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Conserved domains on  [gi|1191866815|ref|XP_020942664|]
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zinc finger protein 169 isoform X1 [Sus scrofa]

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|1.10.287.1360
Gene Ontology:  GO:0003677|GO:0008270|GO:0005515|GO:0001217|GO:0003700
PubMed:  8183940|22803940|2023909|8183939|8183940|10748030|27867147|28765213|11361095|30718982|10940247
SCOP:  4003583|4002243

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
KRAB smart00349
krueppel associated box;
32-91 7.70e-33

krueppel associated box;


:

Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 120.00  E-value: 7.70e-33
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191866815   32 MAFRDVAVAFSQKEWKLLSPAQRTLYRDVMLENYSLLVSLGIAFPKPKLITQLEQGDEPW 91
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQVPKPDLISQLEQGEEPW 60
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
237-603 1.00e-12

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


:

Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 70.49  E-value: 1.00e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191866815 237 STKSSLFSLQKH---HMCPECGRSFCQRSDLIKHQRTHTGEKPYSCRECGRG--FGRKSSLTIHQRKHSGEKPYmcRECG 311
Cdd:COG5048    19 TPKSTLKSLSNAprpDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYSGCDksFSRPLELSRHLRTHHNNPSD--LNSK 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191866815 312 QHFRYTSSLTNHKRIHSG-ERPFVCQECGRGF----RQKIALILHQRTHLEEKPfvCPECGRGFC--------------- 371
Cdd:COG5048    97 SLPLSNSKASSSSLSSSSsNSNDNNLLSSHSLppssRDPQLPDLLSISNLRNNP--LPGNNSSSVntpqsnslhpplpan 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191866815 372 -------------------------------QKASLLQHRSSHSGERPFL----CLECGRGFRQQSLLISHQVTHSGEKP 416
Cdd:COG5048   175 slskdpssnlsllissnvstsipsssensplSSSYSIPSSSSDQNLENSSsslpLTTNSQLSPKSLLSQSPSSLSSSDSS 254

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191866815 417 YVCAECGHSFRQKVTLIRHQRTHTGE-------KPYLCSECGRGFSQKVSLMGHQRT--HTGE--KPYVCPE--CGRGFG 483
Cdd:COG5048   255 SSASESPRSSLPTASSQSSSPNESDSssekgfsLPIKSKQCNISFSRSSPLTRHLRSvnHSGEslKPFSCPYslCGKLFS 334

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191866815 484 QKVTLIRHQRTHTGEKPYLCPECGHTFGFKSLLT--RHQKT--HSGEKADVYRVCEQRLSQKNLTSD--------QRTWS 551
Cdd:COG5048   335 RNDALKRHILLHTSISPAKEKLLNSSSKFSPLLNnePPQSLqqYKDLKNDKKSETLSNSCIRNFKRDsnlslhiiTHLSF 414

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1191866815 552 GEKPCVCDECGRGFGFKSALIRHQRTHSGEKPYICRECGRGFSQKSHLHRHR 603
Cdd:COG5048   415 RPYNCKNPPCSKSFNRHYNLIPHKKIHTNHAPLLCSILKSFRRDLDLSNHGK 466
 
Name Accession Description Interval E-value
KRAB smart00349
krueppel associated box;
32-91 7.70e-33

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 120.00  E-value: 7.70e-33
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191866815   32 MAFRDVAVAFSQKEWKLLSPAQRTLYRDVMLENYSLLVSLGIAFPKPKLITQLEQGDEPW 91
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQVPKPDLISQLEQGEEPW 60
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
 31-72 1.92e-22

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: 90.22  E-value: 1.92e-22
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1191866815  31 LMAFRDVAVAFSQKEWKLLSPAQRTLYRDVMLENYSLLVSLG 72
Cdd:pfam01352   1 SVTFEDVAVDFTQEEWALLDPAQRNLYRDVMLENYRNLVSLG 42
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
 32-71 1.64e-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: 1.64e-18
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1191866815  32 MAFRDVAVAFSQKEWKLLSPAQRTLYRDVMLENYSLLVSL 71
Cdd:cd07765     1 VTFEDVAVYFSQEEWELLDPAQRDLYRDVMLENYENLVSL 40
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
237-603 1.00e-12

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 70.49  E-value: 1.00e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191866815 237 STKSSLFSLQKH---HMCPECGRSFCQRSDLIKHQRTHTGEKPYSCRECGRG--FGRKSSLTIHQRKHSGEKPYmcRECG 311
Cdd:COG5048    19 TPKSTLKSLSNAprpDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYSGCDksFSRPLELSRHLRTHHNNPSD--LNSK 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191866815 312 QHFRYTSSLTNHKRIHSG-ERPFVCQECGRGF----RQKIALILHQRTHLEEKPfvCPECGRGFC--------------- 371
Cdd:COG5048    97 SLPLSNSKASSSSLSSSSsNSNDNNLLSSHSLppssRDPQLPDLLSISNLRNNP--LPGNNSSSVntpqsnslhpplpan 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191866815 372 -------------------------------QKASLLQHRSSHSGERPFL----CLECGRGFRQQSLLISHQVTHSGEKP 416
Cdd:COG5048   175 slskdpssnlsllissnvstsipsssensplSSSYSIPSSSSDQNLENSSsslpLTTNSQLSPKSLLSQSPSSLSSSDSS 254

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191866815 417 YVCAECGHSFRQKVTLIRHQRTHTGE-------KPYLCSECGRGFSQKVSLMGHQRT--HTGE--KPYVCPE--CGRGFG 483
Cdd:COG5048   255 SSASESPRSSLPTASSQSSSPNESDSssekgfsLPIKSKQCNISFSRSSPLTRHLRSvnHSGEslKPFSCPYslCGKLFS 334

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191866815 484 QKVTLIRHQRTHTGEKPYLCPECGHTFGFKSLLT--RHQKT--HSGEKADVYRVCEQRLSQKNLTSD--------QRTWS 551
Cdd:COG5048   335 RNDALKRHILLHTSISPAKEKLLNSSSKFSPLLNnePPQSLqqYKDLKNDKKSETLSNSCIRNFKRDsnlslhiiTHLSF 414

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1191866815 552 GEKPCVCDECGRGFGFKSALIRHQRTHSGEKPYICRECGRGFSQKSHLHRHR 603
Cdd:COG5048   415 RPYNCKNPPCSKSFNRHYNLIPHKKIHTNHAPLLCSILKSFRRDLDLSNHGK 466
zf-H2C2_2 pfam13465
Zinc-finger double domain;
488-510 5.93e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 37.35  E-value: 5.93e-04
                          10        20
                  ....*....|....*....|...
gi 1191866815 488 LIRHQRTHTGEKPYLCPECGHTF 510
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSF 24
SUF4-like cd20908
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
 254-295 4.10e-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: 36.38  E-value: 4.10e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1191866815 254 CGRSFCQRSDLIKHQRTHTgekpYSCRECGRGFGRKSSLTIH 295
Cdd:cd20908     7 CDREFDDEKILIQHQKAKH----FKCHICHKKLYTAGGLAVH 44
 
Name Accession Description Interval E-value
KRAB smart00349
krueppel associated box;
32-91 7.70e-33

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 120.00  E-value: 7.70e-33
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191866815   32 MAFRDVAVAFSQKEWKLLSPAQRTLYRDVMLENYSLLVSLGIAFPKPKLITQLEQGDEPW 91
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQVPKPDLISQLEQGEEPW 60
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
 31-72 1.92e-22

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: 90.22  E-value: 1.92e-22
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1191866815  31 LMAFRDVAVAFSQKEWKLLSPAQRTLYRDVMLENYSLLVSLG 72
Cdd:pfam01352   1 SVTFEDVAVDFTQEEWALLDPAQRNLYRDVMLENYRNLVSLG 42
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
 32-71 1.64e-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: 1.64e-18
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1191866815  32 MAFRDVAVAFSQKEWKLLSPAQRTLYRDVMLENYSLLVSL 71
Cdd:cd07765     1 VTFEDVAVYFSQEEWELLDPAQRDLYRDVMLENYENLVSL 40
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
237-603 1.00e-12

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 70.49  E-value: 1.00e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191866815 237 STKSSLFSLQKH---HMCPECGRSFCQRSDLIKHQRTHTGEKPYSCRECGRG--FGRKSSLTIHQRKHSGEKPYmcRECG 311
Cdd:COG5048    19 TPKSTLKSLSNAprpDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYSGCDksFSRPLELSRHLRTHHNNPSD--LNSK 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191866815 312 QHFRYTSSLTNHKRIHSG-ERPFVCQECGRGF----RQKIALILHQRTHLEEKPfvCPECGRGFC--------------- 371
Cdd:COG5048    97 SLPLSNSKASSSSLSSSSsNSNDNNLLSSHSLppssRDPQLPDLLSISNLRNNP--LPGNNSSSVntpqsnslhpplpan 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191866815 372 -------------------------------QKASLLQHRSSHSGERPFL----CLECGRGFRQQSLLISHQVTHSGEKP 416
Cdd:COG5048   175 slskdpssnlsllissnvstsipsssensplSSSYSIPSSSSDQNLENSSsslpLTTNSQLSPKSLLSQSPSSLSSSDSS 254

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191866815 417 YVCAECGHSFRQKVTLIRHQRTHTGE-------KPYLCSECGRGFSQKVSLMGHQRT--HTGE--KPYVCPE--CGRGFG 483
Cdd:COG5048   255 SSASESPRSSLPTASSQSSSPNESDSssekgfsLPIKSKQCNISFSRSSPLTRHLRSvnHSGEslKPFSCPYslCGKLFS 334

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191866815 484 QKVTLIRHQRTHTGEKPYLCPECGHTFGFKSLLT--RHQKT--HSGEKADVYRVCEQRLSQKNLTSD--------QRTWS 551
Cdd:COG5048   335 RNDALKRHILLHTSISPAKEKLLNSSSKFSPLLNnePPQSLqqYKDLKNDKKSETLSNSCIRNFKRDsnlslhiiTHLSF 414

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1191866815 552 GEKPCVCDECGRGFGFKSALIRHQRTHSGEKPYICRECGRGFSQKSHLHRHR 603
Cdd:COG5048   415 RPYNCKNPPCSKSFNRHYNLIPHKKIHTNHAPLLCSILKSFRRDLDLSNHGK 466
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
331-618 2.43e-04

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 43.92  E-value: 2.43e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191866815 331 RPFVCQECGRGFRQKIALILHQRTHLEEKPFVCPECGRG--FCQKASLLQHRSSHSGERPFLCleCGRGFRQQSLLISHQ 408
Cdd:COG5048    32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYSGCDksFSRPLELSRHLRTHHNNPSDLN--SKSLPLSNSKASSSS 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191866815 409 VTHSGEKP-YVCAECGHSFRQKvtlIRHQRTHTGEKPY--LCSECGRGFSQKVSLMGHQRTHtGEKPYVCPeCGRGFGQK 485
Cdd:COG5048   110 LSSSSSNSnDNNLLSSHSLPPS---SRDPQLPDLLSISnlRNNPLPGNNSSSVNTPQSNSLH-PPLPANSL-SKDPSSNL 184

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191866815 486 VTLIRHQRTHTGEKPYLCPECGHTFGFKSLLTRHQKTHSgeKADVYRVCEQRLSQKNLTSDQR--TWSGEKPCVCDECGR 563
Cdd:COG5048   185 SLLISSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENS--SSSLPLTTNSQLSPKSLLSQSPssLSSSDSSSSASESPR 262

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1191866815 564 GFGFKSALIRHQRTHSGE-------KPYICRECGRGFSQKSHLHRHRRTK--SGHHLLPQELFS 618
Cdd:COG5048   263 SSLPTASSQSSSPNESDSssekgfsLPIKSKQCNISFSRSSPLTRHLRSVnhSGESLKPFSCPY 326
zf-H2C2_2 pfam13465
Zinc-finger double domain;
488-510 5.93e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 37.35  E-value: 5.93e-04
                          10        20
                  ....*....|....*....|...
gi 1191866815 488 LIRHQRTHTGEKPYLCPECGHTF 510
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSF 24
zf-H2C2_2 pfam13465
Zinc-finger double domain;
432-456 9.14e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.97  E-value: 9.14e-04
                          10        20
                  ....*....|....*....|....*
gi 1191866815 432 LIRHQRTHTGEKPYLCSECGRGFSQ 456
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 249-271 1.04e-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: 1.04e-03
                          10        20
                  ....*....|....*....|...
gi 1191866815 249 HMCPECGRSFCQRSDLIKHQRTH 271
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
459-482 1.52e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.20  E-value: 1.52e-03
                          10        20
                  ....*....|....*....|....
gi 1191866815 459 SLMGHQRTHTGEKPYVCPECGRGF 482
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSF 24
SUF4-like cd20908
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
 254-295 4.10e-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: 36.38  E-value: 4.10e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1191866815 254 CGRSFCQRSDLIKHQRTHTgekpYSCRECGRGFGRKSSLTIH 295
Cdd:cd20908     7 CDREFDDEKILIQHQKAKH----FKCHICHKKLYTAGGLAVH 44
zf-H2C2_2 pfam13465
Zinc-finger double domain;
263-286 4.27e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.04  E-value: 4.27e-03
                          10        20
                  ....*....|....*....|....
gi 1191866815 263 DLIKHQRTHTGEKPYSCRECGRGF 286
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSF 24
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 417-439 7.81e-03

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


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 34.20  E-value: 7.81e-03
                          10        20
                  ....*....|....*....|...
gi 1191866815 417 YVCAECGHSFRQKVTLIRHQRTH 439
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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