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Conserved domains on  [gi|1034625409|ref|XP_016883426|]
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zinc finger protein 334 isoform X3 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
KRAB smart00349
krueppel associated box;
33-93 2.30e-36

krueppel associated box;


:

Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 130.40  E-value: 2.30e-36
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034625409   33 VSFQDLTVNFTQEEWQQLDPAQRLLYRDVMLENYSNLVSVGYHVSKPDVIFKLEQGEEPWI 93
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQVPKPDLISQLEQGEEPWI 61
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
342-697 2.56e-06

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


:

Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 50.46  E-value: 2.56e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034625409 342 KSYECNECGKTFFRKSALAEHFRSHTGEKPYEC--KECGNAFSKKSYLVVHQRTHRGEKPNECKECGKTffCQSALTAHQ 419
Cdd:COG5048    32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCsySGCDKSFSRPLELSRHLRTHHNNPSDLNSKSLPL--SNSKASSSS 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034625409 420 RIHTGEKPYECSECEKTFFCQSAL-----NVHRRSHTGEKPYECSQCGKFLCTKSALIAHQITHrgkksyecNECGKFFC 494
Cdd:COG5048   110 LSSSSSNSNDNNLLSSHSLPPSSRdpqlpDLLSISNLRNNPLPGNNSSSVNTPQSNSLHPPLPA--------NSLSKDPS 181

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034625409 495 HKSTLTIHQRTHTGEKHGVFNKCGRISIVKSNCSQCKRMNTKENLYECSEHGHAVSKN----SHLIVHQRTIWERPYECN 570
Cdd:COG5048   182 SNLSLLISSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSllsqSPSSLSSSDSSSSASESP 261

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034625409 571 ECGRTY---CRKSALTHHQRTHTGQR-PYECNECGKTFCQKFSFVEHQRT--HTGE--KPYECNE--CGKSFCHKSAFRV 640
Cdd:COG5048   262 RSSLPTassQSSSPNESDSSSEKGFSlPIKSKQCNISFSRSSPLTRHLRSvnHSGEslKPFSCPYslCGKLFSRNDALKR 341

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034625409 641 HRRIHTGEKPYEC--NQCGKTYRRL-----WTLTEHQKIHTGEKPYEC--NKCEKTFRHKSNFLLH 697
Cdd:COG5048   342 HILLHTSISPAKEklLNSSSKFSPLlnnepPQSLQQYKDLKNDKKSETlsNSCIRNFKRDSNLSLH 407
SUF4-like super family cl41227
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
 314-363 4.66e-05

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.


The actual alignment was detected with superfamily member cd20908:

Pssm-ID: 411020 [Multi-domain]  Cd Length: 82  Bit Score: 42.16  E-value: 4.66e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1034625409 314 RPYeCSECRKTFIDKSALIVHQKihggEKSYECNECGKTFFRKSALAEHF 363
Cdd:cd20908     1 KPW-CYYCDREFDDEKILIQHQK----AKHFKCHICHKKLYTAGGLAVHC 45
 
Name Accession Description Interval E-value
KRAB smart00349
krueppel associated box;
33-93 2.30e-36

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 130.40  E-value: 2.30e-36
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034625409   33 VSFQDLTVNFTQEEWQQLDPAQRLLYRDVMLENYSNLVSVGYHVSKPDVIFKLEQGEEPWI 93
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQVPKPDLISQLEQGEEPWI 61
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
 32-73 2.39e-24

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: 95.62  E-value: 2.39e-24
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1034625409  32 PVSFQDLTVNFTQEEWQQLDPAQRLLYRDVMLENYSNLVSVG 73
Cdd:pfam01352   1 SVTFEDVAVDFTQEEWALLDPAQRNLYRDVMLENYRNLVSLG 42
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
 33-71 1.34e-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: 82.21  E-value: 1.34e-19
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1034625409  33 VSFQDLTVNFTQEEWQQLDPAQRLLYRDVMLENYSNLVS 71
Cdd:cd07765     1 VTFEDVAVYFSQEEWELLDPAQRDLYRDVMLENYENLVS 39
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
342-697 2.56e-06

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 50.46  E-value: 2.56e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034625409 342 KSYECNECGKTFFRKSALAEHFRSHTGEKPYEC--KECGNAFSKKSYLVVHQRTHRGEKPNECKECGKTffCQSALTAHQ 419
Cdd:COG5048    32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCsySGCDKSFSRPLELSRHLRTHHNNPSDLNSKSLPL--SNSKASSSS 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034625409 420 RIHTGEKPYECSECEKTFFCQSAL-----NVHRRSHTGEKPYECSQCGKFLCTKSALIAHQITHrgkksyecNECGKFFC 494
Cdd:COG5048   110 LSSSSSNSNDNNLLSSHSLPPSSRdpqlpDLLSISNLRNNPLPGNNSSSVNTPQSNSLHPPLPA--------NSLSKDPS 181

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034625409 495 HKSTLTIHQRTHTGEKHGVFNKCGRISIVKSNCSQCKRMNTKENLYECSEHGHAVSKN----SHLIVHQRTIWERPYECN 570
Cdd:COG5048   182 SNLSLLISSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSllsqSPSSLSSSDSSSSASESP 261

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034625409 571 ECGRTY---CRKSALTHHQRTHTGQR-PYECNECGKTFCQKFSFVEHQRT--HTGE--KPYECNE--CGKSFCHKSAFRV 640
Cdd:COG5048   262 RSSLPTassQSSSPNESDSSSEKGFSlPIKSKQCNISFSRSSPLTRHLRSvnHSGEslKPFSCPYslCGKLFSRNDALKR 341

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034625409 641 HRRIHTGEKPYEC--NQCGKTYRRL-----WTLTEHQKIHTGEKPYEC--NKCEKTFRHKSNFLLH 697
Cdd:COG5048   342 HILLHTSISPAKEklLNSSSKFSPLlnnepPQSLQQYKDLKNDKKSETlsNSCIRNFKRDSNLSLH 407
SUF4-like cd20908
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
 314-363 4.66e-05

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: 42.16  E-value: 4.66e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1034625409 314 RPYeCSECRKTFIDKSALIVHQKihggEKSYECNECGKTFFRKSALAEHF 363
Cdd:cd20908     1 KPW-CYYCDREFDDEKILIQHQK----AKHFKCHICHKKLYTAGGLAVHC 45
zf-H2C2_2 pfam13465
Zinc-finger double domain;
609-632 2.23e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.81  E-value: 2.23e-03
                          10        20
                  ....*....|....*....|....
gi 1034625409 609 SFVEHQRTHTGEKPYECNECGKSF 632
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSF 24
 
Name Accession Description Interval E-value
KRAB smart00349
krueppel associated box;
33-93 2.30e-36

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 130.40  E-value: 2.30e-36
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034625409   33 VSFQDLTVNFTQEEWQQLDPAQRLLYRDVMLENYSNLVSVGYHVSKPDVIFKLEQGEEPWI 93
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQVPKPDLISQLEQGEEPWI 61
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
 32-73 2.39e-24

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: 95.62  E-value: 2.39e-24
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1034625409  32 PVSFQDLTVNFTQEEWQQLDPAQRLLYRDVMLENYSNLVSVG 73
Cdd:pfam01352   1 SVTFEDVAVDFTQEEWALLDPAQRNLYRDVMLENYRNLVSLG 42
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
 33-71 1.34e-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: 82.21  E-value: 1.34e-19
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1034625409  33 VSFQDLTVNFTQEEWQQLDPAQRLLYRDVMLENYSNLVS 71
Cdd:cd07765     1 VTFEDVAVYFSQEEWELLDPAQRDLYRDVMLENYENLVS 39
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
342-697 2.56e-06

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 50.46  E-value: 2.56e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034625409 342 KSYECNECGKTFFRKSALAEHFRSHTGEKPYEC--KECGNAFSKKSYLVVHQRTHRGEKPNECKECGKTffCQSALTAHQ 419
Cdd:COG5048    32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCsySGCDKSFSRPLELSRHLRTHHNNPSDLNSKSLPL--SNSKASSSS 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034625409 420 RIHTGEKPYECSECEKTFFCQSAL-----NVHRRSHTGEKPYECSQCGKFLCTKSALIAHQITHrgkksyecNECGKFFC 494
Cdd:COG5048   110 LSSSSSNSNDNNLLSSHSLPPSSRdpqlpDLLSISNLRNNPLPGNNSSSVNTPQSNSLHPPLPA--------NSLSKDPS 181

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034625409 495 HKSTLTIHQRTHTGEKHGVFNKCGRISIVKSNCSQCKRMNTKENLYECSEHGHAVSKN----SHLIVHQRTIWERPYECN 570
Cdd:COG5048   182 SNLSLLISSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSllsqSPSSLSSSDSSSSASESP 261

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034625409 571 ECGRTY---CRKSALTHHQRTHTGQR-PYECNECGKTFCQKFSFVEHQRT--HTGE--KPYECNE--CGKSFCHKSAFRV 640
Cdd:COG5048   262 RSSLPTassQSSSPNESDSSSEKGFSlPIKSKQCNISFSRSSPLTRHLRSvnHSGEslKPFSCPYslCGKLFSRNDALKR 341

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034625409 641 HRRIHTGEKPYEC--NQCGKTYRRL-----WTLTEHQKIHTGEKPYEC--NKCEKTFRHKSNFLLH 697
Cdd:COG5048   342 HILLHTSISPAKEklLNSSSKFSPLlnnepPQSLQQYKDLKNDKKSETlsNSCIRNFKRDSNLSLH 407
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
286-703 2.82e-05

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 47.38  E-value: 2.82e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034625409 286 KPYVCSDCRKTFRVKTSLTRHRRIHTGERPYECS--ECRKTFIDKSALIVHQKIHGGEKSYECNECGKTFFRKSALAEHF 363
Cdd:COG5048    32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSysGCDKSFSRPLELSRHLRTHHNNPSDLNSKSLPLSNSKASSSSLS 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034625409 364 RSHTGE-KPYECKECGNAFSKKSYLV--VHQRTHRGEKPNEcKECGKTFFCQSALTAHQRIHTGEKPyecseceKTFFCQ 440
Cdd:COG5048   112 SSSSNSnDNNLLSSHSLPPSSRDPQLpdLLSISNLRNNPLP-GNNSSSVNTPQSNSLHPPLPANSLS-------KDPSSN 183

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034625409 441 SALNVHRRSHTGEKPYECSQCGKFLCTKSALIAHQITHRGKKSYECNECGkFFCHKStLTIHQRTHTGEKHgvfnkcgri 520
Cdd:COG5048   184 LSLLISSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNS-QLSPKS-LLSQSPSSLSSSD--------- 252

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034625409 521 sivksNCSQCKRMNTKENLYEcsehGHAVSKNSHLIVHQRTIWERPYECNECGRTYCRKSALTHHQRT--HTGQ--RPYE 596
Cdd:COG5048   253 -----SSSSASESPRSSLPTA----SSQSSSPNESDSSSEKGFSLPIKSKQCNISFSRSSPLTRHLRSvnHSGEslKPFS 323

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034625409 597 CNE--CGKTFCQKFSFVEHQRTHTGEKPYEC--NECGKSFCHKS-----AFRVHRRIHTGEKPYEC--NQCGKTYRRLWT 665
Cdd:COG5048   324 CPYslCGKLFSRNDALKRHILLHTSISPAKEklLNSSSKFSPLLnneppQSLQQYKDLKNDKKSETlsNSCIRNFKRDSN 403

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|
gi 1034625409 666 LTEHQKIHTGEKPYECN--KCEKTFRHKSNFLLHQKSHKE 703
Cdd:COG5048   404 LSLHIITHLSFRPYNCKnpPCSKSFNRHYNLIPHKKIHTN 443
SUF4-like cd20908
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
 314-363 4.66e-05

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: 42.16  E-value: 4.66e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1034625409 314 RPYeCSECRKTFIDKSALIVHQKihggEKSYECNECGKTFFRKSALAEHF 363
Cdd:cd20908     1 KPW-CYYCDREFDDEKILIQHQK----AKHFKCHICHKKLYTAGGLAVHC 45
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
249-689 4.86e-05

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 46.61  E-value: 4.86e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034625409 249 TQKGRQTERKPNECNECRKTFSKRSTLIVHQRIHTGEKPYVCSD--CRKTFRVKTSLTRHRRIHTGERPYECS-ECRKTF 325
Cdd:COG5048    23 TLKSLSNAPRPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYsgCDKSFSRPLELSRHLRTHHNNPSDLNSkSLPLSN 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034625409 326 IDKSALIVHQKIHGGEKSYECNECGKTFFRKSALAEHFRSHTgeKPYECKECGNAFSKKSYLVVHQRTHRGEKPNECKEc 405
Cdd:COG5048   103 SKASSSSLSSSSSNSNDNNLLSSHSLPPSSRDPQLPDLLSIS--NLRNNPLPGNNSSSVNTPQSNSLHPPLPANSLSKD- 179

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034625409 406 gkTFFCQSALTAHQRIHTGEKPYECSECEKtffcQSALNVHRRSHTGEKPYECSQCGKFLCTKSALIAHQITHRGKKSYE 485
Cdd:COG5048   180 --PSSNLSLLISSNVSTSIPSSSENSPLSS----SYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLSSSDS 253

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034625409 486 CNECGKFFCHKSTLTIHQRTHTGEKHGVFNKCGRISIVKSNCSQCkrmntkenlyeCSEHGHAVSKNSHLIVHQRTIweR 565
Cdd:COG5048   254 SSSASESPRSSLPTASSQSSSPNESDSSSEKGFSLPIKSKQCNIS-----------FSRSSPLTRHLRSVNHSGESL--K 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034625409 566 PYECNE--CGRTYCRKSALTHHQRTHTGQRPYEC--NECGKTFCQK-----FSFVEHQRTHTGEKPYEC--NECGKSFCH 634
Cdd:COG5048   321 PFSCPYslCGKLFSRNDALKRHILLHTSISPAKEklLNSSSKFSPLlnnepPQSLQQYKDLKNDKKSETlsNSCIRNFKR 400

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1034625409 635 KSAFRVHRRIHTGEKPYECN--QCGKTYRRLWTLTEHQKIHTGEKPYECNKCEKTFR 689
Cdd:COG5048   401 DSNLSLHIITHLSFRPYNCKnpPCSKSFNRHYNLIPHKKIHTNHAPLLCSILKSFRR 457
zf-H2C2_2 pfam13465
Zinc-finger double domain;
609-632 2.23e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.81  E-value: 2.23e-03
                          10        20
                  ....*....|....*....|....
gi 1034625409 609 SFVEHQRTHTGEKPYECNECGKSF 632
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSF 24
zf-H2C2_2 pfam13465
Zinc-finger double domain;
358-383 2.25e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.81  E-value: 2.25e-03
                          10        20
                  ....*....|....*....|....*.
gi 1034625409 358 ALAEHFRSHTGEKPYECKECGNAFSK 383
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
302-325 2.27e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.81  E-value: 2.27e-03
                          10        20
                  ....*....|....*....|....
gi 1034625409 302 SLTRHRRIHTGERPYECSECRKTF 325
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSF 24
zf-H2C2_2 pfam13465
Zinc-finger double domain;
666-690 3.87e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.42  E-value: 3.87e-03
                          10        20
                  ....*....|....*....|....*
gi 1034625409 666 LTEHQKIHTGEKPYECNKCEKTFRH 690
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 484-506 5.06e-03

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


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 34.97  E-value: 5.06e-03
                          10        20
                  ....*....|....*....|...
gi 1034625409 484 YECNECGKFFCHKSTLTIHQRTH 506
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
414-437 5.45e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 34.65  E-value: 5.45e-03
                          10        20
                  ....*....|....*....|....
gi 1034625409 414 ALTAHQRIHTGEKPYECSECEKTF 437
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSF 24
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 567-589 5.75e-03

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


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 34.58  E-value: 5.75e-03
                          10        20
                  ....*....|....*....|...
gi 1034625409 567 YECNECGRTYCRKSALTHHQRTH 589
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
637-662 6.70e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 34.65  E-value: 6.70e-03
                          10        20
                  ....*....|....*....|....*.
gi 1034625409 637 AFRVHRRIHTGEKPYECNQCGKTYRR 662
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 623-645 9.49e-03

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


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 34.20  E-value: 9.49e-03
                          10        20
                  ....*....|....*....|...
gi 1034625409 623 YECNECGKSFCHKSAFRVHRRIH 645
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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