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Conserved domains on  [gi|298228999|ref|NP_001177184|]
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zinc finger protein 630 isoform 2 [Homo sapiens]

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;
4-54 6.81e-24

krueppel associated box;


:

Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 94.97  E-value: 6.81e-24
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 298228999     4 SQEEWQQLNPAQKTLHRDVMLETYNHLVSVGCSGIKPDVIFKLEHGKDPWI 54
Cdd:smart00349  11 TQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQVPKPDLISQLEQGEEPWI 61
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
315-564 5.60e-11

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


:

Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 65.10  E-value: 5.60e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298228999 315 SRKSPFTVHQRVHTGEKPYECFECPKAFSQKSHLIIHQrvhTREKPFECSECRKAFCEMSHLFIHQITHTGKKPYECTEC 394
Cdd:COG5048  181 SSNLSLLISSNVSTSIPSSSENSPLSSSYSIPSSSSDQ---NLENSSSSLPLTTNSQLSPKSLLSQSPSSLSSSDSSSSA 257

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298228999 395 GKTFPRKTQLIIHQRTH----------TGEKPYKCGECGKTFCQQSHLIGHQR--IHTGE--KPYVCT--DCGKAFSQKS 458
Cdd:COG5048  258 SESPRSSLPTASSQSSSpnesdsssekGFSLPIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCPysLCGKLFSRND 337

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298228999 459 HLTGHQRLHTGEKPYMC--TECGKSFSQKSP-----LIIHQRIHTGEKPYQC--GECGKTFSQKSLLIIHLRVHTGEKPY 529
Cdd:COG5048  338 ALKRHILLHTSISPAKEklLNSSSKFSPLLNneppqSLQQYKDLKNDKKSETlsNSCIRNFKRDSNLSLHIITHLSFRPY 417

                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 298228999 530 ECTECGRAFSLKSHLIL--HQRGHTGEKPYECSECGK 564
Cdd:COG5048  418 NCKNPPCSKSFNRHYNLipHKKIHTNHAPLLCSILKS 454
 
Name Accession Description Interval E-value
KRAB smart00349
krueppel associated box;
4-54 6.81e-24

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 94.97  E-value: 6.81e-24
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 298228999     4 SQEEWQQLNPAQKTLHRDVMLETYNHLVSVGCSGIKPDVIFKLEHGKDPWI 54
Cdd:smart00349  11 TQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQVPKPDLISQLEQGEEPWI 61
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
 4-34 3.52e-15

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: 69.42  E-value: 3.52e-15
                          10        20        30
                  ....*....|....*....|....*....|.
gi 298228999    4 SQEEWQQLNPAQKTLHRDVMLETYNHLVSVG 34
Cdd:pfam01352  12 TQEEWALLDPAQRNLYRDVMLENYRNLVSLG 42
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
 4-32 1.79e-11

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: 59.10  E-value: 1.79e-11
                         10        20
                 ....*....|....*....|....*....
gi 298228999   4 SQEEWQQLNPAQKTLHRDVMLETYNHLVS 32
Cdd:cd07765   11 SQEEWELLDPAQRDLYRDVMLENYENLVS 39
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
315-564 5.60e-11

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 65.10  E-value: 5.60e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298228999 315 SRKSPFTVHQRVHTGEKPYECFECPKAFSQKSHLIIHQrvhTREKPFECSECRKAFCEMSHLFIHQITHTGKKPYECTEC 394
Cdd:COG5048  181 SSNLSLLISSNVSTSIPSSSENSPLSSSYSIPSSSSDQ---NLENSSSSLPLTTNSQLSPKSLLSQSPSSLSSSDSSSSA 257

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298228999 395 GKTFPRKTQLIIHQRTH----------TGEKPYKCGECGKTFCQQSHLIGHQR--IHTGE--KPYVCT--DCGKAFSQKS 458
Cdd:COG5048  258 SESPRSSLPTASSQSSSpnesdsssekGFSLPIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCPysLCGKLFSRND 337

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298228999 459 HLTGHQRLHTGEKPYMC--TECGKSFSQKSP-----LIIHQRIHTGEKPYQC--GECGKTFSQKSLLIIHLRVHTGEKPY 529
Cdd:COG5048  338 ALKRHILLHTSISPAKEklLNSSSKFSPLLNneppqSLQQYKDLKNDKKSETlsNSCIRNFKRDSNLSLHIITHLSFRPY 417

                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 298228999 530 ECTECGRAFSLKSHLIL--HQRGHTGEKPYECSECGK 564
Cdd:COG5048  418 NCKNPPCSKSFNRHYNLipHKKIHTNHAPLLCSILKS 454
zf-H2C2_2 pfam13465
Zinc-finger double domain;
431-456 2.15e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.81  E-value: 2.15e-03
                          10        20
                  ....*....|....*....|....*.
gi 298228999  431 HLIGHQRIHTGEKPYVCTDCGKAFSQ 456
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
SUF4-like cd20908
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
 471-523 5.68e-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: 5.68e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 298228999 471 KPYmCTECGKSFSQKSPLIIHQRIHTgekpYQCGECGKTFSQKSLLIIH-LRVH 523
Cdd:cd20908    1 KPW-CYYCDREFDDEKILIQHQKAKH----FKCHICHKKLYTAGGLAVHcLQVH 49
 
Name Accession Description Interval E-value
KRAB smart00349
krueppel associated box;
4-54 6.81e-24

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 94.97  E-value: 6.81e-24
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 298228999     4 SQEEWQQLNPAQKTLHRDVMLETYNHLVSVGCSGIKPDVIFKLEHGKDPWI 54
Cdd:smart00349  11 TQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQVPKPDLISQLEQGEEPWI 61
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
 4-34 3.52e-15

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: 69.42  E-value: 3.52e-15
                          10        20        30
                  ....*....|....*....|....*....|.
gi 298228999    4 SQEEWQQLNPAQKTLHRDVMLETYNHLVSVG 34
Cdd:pfam01352  12 TQEEWALLDPAQRNLYRDVMLENYRNLVSLG 42
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
 4-32 1.79e-11

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: 59.10  E-value: 1.79e-11
                         10        20
                 ....*....|....*....|....*....
gi 298228999   4 SQEEWQQLNPAQKTLHRDVMLETYNHLVS 32
Cdd:cd07765   11 SQEEWELLDPAQRDLYRDVMLENYENLVS 39
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
315-564 5.60e-11

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 65.10  E-value: 5.60e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298228999 315 SRKSPFTVHQRVHTGEKPYECFECPKAFSQKSHLIIHQrvhTREKPFECSECRKAFCEMSHLFIHQITHTGKKPYECTEC 394
Cdd:COG5048  181 SSNLSLLISSNVSTSIPSSSENSPLSSSYSIPSSSSDQ---NLENSSSSLPLTTNSQLSPKSLLSQSPSSLSSSDSSSSA 257

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298228999 395 GKTFPRKTQLIIHQRTH----------TGEKPYKCGECGKTFCQQSHLIGHQR--IHTGE--KPYVCT--DCGKAFSQKS 458
Cdd:COG5048  258 SESPRSSLPTASSQSSSpnesdsssekGFSLPIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCPysLCGKLFSRND 337

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298228999 459 HLTGHQRLHTGEKPYMC--TECGKSFSQKSP-----LIIHQRIHTGEKPYQC--GECGKTFSQKSLLIIHLRVHTGEKPY 529
Cdd:COG5048  338 ALKRHILLHTSISPAKEklLNSSSKFSPLLNneppqSLQQYKDLKNDKKSETlsNSCIRNFKRDSNLSLHIITHLSFRPY 417

                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 298228999 530 ECTECGRAFSLKSHLIL--HQRGHTGEKPYECSECGK 564
Cdd:COG5048  418 NCKNPPCSKSFNRHYNLipHKKIHTNHAPLLCSILKS 454
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
275-622 1.00e-07

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 54.70  E-value: 1.00e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298228999 275 KPYVCGDCRKAFSEKSHLIVHQRIHTGEKPYECTKYGRA--FSRKSPFTVHQRVHTGEKPYEC----------------F 336
Cdd:COG5048   32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYSGCDksFSRPLELSRHLRTHHNNPSDLNskslplsnskasssslS 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298228999 337 ECPKAFSQKSHL---IIHQRVHTREKPFECSECRKAFCE---MSHLFIHQITHTGKK-PYECTECGKTFPRKTQLIIHQR 409
Cdd:COG5048  112 SSSSNSNDNNLLsshSLPPSSRDPQLPDLLSISNLRNNPlpgNNSSSVNTPQSNSLHpPLPANSLSKDPSSNLSLLISSN 191

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298228999 410 THTGEKPYKCGECGKTFCQQSHLIGHQRIHTGEKPYVCTDCGKAF------SQKSHLTGHQRLHTGEKPYMCTECGKSFS 483
Cdd:COG5048  192 VSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSpksllsQSPSSLSSSDSSSSASESPRSSLPTASSQ 271

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298228999 484 QKSPLIIHQRIHTG-EKPYQCGECGKTFSQKSLLIIHLR--VHTGE--KPYECTE--CGRAFSLKSHLILHQRGHTGEKP 556
Cdd:COG5048  272 SSSPNESDSSSEKGfSLPIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCPYslCGKLFSRNDALKRHILLHTSISP 351

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 298228999 557 YECSEC------GKAFCGKSPLIIHQKTHPREKTPECAESGMTFFWKSQMITYQR---RHTGEKPS--RCSDCGKAF 622
Cdd:COG5048  352 AKEKLLnssskfSPLLNNEPPQSLQQYKDLKNDKKSETLSNSCIRNFKRDSNLSLhiiTHLSFRPYncKNPPCSKSF 428
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
156-515 5.99e-05

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 45.84  E-value: 5.99e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298228999 156 PLSQKFHKFDSCENSLKSNSDLLNYNRSYARKNptKRFRCGRPPKYNASCSVPEKEGFIHTGMEPYGDSqcEKVLSHKQA 235
Cdd:COG5048   76 PLELSRHLRTHHNNPSDLNSKSLPLSNSKASSS--SLSSSSSNSNDNNLLSSHSLPPSSRDPQLPDLLS--ISNLRNNPL 151

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298228999 236 HVQYKKFQAREKPN-------VCSMCGKAFIKKSQLIIHQRIHTGEKPYVCGDCRKaFSEKSHLIVHQRIHTGEKPYECT 308
Cdd:COG5048  152 PGNNSSSVNTPQSNslhpplpANSLSKDPSSNLSLLISSNVSTSIPSSSENSPLSS-SYSIPSSSSDQNLENSSSSLPLT 230

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298228999 309 KYGRAFSRKSP------FTVHQRVHTGEKPYECFECPKAFSQKSHLIIHQRVHTR-EKPFECSECRKAFCEMSHLFIHQ- 380
Cdd:COG5048  231 TNSQLSPKSLLsqspssLSSSDSSSSASESPRSSLPTASSQSSSPNESDSSSEKGfSLPIKSKQCNISFSRSSPLTRHLr 310

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298228999 381 -ITHTGK--KPYECTE--CGKTFPRKTQLIIHQRTHTGEKPYKC--GECGKTF------CQQSHLIGHQRIHTgEKPYVC 447
Cdd:COG5048  311 sVNHSGEslKPFSCPYslCGKLFSRNDALKRHILLHTSISPAKEklLNSSSKFspllnnEPPQSLQQYKDLKN-DKKSET 389

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 298228999 448 TD--CGKAFSQKSHLTGHQRLHTGEKPYMCT--ECGKSFSQKSPLIIHQRIHTGEKPYQCGECGKTFSQKSL 515
Cdd:COG5048  390 LSnsCIRNFKRDSNLSLHIITHLSFRPYNCKnpPCSKSFNRHYNLIPHKKIHTNHAPLLCSILKSFRRDLDL 461
zf-H2C2_2 pfam13465
Zinc-finger double domain;
431-456 2.15e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.81  E-value: 2.15e-03
                          10        20
                  ....*....|....*....|....*.
gi 298228999  431 HLIGHQRIHTGEKPYVCTDCGKAFSQ 456
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
491-512 2.44e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.81  E-value: 2.44e-03
                          10        20
                  ....*....|....*....|..
gi 298228999  491 HQRIHTGEKPYQCGECGKTFSQ 512
Cdd:pfam13465   5 HMRTHTGEKPYKCPECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 389-411 3.01e-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: 3.01e-03
                          10        20
                  ....*....|....*....|...
gi 298228999  389 YECTECGKTFPRKTQLIIHQRTH 411
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 501-523 3.16e-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: 3.16e-03
                          10        20
                  ....*....|....*....|...
gi 298228999  501 YQCGECGKTFSQKSLLIIHLRVH 523
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
459-484 3.54e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.42  E-value: 3.54e-03
                          10        20
                  ....*....|....*....|....*.
gi 298228999  459 HLTGHQRLHTGEKPYMCTECGKSFSQ 484
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
407-426 3.76e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.04  E-value: 3.76e-03
                          10        20
                  ....*....|....*....|
gi 298228999  407 HQRTHTGEKPYKCGECGKTF 426
Cdd:pfam13465   5 HMRTHTGEKPYKCPECGKSF 24
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
386-633 3.97e-03

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 40.06  E-value: 3.97e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298228999 386 KKPYECTECGKTFPRKTQLIIHQRTHTGEKPYKCG--ECGKTFCQQSHLIGHQRIHTGEKPYVCTD-CGKAFSQKSHLTG 462
Cdd:COG5048   31 PRPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSysGCDKSFSRPLELSRHLRTHHNNPSDLNSKsLPLSNSKASSSSL 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298228999 463 HQRLHTGEKPYMCTECGKSFSQKSPLII--HQRIHTGEKPYQ-CGECGKTFSQKSLLI-------------------IHL 520
Cdd:COG5048  111 SSSSSNSNDNNLLSSHSLPPSSRDPQLPdlLSISNLRNNPLPgNNSSSVNTPQSNSLHpplpanslskdpssnlsllISS 190

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298228999 521 RVHTGEKPYECTECGRAFSLKSHLILHQRGHTGEKPYECSECGKAFCGKSPLIIHQKTHPREKTPECAESGMTFFWKSQM 600
Cdd:COG5048  191 NVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLSSSDSSSSASESPRSSLPTASS 270

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 298228999 601 ITYQ------RRHTG-EKPSRCSDCGKAFCQHVYFTGHQN 633
Cdd:COG5048  271 QSSSpnesdsSSEKGfSLPIKSKQCNISFSRSSPLTRHLR 310
zf-H2C2_2 pfam13465
Zinc-finger double domain;
543-566 3.98e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.04  E-value: 3.98e-03
                          10        20
                  ....*....|....*....|....
gi 298228999  543 HLILHQRGHTGEKPYECSECGKAF 566
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSF 24
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 445-467 4.64e-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: 4.64e-03
                          10        20
                  ....*....|....*....|...
gi 298228999  445 YVCTDCGKAFSQKSHLTGHQRLH 467
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 417-439 5.02e-03

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


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 34.97  E-value: 5.02e-03
                          10        20
                  ....*....|....*....|...
gi 298228999  417 YKCGECGKTFCQQSHLIGHQRIH 439
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
SUF4-like cd20908
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
 471-523 5.68e-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: 5.68e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 298228999 471 KPYmCTECGKSFSQKSPLIIHQRIHTgekpYQCGECGKTFSQKSLLIIH-LRVH 523
Cdd:cd20908    1 KPW-CYYCDREFDDEKILIQHQKAKH----FKCHICHKKLYTAGGLAVHcLQVH 49
zf-H2C2_2 pfam13465
Zinc-finger double domain;
323-344 6.91e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 34.27  E-value: 6.91e-03
                          10        20
                  ....*....|....*....|..
gi 298228999  323 HQRVHTGEKPYECFECPKAFSQ 344
Cdd:pfam13465   5 HMRTHTGEKPYKCPECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 333-355 7.15e-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: 34.20  E-value: 7.15e-03
                          10        20
                  ....*....|....*....|...
gi 298228999  333 YECFECPKAFSQKSHLIIHQRVH 355
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
519-539 7.70e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 34.27  E-value: 7.70e-03
                          10        20
                  ....*....|....*....|.
gi 298228999  519 HLRVHTGEKPYECTECGRAFS 539
Cdd:pfam13465   5 HMRTHTGEKPYKCPECGKSFK 25
zf-H2C2_2 pfam13465
Zinc-finger double domain;
375-398 7.85e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 34.27  E-value: 7.85e-03
                          10        20
                  ....*....|....*....|....
gi 298228999  375 HLFIHQITHTGKKPYECTECGKTF 398
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSF 24
 
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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