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Conserved domains on  [gi|823683790|ref|NP_001296317|]
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zinc finger protein 141 isoform 1 [Mus musculus]

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;
18-78 5.18e-31

krueppel associated box;


:

Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 115.38  E-value: 5.18e-31
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 823683790    18 LTFKDVAIEFSKEEWECLDSAQRTLYRDVMLEIYSILVSVGLSISKPELLTYLEQNEEPYI 78
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQVPKPDLISQLEQGEEPWI 61
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
445-685 6.84e-07

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


:

Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 52.39  E-value: 6.84e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823683790 445 KSFTHGYSLRIHHRFHTGEKPYKCKDCGRSFAEGSSLKSHHRIHTGEKPYKCKECGKSFAKQSNFETHSRIHTGDRPYKC 524
Cdd:COG5048  178 KDPSSNLSLLISSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLSSSDSSSSA 257
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823683790 525 TDCG-KSFTRSFCLRKHHKTHTGEKA------YKCEECGKAFTQRSTLKTHYR--IHTGE--KPYKCNE--CGKSFTEGS 591
Cdd:COG5048  258 SESPrSSLPTASSQSSSPNESDSSSEkgfslpIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCPYslCGKLFSRND 337
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823683790 592 TLKTHLKIHTGEKPYKCKEC------GKSFAEASTLKTHHRIHTGEKPYKCTD---CGKSFTQSSHLQSHCRIHTGEKP- 661
Cdd:COG5048  338 ALKRHILLHTSISPAKEKLLnssskfSPLLNNEPPQSLQQYKDLKNDKKSETLsnsCIRNFKRDSNLSLHIITHLSFRPy 417
                        250       260
                 ....*....|....*....|....*
gi 823683790 662 -YKCKECGKSFAKDSSLQKHHRIHS 685
Cdd:COG5048  418 nCKNPPCSKSFNRHYNLIPHKKIHT 442
zf-H2C2_2 pfam13465
Zinc-finger double domain;
424-449 5.93e-05

Zinc-finger double domain;


:

Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 40.43  E-value: 5.93e-05
                          10        20
                  ....*....|....*....|....*.
gi 823683790  424 YLQAHQRIHTGEKPYKCKECGKSFTH 449
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
 
Name Accession Description Interval E-value
KRAB smart00349
krueppel associated box;
18-78 5.18e-31

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 115.38  E-value: 5.18e-31
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 823683790    18 LTFKDVAIEFSKEEWECLDSAQRTLYRDVMLEIYSILVSVGLSISKPELLTYLEQNEEPYI 78
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQVPKPDLISQLEQGEEPWI 61
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
17-58 2.71e-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: 87.14  E-value: 2.71e-21
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 823683790   17 LLTFKDVAIEFSKEEWECLDSAQRTLYRDVMLEIYSILVSVG 58
Cdd:pfam01352   1 SVTFEDVAVDFTQEEWALLDPAQRNLYRDVMLENYRNLVSLG 42
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
18-56 6.57e-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: 77.20  E-value: 6.57e-18
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 823683790  18 LTFKDVAIEFSKEEWECLDSAQRTLYRDVMLEIYSILVS 56
Cdd:cd07765    1 VTFEDVAVYFSQEEWELLDPAQRDLYRDVMLENYENLVS 39
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
445-685 6.84e-07

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 52.39  E-value: 6.84e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823683790 445 KSFTHGYSLRIHHRFHTGEKPYKCKDCGRSFAEGSSLKSHHRIHTGEKPYKCKECGKSFAKQSNFETHSRIHTGDRPYKC 524
Cdd:COG5048  178 KDPSSNLSLLISSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLSSSDSSSSA 257
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823683790 525 TDCG-KSFTRSFCLRKHHKTHTGEKA------YKCEECGKAFTQRSTLKTHYR--IHTGE--KPYKCNE--CGKSFTEGS 591
Cdd:COG5048  258 SESPrSSLPTASSQSSSPNESDSSSEkgfslpIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCPYslCGKLFSRND 337
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823683790 592 TLKTHLKIHTGEKPYKCKEC------GKSFAEASTLKTHHRIHTGEKPYKCTD---CGKSFTQSSHLQSHCRIHTGEKP- 661
Cdd:COG5048  338 ALKRHILLHTSISPAKEKLLnssskfSPLLNNEPPQSLQQYKDLKNDKKSETLsnsCIRNFKRDSNLSLHIITHLSFRPy 417
                        250       260
                 ....*....|....*....|....*
gi 823683790 662 -YKCKECGKSFAKDSSLQKHHRIHS 685
Cdd:COG5048  418 nCKNPPCSKSFNRHYNLIPHKKIHT 442
zf-H2C2_2 pfam13465
Zinc-finger double domain;
648-673 2.27e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 41.59  E-value: 2.27e-05
                          10        20
                  ....*....|....*....|....*.
gi 823683790  648 HLQSHCRIHTGEKPYKCKECGKSFAK 673
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
424-449 5.93e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 40.43  E-value: 5.93e-05
                          10        20
                  ....*....|....*....|....*.
gi 823683790  424 YLQAHQRIHTGEKPYKCKECGKSFTH 449
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
SUF4-like cd20908
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
408-456 2.05e-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: 40.23  E-value: 2.05e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 823683790 408 KPYkCKICKRSFTTGSYLQAHQRIHTgekpYKCKECGKSFTHGYSLRIH 456
Cdd:cd20908    1 KPW-CYYCDREFDDEKILIQHQKAKH----FKCHICHKKLYTAGGLAVH 44
 
Name Accession Description Interval E-value
KRAB smart00349
krueppel associated box;
18-78 5.18e-31

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 115.38  E-value: 5.18e-31
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 823683790    18 LTFKDVAIEFSKEEWECLDSAQRTLYRDVMLEIYSILVSVGLSISKPELLTYLEQNEEPYI 78
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQVPKPDLISQLEQGEEPWI 61
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
17-58 2.71e-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: 87.14  E-value: 2.71e-21
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 823683790   17 LLTFKDVAIEFSKEEWECLDSAQRTLYRDVMLEIYSILVSVG 58
Cdd:pfam01352   1 SVTFEDVAVDFTQEEWALLDPAQRNLYRDVMLENYRNLVSLG 42
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
18-56 6.57e-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: 77.20  E-value: 6.57e-18
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 823683790  18 LTFKDVAIEFSKEEWECLDSAQRTLYRDVMLEIYSILVS 56
Cdd:cd07765    1 VTFEDVAVYFSQEEWELLDPAQRDLYRDVMLENYENLVS 39
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
445-685 6.84e-07

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 52.39  E-value: 6.84e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823683790 445 KSFTHGYSLRIHHRFHTGEKPYKCKDCGRSFAEGSSLKSHHRIHTGEKPYKCKECGKSFAKQSNFETHSRIHTGDRPYKC 524
Cdd:COG5048  178 KDPSSNLSLLISSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLSSSDSSSSA 257
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823683790 525 TDCG-KSFTRSFCLRKHHKTHTGEKA------YKCEECGKAFTQRSTLKTHYR--IHTGE--KPYKCNE--CGKSFTEGS 591
Cdd:COG5048  258 SESPrSSLPTASSQSSSPNESDSSSEkgfslpIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCPYslCGKLFSRND 337
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823683790 592 TLKTHLKIHTGEKPYKCKEC------GKSFAEASTLKTHHRIHTGEKPYKCTD---CGKSFTQSSHLQSHCRIHTGEKP- 661
Cdd:COG5048  338 ALKRHILLHTSISPAKEKLLnssskfSPLLNNEPPQSLQQYKDLKNDKKSETLsnsCIRNFKRDSNLSLHIITHLSFRPy 417
                        250       260
                 ....*....|....*....|....*
gi 823683790 662 -YKCKECGKSFAKDSSLQKHHRIHS 685
Cdd:COG5048  418 nCKNPPCSKSFNRHYNLIPHKKIHT 442
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
436-598 5.73e-06

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 49.31  E-value: 5.73e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823683790 436 KPYKCKECGKSFTHGYSLRIH--HRFHTGE--KPYKC--KDCGRSFAEGSSLKSHHRIHTGEKPYKCKECGKSFAKQSNF 509
Cdd:COG5048  288 LPIKSKQCNISFSRSSPLTRHlrSVNHSGEslKPFSCpySLCGKLFSRNDALKRHILLHTSISPAKEKLLNSSSKFSPLL 367
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823683790 510 ET-------HSRIHTGDRPYKCTD--CGKSFTRSFCLRKHHKTHT--GEKAYKCEECGKAFTQRSTLKTHYRIHTgEKPY 578
Cdd:COG5048  368 NNeppqslqQYKDLKNDKKSETLSnsCIRNFKRDSNLSLHIITHLsfRPYNCKNPPCSKSFNRHYNLIPHKKIHT-NHAP 446
                        170       180
                 ....*....|....*....|
gi 823683790 579 KCNECGKSFTEGSTLKTHLK 598
Cdd:COG5048  447 LLCSILKSFRRDLDLSNHGK 466
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
408-685 2.03e-05

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 47.77  E-value: 2.03e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823683790 408 KPYKCKICKRSFTTGSYLQAHQRIHTGEKPYKC--KECGKSFTHGYSLRIHHRFHTGEKPYKC-KDCGRSFAEGSSLKSH 484
Cdd:COG5048   32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCsySGCDKSFSRPLELSRHLRTHHNNPSDLNsKSLPLSNSKASSSSLS 111
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823683790 485 HRIHTGEKPYKCKECGKSFAKQSNFETHSRIHTGDRPYKCTDCGKSF------------TRSFCLRK----------HHK 542
Cdd:COG5048  112 SSSSNSNDNNLLSSHSLPPSSRDPQLPDLLSISNLRNNPLPGNNSSSvntpqsnslhppLPANSLSKdpssnlslliSSN 191
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823683790 543 THTGEKAYKCEECGKAFTQRSTLKTHYRIHTGEKPYKCNECGKSFTEGSTLKTHLKIHTGEKPYKCKECGKSFAEASTLK 622
Cdd:COG5048  192 VSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLSSSDSSSSASESPRSSLPTASSQ 271
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 823683790 623 THHRIHTGE-------KPYKCTDCGKSFTQSSHLQSH--CRIHTGE--KPYKCKE--CGKSFAKDSSLQKHHRIHS 685
Cdd:COG5048  272 SSSPNESDSssekgfsLPIKSKQCNISFSRSSPLTRHlrSVNHSGEslKPFSCPYslCGKLFSRNDALKRHILLHT 347
zf-H2C2_2 pfam13465
Zinc-finger double domain;
648-673 2.27e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 41.59  E-value: 2.27e-05
                          10        20
                  ....*....|....*....|....*.
gi 823683790  648 HLQSHCRIHTGEKPYKCKECGKSFAK 673
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
428-682 5.49e-05

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 46.23  E-value: 5.49e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823683790 428 HQRIHTGEKPYKCKECGKSFTHGYSLRIHHRFHTGEKPYKCKDCGRSF------AEGSSLKSHHRIHTGEKPYKCKECGK 501
Cdd:COG5048  189 SSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSpksllsQSPSSLSSSDSSSSASESPRSSLPTA 268
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823683790 502 SFAKQSNFETHSRIHTG-DRPYKCTDCGKSFTRSFCLRKH--HKTHTGEKAYKCEE----CGKAFTQRSTLKTHYRIHTG 574
Cdd:COG5048  269 SSQSSSPNESDSSSEKGfSLPIKSKQCNISFSRSSPLTRHlrSVNHSGESLKPFSCpyslCGKLFSRNDALKRHILLHTS 348
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823683790 575 EKPYKC--NECGKSFTEGSTLKTHLKI--HTGEKPYKCKE-----CGKSFAEASTLKTHHRIHTGEKP--YKCTDCGKSF 643
Cdd:COG5048  349 ISPAKEklLNSSSKFSPLLNNEPPQSLqqYKDLKNDKKSEtlsnsCIRNFKRDSNLSLHIITHLSFRPynCKNPPCSKSF 428
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 823683790 644 TQSSHLQSHCRIHTGEKPYKCkECGKSFAKDSSLQKHHR 682
Cdd:COG5048  429 NRHYNLIPHKKIHTNHAPLLC-SILKSFRRDLDLSNHGK 466
zf-H2C2_2 pfam13465
Zinc-finger double domain;
424-449 5.93e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 40.43  E-value: 5.93e-05
                          10        20
                  ....*....|....*....|....*.
gi 823683790  424 YLQAHQRIHTGEKPYKCKECGKSFTH 449
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
480-505 9.13e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 39.66  E-value: 9.13e-05
                          10        20
                  ....*....|....*....|....*.
gi 823683790  480 SLKSHHRIHTGEKPYKCKECGKSFAK 505
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
593-616 1.05e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 39.66  E-value: 1.05e-04
                          10        20
                  ....*....|....*....|....
gi 823683790  593 LKTHLKIHTGEKPYKCKECGKSFA 616
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFK 25
zf-H2C2_2 pfam13465
Zinc-finger double domain;
565-588 1.98e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.89  E-value: 1.98e-04
                          10        20
                  ....*....|....*....|....
gi 823683790  565 LKTHYRIHTGEKPYKCNECGKSFT 588
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFK 25
zf-H2C2_2 pfam13465
Zinc-finger double domain;
621-645 2.02e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.89  E-value: 2.02e-04
                          10        20
                  ....*....|....*....|....*
gi 823683790  621 LKTHHRIHTGEKPYKCTDCGKSFTQ 645
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 26
SUF4-like cd20908
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
408-456 2.05e-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: 40.23  E-value: 2.05e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 823683790 408 KPYkCKICKRSFTTGSYLQAHQRIHTgekpYKCKECGKSFTHGYSLRIH 456
Cdd:cd20908    1 KPW-CYYCDREFDDEKILIQHQKAKH----FKCHICHKKLYTAGGLAVH 44
SFP1 COG5189
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ...
602-685 3.22e-04

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


Pssm-ID: 227516 [Multi-domain]  Cd Length: 423  Bit Score: 43.55  E-value: 3.22e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823683790 602 GEKPYKCK--ECGKSFAEASTLKtHHRIHTgekpykctDCGKSFTQSSHLQSHCRIHTGEKPYKCKECGKSFAKDSSLqK 679
Cdd:COG5189  346 DGKPYKCPveGCNKKYKNQNGLK-YHMLHG--------HQNQKLHENPSPEKMNIFSAKDKPYRCEVCDKRYKNLNGL-K 415

                 ....*.
gi 823683790 680 HHRIHS 685
Cdd:COG5189  416 YHRKHS 421
zf-H2C2_2 pfam13465
Zinc-finger double domain;
508-533 7.46e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 37.35  E-value: 7.46e-04
                          10        20
                  ....*....|....*....|....*.
gi 823683790  508 NFETHSRIHTGDRPYKCTDCGKSFTR 533
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
537-561 8.06e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.97  E-value: 8.06e-04
                          10        20
                  ....*....|....*....|....*
gi 823683790  537 LRKHHKTHTGEKAYKCEECGKAFTQ 561
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 26
SFP1 COG5189
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ...
546-629 8.96e-04

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


Pssm-ID: 227516 [Multi-domain]  Cd Length: 423  Bit Score: 42.40  E-value: 8.96e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823683790 546 GEKAYKCE--ECGKAFTQRSTLKTHyRIHtgekpykcNECGKSFTEGSTLKTHLKIHTGEKPYKCKECGKSFAEASTLKt 623
Cdd:COG5189  346 DGKPYKCPveGCNKKYKNQNGLKYH-MLH--------GHQNQKLHENPSPEKMNIFSAKDKPYRCEVCDKRYKNLNGLK- 415

                 ....*.
gi 823683790 624 HHRIHT 629
Cdd:COG5189  416 YHRKHS 421
SFP1 COG5189
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ...
518-598 9.52e-04

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: 9.52e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823683790 518 GDRPYKC--TDCGKSFTRSFCLrKHHKTHTgekaykceECGKAFTQRSTLKTHYRIHTGEKPYKCNECGKSFTEGSTLKT 595
Cdd:COG5189  346 DGKPYKCpvEGCNKKYKNQNGL-KYHMLHG--------HQNQKLHENPSPEKMNIFSAKDKPYRCEVCDKRYKNLNGLKY 416

                 ...
gi 823683790 596 HLK 598
Cdd:COG5189  417 HRK 419
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
522-544 2.39e-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: 35.74  E-value: 2.39e-03
                          10        20
                  ....*....|....*....|...
gi 823683790  522 YKCTDCGKSFTRSFCLRKHHKTH 544
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
452-476 2.42e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.81  E-value: 2.42e-03
                          10        20
                  ....*....|....*....|....*
gi 823683790  452 SLRIHHRFHTGEKPYKCKDCGRSFA 476
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFK 25
SFP1 COG5189
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ...
406-489 2.43e-03

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


Pssm-ID: 227516 [Multi-domain]  Cd Length: 423  Bit Score: 40.86  E-value: 2.43e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823683790 406 GEKPYKCKI--CKRSFTTGSYLQAHqRIHtgekpykcKECGKSFTHGYSLRIHHRFHTGEKPYKCKDCGRSFAEGSSLKs 483
Cdd:COG5189  346 DGKPYKCPVegCNKKYKNQNGLKYH-MLH--------GHQNQKLHENPSPEKMNIFSAKDKPYRCEVCDKRYKNLNGLK- 415

                 ....*.
gi 823683790 484 HHRIHT 489
Cdd:COG5189  416 YHRKHS 421
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
550-572 3.30e-03

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


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 35.35  E-value: 3.30e-03
                          10        20
                  ....*....|....*....|...
gi 823683790  550 YKCEECGKAFTQRSTLKTHYRIH 572
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
SFP1 COG5189
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ...
434-519 8.51e-03

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


Pssm-ID: 227516 [Multi-domain]  Cd Length: 423  Bit Score: 39.32  E-value: 8.51e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823683790 434 GEKPYKCK--ECGKSFTHGYSLRiHHRFHtgekpykcKDCGRSFAEGSSLKSHHRIHTGEKPYKCKECGKSFAKQSNFET 511
Cdd:COG5189  346 DGKPYKCPveGCNKKYKNQNGLK-YHMLH--------GHQNQKLHENPSPEKMNIFSAKDKPYRCEVCDKRYKNLNGLKY 416

                 ....*...
gi 823683790 512 HsRIHTGD 519
Cdd:COG5189  417 H-RKHSHD 423
 
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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