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Conserved domains on  [gi|1387284646|ref|XP_002688547|]
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zinc finger protein 354C isoform X2 [Bos taurus]

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

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List of domain hits

 Name Accession Description Interval E-value
KRAB smart00349
krueppel associated box;
14-74 2.33e-29

krueppel associated box;


:

Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 109.99  E-value: 2.33e-29
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1387284646   14 VTFRDIAVLFSRDEWLHLDAAQRTLYREVMLENYSTLVSLGIPFSMPKLICQLQQGEDPCM 74
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQVPKPDLISQLEQGEEPWI 61
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
212-521 6.82e-11

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


:

Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 64.33  E-value: 6.82e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387284646 212 KPHIYNACDKSFNQSLHLIERQRIHTGEKPYKCS--ECGKTFSHRSSLLAHQRIHTGEKPYKCNQCE------KAFSSSS 283
Cdd:COG5048    32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSysGCDKSFSRPLELSRHLRTHHNNPSDLNSKSLplsnskASSSSLS 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387284646 284 TLIKHLRVHTGEKPYQCKDCGKAFSQCSTLTVHQRIHtgEKLYKCGECEKAFNCRAKLH-------------------RH 344
Cdd:COG5048   112 SSSSNSNDNNLLSSHSLPPSSRDPQLPDLLSISNLRN--NPLPGNNSSSVNTPQSNSLHpplpanslskdpssnlsllIS 189

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387284646 345 QQIHTGEKPYKCSECGKSYSQFTSLAEHQRLHTGEQLCKCLECGRNFTRISTFIEHQRIHTGQKPYQCNECGKAFNQYSS 424
Cdd:COG5048   190 SNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLSSSDSSSSASESPRSSLPTAS 269

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387284646 425 FNDHRKIHTGE-------KLYTCGECGKAFGCKSNLYRHQR--IHTGE--KPYQC--NQCGKAFSQYSFLTEHERIHTGE 491
Cdd:COG5048   270 SQSSSPNESDSssekgfsLPIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCpySLCGKLFSRNDALKRHILLHTSI 349

                         330       340       350
                  ....*....|....*....|....*....|..
gi 1387284646 492 KLYKCM--ECGKAYSYRSNLCRHKKVHNKEKL 521
Cdd:COG5048   350 SPAKEKllNSSSKFSPLLNNEPPQSLQQYKDL 381
 
Name Accession Description Interval E-value
KRAB smart00349
krueppel associated box;
14-74 2.33e-29

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 109.99  E-value: 2.33e-29
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1387284646   14 VTFRDIAVLFSRDEWLHLDAAQRTLYREVMLENYSTLVSLGIPFSMPKLICQLQQGEDPCM 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 2.34e-20

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: 84.06  E-value: 2.34e-20
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1387284646  13 SVTFRDIAVLFSRDEWLHLDAAQRTLYREVMLENYSTLVSLG 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 1.46e-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: 78.75  E-value: 1.46e-18
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1387284646  14 VTFRDIAVLFSRDEWLHLDAAQRTLYREVMLENYSTLVSL 53
Cdd:cd07765     1 VTFEDVAVYFSQEEWELLDPAQRDLYRDVMLENYENLVSL 40
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
212-521 6.82e-11

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 64.33  E-value: 6.82e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387284646 212 KPHIYNACDKSFNQSLHLIERQRIHTGEKPYKCS--ECGKTFSHRSSLLAHQRIHTGEKPYKCNQCE------KAFSSSS 283
Cdd:COG5048    32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSysGCDKSFSRPLELSRHLRTHHNNPSDLNSKSLplsnskASSSSLS 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387284646 284 TLIKHLRVHTGEKPYQCKDCGKAFSQCSTLTVHQRIHtgEKLYKCGECEKAFNCRAKLH-------------------RH 344
Cdd:COG5048   112 SSSSNSNDNNLLSSHSLPPSSRDPQLPDLLSISNLRN--NPLPGNNSSSVNTPQSNSLHpplpanslskdpssnlsllIS 189

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387284646 345 QQIHTGEKPYKCSECGKSYSQFTSLAEHQRLHTGEQLCKCLECGRNFTRISTFIEHQRIHTGQKPYQCNECGKAFNQYSS 424
Cdd:COG5048   190 SNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLSSSDSSSSASESPRSSLPTAS 269

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387284646 425 FNDHRKIHTGE-------KLYTCGECGKAFGCKSNLYRHQR--IHTGE--KPYQC--NQCGKAFSQYSFLTEHERIHTGE 491
Cdd:COG5048   270 SQSSSPNESDSssekgfsLPIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCpySLCGKLFSRNDALKRHILLHTSI 349

                         330       340       350
                  ....*....|....*....|....*....|..
gi 1387284646 492 KLYKCM--ECGKAYSYRSNLCRHKKVHNKEKL 521
Cdd:COG5048   350 SPAKEKllNSSSKFSPLLNNEPPQSLQQYKDL 381
zf-H2C2_2 pfam13465
Zinc-finger double domain;
452-477 5.42e-06

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 43.13  E-value: 5.42e-06
                          10        20
                  ....*....|....*....|....*.
gi 1387284646 452 NLYRHQRIHTGEKPYQCNQCGKAFSQ 477
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
SUF4-like cd20908
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
 240-292 8.06e-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: 38.31  E-value: 8.06e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1387284646 240 KPYkCSECGKTFSHRSSLLAHQRIHTgekpYKCNQCEKAFSSSSTLIKH-LRVH 292
Cdd:cd20908     1 KPW-CYYCDREFDDEKILIQHQKAKH----FKCHICHKKLYTAGGLAVHcLQVH 49
 
Name Accession Description Interval E-value
KRAB smart00349
krueppel associated box;
14-74 2.33e-29

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 109.99  E-value: 2.33e-29
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1387284646   14 VTFRDIAVLFSRDEWLHLDAAQRTLYREVMLENYSTLVSLGIPFSMPKLICQLQQGEDPCM 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 2.34e-20

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: 84.06  E-value: 2.34e-20
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1387284646  13 SVTFRDIAVLFSRDEWLHLDAAQRTLYREVMLENYSTLVSLG 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 1.46e-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: 78.75  E-value: 1.46e-18
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1387284646  14 VTFRDIAVLFSRDEWLHLDAAQRTLYREVMLENYSTLVSL 53
Cdd:cd07765     1 VTFEDVAVYFSQEEWELLDPAQRDLYRDVMLENYENLVSL 40
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
212-521 6.82e-11

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 64.33  E-value: 6.82e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387284646 212 KPHIYNACDKSFNQSLHLIERQRIHTGEKPYKCS--ECGKTFSHRSSLLAHQRIHTGEKPYKCNQCE------KAFSSSS 283
Cdd:COG5048    32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSysGCDKSFSRPLELSRHLRTHHNNPSDLNSKSLplsnskASSSSLS 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387284646 284 TLIKHLRVHTGEKPYQCKDCGKAFSQCSTLTVHQRIHtgEKLYKCGECEKAFNCRAKLH-------------------RH 344
Cdd:COG5048   112 SSSSNSNDNNLLSSHSLPPSSRDPQLPDLLSISNLRN--NPLPGNNSSSVNTPQSNSLHpplpanslskdpssnlsllIS 189

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387284646 345 QQIHTGEKPYKCSECGKSYSQFTSLAEHQRLHTGEQLCKCLECGRNFTRISTFIEHQRIHTGQKPYQCNECGKAFNQYSS 424
Cdd:COG5048   190 SNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLSSSDSSSSASESPRSSLPTAS 269

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387284646 425 FNDHRKIHTGE-------KLYTCGECGKAFGCKSNLYRHQR--IHTGE--KPYQC--NQCGKAFSQYSFLTEHERIHTGE 491
Cdd:COG5048   270 SQSSSPNESDSssekgfsLPIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCpySLCGKLFSRNDALKRHILLHTSI 349

                         330       340       350
                  ....*....|....*....|....*....|..
gi 1387284646 492 KLYKCM--ECGKAYSYRSNLCRHKKVHNKEKL 521
Cdd:COG5048   350 SPAKEKllNSSSKFSPLLNNEPPQSLQQYKDL 381
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
240-525 4.51e-10

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 62.02  E-value: 4.51e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387284646 240 KPYKCSECGKTFSHRSSLLAHQRIHTGEKPYKCNQ--CEKAFSSSSTLIKHLRVHTGEKPY-QCKDCGKAFSQCSTLTVH 316
Cdd:COG5048    32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYsgCDKSFSRPLELSRHLRTHHNNPSDlNSKSLPLSNSKASSSSLS 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387284646 317 QRIHTGEKLYKCGECEKAFNcraklHRHQQIHTGEKPYKCSECGKSYSQFTSLAEHQRLHTGEQLCKCLECGRNFTRIST 396
Cdd:COG5048   112 SSSSNSNDNNLLSSHSLPPS-----SRDPQLPDLLSISNLRNNPLPGNNSSSVNTPQSNSLHPPLPANSLSKDPSSNLSL 186

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387284646 397 FIeHQRIHTGQKPYQCNECGKAFNQYSSFNDHRKIHTGEKLYTCGECGKAF------------------GCKSNLYRHQR 458
Cdd:COG5048   187 LI-SSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSpksllsqspsslsssdssSSASESPRSSL 265

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387284646 459 IHTGE-----------------KPYQCNQCGKAFSQYSFLTEHER--IHTGEKL--YKCME--CGKAYSYRSNLCRHKKV 515
Cdd:COG5048   266 PTASSqssspnesdsssekgfsLPIKSKQCNISFSRSSPLTRHLRsvNHSGESLkpFSCPYslCGKLFSRNDALKRHILL 345

                         330
                  ....*....|
gi 1387284646 516 HNKEKLYKWK 525
Cdd:COG5048   346 HTSISPAKEK 355
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
268-428 1.54e-07

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 53.93  E-value: 1.54e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387284646 268 KPYKCNQCEKAFSSSSTLIKHLR--VHTGE--KPYQC--KDCGKAFSQCSTLTVHQRIHTGEKLYKC--GECEKAF---- 335
Cdd:COG5048   288 LPIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCpySLCGKLFSRNDALKRHILLHTSISPAKEklLNSSSKFspll 367

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387284646 336 -NCRAKLHRHQQIHTGEKPYKCSecGKSYSQFTSLAEHQRLHTGEQL------CKCLECGRNFTRISTFIEHQRIHTgQK 408
Cdd:COG5048   368 nNEPPQSLQQYKDLKNDKKSETL--SNSCIRNFKRDSNLSLHIITHLsfrpynCKNPPCSKSFNRHYNLIPHKKIHT-NH 444

                         170       180
                  ....*....|....*....|
gi 1387284646 409 PYQCNECGKAFNQYSSFNDH 428
Cdd:COG5048   445 APLLCSILKSFRRDLDLSNH 464
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
220-477 3.07e-06

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 49.69  E-value: 3.07e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387284646 220 DKSFNQSLHLIERqrIHTGEKPYKCSECGKTFSHRSSLLAHQRIHTGEKPYKCNQCEKAFSSSSTLIKHLRVHTGEKPYQ 299
Cdd:COG5048   179 DPSSNLSLLISSN--VSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLSSSDSSSS 256

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387284646 300 CKDCGKAFSQCSTLTVHQRIHTGE-------KLYKCGECEKAFNCRAKLHRHQQ--IHTGE--KPYKCSE--CGKSYSQF 366
Cdd:COG5048   257 ASESPRSSLPTASSQSSSPNESDSssekgfsLPIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCPYslCGKLFSRN 336

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387284646 367 TSLAEHQRLHTGEQL--CKCLECGRNFTRIST-----FIEHQRIHTGQKPYQC--NECGKAFNQYSSFNDHRKIHT--GE 435
Cdd:COG5048   337 DALKRHILLHTSISPakEKLLNSSSKFSPLLNneppqSLQQYKDLKNDKKSETlsNSCIRNFKRDSNLSLHIITHLsfRP 416

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1387284646 436 KLYTCGECGKAFGCKSNLYRHQRIHTGEKPYQCNQCGKAFSQ 477
Cdd:COG5048   417 YNCKNPPCSKSFNRHYNLIPHKKIHTNHAPLLCSILKSFRRD 458
zf-H2C2_2 pfam13465
Zinc-finger double domain;
452-477 5.42e-06

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 43.13  E-value: 5.42e-06
                          10        20
                  ....*....|....*....|....*.
gi 1387284646 452 NLYRHQRIHTGEKPYQCNQCGKAFSQ 477
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
285-309 1.98e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.51  E-value: 1.98e-04
                          10        20
                  ....*....|....*....|....*
gi 1387284646 285 LIKHLRVHTGEKPYQCKDCGKAFSQ 309
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
256-281 2.61e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.12  E-value: 2.61e-04
                          10        20
                  ....*....|....*....|....*.
gi 1387284646 256 SLLAHQRIHTGEKPYKCNQCEKAFSS 281
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
399-421 2.82e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.12  E-value: 2.82e-04
                          10        20
                  ....*....|....*....|...
gi 1387284646 399 EHQRIHTGQKPYQCNECGKAFNQ 421
Cdd:pfam13465   4 RHMRTHTGEKPYKCPECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 242-264 4.92e-04

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: 37.28  E-value: 4.92e-04
                          10        20
                  ....*....|....*....|...
gi 1387284646 242 YKCSECGKTFSHRSSLLAHQRIH 264
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
343-365 6.12e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 37.35  E-value: 6.12e-04
                          10        20
                  ....*....|....*....|...
gi 1387284646 343 RHQQIHTGEKPYKCSECGKSYSQ 365
Cdd:pfam13465   4 RHMRTHTGEKPYKCPECGKSFKS 26
SFP1 COG5189
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ...
 350-430 7.88e-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: 7.88e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387284646 350 GEKPYKCS--ECGKSYSQFTSLAEHqRLHTgeqlckclECGRNFTRISTFIEHQRIHTGQKPYQCNECGKAFNQYSSFND 427
Cdd:COG5189   346 DGKPYKCPveGCNKKYKNQNGLKYH-MLHG--------HQNQKLHENPSPEKMNIFSAKDKPYRCEVCDKRYKNLNGLKY 416


                  ...
gi 1387284646 428 HRK 430
Cdd:COG5189   417 HRK 419
SUF4-like cd20908
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
 240-292 8.06e-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: 38.31  E-value: 8.06e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1387284646 240 KPYkCSECGKTFSHRSSLLAHQRIHTgekpYKCNQCEKAFSSSSTLIKH-LRVH 292
Cdd:cd20908     1 KPW-CYYCDREFDDEKILIQHQKAKH----FKCHICHKKLYTAGGLAVHcLQVH 49
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 298-320 1.15e-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: 36.51  E-value: 1.15e-03
                          10        20
                  ....*....|....*....|...
gi 1387284646 298 YQCKDCGKAFSQCSTLTVHQRIH 320
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
SFP1 COG5189
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ...
 294-377 1.22e-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: 1.22e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387284646 294 GEKPYQCK--DCGKAFSQCSTLTVHqRIHtgeklykcGECEKAFNCRAKLHRHQQIHTGEKPYKCSECGKSYSQFTSLAE 371
Cdd:COG5189   346 DGKPYKCPveGCNKKYKNQNGLKYH-MLH--------GHQNQKLHENPSPEKMNIFSAKDKPYRCEVCDKRYKNLNGLKY 416


                  ....*.
gi 1387284646 372 HqRLHT 377
Cdd:COG5189   417 H-RKHS 421
zf-H2C2_2 pfam13465
Zinc-finger double domain;
481-505 3.18e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.04  E-value: 3.18e-03
                          10        20
                  ....*....|....*....|....*
gi 1387284646 481 LTEHERIHTGEKLYKCMECGKAYSY 505
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 270-292 3.57e-03

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


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 34.97  E-value: 3.57e-03
                          10        20
                  ....*....|....*....|...
gi 1387284646 270 YKCNQCEKAFSSSSTLIKHLRVH 292
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
233-253 4.03e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.04  E-value: 4.03e-03
                          10        20
                  ....*....|....*....|.
gi 1387284646 233 QRIHTGEKPYKCSECGKTFSH 253
Cdd:pfam13465   6 MRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
313-337 5.58e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 34.65  E-value: 5.58e-03
                          10        20
                  ....*....|....*....|....*
gi 1387284646 313 LTVHQRIHTGEKLYKCGECEKAFNC 337
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 26
 
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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