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Conserved domains on  [gi|27734192|ref|NP_775563|]
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zinc finger protein 879 isoform 1 [Mus musculus]

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;
14-70 1.15e-30

krueppel associated box;


:

Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 113.84  E-value: 1.15e-30
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 27734192     14 VTFRDVAVSFSQDEWLHLDPAQRTLYREVMLENYSNLVSLGILFSKPKVIAQLEQAE 70
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQVPKPDLISQLEQGE 57
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
205-558 1.67e-16

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


:

Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 82.05  E-value: 1.67e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27734192 205 KCNICGKVFFHSSSLSKHQRTHTGEKLYKC--QGCRKAFSQRSSLAQHLRVHTGEKPYLCSD----------------CG 266
Cdd:COG5048  35 SCPNCTDSFSRLEHLTRHIRSHTGEKPSQCsySGCDKSFSRPLELSRHLRTHHNNPSDLNSKslplsnskasssslssSS 114
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27734192 267 KAFSFTTSL---------------IGHQRMHTGERPYE-CKECGKTFKGSSSLH-------------------NHQRIHT 311
Cdd:COG5048 115 SNSNDNNLLsshslppssrdpqlpDLLSISNLRNNPLPgNNSSSVNTPQSNSLHpplpanslskdpssnlsllISSNVST 194
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27734192 312 GEKPYKCNECGRAFSQCSSLIQHHRIHTGEKPYECSQCGKAFTSISRLSRH------HRVHTGEKPFHCNVCGKVFSYHS 385
Cdd:COG5048 195 SIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQSPsslsssDSSSSASESPRSSLPTASSQSSS 274
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27734192 386 ALTIHQRTHTG-EKPYACKECGKAFSQSSALTQHQR--IHTGE--KPYKCAE--CGKAFSWLSRLNIHHRIHTGEKPYHC 458
Cdd:COG5048 275 PNESDSSSEKGfSLPIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCPYslCGKLFSRNDALKRHILLHTSISPAKE 354
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27734192 459 KECGKAFSSHSAVNT-------HRKIHTGEKPYKCSD--CEKAFNQSSALIQHQRIHTGEKP--FNCKVCGKAFRQSSSL 527
Cdd:COG5048 355 KLLNSSSKFSPLLNNeppqslqQYKDLKNDKKSETLSnsCIRNFKRDSNLSLHIITHLSFRPynCKNPPCSKSFNRHYNL 434
                       410       420       430
                ....*....|....*....|....*....|.
gi 27734192 528 MTHMRIHTGERPYRCEACGKaFSQSSSLANH 558
Cdd:COG5048 435 IPHKKIHTNHAPLLCSILKS-FRRDLDLSNH 464
 
Name Accession Description Interval E-value
KRAB smart00349
krueppel associated box;
14-70 1.15e-30

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 113.84  E-value: 1.15e-30
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 27734192     14 VTFRDVAVSFSQDEWLHLDPAQRTLYREVMLENYSNLVSLGILFSKPKVIAQLEQAE 70
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQVPKPDLISQLEQGE 57
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
13-54 1.58e-24

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


Pssm-ID: 460171  Cd Length: 42  Bit Score: 96.00  E-value: 1.58e-24
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 27734192    13 PVTFRDVAVSFSQDEWLHLDPAQRTLYREVMLENYSNLVSLG 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 1.86e-21

KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression module, found in a subgroup of the zinc finger proteins (ZFPs) of the C2H2 family, KRAB-ZFPs. KRAB-ZFPs comprise the largest group of transcriptional regulators in mammals, and are only found in tetrapods. These proteins have been shown to play important roles in cell differentiation and organ development, and in regulating viral replication and transcription. A KRAB domain may consist of an A-box, or of an A-box plus either a B-box, a divergent B-box (b), or a C-box. Only the A-box is included in this model. The A-box is needed for repression, the B- and C- boxes are not. KRAB-ZFPs have one or two KRAB domains at their amino-terminal end, and multiple C2H2 zinc finger motifs at their C-termini. Some KRAB-ZFPs also contain a SCAN domain which mediates homo- and hetero-oligomerization. The KRAB domain is a protein-protein interaction module which represses transcription through recruiting corepressors. A key mechanism appears to be the following: KRAB-AFPs tethered to DNA recruit, via their KRAB domain, the repressor KAP1 (KRAB-associated protein-1, also known as transcription intermediary factor 1 beta , KRAB-A interacting protein , and tripartite motif protein 28). The KAP1/ KRAB-AFP complex in turn recruits the heterochromatin protein 1 (HP1) family, and other chromatin modulating proteins, leading to transcriptional repression through heterochromatin formation.


Pssm-ID: 143639  Cd Length: 40  Bit Score: 87.22  E-value: 1.86e-21
                        10        20        30        40
                ....*....|....*....|....*....|....*....|
gi 27734192  14 VTFRDVAVSFSQDEWLHLDPAQRTLYREVMLENYSNLVSL 53
Cdd:cd07765   1 VTFEDVAVYFSQEEWELLDPAQRDLYRDVMLENYENLVSL 40
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
205-558 1.67e-16

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 82.05  E-value: 1.67e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27734192 205 KCNICGKVFFHSSSLSKHQRTHTGEKLYKC--QGCRKAFSQRSSLAQHLRVHTGEKPYLCSD----------------CG 266
Cdd:COG5048  35 SCPNCTDSFSRLEHLTRHIRSHTGEKPSQCsySGCDKSFSRPLELSRHLRTHHNNPSDLNSKslplsnskasssslssSS 114
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27734192 267 KAFSFTTSL---------------IGHQRMHTGERPYE-CKECGKTFKGSSSLH-------------------NHQRIHT 311
Cdd:COG5048 115 SNSNDNNLLsshslppssrdpqlpDLLSISNLRNNPLPgNNSSSVNTPQSNSLHpplpanslskdpssnlsllISSNVST 194
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27734192 312 GEKPYKCNECGRAFSQCSSLIQHHRIHTGEKPYECSQCGKAFTSISRLSRH------HRVHTGEKPFHCNVCGKVFSYHS 385
Cdd:COG5048 195 SIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQSPsslsssDSSSSASESPRSSLPTASSQSSS 274
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27734192 386 ALTIHQRTHTG-EKPYACKECGKAFSQSSALTQHQR--IHTGE--KPYKCAE--CGKAFSWLSRLNIHHRIHTGEKPYHC 458
Cdd:COG5048 275 PNESDSSSEKGfSLPIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCPYslCGKLFSRNDALKRHILLHTSISPAKE 354
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27734192 459 KECGKAFSSHSAVNT-------HRKIHTGEKPYKCSD--CEKAFNQSSALIQHQRIHTGEKP--FNCKVCGKAFRQSSSL 527
Cdd:COG5048 355 KLLNSSSKFSPLLNNeppqslqQYKDLKNDKKSETLSnsCIRNFKRDSNLSLHIITHLSFRPynCKNPPCSKSFNRHYNL 434
                       410       420       430
                ....*....|....*....|....*....|.
gi 27734192 528 MTHMRIHTGERPYRCEACGKaFSQSSSLANH 558
Cdd:COG5048 435 IPHKKIHTNHAPLLCSILKS-FRRDLDLSNH 464
zf-H2C2_2 pfam13465
Zinc-finger double domain;
526-551 4.27e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 40.43  E-value: 4.27e-05
                          10        20
                  ....*....|....*....|....*.
gi 27734192   526 SLMTHMRIHTGERPYRCEACGKAFSQ 551
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
SUF4-like cd20908
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
482-531 2.66e-04

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


Pssm-ID: 411020 [Multi-domain]  Cd Length: 82  Bit Score: 39.85  E-value: 2.66e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 27734192 482 KPYkCSDCEKAFNQSSALIQHQRIHTgekpFNCKVCGKAFRQSSSLMTHM 531
Cdd:cd20908   1 KPW-CYYCDREFDDEKILIQHQKAKH----FKCHICHKKLYTAGGLAVHC 45
PHA00733 PHA00733
hypothetical protein
483-531 1.21e-03

hypothetical protein


Pssm-ID: 177301  Cd Length: 128  Bit Score: 39.09  E-value: 1.21e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 27734192  483 PYKCSDCEKAFNQSSALIQHQRIHTGEKpfNCKVCGKAFRQSSSLMTHM 531
Cdd:PHA00733  73 PYVCPLCLMPFSSSVSLKQHIRYTEHSK--VCPVCGKEFRNTDSTLDHV 119
 
Name Accession Description Interval E-value
KRAB smart00349
krueppel associated box;
14-70 1.15e-30

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 113.84  E-value: 1.15e-30
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 27734192     14 VTFRDVAVSFSQDEWLHLDPAQRTLYREVMLENYSNLVSLGILFSKPKVIAQLEQAE 70
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQVPKPDLISQLEQGE 57
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
13-54 1.58e-24

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


Pssm-ID: 460171  Cd Length: 42  Bit Score: 96.00  E-value: 1.58e-24
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 27734192    13 PVTFRDVAVSFSQDEWLHLDPAQRTLYREVMLENYSNLVSLG 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 1.86e-21

KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression module, found in a subgroup of the zinc finger proteins (ZFPs) of the C2H2 family, KRAB-ZFPs. KRAB-ZFPs comprise the largest group of transcriptional regulators in mammals, and are only found in tetrapods. These proteins have been shown to play important roles in cell differentiation and organ development, and in regulating viral replication and transcription. A KRAB domain may consist of an A-box, or of an A-box plus either a B-box, a divergent B-box (b), or a C-box. Only the A-box is included in this model. The A-box is needed for repression, the B- and C- boxes are not. KRAB-ZFPs have one or two KRAB domains at their amino-terminal end, and multiple C2H2 zinc finger motifs at their C-termini. Some KRAB-ZFPs also contain a SCAN domain which mediates homo- and hetero-oligomerization. The KRAB domain is a protein-protein interaction module which represses transcription through recruiting corepressors. A key mechanism appears to be the following: KRAB-AFPs tethered to DNA recruit, via their KRAB domain, the repressor KAP1 (KRAB-associated protein-1, also known as transcription intermediary factor 1 beta , KRAB-A interacting protein , and tripartite motif protein 28). The KAP1/ KRAB-AFP complex in turn recruits the heterochromatin protein 1 (HP1) family, and other chromatin modulating proteins, leading to transcriptional repression through heterochromatin formation.


Pssm-ID: 143639  Cd Length: 40  Bit Score: 87.22  E-value: 1.86e-21
                        10        20        30        40
                ....*....|....*....|....*....|....*....|
gi 27734192  14 VTFRDVAVSFSQDEWLHLDPAQRTLYREVMLENYSNLVSL 53
Cdd:cd07765   1 VTFEDVAVYFSQEEWELLDPAQRDLYRDVMLENYENLVSL 40
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
205-558 1.67e-16

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 82.05  E-value: 1.67e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27734192 205 KCNICGKVFFHSSSLSKHQRTHTGEKLYKC--QGCRKAFSQRSSLAQHLRVHTGEKPYLCSD----------------CG 266
Cdd:COG5048  35 SCPNCTDSFSRLEHLTRHIRSHTGEKPSQCsySGCDKSFSRPLELSRHLRTHHNNPSDLNSKslplsnskasssslssSS 114
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27734192 267 KAFSFTTSL---------------IGHQRMHTGERPYE-CKECGKTFKGSSSLH-------------------NHQRIHT 311
Cdd:COG5048 115 SNSNDNNLLsshslppssrdpqlpDLLSISNLRNNPLPgNNSSSVNTPQSNSLHpplpanslskdpssnlsllISSNVST 194
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27734192 312 GEKPYKCNECGRAFSQCSSLIQHHRIHTGEKPYECSQCGKAFTSISRLSRH------HRVHTGEKPFHCNVCGKVFSYHS 385
Cdd:COG5048 195 SIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQSPsslsssDSSSSASESPRSSLPTASSQSSS 274
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27734192 386 ALTIHQRTHTG-EKPYACKECGKAFSQSSALTQHQR--IHTGE--KPYKCAE--CGKAFSWLSRLNIHHRIHTGEKPYHC 458
Cdd:COG5048 275 PNESDSSSEKGfSLPIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCPYslCGKLFSRNDALKRHILLHTSISPAKE 354
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27734192 459 KECGKAFSSHSAVNT-------HRKIHTGEKPYKCSD--CEKAFNQSSALIQHQRIHTGEKP--FNCKVCGKAFRQSSSL 527
Cdd:COG5048 355 KLLNSSSKFSPLLNNeppqslqQYKDLKNDKKSETLSnsCIRNFKRDSNLSLHIITHLSFRPynCKNPPCSKSFNRHYNL 434
                       410       420       430
                ....*....|....*....|....*....|.
gi 27734192 528 MTHMRIHTGERPYRCEACGKaFSQSSSLANH 558
Cdd:COG5048 435 IPHKKIHTNHAPLLCSILKS-FRRDLDLSNH 464
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
216-562 2.57e-13

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 72.42  E-value: 2.57e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27734192 216 SSSLSKHQRTHTGE----KLYKCQGCRKAFSQRSSLAQHLRVHTGEKPYLCSDCGKAFSFTTSLIG--HQRMHTGERPYE 289
Cdd:COG5048  14 SVLSSTPKSTLKSLsnapRPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYSGCDKSFSRPLELsrHLRTHHNNPSDL 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27734192 290 C--KECGKTFKGSSSLHNHQrIHTGEKPYKCNECGRAFSQCSSLIQHHRIHTGEKPYECSQC-GKAFTSISRLSRHHRVH 366
Cdd:COG5048  94 NskSLPLSNSKASSSSLSSS-SSNSNDNNLLSSHSLPPSSRDPQLPDLLSISNLRNNPLPGNnSSSVNTPQSNSLHPPLP 172
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27734192 367 TgekpfhcNVCGKVFSYHSALTIHQRTHTGEKPYACKECGKAFSQSSALTQHQRIHTGEKPYKCAECGKAFSWLSRLNIH 446
Cdd:COG5048 173 A-------NSLSKDPSSNLSLLISSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQSP 245
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27734192 447 HRIHTGEKPYHCKECGKAFSSHSAVNTHRKIHTGE-------KPYKCSDCEKAFNQSSALIQHQR--IHTGE--KPFNCK 515
Cdd:COG5048 246 SSLSSSDSSSSASESPRSSLPTASSQSSSPNESDSssekgfsLPIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCP 325
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|.
gi 27734192 516 V--CGKAFRQSSSLMTHMRIHTGERPYRC--EACGKAFSQSSSLANHQKTH 562
Cdd:COG5048 326 YslCGKLFSRNDALKRHILLHTSISPAKEklLNSSSKFSPLLNNEPPQSLQ 376
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
286-563 3.37e-10

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 62.41  E-value: 3.37e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27734192 286 RPYECKECGKTFKGSSSLHNHQRIHTGEKPYKCNECGRA--FSQCSSLIQHHRIHTGEKPYECSQCGKAFTSISRLSRHH 363
Cdd:COG5048  32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYSGCDksFSRPLELSRHLRTHHNNPSDLNSKSLPLSNSKASSSSLS 111
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27734192 364 RVHTGE-KPFHCNVCGKVFSYHSALTI--HQRTHTGEKP-YACKECGKAFSQSS-------------------ALTQHQR 420
Cdd:COG5048 112 SSSSNSnDNNLLSSHSLPPSSRDPQLPdlLSISNLRNNPlPGNNSSSVNTPQSNslhpplpanslskdpssnlSLLISSN 191
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27734192 421 IHTGEKPYKCAECGKAFSWLSRLNIHHRIHTGEKPYHCKECGKAFSSHSAVNTHRKIHTGEKPYKCSDCEKAFNQSSALI 500
Cdd:COG5048 192 VSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLSSSDSSSSASESPRSSLPTASSQ 271
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 27734192 501 QHQRIHTGE-------KPFNCKVCGKAFRQSSSLMTHMR--IHTGE--RPYRC--EACGKAFSQSSSLANHQKTHY 563
Cdd:COG5048 272 SSSPNESDSssekgfsLPIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCpySLCGKLFSRNDALKRHILLHT 347
zf-H2C2_2 pfam13465
Zinc-finger double domain;
526-551 4.27e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 40.43  E-value: 4.27e-05
                          10        20
                  ....*....|....*....|....*.
gi 27734192   526 SLMTHMRIHTGERPYRCEACGKAFSQ 551
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
300-475 6.20e-05

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 45.84  E-value: 6.20e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27734192 300 SSSLHNHQRIHTGE-----KPYKCNECGRAFSQCSSLIQH--HRIHTGE--KPYEC--SQCGKAFTSISRLSRHHRVHTG 368
Cdd:COG5048 269 SSQSSSPNESDSSSekgfsLPIKSKQCNISFSRSSPLTRHlrSVNHSGEslKPFSCpySLCGKLFSRNDALKRHILLHTS 348
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27734192 369 EKPFHC--NVCGKVFS-----YHSALTIHQRTHTGEKPYAC--KECGKAFSQSSALTQHQRIHTGEKP--YKCAECGKAF 437
Cdd:COG5048 349 ISPAKEklLNSSSKFSpllnnEPPQSLQQYKDLKNDKKSETlsNSCIRNFKRDSNLSLHIITHLSFRPynCKNPPCSKSF 428
                       170       180       190
                ....*....|....*....|....*....|....*...
gi 27734192 438 SWLSRLNIHHRIHTGEKPYHCKECGKAFSSHSAVNTHR 475
Cdd:COG5048 429 NRHYNLIPHKKIHTNHAPLLCSILKSFRRDLDLSNHGK 466
SFP1 COG5189
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ...
480-563 1.28e-04

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


Pssm-ID: 227516 [Multi-domain]  Cd Length: 423  Bit Score: 44.71  E-value: 1.28e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27734192 480 GEKPYKCS--DCEKAFNQSSALIQHqRIHTGekpfnckvCGKAFRQSSSLMTHMRIHTGERPYRCEACGKAFSQSSSLAN 557
Cdd:COG5189 346 DGKPYKCPveGCNKKYKNQNGLKYH-MLHGH--------QNQKLHENPSPEKMNIFSAKDKPYRCEVCDKRYKNLNGLKY 416

                ....*.
gi 27734192 558 HqKTHY 563
Cdd:COG5189 417 H-RKHS 421
zf-H2C2_2 pfam13465
Zinc-finger double domain;
414-438 1.34e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 39.28  E-value: 1.34e-04
                          10        20
                  ....*....|....*....|....*
gi 27734192   414 ALTQHQRIHTGEKPYKCAECGKAFS 438
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFK 25
SUF4-like cd20908
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
482-531 2.66e-04

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


Pssm-ID: 411020 [Multi-domain]  Cd Length: 82  Bit Score: 39.85  E-value: 2.66e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 27734192 482 KPYkCSDCEKAFNQSSALIQHQRIHTgekpFNCKVCGKAFRQSSSLMTHM 531
Cdd:cd20908   1 KPW-CYYCDREFDDEKILIQHQKAKH----FKCHICHKKLYTAGGLAVHC 45
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
287-446 3.19e-04

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 43.53  E-value: 3.19e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27734192 287 PYECKECGKTFKGSSSLHNHQR--IHTGE--KPYKCNE--CGRAFSQCSSLIQHHRIHTGEKPYEC--SQCGKAFTSIS- 357
Cdd:COG5048 289 PIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCPYslCGKLFSRNDALKRHILLHTSISPAKEklLNSSSKFSPLLn 368
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27734192 358 ---RLSRHHRVH-TGEKPFHCNV--CGKVFSYHSALTIHQRTHTGEKPYACK--ECGKAFSQSSALTQHQRIHTGEKPYK 429
Cdd:COG5048 369 nepPQSLQQYKDlKNDKKSETLSnsCIRNFKRDSNLSLHIITHLSFRPYNCKnpPCSKSFNRHYNLIPHKKIHTNHAPLL 448
                       170
                ....*....|....*..
gi 27734192 430 CAECGKAFSWLSRLNIH 446
Cdd:COG5048 449 CSILKSFRRDLDLSNHG 465
zf-H2C2_2 pfam13465
Zinc-finger double domain;
498-523 3.28e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.12  E-value: 3.28e-04
                          10        20
                  ....*....|....*....|....*.
gi 27734192   498 ALIQHQRIHTGEKPFNCKVCGKAFRQ 523
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
386-411 3.38e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.12  E-value: 3.38e-04
                          10        20
                  ....*....|....*....|....*.
gi 27734192   386 ALTIHQRTHTGEKPYACKECGKAFSQ 411
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
330-355 3.69e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 37.74  E-value: 3.69e-04
                          10        20
                  ....*....|....*....|....*.
gi 27734192   330 SLIQHHRIHTGEKPYECSQCGKAFTS 355
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
SUF4-like cd20908
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
286-334 3.90e-04

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


Pssm-ID: 411020 [Multi-domain]  Cd Length: 82  Bit Score: 39.46  E-value: 3.90e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*....
gi 27734192 286 RPYeCKECGKTFKGSSSLHNHQRIHTgekpYKCNECGRAFSQCSSLIQH 334
Cdd:cd20908   1 KPW-CYYCDREFDDEKILIQHQKAKH----FKCHICHKKLYTAGGLAVH 44
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
204-365 4.33e-04

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 43.15  E-value: 4.33e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27734192 204 CKCNICGKVFFHSSSLSKHQRT--HTGEKLYKCQ----GCRKAFSQRSSLAQHLRVHTGEKPYLCSDCGKAFSFTTSLIG 277
Cdd:COG5048 290 IKSKQCNISFSRSSPLTRHLRSvnHSGESLKPFScpysLCGKLFSRNDALKRHILLHTSISPAKEKLLNSSSKFSPLLNN 369
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27734192 278 --HQRMH-----TGERPYEC--KECGKTFKGSS--SLHNHQRIHTGEKPYKCNECGRAFSQCSSLIQHHRIHTGEKPYEC 346
Cdd:COG5048 370 epPQSLQqykdlKNDKKSETlsNSCIRNFKRDSnlSLHIITHLSFRPYNCKNPPCSKSFNRHYNLIPHKKIHTNHAPLLC 449
                       170
                ....*....|....*....
gi 27734192 347 SQCGKaFTSISRLSRHHRV 365
Cdd:COG5048 450 SILKS-FRRDLDLSNHGKD 467
zf-H2C2_2 pfam13465
Zinc-finger double domain;
442-467 4.58e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 37.74  E-value: 4.58e-04
                          10        20
                  ....*....|....*....|....*.
gi 27734192   442 RLNIHHRIHTGEKPYHCKECGKAFSS 467
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
SFP1 COG5189
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ...
284-367 6.46e-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: 6.46e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27734192 284 GERPYECK--ECGKTFKGSSSL-----HNHQRIHTGEKPykcnecgrafsqcsSLIQHHRIHTGEKPYECSQCGKAFTSI 356
Cdd:COG5189 346 DGKPYKCPveGCNKKYKNQNGLkyhmlHGHQNQKLHENP--------------SPEKMNIFSAKDKPYRCEVCDKRYKNL 411
                        90
                ....*....|.
gi 27734192 357 SRLsRHHRVHT 367
Cdd:COG5189 412 NGL-KYHRKHS 421
zf-H2C2_2 pfam13465
Zinc-finger double domain;
358-383 7.71e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.97  E-value: 7.71e-04
                          10        20
                  ....*....|....*....|....*.
gi 27734192   358 RLSRHHRVHTGEKPFHCNVCGKVFSY 383
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
306-327 9.66e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.58  E-value: 9.66e-04
                          10        20
                  ....*....|....*....|..
gi 27734192   306 HQRIHTGEKPYKCNECGRAFSQ 327
Cdd:pfam13465   5 HMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
278-298 1.20e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.58  E-value: 1.20e-03
                          10        20
                  ....*....|....*....|.
gi 27734192   278 HQRMHTGERPYECKECGKTFK 298
Cdd:pfam13465   5 HMRTHTGEKPYKCPECGKSFK 25
PHA00733 PHA00733
hypothetical protein
483-531 1.21e-03

hypothetical protein


Pssm-ID: 177301  Cd Length: 128  Bit Score: 39.09  E-value: 1.21e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 27734192  483 PYKCSDCEKAFNQSSALIQHQRIHTGEKpfNCKVCGKAFRQSSSLMTHM 531
Cdd:PHA00733  73 PYVCPLCLMPFSSSVSLKQHIRYTEHSK--VCPVCGKEFRNTDSTLDHV 119
zf-H2C2_2 pfam13465
Zinc-finger double domain;
246-270 1.30e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.20  E-value: 1.30e-03
                          10        20
                  ....*....|....*....|....*
gi 27734192   246 SLAQHLRVHTGEKPYLCSDCGKAFS 270
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFK 25
SFP1 COG5189
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ...
228-306 1.42e-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: 1.42e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27734192 228 GEKLYKCQ--GCRKAFSQRSSLAQHlRVHtgekpylcSDCGKAFSFTTSLIGHQRMHTGERPYECKECGKTFKGSSSLHN 305
Cdd:COG5189 346 DGKPYKCPveGCNKKYKNQNGLKYH-MLH--------GHQNQKLHENPSPEKMNIFSAKDKPYRCEVCDKRYKNLNGLKY 416

                .
gi 27734192 306 H 306
Cdd:COG5189 417 H 417
zf-H2C2_2 pfam13465
Zinc-finger double domain;
470-495 1.79e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.81  E-value: 1.79e-03
                          10        20
                  ....*....|....*....|....*.
gi 27734192   470 AVNTHRKIHTGEKPYKCSDCEKAFNQ 495
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
512-534 2.89e-03

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


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 35.35  E-value: 2.89e-03
                          10        20
                  ....*....|....*....|...
gi 27734192   512 FNCKVCGKAFRQSSSLMTHMRIH 534
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
400-422 4.67e-03

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


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 34.58  E-value: 4.67e-03
                          10        20
                  ....*....|....*....|...
gi 27734192   400 YACKECGKAFSQSSALTQHQRIH 422
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
204-226 5.26e-03

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


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 34.58  E-value: 5.26e-03
                          10        20
                  ....*....|....*....|...
gi 27734192   204 CKCNICGKVFFHSSSLSKHQRTH 226
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
218-243 5.34e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 34.65  E-value: 5.34e-03
                          10        20
                  ....*....|....*....|....*.
gi 27734192   218 SLSKHQRTHTGEKLYKCQGCRKAFSQ 243
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
288-310 5.97e-03

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


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 34.58  E-value: 5.97e-03
                          10        20
                  ....*....|....*....|...
gi 27734192   288 YECKECGKTFKGSSSLHNHQRIH 310
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
372-394 7.34e-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: 7.34e-03
                          10        20
                  ....*....|....*....|...
gi 27734192   372 FHCNVCGKVFSYHSALTIHQRTH 394
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
316-338 8.94e-03

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


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 33.81  E-value: 8.94e-03
                          10        20
                  ....*....|....*....|...
gi 27734192   316 YKCNECGRAFSQCSSLIQHHRIH 338
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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