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Conserved domains on  [gi|1622948574|ref|XP_028705808|]
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zinc finger protein 2 homolog isoform X2 [Macaca mulatta]

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
KRAB smart00349
krueppel associated box;
39-96 4.35e-22

krueppel associated box;


:

Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 89.57  E-value: 4.35e-22
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1622948574   39 VTFKDVSIDFSWEEWIQADSSQRmTMYGEVMLENYRNLFSPGNHLSKPSVTSQLDREE 96
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQK-NLYRDVMLENYSNLVSLGFQVPKPDLISQLEQGE 57
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
235-587 4.29e-13

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


:

Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 71.65  E-value: 4.29e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622948574 235 KKIYECNQCSKTFSQSSSLLKHQRIHTGEKPFKCNV--CGKHFIERSSLNVHQRIHTGEKPYKC---------------- 296
Cdd:COG5048    31 PRPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYsgCDKSFSRPLELSRHLRTHHNNPSDLNskslplsnskassssl 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622948574 297 NECGKAF-----SQSMNLTVHQRTHTGKKPYQCKECGKAFHKNSSLIQHERIHTGEK--PYRCNECGKAFTQSMNLTVHQ 369
Cdd:COG5048   111 SSSSSNSndnnlLSSHSLPPSSRDPQLPDLLSISNLRNNPLPGNNSSSVNTPQSNSLhpPLPANSLSKDPSSNLSLLISS 190

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622948574 370 RTHTGEKPYECNECGKAFSQSMHLIVHQRSHTGEKPYECSQCGKAFSKSSTLTLHQRNHTGE------------------ 431
Cdd:COG5048   191 NVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLSSSDssssasesprsslptass 270

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622948574 432 -----------------KPYKCNKCEKSFSQSTYLIEHQR--LHSG--VKPFEC--NQCGKAFSKNSSLTQHRRIHTGEK 488
Cdd:COG5048   271 qssspnesdsssekgfsLPIKSKQCNISFSRSSPLTRHLRsvNHSGesLKPFSCpySLCGKLFSRNDALKRHILLHTSIS 350

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622948574 489 PYECM--VCGKHFTGRS-----SLTVHQVIHTGEKPYEC--NECGKAFSQSAYLIEHQRIHTGEKPYECD--QCGKAFIK 557
Cdd:COG5048   351 PAKEKllNSSSKFSPLLnneppQSLQQYKDLKNDKKSETlsNSCIRNFKRDSNLSLHIITHLSFRPYNCKnpPCSKSFNR 430

                         410       420       430
                  ....*....|....*....|....*....|
gi 1622948574 558 NSSLTVHQRTHTGEKPYQCNECGKAFSRST 587
Cdd:COG5048   431 HYNLIPHKKIHTNHAPLLCSILKSFRRDLD 460
 
Name Accession Description Interval E-value
KRAB smart00349
krueppel associated box;
39-96 4.35e-22

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 89.57  E-value: 4.35e-22
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1622948574   39 VTFKDVSIDFSWEEWIQADSSQRmTMYGEVMLENYRNLFSPGNHLSKPSVTSQLDREE 96
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQK-NLYRDVMLENYSNLVSLGFQVPKPDLISQLEQGE 57
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
 38-78 8.03e-17

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: 74.04  E-value: 8.03e-17
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1622948574  38 SVTFKDVSIDFSWEEWIQADSSQRmTMYGEVMLENYRNLFS 78
Cdd:pfam01352   1 SVTFEDVAVDFTQEEWALLDPAQR-NLYRDVMLENYRNLVS 40
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
 39-78 2.42e-14

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: 67.19  E-value: 2.42e-14
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1622948574  39 VTFKDVSIDFSWEEWIQADSSQRmTMYGEVMLENYRNLFS 78
Cdd:cd07765     1 VTFEDVAVYFSQEEWELLDPAQR-DLYRDVMLENYENLVS 39
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
235-587 4.29e-13

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 71.65  E-value: 4.29e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622948574 235 KKIYECNQCSKTFSQSSSLLKHQRIHTGEKPFKCNV--CGKHFIERSSLNVHQRIHTGEKPYKC---------------- 296
Cdd:COG5048    31 PRPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYsgCDKSFSRPLELSRHLRTHHNNPSDLNskslplsnskassssl 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622948574 297 NECGKAF-----SQSMNLTVHQRTHTGKKPYQCKECGKAFHKNSSLIQHERIHTGEK--PYRCNECGKAFTQSMNLTVHQ 369
Cdd:COG5048   111 SSSSSNSndnnlLSSHSLPPSSRDPQLPDLLSISNLRNNPLPGNNSSSVNTPQSNSLhpPLPANSLSKDPSSNLSLLISS 190

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622948574 370 RTHTGEKPYECNECGKAFSQSMHLIVHQRSHTGEKPYECSQCGKAFSKSSTLTLHQRNHTGE------------------ 431
Cdd:COG5048   191 NVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLSSSDssssasesprsslptass 270

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622948574 432 -----------------KPYKCNKCEKSFSQSTYLIEHQR--LHSG--VKPFEC--NQCGKAFSKNSSLTQHRRIHTGEK 488
Cdd:COG5048   271 qssspnesdsssekgfsLPIKSKQCNISFSRSSPLTRHLRsvNHSGesLKPFSCpySLCGKLFSRNDALKRHILLHTSIS 350

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622948574 489 PYECM--VCGKHFTGRS-----SLTVHQVIHTGEKPYEC--NECGKAFSQSAYLIEHQRIHTGEKPYECD--QCGKAFIK 557
Cdd:COG5048   351 PAKEKllNSSSKFSPLLnneppQSLQQYKDLKNDKKSETlsNSCIRNFKRDSNLSLHIITHLSFRPYNCKnpPCSKSFNR 430

                         410       420       430
                  ....*....|....*....|....*....|
gi 1622948574 558 NSSLTVHQRTHTGEKPYQCNECGKAFSRST 587
Cdd:COG5048   431 HYNLIPHKKIHTNHAPLLCSILKSFRRDLD 460
zf-H2C2_2 pfam13465
Zinc-finger double domain;
280-305 3.94e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 40.82  E-value: 3.94e-05
                          10        20
                  ....*....|....*....|....*.
gi 1622948574 280 SLNVHQRIHTGEKPYKCNECGKAFSQ 305
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
SUF4-like cd20908
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
 320-368 1.62e-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: 37.54  E-value: 1.62e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1622948574 320 KPYqCKECGKAFHKNSSLIQHERIHTgekpYRCNECGKAFTQSMNLTVH 368
Cdd:cd20908     1 KPW-CYYCDREFDDEKILIQHQKAKH----FKCHICHKKLYTAGGLAVH 44
PLN03086 PLN03086
PRLI-interacting factor K; Provisional
 268-399 7.41e-03

PRLI-interacting factor K; Provisional


Pssm-ID: 178635 [Multi-domain]  Cd Length: 567  Bit Score: 39.08  E-value: 7.41e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622948574 268 CNVCgKHFIERSSLNVHQ-------------------RIHTGEKPYKCNECGKAFSQSmNLTVHQRTHtgKKPYQCKeCG 328
Cdd:PLN03086  410 CRNC-KHYIPSRSIALHEaycsrhnvvcphdgcgivlRVEEAKNHVHCEKCGQAFQQG-EMEKHMKVF--HEPLQCP-CG 484

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622948574 329 KAFHKNsSLIQHErihTGEKPYR---CNECG---KAFTQSM-------NLTVHQRThTGEKPYECNECGKAF---SQSMH 392
Cdd:PLN03086  485 VVLEKE-QMVQHQ---ASTCPLRlitCRFCGdmvQAGGSAMdvrdrlrGMSEHESI-CGSRTAPCDSCGRSVmlkEMDIH 559


                  ....*...
gi 1622948574 393 LI-VHQRS 399
Cdd:PLN03086  560 QIaVHQKS 567
 
Name Accession Description Interval E-value
KRAB smart00349
krueppel associated box;
39-96 4.35e-22

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 89.57  E-value: 4.35e-22
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1622948574   39 VTFKDVSIDFSWEEWIQADSSQRmTMYGEVMLENYRNLFSPGNHLSKPSVTSQLDREE 96
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQK-NLYRDVMLENYSNLVSLGFQVPKPDLISQLEQGE 57
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
 38-78 8.03e-17

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: 74.04  E-value: 8.03e-17
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1622948574  38 SVTFKDVSIDFSWEEWIQADSSQRmTMYGEVMLENYRNLFS 78
Cdd:pfam01352   1 SVTFEDVAVDFTQEEWALLDPAQR-NLYRDVMLENYRNLVS 40
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
 39-78 2.42e-14

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: 67.19  E-value: 2.42e-14
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1622948574  39 VTFKDVSIDFSWEEWIQADSSQRmTMYGEVMLENYRNLFS 78
Cdd:cd07765     1 VTFEDVAVYFSQEEWELLDPAQR-DLYRDVMLENYENLVS 39
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
235-587 4.29e-13

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 71.65  E-value: 4.29e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622948574 235 KKIYECNQCSKTFSQSSSLLKHQRIHTGEKPFKCNV--CGKHFIERSSLNVHQRIHTGEKPYKC---------------- 296
Cdd:COG5048    31 PRPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYsgCDKSFSRPLELSRHLRTHHNNPSDLNskslplsnskassssl 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622948574 297 NECGKAF-----SQSMNLTVHQRTHTGKKPYQCKECGKAFHKNSSLIQHERIHTGEK--PYRCNECGKAFTQSMNLTVHQ 369
Cdd:COG5048   111 SSSSSNSndnnlLSSHSLPPSSRDPQLPDLLSISNLRNNPLPGNNSSSVNTPQSNSLhpPLPANSLSKDPSSNLSLLISS 190

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622948574 370 RTHTGEKPYECNECGKAFSQSMHLIVHQRSHTGEKPYECSQCGKAFSKSSTLTLHQRNHTGE------------------ 431
Cdd:COG5048   191 NVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLSSSDssssasesprsslptass 270

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622948574 432 -----------------KPYKCNKCEKSFSQSTYLIEHQR--LHSG--VKPFEC--NQCGKAFSKNSSLTQHRRIHTGEK 488
Cdd:COG5048   271 qssspnesdsssekgfsLPIKSKQCNISFSRSSPLTRHLRsvNHSGesLKPFSCpySLCGKLFSRNDALKRHILLHTSIS 350

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622948574 489 PYECM--VCGKHFTGRS-----SLTVHQVIHTGEKPYEC--NECGKAFSQSAYLIEHQRIHTGEKPYECD--QCGKAFIK 557
Cdd:COG5048   351 PAKEKllNSSSKFSPLLnneppQSLQQYKDLKNDKKSETlsNSCIRNFKRDSNLSLHIITHLSFRPYNCKnpPCSKSFNR 430

                         410       420       430
                  ....*....|....*....|....*....|
gi 1622948574 558 NSSLTVHQRTHTGEKPYQCNECGKAFSRST 587
Cdd:COG5048   431 HYNLIPHKKIHTNHAPLLCSILKSFRRDLD 460
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
209-472 4.81e-07

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 52.39  E-value: 4.81e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622948574 209 PHNCNSHGEDATQNSELVKTQRMLVGKKIYECNQCSKTFSQSSSLLKHQRIHTGEKPFKCNVCG----KHFIERSSLNVH 284
Cdd:COG5048   170 PLPANSLSKDPSSNLSLLISSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSqlspKSLLSQSPSSLS 249

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622948574 285 QRIHTGEKPYKCNECG--KAFSQSMNLTVHQRTHTGK-KPYQCKECGKAFHKNSSLIQHER--IHTGE--KPYRCNE--C 355
Cdd:COG5048   250 SSDSSSSASESPRSSLptASSQSSSPNESDSSSEKGFsLPIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCPYslC 329

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622948574 356 GKAFTQSMNLTVHQRTHTGEKPYEC--NECGKAFSQSMH-----LIVHQRSHTGEKPYEC--SQCGKAFSKSSTLTLHQR 426
Cdd:COG5048   330 GKLFSRNDALKRHILLHTSISPAKEklLNSSSKFSPLLNneppqSLQQYKDLKNDKKSETlsNSCIRNFKRDSNLSLHII 409

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1622948574 427 NHTGEKP--YKCNKCEKSFSQSTYLIEHQRLHSGVKPFECNQCGKAFS 472
Cdd:COG5048   410 THLSFRPynCKNPPCSKSFNRHYNLIPHKKIHTNHAPLLCSILKSFRR 457
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
240-448 1.51e-05

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 47.77  E-value: 1.51e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622948574 240 CNQCSKTFSQSSSLLKHQRIHTGEKPFKCNVCGKHFIERSSLNVHQRIHTG-EKPYKCNECGKAFSQSMNLTVHQRT--H 316
Cdd:COG5048   235 LSPKSLLSQSPSSLSSSDSSSSASESPRSSLPTASSQSSSPNESDSSSEKGfSLPIKSKQCNISFSRSSPLTRHLRSvnH 314

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622948574 317 TGK--KPYQCKE--CGKAFHKNSSLIQHERIHTGEKPYRC--NECGKAFTQSMN-----LTVHQRTHTGEKPYEC--NEC 383
Cdd:COG5048   315 SGEslKPFSCPYslCGKLFSRNDALKRHILLHTSISPAKEklLNSSSKFSPLLNneppqSLQQYKDLKNDKKSETlsNSC 394

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622948574 384 GKAFSQSMHLIVHQRSHTGEKPYEC--SQCGKAFSKSSTLTLHQRNHTGEKPYKCNKCEKSFSQSTY 448
Cdd:COG5048   395 IRNFKRDSNLSLHIITHLSFRPYNCknPPCSKSFNRHYNLIPHKKIHTNHAPLLCSILKSFRRDLDL 461
zf-H2C2_2 pfam13465
Zinc-finger double domain;
280-305 3.94e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 40.82  E-value: 3.94e-05
                          10        20
                  ....*....|....*....|....*.
gi 1622948574 280 SLNVHQRIHTGEKPYKCNECGKAFSQ 305
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
364-389 4.10e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 40.82  E-value: 4.10e-05
                          10        20
                  ....*....|....*....|....*.
gi 1622948574 364 NLTVHQRTHTGEKPYECNECGKAFSQ 389
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
336-361 5.29e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 40.43  E-value: 5.29e-05
                          10        20
                  ....*....|....*....|....*.
gi 1622948574 336 SLIQHERIHTGEKPYRCNECGKAFTQ 361
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
560-585 1.00e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 39.66  E-value: 1.00e-04
                          10        20
                  ....*....|....*....|....*.
gi 1622948574 560 SLTVHQRTHTGEKPYQCNECGKAFSR 585
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 574-596 1.04e-04

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


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 39.59  E-value: 1.04e-04
                          10        20
                  ....*....|....*....|...
gi 1622948574 574 YQCNECGKAFSRSTNLTRHQRTH 596
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
308-331 1.30e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 39.28  E-value: 1.30e-04
                          10        20
                  ....*....|....*....|....
gi 1622948574 308 NLTVHQRTHTGKKPYQCKECGKAF 331
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSF 24
SFP1 COG5189
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ...
 290-373 1.33e-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: 1.33e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622948574 290 GEKPYKCN--ECGKAFSQSMNLTVHqRTHtgkkpyqcKECGKAFHKNSSLIQHERIHTGEKPYRCNECGKAFTQSMNLTV 367
Cdd:COG5189   346 DGKPYKCPveGCNKKYKNQNGLKYH-MLH--------GHQNQKLHENPSPEKMNIFSAKDKPYRCEVCDKRYKNLNGLKY 416


                  ....*.
gi 1622948574 368 HqRTHT 373
Cdd:COG5189   417 H-RKHS 421
zf-H2C2_2 pfam13465
Zinc-finger double domain;
532-555 1.59e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.89  E-value: 1.59e-04
                          10        20
                  ....*....|....*....|....
gi 1622948574 532 YLIEHQRIHTGEKPYECDQCGKAF 555
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSF 24
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
544-597 2.47e-04

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 43.92  E-value: 2.47e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1622948574 544 KPYECDQCGKAFIKNSSLTVHQRTHTGEKPYQCN--ECGKAFSRSTNLTRHQRTHT 597
Cdd:COG5048    32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSysGCDKSFSRPLELSRHLRTHH 87
zf-H2C2_2 pfam13465
Zinc-finger double domain;
392-417 2.80e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.12  E-value: 2.80e-04
                          10        20
                  ....*....|....*....|....*.
gi 1622948574 392 HLIVHQRSHTGEKPYECSQCGKAFSK 417
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
421-445 4.81e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 37.74  E-value: 4.81e-04
                          10        20
                  ....*....|....*....|....*
gi 1622948574 421 LTLHQRNHTGEKPYKCNKCEKSFSQ 445
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
476-500 5.41e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 37.35  E-value: 5.41e-04
                          10        20
                  ....*....|....*....|....*
gi 1622948574 476 SLTQHRRIHTGEKPYECMVCGKHFT 500
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFK 25
zf-H2C2_2 pfam13465
Zinc-finger double domain;
252-275 5.57e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 37.35  E-value: 5.57e-04
                          10        20
                  ....*....|....*....|....
gi 1622948574 252 SLLKHQRIHTGEKPFKCNVCGKHF 275
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSF 24
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 294-316 6.69e-04

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


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 37.28  E-value: 6.69e-04
                          10        20
                  ....*....|....*....|...
gi 1622948574 294 YKCNECGKAFSQSMNLTVHQRTH 316
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 350-372 9.16e-04

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


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 36.89  E-value: 9.16e-04
                          10        20
                  ....*....|....*....|...
gi 1622948574 350 YRCNECGKAFTQSMNLTVHQRTH 372
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
504-529 9.65e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.58  E-value: 9.65e-04
                          10        20
                  ....*....|....*....|....*.
gi 1622948574 504 SLTVHQVIHTGEKPYECNECGKAFSQ 529
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
SFP1 COG5189
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ...
 430-508 1.53e-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: 1.53e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622948574 430 GEKPYKCN--KCEKSFSQSTYLIEHqRLHSgvkpfecnQCGKAFSKNSSLTQHRRIHTGEKPYECMVCGKHFTGRSSLTV 507
Cdd:COG5189   346 DGKPYKCPveGCNKKYKNQNGLKYH-MLHG--------HQNQKLHENPSPEKMNIFSAKDKPYRCEVCDKRYKNLNGLKY 416


                  .
gi 1622948574 508 H 508
Cdd:COG5189   417 H 417
SUF4-like cd20908
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
 320-368 1.62e-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: 37.54  E-value: 1.62e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1622948574 320 KPYqCKECGKAFHKNSSLIQHERIHTgekpYRCNECGKAFTQSMNLTVH 368
Cdd:cd20908     1 KPW-CYYCDREFDDEKILIQHQKAKH----FKCHICHKKLYTAGGLAVH 44
SUF4-like cd20908
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
 240-288 2.70e-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: 37.15  E-value: 2.70e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1622948574 240 CNQCSKTFSQSSSLLKHQRIHTgekpFKCNVCGKHFIERSSLNVH-QRIH 288
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 ...
 378-400 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 1622948574 378 YECNECGKAFSQSMHLIVHQRSH 400
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 238-260 3.62e-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: 3.62e-03
                          10        20
                  ....*....|....*....|...
gi 1622948574 238 YECNQCSKTFSQSSSLLKHQRIH 260
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
SFP1 COG5189
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ...
 470-569 4.07e-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: 4.07e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622948574 470 AFSKNSSL---TQHRRIHT-GEKPYECMV--CGKHFTGRSSLTVHQvIHtgekpyecNECGKAFSQSAYLIEHQRIHTGE 543
Cdd:COG5189   326 KLAHGGERnidTPSRMLKVkDGKPYKCPVegCNKKYKNQNGLKYHM-LH--------GHQNQKLHENPSPEKMNIFSAKD 396

                          90       100
                  ....*....|....*....|....*.
gi 1622948574 544 KPYECDQCGKAFIKNSSLTVHqRTHT 569
Cdd:COG5189   397 KPYRCEVCDKRYKNLNGLKYH-RKHS 421
zf-H2C2_2 pfam13465
Zinc-finger double domain;
448-473 4.46e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.04  E-value: 4.46e-03
                          10        20
                  ....*....|....*....|....*.
gi 1622948574 448 YLIEHQRLHSGVKPFECNQCGKAFSK 473
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 546-568 4.76e-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: 4.76e-03
                          10        20
                  ....*....|....*....|...
gi 1622948574 546 YECDQCGKAFIKNSSLTVHQRTH 568
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 462-484 4.95e-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: 4.95e-03
                          10        20
                  ....*....|....*....|...
gi 1622948574 462 FECNQCGKAFSKNSSLTQHRRIH 484
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 518-540 5.25e-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: 5.25e-03
                          10        20
                  ....*....|....*....|...
gi 1622948574 518 YECNECGKAFSQSAYLIEHQRIH 540
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
SFP1 COG5189
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ...
 194-317 6.12e-03

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


Pssm-ID: 227516 [Multi-domain]  Cd Length: 423  Bit Score: 39.32  E-value: 6.12e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622948574 194 DSILDTQQSIPMVKRPHNCNSHGEDATQNSELV--KTQRML--VGKKIYECN--QCSKTFsQSSSLLKHQRIHtgekpfk 267
Cdd:COG5189   302 RGGISTGEMIDVRKLPCTNSSSNGKLAHGGERNidTPSRMLkvKDGKPYKCPveGCNKKY-KNQNGLKYHMLH------- 373

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1622948574 268 cNVCGKHFIERSSLNVHQRIHTGEKPYKCNECGKAFSQSMNLTVHqRTHT 317
Cdd:COG5189   374 -GHQNQKLHENPSPEKMNIFSAKDKPYRCEVCDKRYKNLNGLKYH-RKHS 421
PLN03086 PLN03086
PRLI-interacting factor K; Provisional
 268-399 7.41e-03

PRLI-interacting factor K; Provisional


Pssm-ID: 178635 [Multi-domain]  Cd Length: 567  Bit Score: 39.08  E-value: 7.41e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622948574 268 CNVCgKHFIERSSLNVHQ-------------------RIHTGEKPYKCNECGKAFSQSmNLTVHQRTHtgKKPYQCKeCG 328
Cdd:PLN03086  410 CRNC-KHYIPSRSIALHEaycsrhnvvcphdgcgivlRVEEAKNHVHCEKCGQAFQQG-EMEKHMKVF--HEPLQCP-CG 484

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622948574 329 KAFHKNsSLIQHErihTGEKPYR---CNECG---KAFTQSM-------NLTVHQRThTGEKPYECNECGKAF---SQSMH 392
Cdd:PLN03086  485 VVLEKE-QMVQHQ---ASTCPLRlitCRFCGdmvQAGGSAMdvrdrlrGMSEHESI-CGSRTAPCDSCGRSVmlkEMDIH 559


                  ....*...
gi 1622948574 393 LI-VHQRS 399
Cdd:PLN03086  560 QIaVHQKS 567
PHA00733 PHA00733
hypothetical protein
 444-508 8.10e-03

hypothetical protein


Pssm-ID: 177301  Cd Length: 128  Bit Score: 36.78  E-value: 8.10e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622948574 444 SQSTYLIEHQRLHSgVKPFECNQCGKAFSKNSSLTQHRRIHTGEKpyECMVCGKHFTGRSSLTVH 508
Cdd:PHA00733   57 DESSYLYKLLTSKA-VSPYVCPLCLMPFSSSVSLKQHIRYTEHSK--VCPVCGKEFRNTDSTLDH 118
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 266-288 9.65e-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: 9.65e-03
                          10        20
                  ....*....|....*....|...
gi 1622948574 266 FKCNVCGKHFIERSSLNVHQRIH 288
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
SUF4-like cd20908
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
 264-312 9.75e-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: 35.61  E-value: 9.75e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1622948574 264 KPFkCNVCGKHFIERSSLNVHQRIHTgekpYKCNECGKAFSQSMNLTVH 312
Cdd:cd20908     1 KPW-CYYCDREFDDEKILIQHQKAKH----FKCHICHKKLYTAGGLAVH 44
 
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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