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Conserved domains on  [gi|1237938189|ref|NP_001341466|]
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zinc finger protein 484 isoform d [Homo sapiens]

Protein Classification

KRAB domain-containing zinc finger protein( domain architecture ID 12204794)

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;
25-84 4.05e-30

krueppel associated box;


:

Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 113.07  E-value: 4.05e-30
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1237938189   25 VSFKDVTVDFSRDEWQQLDLAQKSLYREVMLENYFNLISVGCQVPKPEVIFSLEQ-EEPCM 84
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQVPKPDLISQLEQgEEPWI 61
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
427-828 2.21e-13

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


:

Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 73.58  E-value: 2.21e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938189 427 KPYVCTECGKAFIRKSHFITHERIHTGEKPYECSD--CGKSFIKKSQLHVHQRIHTGENPFICSECGKVFTHKT-NLIIH 503
Cdd:COG5048    32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYsgCDKSFSRPLELSRHLRTHHNNPSDLNSKSLPLSNSKAsSSSLS 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938189 504 QKIHTGERPYICTVCGKAFTDRSNLIKHQKIHTGEKPYKCSDCGKSFTW-KSRLRIHQKCHTGERHYECSECGKAFIQKS 582
Cdd:COG5048   112 SSSSNSNDNNLLSSHSLPPSSRDPQLPDLLSISNLRNNPLPGNNSSSVNtPQSNSLHPPLPANSLSKDPSSNLSLLISSN 191

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938189 583 TLSMHQRIHrgekpyvCTECGKAFFHKSHFITHERIHTGEKPYECSICGKSFTKKSQLHVHQQIHTGEKPYRCAECGKAF 662
Cdd:COG5048   192 VSTSIPSSS-------ENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLSSSDSSSSASESPRSS 264

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938189 663 TDRSNLFTHQKIHTGE-------KPYKCSDCGKAFTRKSGLHIHQQS--HTGERHYECSE----CGKAFARKSTLIMHQR 729
Cdd:COG5048   265 LPTASSQSSSPNESDSssekgfsLPIKSKQCNISFSRSSPLTRHLRSvnHSGESLKPFSCpyslCGKLFSRNDALKRHIL 344

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938189 730 IHTGEKPYIC--NECGKSFIQKSHLNRH-----RRIHTGEKPYECSDCGKSFIKKS----QLHEHHRIHTGEKPYICAEC 798
Cdd:COG5048   345 LHTSISPAKEklLNSSSKFSPLLNNEPPqslqqYKDLKNDKKSETLSNSCIRNFKRdsnlSLHIITHLSFRPYNCKNPPC 424

                         410       420       430
                  ....*....|....*....|....*....|
gi 1237938189 799 GKAFTIRSNLIKHQKIHTKQKPYKCSDLGK 828
Cdd:COG5048   425 SKSFNRHYNLIPHKKIHTNHAPLLCSILKS 454
zf-H2C2_2 pfam13465
Zinc-finger double domain;
387-412 4.86e-03

Zinc-finger double domain;


:

Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.42  E-value: 4.86e-03
                          10        20
                  ....*....|....*....|....*.
gi 1237938189 387 NLNIHKKIHTGGKHFECTECGKAFTR 412
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
 
Name Accession Description Interval E-value
KRAB smart00349
krueppel associated box;
25-84 4.05e-30

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 113.07  E-value: 4.05e-30
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1237938189   25 VSFKDVTVDFSRDEWQQLDLAQKSLYREVMLENYFNLISVGCQVPKPEVIFSLEQ-EEPCM 84
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQVPKPDLISQLEQgEEPWI 61
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
 24-65 2.44e-21

KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc finger proteins containing C2H2 fingers. The KRAB domain is found to be involved in protein-protein interactions. The KRAB domain is generally encoded by two exons. The regions coded by the two exons are known as KRAB-A and KRAB-B. The A box plays an important role in repression by binding to corepressors, while the B box is thought to enhance this repression brought about by the A box. KRAB-containing proteins are thought to have critical functions in cell proliferation and differentiation, apoptosis and neoplastic transformation.


Pssm-ID: 460171  Cd Length: 42  Bit Score: 87.53  E-value: 2.44e-21
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1237938189  24 SVSFKDVTVDFSRDEWQQLDLAQKSLYREVMLENYFNLISVG 65
Cdd:pfam01352   1 SVTFEDVAVDFTQEEWALLDPAQRNLYRDVMLENYRNLVSLG 42
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
 25-63 6.90e-18

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: 77.59  E-value: 6.90e-18
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1237938189  25 VSFKDVTVDFSRDEWQQLDLAQKSLYREVMLENYFNLIS 63
Cdd:cd07765     1 VTFEDVAVYFSQEEWELLDPAQRDLYRDVMLENYENLVS 39
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
427-828 2.21e-13

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 73.58  E-value: 2.21e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938189 427 KPYVCTECGKAFIRKSHFITHERIHTGEKPYECSD--CGKSFIKKSQLHVHQRIHTGENPFICSECGKVFTHKT-NLIIH 503
Cdd:COG5048    32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYsgCDKSFSRPLELSRHLRTHHNNPSDLNSKSLPLSNSKAsSSSLS 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938189 504 QKIHTGERPYICTVCGKAFTDRSNLIKHQKIHTGEKPYKCSDCGKSFTW-KSRLRIHQKCHTGERHYECSECGKAFIQKS 582
Cdd:COG5048   112 SSSSNSNDNNLLSSHSLPPSSRDPQLPDLLSISNLRNNPLPGNNSSSVNtPQSNSLHPPLPANSLSKDPSSNLSLLISSN 191

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938189 583 TLSMHQRIHrgekpyvCTECGKAFFHKSHFITHERIHTGEKPYECSICGKSFTKKSQLHVHQQIHTGEKPYRCAECGKAF 662
Cdd:COG5048   192 VSTSIPSSS-------ENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLSSSDSSSSASESPRSS 264

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938189 663 TDRSNLFTHQKIHTGE-------KPYKCSDCGKAFTRKSGLHIHQQS--HTGERHYECSE----CGKAFARKSTLIMHQR 729
Cdd:COG5048   265 LPTASSQSSSPNESDSssekgfsLPIKSKQCNISFSRSSPLTRHLRSvnHSGESLKPFSCpyslCGKLFSRNDALKRHIL 344

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938189 730 IHTGEKPYIC--NECGKSFIQKSHLNRH-----RRIHTGEKPYECSDCGKSFIKKS----QLHEHHRIHTGEKPYICAEC 798
Cdd:COG5048   345 LHTSISPAKEklLNSSSKFSPLLNNEPPqslqqYKDLKNDKKSETLSNSCIRNFKRdsnlSLHIITHLSFRPYNCKNPPC 424

                         410       420       430
                  ....*....|....*....|....*....|
gi 1237938189 799 GKAFTIRSNLIKHQKIHTKQKPYKCSDLGK 828
Cdd:COG5048   425 SKSFNRHYNLIPHKKIHTNHAPLLCSILKS 454
zf-H2C2_2 pfam13465
Zinc-finger double domain;
751-774 1.68e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 39.28  E-value: 1.68e-04
                          10        20
                  ....*....|....*....|....
gi 1237938189 751 HLNRHRRIHTGEKPYECSDCGKSF 774
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSF 24
SUF4-like cd20908
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
 651-703 8.59e-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: 8.59e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1237938189 651 KPYrCAECGKAFTDRSNLFTHQKIHTgekpYKCSDCGKAFTRKSGLHIH-QQSH 703
Cdd:cd20908     1 KPW-CYYCDREFDDEKILIQHQKAKH----FKCHICHKKLYTAGGLAVHcLQVH 49
zf-H2C2_2 pfam13465
Zinc-finger double domain;
387-412 4.86e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.42  E-value: 4.86e-03
                          10        20
                  ....*....|....*....|....*.
gi 1237938189 387 NLNIHKKIHTGGKHFECTECGKAFTR 412
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
 
Name Accession Description Interval E-value
KRAB smart00349
krueppel associated box;
25-84 4.05e-30

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 113.07  E-value: 4.05e-30
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1237938189   25 VSFKDVTVDFSRDEWQQLDLAQKSLYREVMLENYFNLISVGCQVPKPEVIFSLEQ-EEPCM 84
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQVPKPDLISQLEQgEEPWI 61
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
 24-65 2.44e-21

KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc finger proteins containing C2H2 fingers. The KRAB domain is found to be involved in protein-protein interactions. The KRAB domain is generally encoded by two exons. The regions coded by the two exons are known as KRAB-A and KRAB-B. The A box plays an important role in repression by binding to corepressors, while the B box is thought to enhance this repression brought about by the A box. KRAB-containing proteins are thought to have critical functions in cell proliferation and differentiation, apoptosis and neoplastic transformation.


Pssm-ID: 460171  Cd Length: 42  Bit Score: 87.53  E-value: 2.44e-21
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1237938189  24 SVSFKDVTVDFSRDEWQQLDLAQKSLYREVMLENYFNLISVG 65
Cdd:pfam01352   1 SVTFEDVAVDFTQEEWALLDPAQRNLYRDVMLENYRNLVSLG 42
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
 25-63 6.90e-18

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: 77.59  E-value: 6.90e-18
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1237938189  25 VSFKDVTVDFSRDEWQQLDLAQKSLYREVMLENYFNLIS 63
Cdd:cd07765     1 VTFEDVAVYFSQEEWELLDPAQRDLYRDVMLENYENLVS 39
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
427-828 2.21e-13

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 73.58  E-value: 2.21e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938189 427 KPYVCTECGKAFIRKSHFITHERIHTGEKPYECSD--CGKSFIKKSQLHVHQRIHTGENPFICSECGKVFTHKT-NLIIH 503
Cdd:COG5048    32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYsgCDKSFSRPLELSRHLRTHHNNPSDLNSKSLPLSNSKAsSSSLS 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938189 504 QKIHTGERPYICTVCGKAFTDRSNLIKHQKIHTGEKPYKCSDCGKSFTW-KSRLRIHQKCHTGERHYECSECGKAFIQKS 582
Cdd:COG5048   112 SSSSNSNDNNLLSSHSLPPSSRDPQLPDLLSISNLRNNPLPGNNSSSVNtPQSNSLHPPLPANSLSKDPSSNLSLLISSN 191

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938189 583 TLSMHQRIHrgekpyvCTECGKAFFHKSHFITHERIHTGEKPYECSICGKSFTKKSQLHVHQQIHTGEKPYRCAECGKAF 662
Cdd:COG5048   192 VSTSIPSSS-------ENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLSSSDSSSSASESPRSS 264

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938189 663 TDRSNLFTHQKIHTGE-------KPYKCSDCGKAFTRKSGLHIHQQS--HTGERHYECSE----CGKAFARKSTLIMHQR 729
Cdd:COG5048   265 LPTASSQSSSPNESDSssekgfsLPIKSKQCNISFSRSSPLTRHLRSvnHSGESLKPFSCpyslCGKLFSRNDALKRHIL 344

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938189 730 IHTGEKPYIC--NECGKSFIQKSHLNRH-----RRIHTGEKPYECSDCGKSFIKKS----QLHEHHRIHTGEKPYICAEC 798
Cdd:COG5048   345 LHTSISPAKEklLNSSSKFSPLLNNEPPqslqqYKDLKNDKKSETLSNSCIRNFKRdsnlSLHIITHLSFRPYNCKNPPC 424

                         410       420       430
                  ....*....|....*....|....*....|
gi 1237938189 799 GKAFTIRSNLIKHQKIHTKQKPYKCSDLGK 828
Cdd:COG5048   425 SKSFNRHYNLIPHKKIHTNHAPLLCSILKS 454
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
483-856 5.51e-12

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 68.95  E-value: 5.51e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938189 483 NPFICSECGKVFTHKTNLIIHQKIHTGERPYICTV--CGKAFTDRSNLIKHQKIHTGEKPYKCSD-CGKSFTWKSRLRIH 559
Cdd:COG5048    32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYsgCDKSFSRPLELSRHLRTHHNNPSDLNSKsLPLSNSKASSSSLS 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938189 560 QKCHTGERHYECSECGKAFIQK---------STLSMHQRIHRGEKPYVCTEC-------------GKAFFHKSHFITHER 617
Cdd:COG5048   112 SSSSNSNDNNLLSSHSLPPSSRdpqlpdllsISNLRNNPLPGNNSSSVNTPQsnslhpplpanslSKDPSSNLSLLISSN 191

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938189 618 IHTGEKPYECSICGKSFTKKSQLHVHQQIHTGEKPYRCAECGKAFTD------RSNLFTHQKIHTGEKPYKCSDCGKAFT 691
Cdd:COG5048   192 VSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKsllsqsPSSLSSSDSSSSASESPRSSLPTASSQ 271

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938189 692 RKSGLHIHQQSHTGERH-YECSECGKAFARKSTLIMHQR--IHTGE--KPYICNE--CGKSFIQKSHLNRHRRIHTGEKP 764
Cdd:COG5048   272 SSSPNESDSSSEKGFSLpIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCPYslCGKLFSRNDALKRHILLHTSISP 351

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938189 765 YEC--SDCGKSFIKKS-----QLHEHHRIHTGEKPYICA--ECGKAFTIRSNLIKHQKIHTKQKPYKCSDLGKALNWKPQ 835
Cdd:COG5048   352 AKEklLNSSSKFSPLLnneppQSLQQYKDLKNDKKSETLsnSCIRNFKRDSNLSLHIITHLSFRPYNCKNPPCSKSFNRH 431

                         410       420
                  ....*....|....*....|..
gi 1237938189 836 LSM-PQKSDNGEVECSMPQLWC 856
Cdd:COG5048   432 YNLiPHKKIHTNHAPLLCSILK 453
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
371-755 1.75e-09

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 60.86  E-value: 1.75e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938189 371 KPYEYSECEKNLPQNSNLNIHKKIHTGGKHFECT--ECGKAFTRKSTLSMHQKIHTGEKPYVCT-ECGKAFIRKSHFITH 447
Cdd:COG5048    32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSysGCDKSFSRPLELSRHLRTHHNNPSDLNSkSLPLSNSKASSSSLS 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938189 448 ERIHTGEKPYECSDCGKSFIKKSQLH------------VHQRIHTGENPFICS----------ECGKVFTHKTNLIIHQK 505
Cdd:COG5048   112 SSSSNSNDNNLLSSHSLPPSSRDPQLpdllsisnlrnnPLPGNNSSSVNTPQSnslhpplpanSLSKDPSSNLSLLISSN 191

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938189 506 IHTGERPYICTVCGKAFTDRSNLIKHQKIHTGEKPYKCSDCGKSFTWKSRLRIHQKCHTGERHYECSECGKAFIQKSTLS 585
Cdd:COG5048   192 VSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLSSSDSSSSASESPRSSLPTASSQ 271

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938189 586 MHQRIHRGE-------KPYVCTECGKAFFHKSHFITHER--IHTGE--KPYEC--SICGKSFTKKSQLHVHQQIHTGEKP 652
Cdd:COG5048   272 SSSPNESDSssekgfsLPIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCpySLCGKLFSRNDALKRHILLHTSISP 351

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938189 653 YRC--AECGKAFTDRSN-----LFTHQKIHTGEKPYKCSD--CGKAFTRKSGLHIHQQSHTGERHYEC--SECGKAFARK 721
Cdd:COG5048   352 AKEklLNSSSKFSPLLNneppqSLQQYKDLKNDKKSETLSnsCIRNFKRDSNLSLHIITHLSFRPYNCknPPCSKSFNRH 431

                         410       420       430
                  ....*....|....*....|....*....|....
gi 1237938189 722 STLIMHQRIHTgEKPYICNECGKSFIQKSHLNRH 755
Cdd:COG5048   432 YNLIPHKKIHT-NHAPLLCSILKSFRRDLDLSNH 464
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
512-701 9.73e-07

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 52.39  E-value: 9.73e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938189 512 PYICTVCGKAFTDRSNLIKHQ--KIHTGE--KPYKC--SDCGKSFTWKSRLRIHQKCHTGERHYEC--SECGKAFIQKST 583
Cdd:COG5048   289 PIKSKQCNISFSRSSPLTRHLrsVNHSGEslKPFSCpySLCGKLFSRNDALKRHILLHTSISPAKEklLNSSSKFSPLLN 368

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938189 584 LSMHQRIHrgekpyvctecgkaffhksHFITHERIHTGEKPYECSICGKSFTKKSQLHVHQQIHTGEKPYRCAECGKAFT 663
Cdd:COG5048   369 NEPPQSLQ-------------------QYKDLKNDKKSETLSNSCIRNFKRDSNLSLHIITHLSFRPYNCKNPPCSKSFN 429

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1237938189 664 DRSNLFTHQKIHTGEKPYKCSDCGKAFTRKSGLHIHQQ 701
Cdd:COG5048   430 RHYNLIPHKKIHTNHAPLLCSILKSFRRDLDLSNHGKD 467
zf-H2C2_2 pfam13465
Zinc-finger double domain;
751-774 1.68e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 39.28  E-value: 1.68e-04
                          10        20
                  ....*....|....*....|....
gi 1237938189 751 HLNRHRRIHTGEKPYECSDCGKSF 774
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSF 24
zf-H2C2_2 pfam13465
Zinc-finger double domain;
667-692 3.40e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.51  E-value: 3.40e-04
                          10        20
                  ....*....|....*....|....*.
gi 1237938189 667 NLFTHQKIHTGEKPYKCSDCGKAFTR 692
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
527-551 4.09e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.12  E-value: 4.09e-04
                          10        20
                  ....*....|....*....|....*
gi 1237938189 527 NLIKHQKIHTGEKPYKCSDCGKSFT 551
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFK 25
SUF4-like cd20908
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
 651-703 8.59e-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: 8.59e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1237938189 651 KPYrCAECGKAFTDRSNLFTHQKIHTgekpYKCSDCGKAFTRKSGLHIH-QQSH 703
Cdd:cd20908     1 KPW-CYYCDREFDDEKILIQHQKAKH----FKCHICHKKLYTAGGLAVHcLQVH 49
zf-H2C2_2 pfam13465
Zinc-finger double domain;
416-440 1.23e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.97  E-value: 1.23e-03
                          10        20
                  ....*....|....*....|....*
gi 1237938189 416 LSMHQKIHTGEKPYVCTECGKAFIR 440
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 737-759 1.31e-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: 36.89  E-value: 1.31e-03
                          10        20
                  ....*....|....*....|...
gi 1237938189 737 YICNECGKSFIQKSHLNRHRRIH 759
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
SFP1 COG5189
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ...
 677-756 1.61e-03

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


Pssm-ID: 227516 [Multi-domain]  Cd Length: 423  Bit Score: 42.01  E-value: 1.61e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938189 677 GEKPYKCS--DCGKAFTRKSGLHIHQQshtgERHyecseCGKAFARKSTLIMHQRIHTGEKPYICNECGKSFIQKSHLNR 754
Cdd:COG5189   346 DGKPYKCPveGCNKKYKNQNGLKYHML----HGH-----QNQKLHENPSPEKMNIFSAKDKPYRCEVCDKRYKNLNGLKY 416


                  ..
gi 1237938189 755 HR 756
Cdd:COG5189   417 HR 418
zf-H2C2_2 pfam13465
Zinc-finger double domain;
611-636 2.67e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.81  E-value: 2.67e-03
                          10        20
                  ....*....|....*....|....*.
gi 1237938189 611 HFITHERIHTGEKPYECSICGKSFTK 636
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
584-606 3.45e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.81  E-value: 3.45e-03
                          10        20
                  ....*....|....*....|...
gi 1237938189 584 LSMHQRIHRGEKPYVCTECGKAF 606
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSF 24
zf-H2C2_2 pfam13465
Zinc-finger double domain;
443-466 3.73e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.42  E-value: 3.73e-03
                          10        20
                  ....*....|....*....|....
gi 1237938189 443 HFITHERIHTGEKPYECSDCGKSF 466
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSF 24
SFP1 COG5189
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ...
 621-704 4.43e-03

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


Pssm-ID: 227516 [Multi-domain]  Cd Length: 423  Bit Score: 40.47  E-value: 4.43e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938189 621 GEKPYECSI--CGKSFT-----KKSQLHVHQQIHTGEKPYrcaecgkafTDRSNLFTHQkihtgEKPYKCSDCGKAFTRK 693
Cdd:COG5189   346 DGKPYKCPVegCNKKYKnqnglKYHMLHGHQNQKLHENPS---------PEKMNIFSAK-----DKPYRCEVCDKRYKNL 411

                          90
                  ....*....|.
gi 1237938189 694 SGLHIHQQSHT 704
Cdd:COG5189   412 NGLKYHRKHSH 422
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 513-535 4.78e-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: 4.78e-03
                          10        20
                  ....*....|....*....|...
gi 1237938189 513 YICTVCGKAFTDRSNLIKHQKIH 535
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
387-412 4.86e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.42  E-value: 4.86e-03
                          10        20
                  ....*....|....*....|....*.
gi 1237938189 387 NLNIHKKIHTGGKHFECTECGKAFTR 412
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 457-479 6.95e-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: 6.95e-03
                          10        20
                  ....*....|....*....|...
gi 1237938189 457 YECSDCGKSFIKKSQLHVHQRIH 479
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
555-580 9.11e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 34.65  E-value: 9.11e-03
                          10        20
                  ....*....|....*....|....*.
gi 1237938189 555 RLRIHQKCHTGERHYECSECGKAFIQ 580
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 625-647 9.24e-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: 9.24e-03
                          10        20
                  ....*....|....*....|...
gi 1237938189 625 YECSICGKSFTKKSQLHVHQQIH 647
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 681-703 9.80e-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: 9.80e-03
                          10        20
                  ....*....|....*....|...
gi 1237938189 681 YKCSDCGKAFTRKSGLHIHQQSH 703
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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