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Conserved domains on  [gi|4507963|ref|NP_003399|]
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zinc finger protein 37 homolog isoform 3 [Homo sapiens]

Protein Classification

KRAB domain-containing zinc finger protein( domain architecture ID 12204268)

KRAB (Kruppel-associated box) domain-containing zinc finger protein (KRAB-ZFP) plays important roles in cell differentiation and organ development, and in regulating viral replication and transcription

CATH:  3.30.160.60
Gene Ontology:  GO:0003700|GO:0046872
PubMed:  22803940
SCOP:  4003583

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
KRAB smart00349
krueppel associated box;
42-91 4.59e-24

krueppel associated box;


:

Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 95.35  E-value: 4.59e-24
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 4507963      42 SAAEWKQLDPAQSNLYNDVMLENYCNQASMGCQAPKPDMISKLEKGEAPW 91
Cdd:smart00349  11 TQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQVPKPDLISQLEQGEEPW 60
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
273-618 5.46e-08

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


:

Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 55.47  E-value: 5.46e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507963  273 KSPSLSSSTKHEKPQACVKPYECNQCGKVLSHKQGLIDHQRVHTGEKPYECNECGIAFSQK--SHLVVHQRTHTGEKPYE 350
Cdd:COG5048  14 SVLSSTPKSTLKSLSNAPRPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYSGCDKSFSrpLELSRHLRTHHNNPSDL 93

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507963  351 CIQCGKAHGHKHALTDHLRIHTGE-KPYECAECGKTFRHSSNLIQHVRSHTGEKPYECKECGKSFR----YNSSLTEHVR 425
Cdd:COG5048  94 NSKSLPLSNSKASSSSLSSSSSNSnDNNLLSSHSLPPSSRDPQLPDLLSISNLRNNPLPGNNSSSVntpqSNSLHPPLPA 173

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507963  426 THTGEIPYECNecgkafkyssSLTKHMRIHTGEKPFECNECGKAFSKKSHLIIHQRTHTKEKPYKCNECGKAFGHSSSLT 505
Cdd:COG5048 174 NSLSKDPSSNL----------SLLISSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQ 243

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507963  506 YHMRTHTGESPFECNQCGKGFKQIEGLTQHQRVHTGE-------KPYECNECGKAFSQKSHLIVHQRT--HTGE--KPYE 574
Cdd:COG5048 244 SPSSLSSSDSSSSASESPRSSLPTASSQSSSPNESDSssekgfsLPIKSKQCNISFSRSSPLTRHLRSvnHSGEslKPFS 323

                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*.
gi 4507963  575 CNE--CEKAFNAKSQLVIHQRSHTGEKPYECNECGKTFKQNASLTK 618
Cdd:COG5048 324 CPYslCGKLFSRNDALKRHILLHTSISPAKEKLLNSSSKFSPLLNN 369
 
Name Accession Description Interval E-value
KRAB smart00349
krueppel associated box;
42-91 4.59e-24

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 95.35  E-value: 4.59e-24
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 4507963      42 SAAEWKQLDPAQSNLYNDVMLENYCNQASMGCQAPKPDMISKLEKGEAPW 91
Cdd:smart00349  11 TQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQVPKPDLISQLEQGEEPW 60
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
 33-71 1.13e-10

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: 56.79  E-value: 1.13e-10
                        10        20        30
                ....*....|....*....|....*....|....*....
gi 4507963   33 EMAVSEPEAsaaEWKQLDPAQSNLYNDVMLENYCNQASM 71
Cdd:cd07765   5 DVAVYFSQE---EWELLDPAQRDLYRDVMLENYENLVSL 40
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
 45-72 1.75e-09

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: 53.24  E-value: 1.75e-09
                          10        20
                  ....*....|....*....|....*...
gi 4507963     45 EWKQLDPAQSNLYNDVMLENYCNQASMG 72
Cdd:pfam01352  15 EWALLDPAQRNLYRDVMLENYRNLVSLG 42
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
273-618 5.46e-08

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 55.47  E-value: 5.46e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507963  273 KSPSLSSSTKHEKPQACVKPYECNQCGKVLSHKQGLIDHQRVHTGEKPYECNECGIAFSQK--SHLVVHQRTHTGEKPYE 350
Cdd:COG5048  14 SVLSSTPKSTLKSLSNAPRPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYSGCDKSFSrpLELSRHLRTHHNNPSDL 93

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507963  351 CIQCGKAHGHKHALTDHLRIHTGE-KPYECAECGKTFRHSSNLIQHVRSHTGEKPYECKECGKSFR----YNSSLTEHVR 425
Cdd:COG5048  94 NSKSLPLSNSKASSSSLSSSSSNSnDNNLLSSHSLPPSSRDPQLPDLLSISNLRNNPLPGNNSSSVntpqSNSLHPPLPA 173

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507963  426 THTGEIPYECNecgkafkyssSLTKHMRIHTGEKPFECNECGKAFSKKSHLIIHQRTHTKEKPYKCNECGKAFGHSSSLT 505
Cdd:COG5048 174 NSLSKDPSSNL----------SLLISSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQ 243

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507963  506 YHMRTHTGESPFECNQCGKGFKQIEGLTQHQRVHTGE-------KPYECNECGKAFSQKSHLIVHQRT--HTGE--KPYE 574
Cdd:COG5048 244 SPSSLSSSDSSSSASESPRSSLPTASSQSSSPNESDSssekgfsLPIKSKQCNISFSRSSPLTRHLRSvnHSGEslKPFS 323

                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*.
gi 4507963  575 CNE--CEKAFNAKSQLVIHQRSHTGEKPYECNECGKTFKQNASLTK 618
Cdd:COG5048 324 CPYslCGKLFSRNDALKRHILLHTSISPAKEKLLNSSSKFSPLLNN 369
zf-H2C2_2 pfam13465
Zinc-finger double domain;
391-416 1.83e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.89  E-value: 1.83e-04
                          10        20
                  ....*....|....*....|....*.
gi 4507963    391 NLIQHVRSHTGEKPYECKECGKSFRY 416
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
SUF4-like cd20908
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
 459-510 1.28e-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: 37.92  E-value: 1.28e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 4507963  459 KPFeCNECGKAFSKKSHLIIHQRTHTkekpYKCNECGKAFGHSSSLTYHMRT 510
Cdd:cd20908   1 KPW-CYYCDREFDDEKILIQHQKAKH----FKCHICHKKLYTAGGLAVHCLQ 47
PLN03086 PLN03086
PRLI-interacting factor K; Provisional
 435-566 8.01e-03

PRLI-interacting factor K; Provisional


Pssm-ID: 178635 [Multi-domain]  Cd Length: 567  Bit Score: 39.08  E-value: 8.01e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507963   435 CNECGKAFKySSSLTKHMRIHtgEKPFECnECGKAFsKKSHLIIHQRTHTKEKPYKCNECGKAfghsssltyhmrTHTGE 514
Cdd:PLN03086 456 CEKCGQAFQ-QGEMEKHMKVF--HEPLQC-PCGVVL-EKEQMVQHQASTCPLRLITCRFCGDM------------VQAGG 518

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 4507963   515 SPFECNQcgkgfkQIEGLTQHQRVhTGEKPYECNECGKAFSQKS---HLI-VHQRT 566
Cdd:PLN03086 519 SAMDVRD------RLRGMSEHESI-CGSRTAPCDSCGRSVMLKEmdiHQIaVHQKS 567
 
Name Accession Description Interval E-value
KRAB smart00349
krueppel associated box;
42-91 4.59e-24

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 95.35  E-value: 4.59e-24
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 4507963      42 SAAEWKQLDPAQSNLYNDVMLENYCNQASMGCQAPKPDMISKLEKGEAPW 91
Cdd:smart00349  11 TQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQVPKPDLISQLEQGEEPW 60
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
 33-71 1.13e-10

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: 56.79  E-value: 1.13e-10
                        10        20        30
                ....*....|....*....|....*....|....*....
gi 4507963   33 EMAVSEPEAsaaEWKQLDPAQSNLYNDVMLENYCNQASM 71
Cdd:cd07765   5 DVAVYFSQE---EWELLDPAQRDLYRDVMLENYENLVSL 40
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
 45-72 1.75e-09

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: 53.24  E-value: 1.75e-09
                          10        20
                  ....*....|....*....|....*...
gi 4507963     45 EWKQLDPAQSNLYNDVMLENYCNQASMG 72
Cdd:pfam01352  15 EWALLDPAQRNLYRDVMLENYRNLVSLG 42
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
273-618 5.46e-08

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 55.47  E-value: 5.46e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507963  273 KSPSLSSSTKHEKPQACVKPYECNQCGKVLSHKQGLIDHQRVHTGEKPYECNECGIAFSQK--SHLVVHQRTHTGEKPYE 350
Cdd:COG5048  14 SVLSSTPKSTLKSLSNAPRPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYSGCDKSFSrpLELSRHLRTHHNNPSDL 93

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507963  351 CIQCGKAHGHKHALTDHLRIHTGE-KPYECAECGKTFRHSSNLIQHVRSHTGEKPYECKECGKSFR----YNSSLTEHVR 425
Cdd:COG5048  94 NSKSLPLSNSKASSSSLSSSSSNSnDNNLLSSHSLPPSSRDPQLPDLLSISNLRNNPLPGNNSSSVntpqSNSLHPPLPA 173

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507963  426 THTGEIPYECNecgkafkyssSLTKHMRIHTGEKPFECNECGKAFSKKSHLIIHQRTHTKEKPYKCNECGKAFGHSSSLT 505
Cdd:COG5048 174 NSLSKDPSSNL----------SLLISSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQ 243

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507963  506 YHMRTHTGESPFECNQCGKGFKQIEGLTQHQRVHTGE-------KPYECNECGKAFSQKSHLIVHQRT--HTGE--KPYE 574
Cdd:COG5048 244 SPSSLSSSDSSSSASESPRSSLPTASSQSSSPNESDSssekgfsLPIKSKQCNISFSRSSPLTRHLRSvnHSGEslKPFS 323

                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*.
gi 4507963  575 CNE--CEKAFNAKSQLVIHQRSHTGEKPYECNECGKTFKQNASLTK 618
Cdd:COG5048 324 CPYslCGKLFSRNDALKRHILLHTSISPAKEKLLNSSSKFSPLLNN 369
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
367-613 8.38e-07

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 52.01  E-value: 8.38e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507963  367 HLRIHTGEKPYECAECGKTFRHSSNLIQHVRSHTGEKPYECKECGKSF------RYNSSLTEHVRTHTGEIPYECNECGK 440
Cdd:COG5048 189 SSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSpksllsQSPSSLSSSDSSSSASESPRSSLPTA 268

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507963  441 AFKYSSSLTKHMRIHTG-EKPFECNECGKAFSKKSHLIIHQRT--HTKE--KPYKCNE--CGKAFGHSSSLTYHMRTHTG 513
Cdd:COG5048 269 SSQSSSPNESDSSSEKGfSLPIKSKQCNISFSRSSPLTRHLRSvnHSGEslKPFSCPYslCGKLFSRNDALKRHILLHTS 348

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507963  514 ESPFEC--NQCGKGFKQI-----EGLTQHQRVHTGEKPYEC--NECGKAFSQKSHLIVHQRTHTGEKPYECN--ECEKAF 582
Cdd:COG5048 349 ISPAKEklLNSSSKFSPLlnnepPQSLQQYKDLKNDKKSETlsNSCIRNFKRDSNLSLHIITHLSFRPYNCKnpPCSKSF 428

                       250       260       270
                ....*....|....*....|....*....|.
gi 4507963  583 NAKSQLVIHQRSHTGEKPYECNECGKTFKQN 613
Cdd:COG5048 429 NRHYNLIPHKKIHTNHAPLLCSILKSFRRDL 459
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
165-499 2.26e-06

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 50.46  E-value: 2.26e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507963  165 KKHVPSKKRLLKFESCGKILKQNLDLPDHSRNCVKRKSDAAKEHKKSFNHSLSDTRKGKKQTGKKHEKLSSHSSSDKCNK 244
Cdd:COG5048  98 LPLSNSKASSSSLSSSSSNSNDNNLLSSHSLPPSSRDPQLPDLLSISNLRNNPLPGNNSSSVNTPQSNSLHPPLPANSLS 177

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507963  245 TGK-KHDKLCCHSSSHIKQDKIQTGEKHEKSPSLSSSTKHEKPQACVKPYECNQCGKVLSH------KQGLIDHQRVHTG 317
Cdd:COG5048 178 KDPsSNLSLLISSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKsllsqsPSSLSSSDSSSSA 257

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507963  318 EKPYECNECGIAFSQKSHLVVHQRTHTG-EKPYECIQCGKAHGHKHALTDHLR--IHTGE--KPYECAE--CGKTFRHSS 390
Cdd:COG5048 258 SESPRSSLPTASSQSSSPNESDSSSEKGfSLPIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCPYslCGKLFSRND 337

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507963  391 NLIQHVRSHTGEKPYECKECGKSFRYNSSLTE-------HVRTHTGEIPYEC--NECGKAFKYSSSLTKHMRIHTGEKP- 460
Cdd:COG5048 338 ALKRHILLHTSISPAKEKLLNSSSKFSPLLNNeppqslqQYKDLKNDKKSETlsNSCIRNFKRDSNLSLHIITHLSFRPy 417

                       330       340       350       360
                ....*....|....*....|....*....|....*....|
gi 4507963  461 -FECNECGKAFSKKSHLIIHQRTHTKEKPYKCNECGKAFG 499
Cdd:COG5048 418 nCKNPPCSKSFNRHYNLIPHKKIHTNHAPLLCSILKSFRR 457
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
375-629 1.81e-04

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 44.30  E-value: 1.81e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507963  375 KPYECAECGKTFRHSSNLIQHVRSHTGEKPYEC--KECGKSFRYNSSLTEHVRTHTGEIPYECNECGKAFKYSSSLTKHM 452
Cdd:COG5048  32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCsySGCDKSFSRPLELSRHLRTHHNNPSDLNSKSLPLSNSKASSSSLS 111

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507963  453 RIHTGEKPFE-CNECGKAFSKKSHLIIHQRTHTKEKPYKCNECGKAFGHSS----------------------SLTYHMR 509
Cdd:COG5048 112 SSSSNSNDNNlLSSHSLPPSSRDPQLPDLLSISNLRNNPLPGNNSSSVNTPqsnslhpplpanslskdpssnlSLLISSN 191

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507963  510 THTGESPFECNQCGKGFKQIEGLTQHQRVHTGEKPYECNECGKAF------SQKSHLIVHQRTHTGEKPYECNECEKAFN 583
Cdd:COG5048 192 VSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSpksllsQSPSSLSSSDSSSSASESPRSSLPTASSQ 271

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*..
gi 4507963  584 AKSQLVIHQRSHTG-EKPYECNECGKTFKQNASLTKHVKTHSEDKSH 629
Cdd:COG5048 272 SSSPNESDSSSEKGfSLPIKSKQCNISFSRSSPLTRHLRSVNHSGES 318
zf-H2C2_2 pfam13465
Zinc-finger double domain;
391-416 1.83e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.89  E-value: 1.83e-04
                          10        20
                  ....*....|....*....|....*.
gi 4507963    391 NLIQHVRSHTGEKPYECKECGKSFRY 416
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
447-472 1.86e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.89  E-value: 1.86e-04
                          10        20
                  ....*....|....*....|....*.
gi 4507963    447 SLTKHMRIHTGEKPFECNECGKAFSK 472
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
543-630 5.39e-04

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 42.76  E-value: 5.39e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507963  543 KPYECNECGKAFSQKSHLIVHQRTHTGEKPYECN--ECEKAFNAKSQLVIHQRSHTGEKPYECNECGKTFKQNASLTKHV 620
Cdd:COG5048  32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSysGCDKSFSRPLELSRHLRTHHNNPSDLNSKSLPLSNSKASSSSLS 111

                        90
                ....*....|
gi 4507963  621 KTHSEDKSHE 630
Cdd:COG5048 112 SSSSNSNDNN 121
zf-H2C2_2 pfam13465
Zinc-finger double domain;
503-528 7.65e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.97  E-value: 7.65e-04
                          10        20
                  ....*....|....*....|....*.
gi 4507963    503 SLTYHMRTHTGESPFECNQCGKGFKQ 528
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
532-556 8.27e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.97  E-value: 8.27e-04
                          10        20
                  ....*....|....*....|....*
gi 4507963    532 LTQHQRVHTGEKPYECNECGKAFSQ 556
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 545-567 1.03e-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: 1.03e-03
                          10        20
                  ....*....|....*....|...
gi 4507963    545 YECNECGKAFSQKSHLIVHQRTH 567
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
363-388 1.20e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.58  E-value: 1.20e-03
                          10        20
                  ....*....|....*....|....*.
gi 4507963    363 ALTDHLRIHTGEKPYECAECGKTFRH 388
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
SUF4-like cd20908
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
 459-510 1.28e-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: 37.92  E-value: 1.28e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 4507963  459 KPFeCNECGKAFSKKSHLIIHQRTHTkekpYKCNECGKAFGHSSSLTYHMRT 510
Cdd:cd20908   1 KPW-CYYCDREFDDEKILIQHQKAKH----FKCHICHKKLYTAGGLAVHCLQ 47
zf-H2C2_2 pfam13465
Zinc-finger double domain;
588-612 1.58e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.20  E-value: 1.58e-03
                          10        20
                  ....*....|....*....|....*
gi 4507963    588 LVIHQRSHTGEKPYECNECGKTFKQ 612
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
559-583 1.60e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.20  E-value: 1.60e-03
                          10        20
                  ....*....|....*....|....*
gi 4507963    559 HLIVHQRTHTGEKPYECNECEKAFN 583
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFK 25
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 433-455 1.62e-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: 36.12  E-value: 1.62e-03
                          10        20
                  ....*....|....*....|...
gi 4507963    433 YECNECGKAFKYSSSLTKHMRIH 455
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 461-483 2.16e-03

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


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 35.74  E-value: 2.16e-03
                          10        20
                  ....*....|....*....|...
gi 4507963    461 FECNECGKAFSKKSHLIIHQRTH 483
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
419-444 2.28e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.81  E-value: 2.28e-03
                          10        20
                  ....*....|....*....|....*.
gi 4507963    419 SLTEHVRTHTGEIPYECNECGKAFKY 444
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
475-498 2.97e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.42  E-value: 2.97e-03
                          10        20
                  ....*....|....*....|....
gi 4507963    475 HLIIHQRTHTKEKPYKCNECGKAF 498
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSF 24
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 489-511 4.55e-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: 4.55e-03
                          10        20
                  ....*....|....*....|...
gi 4507963    489 YKCNECGKAFGHSSSLTYHMRTH 511
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 405-427 5.87e-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: 5.87e-03
                          10        20
                  ....*....|....*....|...
gi 4507963    405 YECKECGKSFRYNSSLTEHVRTH 427
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 601-623 6.17e-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: 6.17e-03
                          10        20
                  ....*....|....*....|...
gi 4507963    601 YECNECGKTFKQNASLTKHVKTH 623
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
335-357 6.45e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 34.65  E-value: 6.45e-03
                          10        20
                  ....*....|....*....|...
gi 4507963    335 HLVVHQRTHTGEKPYECIQCGKA 357
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKS 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 377-399 7.43e-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: 7.43e-03
                          10        20
                  ....*....|....*....|...
gi 4507963    377 YECAECGKTFRHSSNLIQHVRSH 399
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
PLN03086 PLN03086
PRLI-interacting factor K; Provisional
 435-566 8.01e-03

PRLI-interacting factor K; Provisional


Pssm-ID: 178635 [Multi-domain]  Cd Length: 567  Bit Score: 39.08  E-value: 8.01e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507963   435 CNECGKAFKySSSLTKHMRIHtgEKPFECnECGKAFsKKSHLIIHQRTHTKEKPYKCNECGKAfghsssltyhmrTHTGE 514
Cdd:PLN03086 456 CEKCGQAFQ-QGEMEKHMKVF--HEPLQC-PCGVVL-EKEQMVQHQASTCPLRLITCRFCGDM------------VQAGG 518

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 4507963   515 SPFECNQcgkgfkQIEGLTQHQRVhTGEKPYECNECGKAFSQKS---HLI-VHQRT 566
Cdd:PLN03086 519 SAMDVRD------RLRGMSEHESI-CGSRTAPCDSCGRSVMLKEmdiHQIaVHQKS 567
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 321-343 8.20e-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: 8.20e-03
                          10        20
                  ....*....|....*....|...
gi 4507963    321 YECNECGIAFSQKSHLVVHQRTH 343
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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