NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1800417208|ref|NP_001364958|]
View 

zinc finger protein 34 isoform 4 [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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
KRAB smart00349
krueppel associated box;
14-80 2.34e-22

krueppel associated box;


:

Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 89.96  E-value: 2.34e-22
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1800417208   14 VTFEDVAVYLSREEWGRLGPAQRGLYRDVMLETYGNLVSLALGTRTEYkELTSQEtfgeedpQGSEP 80
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQVPKPD-LISQLE-------QGEEP 59
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
127-493 1.13e-13

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


:

Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 73.19  E-value: 1.13e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800417208 127 PVPDQRPHKCDICEQSFEQRSYLNNHKRVHRSKKTNTVRNSG--EIFSANLVVKEDQKIPTGKKLHYCSYCGKTFRYSAN 204
Cdd:COG5048    27 LSNAPRPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYSGcdKSFSRPLELSRHLRTHHNNPSDLNSKSLPLSNSKAS 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800417208 205 LVKHQRLHTEE-KPYKCDECGKAFSQSCEFINHRRMHSGEIPYRCDECGKTFTRRPN----------------------L 261
Cdd:COG5048   107 SSSLSSSSSNSnDNNLLSSHSLPPSSRDPQLPDLLSISNLRNNPLPGNNSSSVNTPQsnslhpplpanslskdpssnlsL 186

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800417208 262 MKHQRIHTGEKPYKCGECGKHFSAYSSLIYHQRIHTGEKPYKCNDCGKAFSDGSILIRHRRTHTGEKPFECKECGKGFTQ 341
Cdd:COG5048   187 LISSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLSSSDSSSSASESPRSSLP 266

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800417208 342 SSNLIQHQRIHTGE-------KPYKCNECEKAFIQKTKLVEHQRS--HTGE--KPYEC--NDCGKVFSQSTHLIQHQRIH 408
Cdd:COG5048   267 TASSQSSSPNESDSssekgfsLPIKSKQCNISFSRSSPLTRHLRSvnHSGEslKPFSCpySLCGKLFSRNDALKRHILLH 346

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800417208 409 TGEKPYKCSEC-------GKAFHNSSRLIHHQRLHHGEKPYRCSD--CKKAFSQSTYLIQHRRIHTGEKP--YKCSECGK 477
Cdd:COG5048   347 TSISPAKEKLLnssskfsPLLNNEPPQSLQQYKDLKNDKKSETLSnsCIRNFKRDSNLSLHIITHLSFRPynCKNPPCSK 426

                         410
                  ....*....|....*.
gi 1800417208 478 AFRHSSNMCQHQRIHL 493
Cdd:COG5048   427 SFNRHYNLIPHKKIHT 442
 
Name Accession Description Interval E-value
KRAB smart00349
krueppel associated box;
14-80 2.34e-22

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 89.96  E-value: 2.34e-22
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1800417208   14 VTFEDVAVYLSREEWGRLGPAQRGLYRDVMLETYGNLVSLALGTRTEYkELTSQEtfgeedpQGSEP 80
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQVPKPD-LISQLE-------QGEEP 59
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
 14-53 2.57e-21

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


Pssm-ID: 460171  Cd Length: 42  Bit Score: 86.76  E-value: 2.57e-21
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1800417208  14 VTFEDVAVYLSREEWGRLGPAQRGLYRDVMLETYGNLVSL 53
Cdd:pfam01352   2 VTFEDVAVDFTQEEWALLDPAQRNLYRDVMLENYRNLVSL 41
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
 14-53 3.14e-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: 86.45  E-value: 3.14e-21
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1800417208  14 VTFEDVAVYLSREEWGRLGPAQRGLYRDVMLETYGNLVSL 53
Cdd:cd07765     1 VTFEDVAVYFSQEEWELLDPAQRDLYRDVMLENYENLVSL 40
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
127-493 1.13e-13

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 73.19  E-value: 1.13e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800417208 127 PVPDQRPHKCDICEQSFEQRSYLNNHKRVHRSKKTNTVRNSG--EIFSANLVVKEDQKIPTGKKLHYCSYCGKTFRYSAN 204
Cdd:COG5048    27 LSNAPRPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYSGcdKSFSRPLELSRHLRTHHNNPSDLNSKSLPLSNSKAS 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800417208 205 LVKHQRLHTEE-KPYKCDECGKAFSQSCEFINHRRMHSGEIPYRCDECGKTFTRRPN----------------------L 261
Cdd:COG5048   107 SSSLSSSSSNSnDNNLLSSHSLPPSSRDPQLPDLLSISNLRNNPLPGNNSSSVNTPQsnslhpplpanslskdpssnlsL 186

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800417208 262 MKHQRIHTGEKPYKCGECGKHFSAYSSLIYHQRIHTGEKPYKCNDCGKAFSDGSILIRHRRTHTGEKPFECKECGKGFTQ 341
Cdd:COG5048   187 LISSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLSSSDSSSSASESPRSSLP 266

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800417208 342 SSNLIQHQRIHTGE-------KPYKCNECEKAFIQKTKLVEHQRS--HTGE--KPYEC--NDCGKVFSQSTHLIQHQRIH 408
Cdd:COG5048   267 TASSQSSSPNESDSssekgfsLPIKSKQCNISFSRSSPLTRHLRSvnHSGEslKPFSCpySLCGKLFSRNDALKRHILLH 346

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800417208 409 TGEKPYKCSEC-------GKAFHNSSRLIHHQRLHHGEKPYRCSD--CKKAFSQSTYLIQHRRIHTGEKP--YKCSECGK 477
Cdd:COG5048   347 TSISPAKEKLLnssskfsPLLNNEPPQSLQQYKDLKNDKKSETLSnsCIRNFKRDSNLSLHIITHLSFRPynCKNPPCSK 426

                         410
                  ....*....|....*.
gi 1800417208 478 AFRHSSNMCQHQRIHL 493
Cdd:COG5048   427 SFNRHYNLIPHKKIHT 442
zf-H2C2_2 pfam13465
Zinc-finger double domain;
344-369 1.12e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 39.28  E-value: 1.12e-04
                          10        20
                  ....*....|....*....|....*.
gi 1800417208 344 NLIQHQRIHTGEKPYKCNECEKAFIQ 369
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
SUF4-like cd20908
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
 384-437 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: 39.08  E-value: 3.90e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1800417208 384 KPYeCNDCGKVFSQSTHLIQHQRIHTgekpYKCSECGKAFHNSSRL-IHHQRLHH 437
Cdd:cd20908     1 KPW-CYYCDREFDDEKILIQHQKAKH----FKCHICHKKLYTAGGLaVHCLQVHK 50
 
Name Accession Description Interval E-value
KRAB smart00349
krueppel associated box;
14-80 2.34e-22

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 89.96  E-value: 2.34e-22
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1800417208   14 VTFEDVAVYLSREEWGRLGPAQRGLYRDVMLETYGNLVSLALGTRTEYkELTSQEtfgeedpQGSEP 80
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQVPKPD-LISQLE-------QGEEP 59
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
 14-53 2.57e-21

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


Pssm-ID: 460171  Cd Length: 42  Bit Score: 86.76  E-value: 2.57e-21
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1800417208  14 VTFEDVAVYLSREEWGRLGPAQRGLYRDVMLETYGNLVSL 53
Cdd:pfam01352   2 VTFEDVAVDFTQEEWALLDPAQRNLYRDVMLENYRNLVSL 41
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
 14-53 3.14e-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: 86.45  E-value: 3.14e-21
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1800417208  14 VTFEDVAVYLSREEWGRLGPAQRGLYRDVMLETYGNLVSL 53
Cdd:cd07765     1 VTFEDVAVYFSQEEWELLDPAQRDLYRDVMLENYENLVSL 40
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
127-493 1.13e-13

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 73.19  E-value: 1.13e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800417208 127 PVPDQRPHKCDICEQSFEQRSYLNNHKRVHRSKKTNTVRNSG--EIFSANLVVKEDQKIPTGKKLHYCSYCGKTFRYSAN 204
Cdd:COG5048    27 LSNAPRPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYSGcdKSFSRPLELSRHLRTHHNNPSDLNSKSLPLSNSKAS 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800417208 205 LVKHQRLHTEE-KPYKCDECGKAFSQSCEFINHRRMHSGEIPYRCDECGKTFTRRPN----------------------L 261
Cdd:COG5048   107 SSSLSSSSSNSnDNNLLSSHSLPPSSRDPQLPDLLSISNLRNNPLPGNNSSSVNTPQsnslhpplpanslskdpssnlsL 186

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800417208 262 MKHQRIHTGEKPYKCGECGKHFSAYSSLIYHQRIHTGEKPYKCNDCGKAFSDGSILIRHRRTHTGEKPFECKECGKGFTQ 341
Cdd:COG5048   187 LISSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLSSSDSSSSASESPRSSLP 266

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800417208 342 SSNLIQHQRIHTGE-------KPYKCNECEKAFIQKTKLVEHQRS--HTGE--KPYEC--NDCGKVFSQSTHLIQHQRIH 408
Cdd:COG5048   267 TASSQSSSPNESDSssekgfsLPIKSKQCNISFSRSSPLTRHLRSvnHSGEslKPFSCpySLCGKLFSRNDALKRHILLH 346

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800417208 409 TGEKPYKCSEC-------GKAFHNSSRLIHHQRLHHGEKPYRCSD--CKKAFSQSTYLIQHRRIHTGEKP--YKCSECGK 477
Cdd:COG5048   347 TSISPAKEKLLnssskfsPLLNNEPPQSLQQYKDLKNDKKSETLSnsCIRNFKRDSNLSLHIITHLSFRPynCKNPPCSK 426

                         410
                  ....*....|....*.
gi 1800417208 478 AFRHSSNMCQHQRIHL 493
Cdd:COG5048   427 SFNRHYNLIPHKKIHT 442
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
300-456 1.83e-09

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 59.71  E-value: 1.83e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800417208 300 KPYKCNDCGKAFSDGSILIRHRRT--HTGE--KPFECKE--CGKGFTQSSNLIQHQRIHTGEKPYKC--NECEKAFIQK- 370
Cdd:COG5048   288 LPIKSKQCNISFSRSSPLTRHLRSvnHSGEslKPFSCPYslCGKLFSRNDALKRHILLHTSISPAKEklLNSSSKFSPLl 367

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800417208 371 ----TKLVEHQRSHTGEKPYEC--NDCGKVFSQ----STHLIQH--QRIHtgekPYKCSECGKAFHNSSRLIHHQRLHHG 438
Cdd:COG5048   368 nnepPQSLQQYKDLKNDKKSETlsNSCIRNFKRdsnlSLHIITHlsFRPY----NCKNPPCSKSFNRHYNLIPHKKIHTN 443

                         170
                  ....*....|....*...
gi 1800417208 439 EKPYRCSDCKKAFSQSTY 456
Cdd:COG5048   444 HAPLLCSILKSFRRDLDL 461
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
245-499 1.50e-06

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 50.46  E-value: 1.50e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800417208 245 PYRCDECGKTFTRRPNLMKHQRIHTGEKPYKCG--ECGKHFSAYSSLIYHQRIHTGEKPYKCNDCG-------------- 308
Cdd:COG5048    33 PDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSysGCDKSFSRPLELSRHLRTHHNNPSDLNSKSLplsnskasssslss 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800417208 309 -----------------------------------------------------------------KAFSDGSILIRHRRT 323
Cdd:COG5048   113 sssnsndnnllsshslppssrdpqlpdllsisnlrnnplpgnnsssvntpqsnslhpplpanslsKDPSSNLSLLISSNV 192

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800417208 324 HTGEKPFECKECGKGFTQSSNLIQHQRIHTGEKPYKCNECekAFIQKTKLVEHQRSHTGEK--PYECNDCGKVFSQSTHL 401
Cdd:COG5048   193 STSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTN--SQLSPKSLLSQSPSSLSSSdsSSSASESPRSSLPTASS 270

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800417208 402 IQHQRIHTGE-------KPYKCSECGKAFHNSSRLIHHQR--LHHGE--KPYRC--SDCKKAFSQSTYLIQHRRIHTGEK 468
Cdd:COG5048   271 QSSSPNESDSssekgfsLPIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCpySLCGKLFSRNDALKRHILLHTSIS 350

                         330       340       350
                  ....*....|....*....|....*....|...
gi 1800417208 469 PYKC--SECGKAFRHSSNMCQHQRIHLREDFSM 499
Cdd:COG5048   351 PAKEklLNSSSKFSPLLNNEPPQSLQQYKDLKN 383
zf-H2C2_2 pfam13465
Zinc-finger double domain;
344-369 1.12e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 39.28  E-value: 1.12e-04
                          10        20
                  ....*....|....*....|....*.
gi 1800417208 344 NLIQHQRIHTGEKPYKCNECEKAFIQ 369
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
400-423 1.56e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.89  E-value: 1.56e-04
                          10        20
                  ....*....|....*....|....
gi 1800417208 400 HLIQHQRIHTGEKPYKCSECGKAF 423
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSF 24
zf-H2C2_2 pfam13465
Zinc-finger double domain;
456-481 1.89e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.51  E-value: 1.89e-04
                          10        20
                  ....*....|....*....|....*.
gi 1800417208 456 YLIQHRRIHTGEKPYKCSECGKAFRH 481
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
260-284 2.31e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.12  E-value: 2.31e-04
                          10        20
                  ....*....|....*....|....*
gi 1800417208 260 NLMKHQRIHTGEKPYKCGECGKHFS 284
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFK 25
zf-H2C2_2 pfam13465
Zinc-finger double domain;
317-341 2.47e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.12  E-value: 2.47e-04
                          10        20
                  ....*....|....*....|....*
gi 1800417208 317 LIRHRRTHTGEKPFECKECGKGFTQ 341
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
204-229 2.78e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.12  E-value: 2.78e-04
                          10        20
                  ....*....|....*....|....*.
gi 1800417208 204 NLVKHQRLHTEEKPYKCDECGKAFSQ 229
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
SUF4-like cd20908
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
 384-437 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: 39.08  E-value: 3.90e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1800417208 384 KPYeCNDCGKVFSQSTHLIQHQRIHTgekpYKCSECGKAFHNSSRL-IHHQRLHH 437
Cdd:cd20908     1 KPW-CYYCDREFDDEKILIQHQKAKH----FKCHICHKKLYTAGGLaVHCLQVHK 50
zf-H2C2_2 pfam13465
Zinc-finger double domain;
288-312 6.15e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.97  E-value: 6.15e-04
                          10        20
                  ....*....|....*....|....*
gi 1800417208 288 SLIYHQRIHTGEKPYKCNDCGKAFS 312
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFK 25
SFP1 COG5189
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ...
 354-437 7.15e-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: 7.15e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800417208 354 GEKPYKCN--ECEKAF-----IQKTKLVEHQRSHTGEKPYEcndcgkvfsqsthlIQHQRIHTGEKPYKCSECGKAFHNS 426
Cdd:COG5189   346 DGKPYKCPveGCNKKYknqngLKYHMLHGHQNQKLHENPSP--------------EKMNIFSAKDKPYRCEVCDKRYKNL 411

                          90
                  ....*....|.
gi 1800417208 427 SRLIHHQRLHH 437
Cdd:COG5189   412 NGLKYHRKHSH 422
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 246-268 1.02e-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: 36.51  E-value: 1.02e-03
                          10        20
                  ....*....|....*....|...
gi 1800417208 246 YRCDECGKTFTRRPNLMKHQRIH 268
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
373-397 1.02e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.58  E-value: 1.02e-03
                          10        20
                  ....*....|....*....|....*
gi 1800417208 373 LVEHQRSHTGEKPYECNDCGKVFSQ 397
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 26
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
340-428 1.18e-03

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 41.22  E-value: 1.18e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800417208 340 TQSSNLIQHQRIHTGE----KPYKCNECEKAFIQKTKLVEHQRSHTGEKPYECND--CGKVFSQSTHLIQHQRIHTGEKP 413
Cdd:COG5048    12 NNSVLSSTPKSTLKSLsnapRPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYsgCDKSFSRPLELSRHLRTHHNNPS 91

                          90
                  ....*....|....*
gi 1800417208 414 YKCSECGKAFHNSSR 428
Cdd:COG5048    92 DLNSKSLPLSNSKAS 106
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 386-408 1.34e-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: 36.12  E-value: 1.34e-03
                          10        20
                  ....*....|....*....|...
gi 1800417208 386 YECNDCGKVFSQSTHLIQHQRIH 408
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 330-352 1.80e-03

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


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 35.74  E-value: 1.80e-03
                          10        20
                  ....*....|....*....|...
gi 1800417208 330 FECKECGKGFTQSSNLIQHQRIH 352
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
SFP1 COG5189
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ...
 214-292 2.09e-03

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


Pssm-ID: 227516 [Multi-domain]  Cd Length: 423  Bit Score: 40.47  E-value: 2.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800417208 214 EEKPYKCD--ECGKAFSQSCEFINHRrMHSgeipyrcdECGKTFTRRPNLMKHQRIHTGEKPYKCGECGKHFSAYSSLIY 291
Cdd:COG5189   346 DGKPYKCPveGCNKKYKNQNGLKYHM-LHG--------HQNQKLHENPSPEKMNIFSAKDKPYRCEVCDKRYKNLNGLKY 416


                  .
gi 1800417208 292 H 292
Cdd:COG5189   417 H 417
SFP1 COG5189
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ...
 410-488 3.23e-03

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


Pssm-ID: 227516 [Multi-domain]  Cd Length: 423  Bit Score: 40.09  E-value: 3.23e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800417208 410 GEKPYKCS--ECGKAFHNSSRLIHHQRLHHgekpyrcsdCKKAFSQSTYLIQHRRIHTGEKPYKCSECGKAFRHSSNMCQ 487
Cdd:COG5189   346 DGKPYKCPveGCNKKYKNQNGLKYHMLHGH---------QNQKLHENPSPEKMNIFSAKDKPYRCEVCDKRYKNLNGLKY 416


                  .
gi 1800417208 488 H 488
Cdd:COG5189   417 H 417
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 470-492 3.28e-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: 3.28e-03
                          10        20
                  ....*....|....*....|...
gi 1800417208 470 YKCSECGKAFRHSSNMCQHQRIH 492
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
193-316 5.73e-03

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 39.29  E-value: 5.73e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800417208 193 SYCGKTFRYSANLVKHQRLHTEEKPYKC--DECGKAFSQ-----SCEFINHRRMHSGEIPYRCD--ECGKTFTRRPNLMK 263
Cdd:COG5048   327 SLCGKLFSRNDALKRHILLHTSISPAKEklLNSSSKFSPllnnePPQSLQQYKDLKNDKKSETLsnSCIRNFKRDSNLSL 406

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1800417208 264 HQRIHTGEKP--YKCGECGKHFSAYSSLIYHQRIHTGEKPYKCNDCGKAFSDGSI 316
Cdd:COG5048   407 HIITHLSFRPynCKNPPCSKSFNRHYNLIPHKKIHTNHAPLLCSILKSFRRDLDL 461
zf-H2C2_2 pfam13465
Zinc-finger double domain;
432-453 6.75e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 34.27  E-value: 6.75e-03
                          10        20
                  ....*....|....*....|..
gi 1800417208 432 HQRLHHGEKPYRCSDCKKAFSQ 453
Cdd:pfam13465   5 HMRTHTGEKPYKCPECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 190-212 9.39e-03

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


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 33.81  E-value: 9.39e-03
                          10        20
                  ....*....|....*....|...
gi 1800417208 190 HYCSYCGKTFRYSANLVKHQRLH 212
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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