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Conserved domains on  [gi|148699212|gb|EDL31159|]
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zinc finger protein 37, isoform CRA_b [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
66-390 2.09e-09

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


:

Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 59.32  E-value: 2.09e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148699212  66 PSKPEKAPGSGKPYECNHCGKVLSHKQGLLDHQRTHTGEKPYECNECGIAFSQK--SHLVVHQRTHTGEKPYECEQCGKA 143
Cdd:COG5048   21 KSTLKSLSNAPRPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYSGCDKSFSrpLELSRHLRTHHNNPSDLNSKSLPL 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148699212 144 HGHKHALTDHLRIHTGE-KPYKCNECGKTFRHSSNLMQHLRSHTGEKPYECKECGKSFR----YNSSLTEHVRTHTGEIP 218
Cdd:COG5048  101 SNSKASSSSLSSSSSNSnDNNLLSSHSLPPSSRDPQLPDLLSISNLRNNPLPGNNSSSVntpqSNSLHPPLPANSLSKDP 180

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148699212 219 YECNecgkafkygsSLTKHMRIHTGEKPFECNECGKTFSKKSHLVIHQRTHTKEKPYKCDECGKAFGHSSSLTYHMRTHT 298
Cdd:COG5048  181 SSNL----------SLLISSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLSS 250

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148699212 299 GDCPFECNQCGKAFKQIEGLTQHQRVHTGE-------KPYECVECGKAFSQKSHLIVHQRT--HTGE--KPFECYE--CG 365
Cdd:COG5048  251 SDSSSSASESPRSSLPTASSQSSSPNESDSssekgfsLPIKSKQCNISFSRSSPLTRHLRSvnHSGEslKPFSCPYslCG 330

                        330       340
                 ....*....|....*....|....*
gi 148699212 366 KAFNAKSQLVIHQRSHTGEKPYECI 390
Cdd:COG5048  331 KLFSRNDALKRHILLHTSISPAKEK 355
KRAB super family cl42959
krueppel associated box;
12-39 2.86e-09

krueppel associated box;


The actual alignment was detected with superfamily member smart00349:

Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 52.98  E-value: 2.86e-09
                           10        20
                   ....*....|....*....|....*...
gi 148699212    12 KEWEQLEPVQRDVYKDTKLENCSNPASM 39
Cdd:smart00349  13 EEWEQLDPAQKNLYRDVMLENYSNLVSL 40
 
Name Accession Description Interval E-value
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
66-390 2.09e-09

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 59.32  E-value: 2.09e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148699212  66 PSKPEKAPGSGKPYECNHCGKVLSHKQGLLDHQRTHTGEKPYECNECGIAFSQK--SHLVVHQRTHTGEKPYECEQCGKA 143
Cdd:COG5048   21 KSTLKSLSNAPRPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYSGCDKSFSrpLELSRHLRTHHNNPSDLNSKSLPL 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148699212 144 HGHKHALTDHLRIHTGE-KPYKCNECGKTFRHSSNLMQHLRSHTGEKPYECKECGKSFR----YNSSLTEHVRTHTGEIP 218
Cdd:COG5048  101 SNSKASSSSLSSSSSNSnDNNLLSSHSLPPSSRDPQLPDLLSISNLRNNPLPGNNSSSVntpqSNSLHPPLPANSLSKDP 180

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148699212 219 YECNecgkafkygsSLTKHMRIHTGEKPFECNECGKTFSKKSHLVIHQRTHTKEKPYKCDECGKAFGHSSSLTYHMRTHT 298
Cdd:COG5048  181 SSNL----------SLLISSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLSS 250

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148699212 299 GDCPFECNQCGKAFKQIEGLTQHQRVHTGE-------KPYECVECGKAFSQKSHLIVHQRT--HTGE--KPFECYE--CG 365
Cdd:COG5048  251 SDSSSSASESPRSSLPTASSQSSSPNESDSssekgfsLPIKSKQCNISFSRSSPLTRHLRSvnHSGEslKPFSCPYslCG 330

                        330       340
                 ....*....|....*....|....*
gi 148699212 366 KAFNAKSQLVIHQRSHTGEKPYECI 390
Cdd:COG5048  331 KLFSRNDALKRHILLHTSISPAKEK 355
KRAB smart00349
krueppel associated box;
12-39 2.86e-09

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 52.98  E-value: 2.86e-09
                           10        20
                   ....*....|....*....|....*...
gi 148699212    12 KEWEQLEPVQRDVYKDTKLENCSNPASM 39
Cdd:smart00349  13 EEWEQLDPAQKNLYRDVMLENYSNLVSL 40
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
 1-39 1.54e-08

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: 50.24  E-value: 1.54e-08
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 148699212   1 MATSEPAEsdakEWEQLEPVQRDVYKDTKLENCSNPASM 39
Cdd:cd07765    6 VAVYFSQE----EWELLDPAQRDLYRDVMLENYENLVSL 40
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
 12-39 8.67e-06

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: 42.46  E-value: 8.67e-06
                          10        20
                  ....*....|....*....|....*...
gi 148699212   12 KEWEQLEPVQRDVYKDTKLENCSNPASM 39
Cdd:pfam01352  14 EEWALLDPAQRNLYRDVMLENYRNLVSL 41
zf-H2C2_2 pfam13465
Zinc-finger double domain;
177-202 1.17e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.89  E-value: 1.17e-04
                          10        20
                  ....*....|....*....|....*.
gi 148699212  177 NLMQHLRSHTGEKPYECKECGKSFRY 202
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
SUF4-like cd20908
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
 245-296 3.88e-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: 36.00  E-value: 3.88e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 148699212 245 KPFeCNECGKTFSKKSHLVIHQRTHTkekpYKCDECGKAFGHSSSLTYHMRT 296
Cdd:cd20908    1 KPW-CYYCDREFDDEKILIQHQKAKH----FKCHICHKKLYTAGGLAVHCLQ 47
 
Name Accession Description Interval E-value
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
66-390 2.09e-09

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 59.32  E-value: 2.09e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148699212  66 PSKPEKAPGSGKPYECNHCGKVLSHKQGLLDHQRTHTGEKPYECNECGIAFSQK--SHLVVHQRTHTGEKPYECEQCGKA 143
Cdd:COG5048   21 KSTLKSLSNAPRPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYSGCDKSFSrpLELSRHLRTHHNNPSDLNSKSLPL 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148699212 144 HGHKHALTDHLRIHTGE-KPYKCNECGKTFRHSSNLMQHLRSHTGEKPYECKECGKSFR----YNSSLTEHVRTHTGEIP 218
Cdd:COG5048  101 SNSKASSSSLSSSSSNSnDNNLLSSHSLPPSSRDPQLPDLLSISNLRNNPLPGNNSSSVntpqSNSLHPPLPANSLSKDP 180

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148699212 219 YECNecgkafkygsSLTKHMRIHTGEKPFECNECGKTFSKKSHLVIHQRTHTKEKPYKCDECGKAFGHSSSLTYHMRTHT 298
Cdd:COG5048  181 SSNL----------SLLISSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLSS 250

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148699212 299 GDCPFECNQCGKAFKQIEGLTQHQRVHTGE-------KPYECVECGKAFSQKSHLIVHQRT--HTGE--KPFECYE--CG 365
Cdd:COG5048  251 SDSSSSASESPRSSLPTASSQSSSPNESDSssekgfsLPIKSKQCNISFSRSSPLTRHLRSvnHSGEslKPFSCPYslCG 330

                        330       340
                 ....*....|....*....|....*
gi 148699212 366 KAFNAKSQLVIHQRSHTGEKPYECI 390
Cdd:COG5048  331 KLFSRNDALKRHILLHTSISPAKEK 355
KRAB smart00349
krueppel associated box;
12-39 2.86e-09

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 52.98  E-value: 2.86e-09
                           10        20
                   ....*....|....*....|....*...
gi 148699212    12 KEWEQLEPVQRDVYKDTKLENCSNPASM 39
Cdd:smart00349  13 EEWEQLDPAQKNLYRDVMLENYSNLVSL 40
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
 1-39 1.54e-08

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: 50.24  E-value: 1.54e-08
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 148699212   1 MATSEPAEsdakEWEQLEPVQRDVYKDTKLENCSNPASM 39
Cdd:cd07765    6 VAVYFSQE----EWELLDPAQRDLYRDVMLENYENLVSL 40
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
153-399 3.03e-08

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 55.47  E-value: 3.03e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148699212 153 HLRIHTGEKPYKCNECGKTFRHSSNLMQHLRSHTGEKPYECKECGKSF------RYNSSLTEHVRTHTGEIPYECNECGK 226
Cdd:COG5048  189 SSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSpksllsQSPSSLSSSDSSSSASESPRSSLPTA 268

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148699212 227 AFKYGSSLTKHMRIHTG-EKPFECNECGKTFSKKSHLVIHQRT--HTKE--KPYKCDE--CGKAFGHSSSLTYHMRTHTG 299
Cdd:COG5048  269 SSQSSSPNESDSSSEKGfSLPIKSKQCNISFSRSSPLTRHLRSvnHSGEslKPFSCPYslCGKLFSRNDALKRHILLHTS 348

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148699212 300 DCPFEC--NQCGKAFKQI-----EGLTQHQRVHTGEKPYECV--ECGKAFSQKSHLIVHQRTHTGEKPFECY--ECGKAF 368
Cdd:COG5048  349 ISPAKEklLNSSSKFSPLlnnepPQSLQQYKDLKNDKKSETLsnSCIRNFKRDSNLSLHIITHLSFRPYNCKnpPCSKSF 428

                        250       260       270
                 ....*....|....*....|....*....|.
gi 148699212 369 NAKSQLVIHQRSHTGEKPYECIECGKAFKQN 399
Cdd:COG5048  429 NRHYNLIPHKKIHTNHAPLLCSILKSFRRDL 459
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
42-285 1.69e-06

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 50.08  E-value: 1.69e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148699212  42 RHSASHTKEDKIQTGEKRKSHCRTPSKPEKAPGSGKPYECNHCGK---VLSHKQGLLDHQRTHTGEKPYECNECGIAFSQ 118
Cdd:COG5048  193 STSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPkslLSQSPSSLSSSDSSSSASESPRSSLPTASSQS 272

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148699212 119 KSHLVVHQRTHTG-EKPYECEQCGKAHGHKHALTDHLR--IHTGE--KPYKCNE--CGKTFRHSSNLMQHLRSHTGEKPY 191
Cdd:COG5048  273 SSPNESDSSSEKGfSLPIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCPYslCGKLFSRNDALKRHILLHTSISPA 352

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148699212 192 ECKECGKSFRYNSSLTE-------HVRTHTGEIPYEC--NECGKAFKYGSSLTKHMRIHTGEKP--FECNECGKTFSKKS 260
Cdd:COG5048  353 KEKLLNSSSKFSPLLNNeppqslqQYKDLKNDKKSETlsNSCIRNFKRDSNLSLHIITHLSFRPynCKNPPCSKSFNRHY 432

                        250       260
                 ....*....|....*....|....*
gi 148699212 261 HLVIHQRTHTKEKPYKCDECGKAFG 285
Cdd:COG5048  433 NLIPHKKIHTNHAPLLCSILKSFRR 457
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
 12-39 8.67e-06

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: 42.46  E-value: 8.67e-06
                          10        20
                  ....*....|....*....|....*...
gi 148699212   12 KEWEQLEPVQRDVYKDTKLENCSNPASM 39
Cdd:pfam01352  14 EEWALLDPAQRNLYRDVMLENYRNLVSL 41
zf-H2C2_2 pfam13465
Zinc-finger double domain;
177-202 1.17e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.89  E-value: 1.17e-04
                          10        20
                  ....*....|....*....|....*.
gi 148699212  177 NLMQHLRSHTGEKPYECKECGKSFRY 202
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
161-416 1.18e-04

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 44.30  E-value: 1.18e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148699212 161 KPYKCNECGKTFRHSSNLMQHLRSHTGEKPYEC--KECGKSFRYNSSLTEHVRTHTGEIPYECNECGKAFKYGSSLTKHM 238
Cdd:COG5048   32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCsySGCDKSFSRPLELSRHLRTHHNNPSDLNSKSLPLSNSKASSSSLS 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148699212 239 RIHTGEKPFE-CNECGKTFSKKSHLVIHQRTHTKEKPYKCDECGKAFGHSS----------------------SLTYHMR 295
Cdd:COG5048  112 SSSSNSNDNNlLSSHSLPPSSRDPQLPDLLSISNLRNNPLPGNNSSSVNTPqsnslhpplpanslskdpssnlSLLISSN 191

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148699212 296 THTGDCPFECNQCGKAFKQIEGLTQHQRVHTGEKPYECVECGKAF------SQKSHLIVHQRTHTGEKPFECYECGKAFN 369
Cdd:COG5048  192 VSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSpksllsQSPSSLSSSDSSSSASESPRSSLPTASSQ 271

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 148699212 370 AKSQLVIHQRSHTG-EKPYECIECGKAFKQNASLTKHM--KIHSEEQSEE 416
Cdd:COG5048  272 SSSPNESDSSSEKGfSLPIKSKQCNISFSRSSPLTRHLrsVNHSGESLKP 321
zf-H2C2_2 pfam13465
Zinc-finger double domain;
233-258 5.38e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.97  E-value: 5.38e-04
                          10        20
                  ....*....|....*....|....*.
gi 148699212  233 SLTKHMRIHTGEKPFECNECGKTFSK 258
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
149-174 1.20e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.20  E-value: 1.20e-03
                          10        20
                  ....*....|....*....|....*.
gi 148699212  149 ALTDHLRIHTGEKPYKCNECGKTFRH 174
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
374-398 1.95e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.42  E-value: 1.95e-03
                          10        20
                  ....*....|....*....|....*
gi 148699212  374 LVIHQRSHTGEKPYECIECGKAFKQ 398
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 163-185 2.10e-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: 2.10e-03
                          10        20
                  ....*....|....*....|...
gi 148699212  163 YKCNECGKTFRHSSNLMQHLRSH 185
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
345-369 2.21e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.42  E-value: 2.21e-03
                          10        20
                  ....*....|....*....|....*
gi 148699212  345 HLIVHQRTHTGEKPFECYECGKAFN 369
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFK 25
zf-H2C2_2 pfam13465
Zinc-finger double domain;
261-284 2.64e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.04  E-value: 2.64e-03
                          10        20
                  ....*....|....*....|....
gi 148699212  261 HLVIHQRTHTKEKPYKCDECGKAF 284
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSF 24
SUF4-like cd20908
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
 245-296 3.88e-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: 36.00  E-value: 3.88e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 148699212 245 KPFeCNECGKTFSKKSHLVIHQRTHTkekpYKCDECGKAFGHSSSLTYHMRT 296
Cdd:cd20908    1 KPW-CYYCDREFDDEKILIQHQKAKH----FKCHICHKKLYTAGGLAVHCLQ 47
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
357-418 3.97e-03

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 39.29  E-value: 3.97e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 148699212 357 KPFECYECGKAFNAKSQLVIHQRSHTGEKPYEC--IECGKAFKQNASLTKHMKIHSEEQSEEED 418
Cdd:COG5048   32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCsySGCDKSFSRPLELSRHLRTHHNNPSDLNS 95
zf-H2C2_2 pfam13465
Zinc-finger double domain;
205-230 4.40e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 34.65  E-value: 4.40e-03
                          10        20
                  ....*....|....*....|....*.
gi 148699212  205 SLTEHVRTHTGEIPYECNECGKAFKY 230
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 247-269 4.61e-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: 4.61e-03
                          10        20
                  ....*....|....*....|...
gi 148699212  247 FECNECGKTFSKKSHLVIHQRTH 269
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 331-353 7.09e-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: 7.09e-03
                          10        20
                  ....*....|....*....|...
gi 148699212  331 YECVECGKAFSQKSHLIVHQRTH 353
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
289-314 7.94e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 33.88  E-value: 7.94e-03
                          10        20
                  ....*....|....*....|....*.
gi 148699212  289 SLTYHMRTHTGDCPFECNQCGKAFKQ 314
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
 
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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