NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1720384203|ref|XP_030104411|]
View 

zinc finger protein 250 isoform X1 [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

 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;
17-77 9.11e-30

krueppel associated box;


:

Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 111.15  E-value: 9.11e-30
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720384203   17 VTFEDVAVLLSQEEWARLGPAQRGLYRHVMMETYGNVVSLGLPGSKPVVISQLERGEDPWV 77
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQVPKPDLISQLEQGEEPWI 61
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
172-512 3.08e-14

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


:

Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 75.12  E-value: 3.08e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720384203 172 RPYICIECGKCFGRSSHLLQHQRIHTGEKPYVCHV--CGKAFSQSSVLSKHRRIHTGEKPYEC----------------N 233
Cdd:COG5048    32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYsgCDKSFSRPLELSRHLRTHHNNPSDLNskslplsnskasssslS 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720384203 234 ECGKAFRVSSDLAQHHKIHTGEKP----------------HECLECGKAFTQ-LSHLIQHQRIHTGERPYVCPLCGKAFN 296
Cdd:COG5048   112 SSSSNSNDNNLLSSHSLPPSSRDPqlpdllsisnlrnnplPGNNSSSVNTPQsNSLHPPLPANSLSKDPSSNLSLLISSN 191

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720384203 297 HSTVLRSHQ----RVHTGEKPHGCSECGK------------TFSVKRTLLQHQRVHTGEK--PYTCSECGKAFSDRSVLI 358
Cdd:COG5048   192 VSTSIPSSSenspLSSSYSIPSSSSDQNLensssslplttnSQLSPKSLLSQSPSSLSSSdsSSSASESPRSSLPTASSQ 271

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720384203 359 QHHNVHTGE-------KPYECSECGKTFSHRSTLMNHER--IHTQE--KPYACYE--CGKAFVQHSHLIQHQRVHTGEKP 425
Cdd:COG5048   272 SSSPNESDSssekgfsLPIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCPYslCGKLFSRNDALKRHILLHTSISP 351

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720384203 426 YVC--GECGHAFS-----ARRSLIQHERIHTGEKPFQCT--ECGKAFSLKATLIVHLRTHTGEKPYECNS--CGKAFSQY 494
Cdd:COG5048   352 AKEklLNSSSKFSpllnnEPPQSLQQYKDLKNDKKSETLsnSCIRNFKRDSNLSLHIITHLSFRPYNCKNppCSKSFNRH 431

                         410
                  ....*....|....*...
gi 1720384203 495 SVLIQHQRIHTGEKPYEC 512
Cdd:COG5048   432 YNLIPHKKIHTNHAPLLC 449
 
Name Accession Description Interval E-value
KRAB smart00349
krueppel associated box;
17-77 9.11e-30

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 111.15  E-value: 9.11e-30
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720384203   17 VTFEDVAVLLSQEEWARLGPAQRGLYRHVMMETYGNVVSLGLPGSKPVVISQLERGEDPWV 77
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQVPKPDLISQLEQGEEPWI 61
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
 17-57 1.07e-19

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: 82.13  E-value: 1.07e-19
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1720384203  17 VTFEDVAVLLSQEEWARLGPAQRGLYRHVMMETYGNVVSLG 57
Cdd:pfam01352   2 VTFEDVAVDFTQEEWALLDPAQRNLYRDVMLENYRNLVSLG 42
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
 17-56 1.34e-18

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


Pssm-ID: 143639  Cd Length: 40  Bit Score: 79.13  E-value: 1.34e-18
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1720384203  17 VTFEDVAVLLSQEEWARLGPAQRGLYRHVMMETYGNVVSL 56
Cdd:cd07765     1 VTFEDVAVYFSQEEWELLDPAQRDLYRDVMLENYENLVSL 40
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
172-512 3.08e-14

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 75.12  E-value: 3.08e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720384203 172 RPYICIECGKCFGRSSHLLQHQRIHTGEKPYVCHV--CGKAFSQSSVLSKHRRIHTGEKPYEC----------------N 233
Cdd:COG5048    32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYsgCDKSFSRPLELSRHLRTHHNNPSDLNskslplsnskasssslS 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720384203 234 ECGKAFRVSSDLAQHHKIHTGEKP----------------HECLECGKAFTQ-LSHLIQHQRIHTGERPYVCPLCGKAFN 296
Cdd:COG5048   112 SSSSNSNDNNLLSSHSLPPSSRDPqlpdllsisnlrnnplPGNNSSSVNTPQsNSLHPPLPANSLSKDPSSNLSLLISSN 191

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720384203 297 HSTVLRSHQ----RVHTGEKPHGCSECGK------------TFSVKRTLLQHQRVHTGEK--PYTCSECGKAFSDRSVLI 358
Cdd:COG5048   192 VSTSIPSSSenspLSSSYSIPSSSSDQNLensssslplttnSQLSPKSLLSQSPSSLSSSdsSSSASESPRSSLPTASSQ 271

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720384203 359 QHHNVHTGE-------KPYECSECGKTFSHRSTLMNHER--IHTQE--KPYACYE--CGKAFVQHSHLIQHQRVHTGEKP 425
Cdd:COG5048   272 SSSPNESDSssekgfsLPIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCPYslCGKLFSRNDALKRHILLHTSISP 351

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720384203 426 YVC--GECGHAFS-----ARRSLIQHERIHTGEKPFQCT--ECGKAFSLKATLIVHLRTHTGEKPYECNS--CGKAFSQY 494
Cdd:COG5048   352 AKEklLNSSSKFSpllnnEPPQSLQQYKDLKNDKKSETLsnSCIRNFKRDSNLSLHIITHLSFRPYNCKNppCSKSFNRH 431

                         410
                  ....*....|....*...
gi 1720384203 495 SVLIQHQRIHTGEKPYEC 512
Cdd:COG5048   432 YNLIPHKKIHTNHAPLLC 449
zf-H2C2_2 pfam13465
Zinc-finger double domain;
188-213 7.68e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 39.66  E-value: 7.68e-05
                          10        20
                  ....*....|....*....|....*.
gi 1720384203 188 HLLQHQRIHTGEKPYVCHVCGKAFSQ 213
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
PHA00733 PHA00733
hypothetical protein
 285-332 2.31e-03

hypothetical protein


Pssm-ID: 177301  Cd Length: 128  Bit Score: 38.32  E-value: 2.31e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1720384203 285 PYVCPLCGKAFNHSTVLRSHQRVHTGEKPhgCSECGKTFSVKRTLLQH 332
Cdd:PHA00733   73 PYVCPLCLMPFSSSVSLKQHIRYTEHSKV--CPVCGKEFRNTDSTLDH 118
SUF4-like cd20908
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
 480-533 2.92e-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: 36.77  E-value: 2.92e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1720384203 480 KPYeCNSCGKAFSQYSVLIQHQRIHTgekpYECGECGRAFNQHGHLIQH-QKVHK 533
Cdd:cd20908     1 KPW-CYYCDREFDDEKILIQHQKAKH----FKCHICHKKLYTAGGLAVHcLQVHK 50
 
Name Accession Description Interval E-value
KRAB smart00349
krueppel associated box;
17-77 9.11e-30

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 111.15  E-value: 9.11e-30
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720384203   17 VTFEDVAVLLSQEEWARLGPAQRGLYRHVMMETYGNVVSLGLPGSKPVVISQLERGEDPWV 77
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQVPKPDLISQLEQGEEPWI 61
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
 17-57 1.07e-19

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: 82.13  E-value: 1.07e-19
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1720384203  17 VTFEDVAVLLSQEEWARLGPAQRGLYRHVMMETYGNVVSLG 57
Cdd:pfam01352   2 VTFEDVAVDFTQEEWALLDPAQRNLYRDVMLENYRNLVSLG 42
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
 17-56 1.34e-18

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


Pssm-ID: 143639  Cd Length: 40  Bit Score: 79.13  E-value: 1.34e-18
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1720384203  17 VTFEDVAVLLSQEEWARLGPAQRGLYRHVMMETYGNVVSL 56
Cdd:cd07765     1 VTFEDVAVYFSQEEWELLDPAQRDLYRDVMLENYENLVSL 40
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
172-512 3.08e-14

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 75.12  E-value: 3.08e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720384203 172 RPYICIECGKCFGRSSHLLQHQRIHTGEKPYVCHV--CGKAFSQSSVLSKHRRIHTGEKPYEC----------------N 233
Cdd:COG5048    32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYsgCDKSFSRPLELSRHLRTHHNNPSDLNskslplsnskasssslS 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720384203 234 ECGKAFRVSSDLAQHHKIHTGEKP----------------HECLECGKAFTQ-LSHLIQHQRIHTGERPYVCPLCGKAFN 296
Cdd:COG5048   112 SSSSNSNDNNLLSSHSLPPSSRDPqlpdllsisnlrnnplPGNNSSSVNTPQsNSLHPPLPANSLSKDPSSNLSLLISSN 191

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720384203 297 HSTVLRSHQ----RVHTGEKPHGCSECGK------------TFSVKRTLLQHQRVHTGEK--PYTCSECGKAFSDRSVLI 358
Cdd:COG5048   192 VSTSIPSSSenspLSSSYSIPSSSSDQNLensssslplttnSQLSPKSLLSQSPSSLSSSdsSSSASESPRSSLPTASSQ 271

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720384203 359 QHHNVHTGE-------KPYECSECGKTFSHRSTLMNHER--IHTQE--KPYACYE--CGKAFVQHSHLIQHQRVHTGEKP 425
Cdd:COG5048   272 SSSPNESDSssekgfsLPIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCPYslCGKLFSRNDALKRHILLHTSISP 351

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720384203 426 YVC--GECGHAFS-----ARRSLIQHERIHTGEKPFQCT--ECGKAFSLKATLIVHLRTHTGEKPYECNS--CGKAFSQY 494
Cdd:COG5048   352 AKEklLNSSSKFSpllnnEPPQSLQQYKDLKNDKKSETLsnSCIRNFKRDSNLSLHIITHLSFRPYNCKNppCSKSFNRH 431

                         410
                  ....*....|....*...
gi 1720384203 495 SVLIQHQRIHTGEKPYEC 512
Cdd:COG5048   432 YNLIPHKKIHTNHAPLLC 449
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
99-324 1.27e-11

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 66.64  E-value: 1.27e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720384203  99 KEENQNTDLNVPPLISDEASATLT-ETPLRKVAEERYKTEPKVCPSPKPIGPQNAHGLNPSVpVARPQTAPSVER----- 172
Cdd:COG5048   210 SIPSSSSDQNLENSSSSLPLTTNSqLSPKSLLSQSPSSLSSSDSSSSASESPRSSLPTASSQ-SSSPNESDSSSEkgfsl 288

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720384203 173 PYICIECGKCFGRSSHLLQHQR--IHTGE--KPYVCHV--CGKAFSQSSVLSKHRRIHTGEKPYEC--NECGKAFRVSSD 244
Cdd:COG5048   289 PIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCPYslCGKLFSRNDALKRHILLHTSISPAKEklLNSSSKFSPLLN 368

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720384203 245 -----LAQHHKIHTGEKPHECL--ECGKAFTQLSHLIQHQRIHTGERPYVC--PLCGKAFNHSTVLRSHQRVHTGEKPHG 315
Cdd:COG5048   369 neppqSLQQYKDLKNDKKSETLsnSCIRNFKRDSNLSLHIITHLSFRPYNCknPPCSKSFNRHYNLIPHKKIHTNHAPLL 448


                  ....*....
gi 1720384203 316 CSECGKTFS 324
Cdd:COG5048   449 CSILKSFRR 457
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
200-364 6.12e-08

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 55.09  E-value: 6.12e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720384203 200 KPYVCHVCGKAFSQSSVLSKHRR--IHTGE--KPYECNE--CGKAFRVSSDLAQHHKIHTGEKPHEC--LECGKAFTQLS 271
Cdd:COG5048   288 LPIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCPYslCGKLFSRNDALKRHILLHTSISPAKEklLNSSSKFSPLL 367

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720384203 272 H-----LIQHQRIHTGERPYVCPL--CGKAFNHSTVLRSHQRVHTGEKPHGC--SECGKTFSVKRTLLQHQRVHTGEKPY 342
Cdd:COG5048   368 NneppqSLQQYKDLKNDKKSETLSnsCIRNFKRDSNLSLHIITHLSFRPYNCknPPCSKSFNRHYNLIPHKKIHTNHAPL 447

                         170       180
                  ....*....|....*....|..
gi 1720384203 343 TCSECGKAFSDRSvlIQHHNVH 364
Cdd:COG5048   448 LCSILKSFRRDLD--LSNHGKD 467
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
256-532 3.69e-07

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 52.78  E-value: 3.69e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720384203 256 KPHECLECGKAFTQLSHLIQHQRIHTGERPYVCPLCGKAFNHSTV--LRSHQRVHTGEKPHGCSECGKTFSVKRTLLQHQ 333
Cdd:COG5048    32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYSGCDKSFSRPleLSRHLRTHHNNPSDLNSKSLPLSNSKASSSSLS 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720384203 334 RVHTGEkPYTCSECGKAFSDRSVLIQHHNVHTGEKPYECSECGKTFSHRST------------------------LMNHE 389
Cdd:COG5048   112 SSSSNS-NDNNLLSSHSLPPSSRDPQLPDLLSISNLRNNPLPGNNSSSVNTpqsnslhpplpanslskdpssnlsLLISS 190

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720384203 390 RIHTQEKPYACYECGKAFVQHSHLIQHQRVHTGEKPYVCGECGHAFSARRSLIQHERIHTGEKPFQCTECGKAFSLKATL 469
Cdd:COG5048   191 NVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLSSSDSSSSASESPRSSLPTASS 270

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720384203 470 IVHLRTHTGE-------KPYECNSCGKAFSQYSVLIQHQR--IHTGE--KPYECGE--CGRAFNQHGHLIQHQKVH 532
Cdd:COG5048   271 QSSSPNESDSssekgfsLPIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCPYslCGKLFSRNDALKRHILLH 346
zf-H2C2_2 pfam13465
Zinc-finger double domain;
188-213 7.68e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 39.66  E-value: 7.68e-05
                          10        20
                  ....*....|....*....|....*.
gi 1720384203 188 HLLQHQRIHTGEKPYVCHVCGKAFSQ 213
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
272-297 9.72e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 39.28  E-value: 9.72e-05
                          10        20
                  ....*....|....*....|....*.
gi 1720384203 272 HLIQHQRIHTGERPYVCPLCGKAFNH 297
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
440-464 1.60e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.89  E-value: 1.60e-04
                          10        20
                  ....*....|....*....|....*
gi 1720384203 440 SLIQHERIHTGEKPFQCTECGKAFS 464
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFK 25
zf-H2C2_2 pfam13465
Zinc-finger double domain;
385-409 2.03e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.51  E-value: 2.03e-04
                          10        20
                  ....*....|....*....|....*
gi 1720384203 385 LMNHERIHTQEKPYACYECGKAFVQ 409
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
469-493 2.92e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.12  E-value: 2.92e-04
                          10        20
                  ....*....|....*....|....*
gi 1720384203 469 LIVHLRTHTGEKPYECNSCGKAFSQ 493
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
217-239 3.34e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.12  E-value: 3.34e-04
                          10        20
                  ....*....|....*....|...
gi 1720384203 217 LSKHRRIHTGEKPYECNECGKAF 239
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSF 24
zf-H2C2_2 pfam13465
Zinc-finger double domain;
244-269 5.36e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 37.35  E-value: 5.36e-04
                          10        20
                  ....*....|....*....|....*.
gi 1720384203 244 DLAQHHKIHTGEKPHECLECGKAFTQ 269
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
329-352 6.27e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 37.35  E-value: 6.27e-04
                          10        20
                  ....*....|....*....|....
gi 1720384203 329 LLQHQRVHTGEKPYTCSECGKAFS 352
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFK 25
SFP1 COG5189
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ...
 221-309 6.74e-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: 6.74e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720384203 221 RRIHT-GEKPYECN--ECGKAFRVSSDLaQHHKIHTgekpheclECGKAFTQLSHLIQHQRIHTGERPYVCPLCGKAFNH 297
Cdd:COG5189   340 RMLKVkDGKPYKCPveGCNKKYKNQNGL-KYHMLHG--------HQNQKLHENPSPEKMNIFSAKDKPYRCEVCDKRYKN 410

                          90
                  ....*....|..
gi 1720384203 298 STVLRSHqRVHT 309
Cdd:COG5189   411 LNGLKYH-RKHS 421
zf-H2C2_2 pfam13465
Zinc-finger double domain;
497-521 6.91e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.97  E-value: 6.91e-04
                          10        20
                  ....*....|....*....|....*
gi 1720384203 497 LIQHQRIHTGEKPYECGECGRAFNQ 521
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 26
PHA00733 PHA00733
hypothetical protein
 285-332 2.31e-03

hypothetical protein


Pssm-ID: 177301  Cd Length: 128  Bit Score: 38.32  E-value: 2.31e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1720384203 285 PYVCPLCGKAFNHSTVLRSHQRVHTGEKPhgCSECGKTFSVKRTLLQH 332
Cdd:PHA00733   73 PYVCPLCLMPFSSSVSLKQHIRYTEHSKV--CPVCGKEFRNTDSTLDH 118
SUF4-like cd20908
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
 480-533 2.92e-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: 36.77  E-value: 2.92e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1720384203 480 KPYeCNSCGKAFSQYSVLIQHQRIHTgekpYECGECGRAFNQHGHLIQH-QKVHK 533
Cdd:cd20908     1 KPW-CYYCDREFDDEKILIQHQKAKH----FKCHICHKKLYTAGGLAVHcLQVHK 50
SUF4-like cd20908
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
 260-308 3.10e-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: 36.77  E-value: 3.10e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1720384203 260 CLECGKAFTQLSHLIQHQRIHTgerpYVCPLCGKAFNHSTVLRSH-QRVH 308
Cdd:cd20908     4 CYYCDREFDDEKILIQHQKAKH----FKCHICHKKLYTAGGLAVHcLQVH 49
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 370-392 4.58e-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: 4.58e-03
                          10        20
                  ....*....|....*....|...
gi 1720384203 370 YECSECGKTFSHRSTLMNHERIH 392
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
412-436 4.88e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 34.65  E-value: 4.88e-03
                          10        20
                  ....*....|....*....|....*
gi 1720384203 412 HLIQHQRVHTGEKPYVCGECGHAFS 436
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFK 25
zf-H2C2_2 pfam13465
Zinc-finger double domain;
301-324 5.28e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 34.65  E-value: 5.28e-03
                          10        20
                  ....*....|....*....|....
gi 1720384203 301 LRSHQRVHTGEKPHGCSECGKTFS 324
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFK 25
zf-H2C2_2 pfam13465
Zinc-finger double domain;
357-381 5.49e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 34.65  E-value: 5.49e-03
                          10        20
                  ....*....|....*....|....*
gi 1720384203 357 LIQHHNVHTGEKPYECSECGKTFSH 381
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 258-280 8.84e-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: 8.84e-03
                          10        20
                  ....*....|....*....|...
gi 1720384203 258 HECLECGKAFTQLSHLIQHQRIH 280
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