNLTNH 578
Cdd:cd20908     1 KPW-CYYCDREFDDEKILIQHQKAKH----FKCHICHKKLYTAGGLAVH 44
zf-H2C2_2 pfam13465
Zinc-finger double domain;
547-570 1.59e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.20  E-value: 1.59e-03
                          10        20
                  ....*....|....*....|....
gi 2462489642 547 LTIHQRIHTGEKPYKCLECGKAFS 570
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFK 25
SFP1 COG5189
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ...
288-410 1.66e-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: 1.66e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462489642 288 NFSWHSDLILHEQIHSGEKPHVCNECGKAFKTRNQL----SMHRIIHTGEKPFNC--TQCGKAFNSRSALCRHKKT-HSG 360
Cdd:COG5189   298 NKEIRGGISTGEMIDVRKLPCTNSSSNGKLAHGGERnidtPSRMLKVKDGKPYKCpvEGCNKKYKNQNGLKYHMLHgHQN 377
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2462489642 361 EKPHECRDCGKafktrnrlcmHQLIHTGEKPYKCNCCGKAFQFKHSLTIH 410
Cdd:COG5189   378 QKLHENPSPEK----------MNIFSAKDKPYRCEVCDKRYKNLNGLKYH 417
zf-H2C2_2 pfam13465
Zinc-finger double domain;
603-627 1.93e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.20  E-value: 1.93e-03
                          10        20
                  ....*....|....*....|....*
gi 2462489642 603 LRQHKRIHTGEKPYTCSECGTSFRQ 627
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 26
SFP1 COG5189
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ...
579-667 1.99e-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: 1.99e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462489642 579 RRIHT-GEKPHKCEV--CGMAFHHSSVLRQHkRIHtgekpytcSECGTSFRQGSALIGHKRVHTGEKPYECEECGKAFRV 655
Cdd:COG5189   340 RMLKVkDGKPYKCPVegCNKKYKNQNGLKYH-MLH--------GHQNQKLHENPSPEKMNIFSAKDKPYRCEVCDKRYKN 410
                          90
                  ....*....|..
gi 2462489642 656 SSNLTGHKKRKH 667
Cdd:COG5189   411 LNGLKYHRKHSH 422
zf-H2C2_2 pfam13465
Zinc-finger double domain;
634-653 2.45e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.81  E-value: 2.45e-03
                          10        20
                  ....*....|....*....|
gi 2462489642 634 HKRVHTGEKPYECEECGKAF 653
Cdd:pfam13465   5 HMRTHTGEKPYKCPECGKSF 24
zf-H2C2_2 pfam13465
Zinc-finger double domain;
323-347 3.38e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.42  E-value: 3.38e-03
                          10        20
                  ....*....|....*....|....*
gi 2462489642 323 LSMHRIIHTGEKPFNCTQCGKAFNS 347
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
490-515 3.42e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.42  E-value: 3.42e-03
                          10        20
                  ....*....|....*....|....*.
gi 2462489642 490 ELTKHRRIHTEEKRYRCEECGKAFRH 515
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
420-442 3.71e-03

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


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 35.35  E-value: 3.71e-03
                          10        20
                  ....*....|....*....|...
gi 2462489642 420 YECEECGKAFSGSSDLTKHIRIH 442
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
560-582 6.69e-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: 6.69e-03
                          10        20
                  ....*....|....*....|...
gi 2462489642 560 YKCLECGKAFSGKSNLTNHRRIH 582
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
448-470 6.83e-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: 6.83e-03
                          10        20
                  ....*....|....*....|...
gi 2462489642 448 YECSKCGRAFSRSSDLSKHKRIH 470
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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