NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|71043914|ref|NP_001020936|]
View 

zinc finger protein 90 [Rattus norvegicus]

Protein Classification

KRAB domain-containing zinc finger protein( domain architecture ID 12204268)

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

CATH:  3.30.160.60
Gene Ontology:  GO:0003700|GO:0046872
PubMed:  22803940
SCOP:  4003583

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
KRAB smart00349
krueppel associated box;
14-74 7.33e-37

krueppel associated box;


:

Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 131.56  E-value: 7.33e-37
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 71043914     14 VTFKDVAVNFTQEEWRHVGPAQRSLYRDVMLENYSHLVSLGYQVSKPEVIFKLEQGEEPWI 74
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQVPKPDLISQLEQGEEPWI 61
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
198-625 4.05e-11

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


:

Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 65.49  E-value: 4.05e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71043914 198 TQSGIPAKKKPYKCDKCRKSFihrsSLNKHEKIHKDDaysngtdqgvPSGRKHHECTD--CGKTFLWRTQLTEHQRIHTG 275
Cdd:COG5048  23 TLKSLSNAPRPDSCPNCTDSF----SRLEHLTRHIRS----------HTGEKPSQCSYsgCDKSFSRPLELSRHLRTHHN 88

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71043914 276 EKPFECNVCGK----AFRHSSSLGQHENAHTGEKPYQCSLCGKAFQRSSSLVQHQRIHTGEKPYRCNLCGRSFRHSTSLT 351
Cdd:COG5048  89 NPSDLNSKSLPlsnsKASSSSLSSSSSNSNDNNLLSSHSLPPSSRDPQLPDLLSISNLRNNPLPGNNSSSVNTPQSNSLH 168

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71043914 352 -QHEVTHSGEKPfqckecgkafSRCSSLVQHERTHTGEKPFECSICGRAFGQSPSLYKHMRIHKRSKPYQSNNFSIAFEP 430
Cdd:COG5048 169 pPLPANSLSKDP----------SSNLSLLISSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPK 238

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71043914 431 NIPLtqgESVLTDVKSYHCIDCGKDFSHITDFTEHQRihAGENSYDSEQALRQQslshpreKPYQCNVCGKAFKRSTSFI 510
Cdd:COG5048 239 SLLS---QSPSSLSSSDSSSSASESPRSSLPTASSQS--SSPNESDSSSEKGFS-------LPIKSKQCNISFSRSSPLT 306

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71043914 511 EH--HRIHTGE--KPYECNE--CGEAFSRLSSLTQHERTHTGEKPYECI------------------------------- 553
Cdd:COG5048 307 RHlrSVNHSGEslKPFSCPYslCGKLFSRNDALKRHILLHTSISPAKEKllnssskfspllnneppqslqqykdlkndkk 386

                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71043914 554 ------DCGKAFSQSSSLIQHERTHTGEKPYECN--ECGRAFRKKTNLHDHQRIHTGEKPYACkeCGKNFSRSSALTKHH 625
Cdd:COG5048 387 setlsnSCIRNFKRDSNLSLHIITHLSFRPYNCKnpPCSKSFNRHYNLIPHKKIHTNHAPLLC--SILKSFRRDLDLSNH 464
 
Name Accession Description Interval E-value
KRAB smart00349
krueppel associated box;
14-74 7.33e-37

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 131.56  E-value: 7.33e-37
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 71043914     14 VTFKDVAVNFTQEEWRHVGPAQRSLYRDVMLENYSHLVSLGYQVSKPEVIFKLEQGEEPWI 74
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQVPKPDLISQLEQGEEPWI 61
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
 13-54 3.35e-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: 95.23  E-value: 3.35e-24
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 71043914    13 SVTFKDVAVNFTQEEWRHVGPAQRSLYRDVMLENYSHLVSLG 54
Cdd:pfam01352   1 SVTFEDVAVDFTQEEWALLDPAQRNLYRDVMLENYRNLVSLG 42
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
 14-53 8.88e-21

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: 85.29  E-value: 8.88e-21
                        10        20        30        40
                ....*....|....*....|....*....|....*....|
gi 71043914  14 VTFKDVAVNFTQEEWRHVGPAQRSLYRDVMLENYSHLVSL 53
Cdd:cd07765   1 VTFEDVAVYFSQEEWELLDPAQRDLYRDVMLENYENLVSL 40
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
198-625 4.05e-11

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 65.49  E-value: 4.05e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71043914 198 TQSGIPAKKKPYKCDKCRKSFihrsSLNKHEKIHKDDaysngtdqgvPSGRKHHECTD--CGKTFLWRTQLTEHQRIHTG 275
Cdd:COG5048  23 TLKSLSNAPRPDSCPNCTDSF----SRLEHLTRHIRS----------HTGEKPSQCSYsgCDKSFSRPLELSRHLRTHHN 88

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71043914 276 EKPFECNVCGK----AFRHSSSLGQHENAHTGEKPYQCSLCGKAFQRSSSLVQHQRIHTGEKPYRCNLCGRSFRHSTSLT 351
Cdd:COG5048  89 NPSDLNSKSLPlsnsKASSSSLSSSSSNSNDNNLLSSHSLPPSSRDPQLPDLLSISNLRNNPLPGNNSSSVNTPQSNSLH 168

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71043914 352 -QHEVTHSGEKPfqckecgkafSRCSSLVQHERTHTGEKPFECSICGRAFGQSPSLYKHMRIHKRSKPYQSNNFSIAFEP 430
Cdd:COG5048 169 pPLPANSLSKDP----------SSNLSLLISSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPK 238

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71043914 431 NIPLtqgESVLTDVKSYHCIDCGKDFSHITDFTEHQRihAGENSYDSEQALRQQslshpreKPYQCNVCGKAFKRSTSFI 510
Cdd:COG5048 239 SLLS---QSPSSLSSSDSSSSASESPRSSLPTASSQS--SSPNESDSSSEKGFS-------LPIKSKQCNISFSRSSPLT 306

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71043914 511 EH--HRIHTGE--KPYECNE--CGEAFSRLSSLTQHERTHTGEKPYECI------------------------------- 553
Cdd:COG5048 307 RHlrSVNHSGEslKPFSCPYslCGKLFSRNDALKRHILLHTSISPAKEKllnssskfspllnneppqslqqykdlkndkk 386

                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71043914 554 ------DCGKAFSQSSSLIQHERTHTGEKPYECN--ECGRAFRKKTNLHDHQRIHTGEKPYACkeCGKNFSRSSALTKHH 625
Cdd:COG5048 387 setlsnSCIRNFKRDSNLSLHIITHLSFRPYNCKnpPCSKSFNRHYNLIPHKKIHTNHAPLLC--SILKSFRRDLDLSNH 464
zf-H2C2_2 pfam13465
Zinc-finger double domain;
536-561 7.81e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 40.05  E-value: 7.81e-05
                          10        20
                  ....*....|....*....|....*.
gi 71043914   536 SLTQHERTHTGEKPYECIDCGKAFSQ 561
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
SUF4-like cd20908
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
 361-416 5.98e-04

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


Pssm-ID: 411020 [Multi-domain]  Cd Length: 82  Bit Score: 39.08  E-value: 5.98e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 71043914 361 KPFqCKECGKAFSRCSSLVQHERTHTgekpFECSICGRAFGQSPSLYKH-MRIHKRS 416
Cdd:cd20908   1 KPW-CYYCDREFDDEKILIQHQKAKH----FKCHICHKKLYTAGGLAVHcLQVHKET 52
PHA00733 PHA00733
hypothetical protein
 306-353 8.08e-03

hypothetical protein


Pssm-ID: 177301  Cd Length: 128  Bit Score: 36.78  E-value: 8.08e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 71043914  306 PYQCSLCGKAFQRSSSLVQHQRIHTGEKpyRCNLCGRSFRHSTSLTQH 353
Cdd:PHA00733  73 PYVCPLCLMPFSSSVSLKQHIRYTEHSK--VCPVCGKEFRNTDSTLDH 118
 
Name Accession Description Interval E-value
KRAB smart00349
krueppel associated box;
14-74 7.33e-37

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 131.56  E-value: 7.33e-37
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 71043914     14 VTFKDVAVNFTQEEWRHVGPAQRSLYRDVMLENYSHLVSLGYQVSKPEVIFKLEQGEEPWI 74
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQVPKPDLISQLEQGEEPWI 61
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
 13-54 3.35e-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: 95.23  E-value: 3.35e-24
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 71043914    13 SVTFKDVAVNFTQEEWRHVGPAQRSLYRDVMLENYSHLVSLG 54
Cdd:pfam01352   1 SVTFEDVAVDFTQEEWALLDPAQRNLYRDVMLENYRNLVSLG 42
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
 14-53 8.88e-21

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: 85.29  E-value: 8.88e-21
                        10        20        30        40
                ....*....|....*....|....*....|....*....|
gi 71043914  14 VTFKDVAVNFTQEEWRHVGPAQRSLYRDVMLENYSHLVSL 53
Cdd:cd07765   1 VTFEDVAVYFSQEEWELLDPAQRDLYRDVMLENYENLVSL 40
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
198-625 4.05e-11

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 65.49  E-value: 4.05e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71043914 198 TQSGIPAKKKPYKCDKCRKSFihrsSLNKHEKIHKDDaysngtdqgvPSGRKHHECTD--CGKTFLWRTQLTEHQRIHTG 275
Cdd:COG5048  23 TLKSLSNAPRPDSCPNCTDSF----SRLEHLTRHIRS----------HTGEKPSQCSYsgCDKSFSRPLELSRHLRTHHN 88

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71043914 276 EKPFECNVCGK----AFRHSSSLGQHENAHTGEKPYQCSLCGKAFQRSSSLVQHQRIHTGEKPYRCNLCGRSFRHSTSLT 351
Cdd:COG5048  89 NPSDLNSKSLPlsnsKASSSSLSSSSSNSNDNNLLSSHSLPPSSRDPQLPDLLSISNLRNNPLPGNNSSSVNTPQSNSLH 168

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71043914 352 -QHEVTHSGEKPfqckecgkafSRCSSLVQHERTHTGEKPFECSICGRAFGQSPSLYKHMRIHKRSKPYQSNNFSIAFEP 430
Cdd:COG5048 169 pPLPANSLSKDP----------SSNLSLLISSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPK 238

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71043914 431 NIPLtqgESVLTDVKSYHCIDCGKDFSHITDFTEHQRihAGENSYDSEQALRQQslshpreKPYQCNVCGKAFKRSTSFI 510
Cdd:COG5048 239 SLLS---QSPSSLSSSDSSSSASESPRSSLPTASSQS--SSPNESDSSSEKGFS-------LPIKSKQCNISFSRSSPLT 306

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71043914 511 EH--HRIHTGE--KPYECNE--CGEAFSRLSSLTQHERTHTGEKPYECI------------------------------- 553
Cdd:COG5048 307 RHlrSVNHSGEslKPFSCPYslCGKLFSRNDALKRHILLHTSISPAKEKllnssskfspllnneppqslqqykdlkndkk 386

                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71043914 554 ------DCGKAFSQSSSLIQHERTHTGEKPYECN--ECGRAFRKKTNLHDHQRIHTGEKPYACkeCGKNFSRSSALTKHH 625
Cdd:COG5048 387 setlsnSCIRNFKRDSNLSLHIITHLSFRPYNCKnpPCSKSFNRHYNLIPHKKIHTNHAPLLC--SILKSFRRDLDLSNH 464
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
333-629 9.91e-11

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 64.33  E-value: 9.91e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71043914 333 KPYRCNLCGRSFRHSTSLTQHEVTHSGEKPFQC--KECGKAFSRCSSLVQHERTHTGEKPFECSICGRAFGQSPSLYK-H 409
Cdd:COG5048  32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCsySGCDKSFSRPLELSRHLRTHHNNPSDLNSKSLPLSNSKASSSSlS 111

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71043914 410 MRIHKRSKPYQSNNFSIAFE---PNIPLTQGESVLTDVKSYHCIDCGKDFSHITDFTEHQRIHAGENSYDSEQALRQQSL 486
Cdd:COG5048 112 SSSSNSNDNNLLSSHSLPPSsrdPQLPDLLSISNLRNNPLPGNNSSSVNTPQSNSLHPPLPANSLSKDPSSNLSLLISSN 191

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71043914 487 SHPREKPYQCNVCGKAFKRSTSFIEHHRIHTGEKPYECNECGEAFSRLSSLTQHERTHTGEKPYECIDCGKAFSQSSSLI 566
Cdd:COG5048 192 VSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLSSSDSSSSASESPRSSLPTASSQ 271

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 71043914 567 QHERTHTGE-------KPYECNECGRAFRKKTNLHDHQR--IHTGE--KPYACKE--CGKNFSRSSALTKHHRIHS 629
Cdd:COG5048 272 SSSPNESDSssekgfsLPIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCPYslCGKLFSRNDALKRHILLHT 347
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
277-631 5.95e-10

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 62.02  E-value: 5.95e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71043914 277 KPFECNVCGKAFRHSSSLGQHENAHTGEKPYQCSL--CGKAFQRSSSLVQHQRIHTGEKPYRCNLCGRSFRHSTS----- 349
Cdd:COG5048  32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYsgCDKSFSRPLELSRHLRTHHNNPSDLNSKSLPLSNSKASsssls 111

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71043914 350 -----------LTQHEVTHSGEKPFQCKEC-----------------------------------GKAFSRCSSLVQHER 383
Cdd:COG5048 112 ssssnsndnnlLSSHSLPPSSRDPQLPDLLsisnlrnnplpgnnsssvntpqsnslhpplpanslSKDPSSNLSLLISSN 191

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71043914 384 THTGEKPFECSICGRAFGQSPSLYKHMRIHKRSKPYQSNNFSIAFEPNIPLtqgESVLTDVKSYHCIDCGKDFSHITDFT 463
Cdd:COG5048 192 VSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLS---QSPSSLSSSDSSSSASESPRSSLPTA 268

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71043914 464 EHQRihAGENSYDSEQALRQQslshpreKPYQCNVCGKAFKRSTSFIEH--HRIHTGE--KPYECNE--CGEAFSRLSSL 537
Cdd:COG5048 269 SSQS--SSPNESDSSSEKGFS-------LPIKSKQCNISFSRSSPLTRHlrSVNHSGEslKPFSCPYslCGKLFSRNDAL 339

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71043914 538 TQHERTHTGEKPYECI--DCGKAFSQSS-----SLIQHERTHTGEKPYEC--NECGRAFRKKTNLHDHQRIHTGEKPYAC 608
Cdd:COG5048 340 KRHILLHTSISPAKEKllNSSSKFSPLLnneppQSLQQYKDLKNDKKSETlsNSCIRNFKRDSNLSLHIITHLSFRPYNC 419

                       410       420
                ....*....|....*....|....*
gi 71043914 609 K--ECGKNFSRSSALTKHHRIHSRN 631
Cdd:COG5048 420 KnpPCSKSFNRHYNLIPHKKIHTNH 444
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
560-633 6.80e-05

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 45.84  E-value: 6.80e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71043914 560 SQSSSLIQHERTHTGE----KPYECNECGRAFRKKTNLHDHQRIHTGEKPYAC--KECGKNFSRSSALTKHHRIHSRNKL 633
Cdd:COG5048  12 NNSVLSSTPKSTLKSLsnapRPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCsySGCDKSFSRPLELSRHLRTHHNNPS 91
zf-H2C2_2 pfam13465
Zinc-finger double domain;
536-561 7.81e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 40.05  E-value: 7.81e-05
                          10        20
                  ....*....|....*....|....*.
gi 71043914   536 SLTQHERTHTGEKPYECIDCGKAFSQ 561
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
266-290 2.61e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.51  E-value: 2.61e-04
                          10        20
                  ....*....|....*....|....*
gi 71043914   266 LTEHQRIHTGEKPFECNVCGKAFRH 290
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
321-346 4.31e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 37.74  E-value: 4.31e-04
                          10        20
                  ....*....|....*....|....*.
gi 71043914   321 SLVQHQRIHTGEKPYRCNLCGRSFRH 346
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
SUF4-like cd20908
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
 361-416 5.98e-04

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


Pssm-ID: 411020 [Multi-domain]  Cd Length: 82  Bit Score: 39.08  E-value: 5.98e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 71043914 361 KPFqCKECGKAFSRCSSLVQHERTHTgekpFECSICGRAFGQSPSLYKH-MRIHKRS 416
Cdd:cd20908   1 KPW-CYYCDREFDDEKILIQHQKAKH----FKCHICHKKLYTAGGLAVHcLQVHKET 52
zf-H2C2_2 pfam13465
Zinc-finger double domain;
564-587 6.07e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 37.35  E-value: 6.07e-04
                          10        20
                  ....*....|....*....|....
gi 71043914   564 SLIQHERTHTGEKPYECNECGRAF 587
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSF 24
zf-H2C2_2 pfam13465
Zinc-finger double domain;
349-374 9.45e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.97  E-value: 9.45e-04
                          10        20
                  ....*....|....*....|....*.
gi 71043914   349 SLTQHEVTHSGEKPFQCKECGKAFSR 374
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
377-400 9.63e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.97  E-value: 9.63e-04
                          10        20
                  ....*....|....*....|....
gi 71043914   377 SLVQHERTHTGEKPFECSICGRAF 400
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSF 24
SFP1 COG5189
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ...
 275-358 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: 41.24  E-value: 1.66e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71043914 275 GEKPFECNV--CGKAFRHSSSLGQHE-NAHtgekpyqcslCGKAFQRSSSLVQHQRIHTGEKPYRCNLCGRSFRHSTSLT 351
Cdd:COG5189 346 DGKPYKCPVegCNKKYKNQNGLKYHMlHGH----------QNQKLHENPSPEKMNIFSAKDKPYRCEVCDKRYKNLNGLK 415


                ....*..
gi 71043914 352 QHeVTHS 358
Cdd:COG5189 416 YH-RKHS 421
zf-H2C2_2 pfam13465
Zinc-finger double domain;
511-533 2.52e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.81  E-value: 2.52e-03
                          10        20
                  ....*....|....*....|...
gi 71043914   511 EHHRIHTGEKPYECNECGEAFSR 533
Cdd:pfam13465   4 RHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
592-617 2.57e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.81  E-value: 2.57e-03
                          10        20
                  ....*....|....*....|....*.
gi 71043914   592 NLHDHQRIHTGEKPYACKECGKNFSR 617
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 606-628 2.82e-03

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


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 35.35  E-value: 2.82e-03
                          10        20
                  ....*....|....*....|...
gi 71043914   606 YACKECGKNFSRSSALTKHHRIH 628
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
SFP1 COG5189
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ...
 546-629 3.02e-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: 3.02e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71043914 546 GEKPYEC--IDCGKAFSQSSSLIQHeRTHtgekpyecNECGRAFRKKTNLHDHQRIHTGEKPYACKECGKNFSRSSALtK 623
Cdd:COG5189 346 DGKPYKCpvEGCNKKYKNQNGLKYH-MLH--------GHQNQKLHENPSPEKMNIFSAKDKPYRCEVCDKRYKNLNGL-K 415


                ....*.
gi 71043914 624 HHRIHS 629
Cdd:COG5189 416 YHRKHS 421
SUF4-like cd20908
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
 305-353 4.78e-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: 36.38  E-value: 4.78e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*....
gi 71043914 305 KPYqCSLCGKAFQRSSSLVQHQRIHTgekpYRCNLCGRSFRHSTSLTQH 353
Cdd:cd20908   1 KPW-CYYCDREFDDEKILIQHQKAKH----FKCHICHKKLYTAGGLAVH 44
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 363-385 5.04e-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: 5.04e-03
                          10        20
                  ....*....|....*....|...
gi 71043914   363 FQCKECGKAFSRCSSLVQHERTH 385
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
PHA00733 PHA00733
hypothetical protein
 306-353 8.08e-03

hypothetical protein


Pssm-ID: 177301  Cd Length: 128  Bit Score: 36.78  E-value: 8.08e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 71043914  306 PYQCSLCGKAFQRSSSLVQHQRIHTGEKpyRCNLCGRSFRHSTSLTQH 353
Cdd:PHA00733  73 PYVCPLCLMPFSSSVSLKQHIRYTEHSK--VCPVCGKEFRNTDSTLDH 118
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 578-600 8.99e-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: 8.99e-03
                          10        20
                  ....*....|....*....|...
gi 71043914   578 YECNECGRAFRKKTNLHDHQRIH 600
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 522-544 9.92e-03

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


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 33.81  E-value: 9.92e-03
                          10        20
                  ....*....|....*....|...
gi 71043914   522 YECNECGEAFSRLSSLTQHERTH 544
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH