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Conserved domains on  [gi|1958789702|ref|XP_038935178|]
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zinc finger protein 7 isoform X4 [Rattus norvegicus]

Protein Classification

KRAB domain-containing zinc finger protein( domain architecture ID 12204378)

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:0003700|GO:0005515|GO:0008270|GO:0003677|GO:0006355|GO:0001217
PubMed:  22803940|8183940|2023909|8183939|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;
3-62 8.76e-31

krueppel associated box;


:

Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 114.61  E-value: 8.76e-31
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789702    3 VTFGDVAVHFSREEWQCLDSGQRALYREVMLENHSSVAGLGFLVFKPELISRLEQGQEPW 62
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQVPKPDLISQLEQGEEPW 60
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
229-618 3.65e-20

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


:

Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 93.99  E-value: 3.65e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789702 229 KKPYGCEECGKVFRLCSQLNQHQRIHTGEKPFKC--VDCGKGFRLSSKLIQHQRIHTGEKPYRCEECGKT--FGQSSSLI 304
Cdd:COG5048    31 PRPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCsySGCDKSFSRPLELSRHLRTHHNNPSDLNSKSLPLsnSKASSSSL 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789702 305 HHQrIHTGERPYSCQECGKSFSQQSQLVRHQRTHTGERPYPCQECGKAFSQ----SSTLAQHQRMHTGEKSQMPRASGSP 380
Cdd:COG5048   111 SSS-SSNSNDNNLLSSHSLPPSSRDPQLPDLLSISNLRNNPLPGNNSSSVNtpqsNSLHPPLPANSLSKDPSSNLSLLIS 189

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789702 381 SllarqRNNTVEKPFKCEECGKAFRWISRLNQHQLIHTGEKPYKCNKCTKAFGCSSRLIRHQRTHTGEKPFKCEECGKGF 460
Cdd:COG5048   190 S-----NVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLSSSDSSSSASESPRSS 264

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789702 461 VQGSHLIQHQRIHTGE-------KPYVCDDCGKAFSQSSSLIYHQR--IHKGE--KPYEC--IQCGKAFSMSTQLTSHQR 527
Cdd:COG5048   265 LPTASSQSSSPNESDSssekgfsLPIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCpySLCGKLFSRNDALKRHIL 344

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789702 528 IHTGERPYKC--SECGKAFSQNST-----LFQHQIIHAGVKPYEC--SECGKAFSRSSYLIEHqRIHTRAQWYYEFGNTT 598
Cdd:COG5048   345 LHTSISPAKEklLNSSSKFSPLLNneppqSLQQYKDLKNDKKSETlsNSCIRNFKRDSNLSLH-IITHLSFRPYNCKNPP 423

                         410       420
                  ....*....|....*....|
gi 1958789702 599 ESSTFLNHKKVNPVKKLHQC 618
Cdd:COG5048   424 CSKSFNRHYNLIPHKKIHTN 443
zf-H2C2_2 pfam13465
Zinc-finger double domain;
630-655 4.20e-04

Zinc-finger double domain;


:

Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 37.74  E-value: 4.20e-04
                          10        20
                  ....*....|....*....|....*.
gi 1958789702 630 HLVIHQRIHTGEKPYRCNACGKAFNR 655
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
 
Name Accession Description Interval E-value
KRAB smart00349
krueppel associated box;
3-62 8.76e-31

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 114.61  E-value: 8.76e-31
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789702    3 VTFGDVAVHFSREEWQCLDSGQRALYREVMLENHSSVAGLGFLVFKPELISRLEQGQEPW 62
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQVPKPDLISQLEQGEEPW 60
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
229-618 3.65e-20

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 93.99  E-value: 3.65e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789702 229 KKPYGCEECGKVFRLCSQLNQHQRIHTGEKPFKC--VDCGKGFRLSSKLIQHQRIHTGEKPYRCEECGKT--FGQSSSLI 304
Cdd:COG5048    31 PRPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCsySGCDKSFSRPLELSRHLRTHHNNPSDLNSKSLPLsnSKASSSSL 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789702 305 HHQrIHTGERPYSCQECGKSFSQQSQLVRHQRTHTGERPYPCQECGKAFSQ----SSTLAQHQRMHTGEKSQMPRASGSP 380
Cdd:COG5048   111 SSS-SSNSNDNNLLSSHSLPPSSRDPQLPDLLSISNLRNNPLPGNNSSSVNtpqsNSLHPPLPANSLSKDPSSNLSLLIS 189

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789702 381 SllarqRNNTVEKPFKCEECGKAFRWISRLNQHQLIHTGEKPYKCNKCTKAFGCSSRLIRHQRTHTGEKPFKCEECGKGF 460
Cdd:COG5048   190 S-----NVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLSSSDSSSSASESPRSS 264

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789702 461 VQGSHLIQHQRIHTGE-------KPYVCDDCGKAFSQSSSLIYHQR--IHKGE--KPYEC--IQCGKAFSMSTQLTSHQR 527
Cdd:COG5048   265 LPTASSQSSSPNESDSssekgfsLPIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCpySLCGKLFSRNDALKRHIL 344

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789702 528 IHTGERPYKC--SECGKAFSQNST-----LFQHQIIHAGVKPYEC--SECGKAFSRSSYLIEHqRIHTRAQWYYEFGNTT 598
Cdd:COG5048   345 LHTSISPAKEklLNSSSKFSPLLNneppqSLQQYKDLKNDKKSETlsNSCIRNFKRDSNLSLH-IITHLSFRPYNCKNPP 423

                         410       420
                  ....*....|....*....|
gi 1958789702 599 ESSTFLNHKKVNPVKKLHQC 618
Cdd:COG5048   424 CSKSFNRHYNLIPHKKIHTN 443
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
 3-43 1.64e-19

KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc finger proteins containing C2H2 fingers. The KRAB domain is found to be involved in protein-protein interactions. The KRAB domain is generally encoded by two exons. The regions coded by the two exons are known as KRAB-A and KRAB-B. The A box plays an important role in repression by binding to corepressors, while the B box is thought to enhance this repression brought about by the A box. KRAB-containing proteins are thought to have critical functions in cell proliferation and differentiation, apoptosis and neoplastic transformation.


Pssm-ID: 460171  Cd Length: 42  Bit Score: 81.75  E-value: 1.64e-19
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1958789702   3 VTFGDVAVHFSREEWQCLDSGQRALYREVMLENHSSVAGLG 43
Cdd:pfam01352   2 VTFEDVAVDFTQEEWALLDPAQRNLYRDVMLENYRNLVSLG 42
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
 3-42 1.50e-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: 1.50e-18
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1958789702   3 VTFGDVAVHFSREEWQCLDSGQRALYREVMLENHSSVAGL 42
Cdd:cd07765     1 VTFEDVAVYFSQEEWELLDPAQRDLYRDVMLENYENLVSL 40
zf-H2C2_2 pfam13465
Zinc-finger double domain;
331-355 9.36e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 39.66  E-value: 9.36e-05
                          10        20
                  ....*....|....*....|....*
gi 1958789702 331 LVRHQRTHTGERPYPCQECGKAFSQ 355
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
630-655 4.20e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 37.74  E-value: 4.20e-04
                          10        20
                  ....*....|....*....|....*.
gi 1958789702 630 HLVIHQRIHTGEKPYRCNACGKAFNR 655
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
SUF4-like cd20908
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
 258-310 1.69e-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: 1.69e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1958789702 258 KPFkCVDCGKGFRLSSKLIQHQRIHTgekpYRCEECGKTFGQSSSL-IHHQRIH 310
Cdd:cd20908     1 KPW-CYYCDREFDDEKILIQHQKAKH----FKCHICHKKLYTAGGLaVHCLQVH 49
 
Name Accession Description Interval E-value
KRAB smart00349
krueppel associated box;
3-62 8.76e-31

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 114.61  E-value: 8.76e-31
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789702    3 VTFGDVAVHFSREEWQCLDSGQRALYREVMLENHSSVAGLGFLVFKPELISRLEQGQEPW 62
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQVPKPDLISQLEQGEEPW 60
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
229-618 3.65e-20

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 93.99  E-value: 3.65e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789702 229 KKPYGCEECGKVFRLCSQLNQHQRIHTGEKPFKC--VDCGKGFRLSSKLIQHQRIHTGEKPYRCEECGKT--FGQSSSLI 304
Cdd:COG5048    31 PRPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCsySGCDKSFSRPLELSRHLRTHHNNPSDLNSKSLPLsnSKASSSSL 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789702 305 HHQrIHTGERPYSCQECGKSFSQQSQLVRHQRTHTGERPYPCQECGKAFSQ----SSTLAQHQRMHTGEKSQMPRASGSP 380
Cdd:COG5048   111 SSS-SSNSNDNNLLSSHSLPPSSRDPQLPDLLSISNLRNNPLPGNNSSSVNtpqsNSLHPPLPANSLSKDPSSNLSLLIS 189

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789702 381 SllarqRNNTVEKPFKCEECGKAFRWISRLNQHQLIHTGEKPYKCNKCTKAFGCSSRLIRHQRTHTGEKPFKCEECGKGF 460
Cdd:COG5048   190 S-----NVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLSSSDSSSSASESPRSS 264

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789702 461 VQGSHLIQHQRIHTGE-------KPYVCDDCGKAFSQSSSLIYHQR--IHKGE--KPYEC--IQCGKAFSMSTQLTSHQR 527
Cdd:COG5048   265 LPTASSQSSSPNESDSssekgfsLPIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCpySLCGKLFSRNDALKRHIL 344

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789702 528 IHTGERPYKC--SECGKAFSQNST-----LFQHQIIHAGVKPYEC--SECGKAFSRSSYLIEHqRIHTRAQWYYEFGNTT 598
Cdd:COG5048   345 LHTSISPAKEklLNSSSKFSPLLNneppqSLQQYKDLKNDKKSETlsNSCIRNFKRDSNLSLH-IITHLSFRPYNCKNPP 423

                         410       420
                  ....*....|....*....|
gi 1958789702 599 ESSTFLNHKKVNPVKKLHQC 618
Cdd:COG5048   424 CSKSFNRHYNLIPHKKIHTN 443
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
 3-43 1.64e-19

KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc finger proteins containing C2H2 fingers. The KRAB domain is found to be involved in protein-protein interactions. The KRAB domain is generally encoded by two exons. The regions coded by the two exons are known as KRAB-A and KRAB-B. The A box plays an important role in repression by binding to corepressors, while the B box is thought to enhance this repression brought about by the A box. KRAB-containing proteins are thought to have critical functions in cell proliferation and differentiation, apoptosis and neoplastic transformation.


Pssm-ID: 460171  Cd Length: 42  Bit Score: 81.75  E-value: 1.64e-19
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1958789702   3 VTFGDVAVHFSREEWQCLDSGQRALYREVMLENHSSVAGLG 43
Cdd:pfam01352   2 VTFEDVAVDFTQEEWALLDPAQRNLYRDVMLENYRNLVSLG 42
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
 3-42 1.50e-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: 1.50e-18
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1958789702   3 VTFGDVAVHFSREEWQCLDSGQRALYREVMLENHSSVAGL 42
Cdd:cd07765     1 VTFEDVAVYFSQEEWELLDPAQRDLYRDVMLENYENLVSL 40
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
314-657 9.13e-12

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 67.80  E-value: 9.13e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789702 314 RPYSCQECGKSFSQQSQLVRHQRTHTGERPYPC--QECGKAFSQSSTLAQHQRMHTGEKSQMPRASGSPSLLAR------ 385
Cdd:COG5048    32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCsySGCDKSFSRPLELSRHLRTHHNNPSDLNSKSLPLSNSKAssssls 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789702 386 ----------------------------------------QRNNTVEKPFKC-----------EECGKAFRWISRLNQHQ 414
Cdd:COG5048   112 ssssnsndnnllsshslppssrdpqlpdllsisnlrnnplPGNNSSSVNTPQsnslhpplpanSLSKDPSSNLSLLISSN 191

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789702 415 LIHTGEKPYKCNKCTKA----FGCS--------SRLIRHQRTHTGEKPFKCEecgkgfvQGSHLIQHQRIHTGEKPYVCD 482
Cdd:COG5048   192 VSTSIPSSSENSPLSSSysipSSSSdqnlenssSSLPLTTNSQLSPKSLLSQ-------SPSSLSSSDSSSSASESPRSS 264

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789702 483 DCGKAFSQSSSLIYHQRIHKG-EKPYECIQCGKAFSMSTQLTSHQR--IHTGE--RPYKCSE--CGKAFSQNSTLFQHQI 555
Cdd:COG5048   265 LPTASSQSSSPNESDSSSEKGfSLPIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCPYslCGKLFSRNDALKRHIL 344

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789702 556 IHAGVKPYEC--SECGKAFSRSS------YLIEHQRIHTRAQWY----YEFGNTTESSTFLNHKKVNPVKKLHQCDD--C 621
Cdd:COG5048   345 LHTSISPAKEklLNSSSKFSPLLnneppqSLQQYKDLKNDKKSEtlsnSCIRNFKRDSNLSLHIITHLSFRPYNCKNppC 424

                         410       420       430
                  ....*....|....*....|....*....|....*.
gi 1958789702 622 DKIFRWRSHLVIHQRIHTGEKPYRCNACGKAFNRSS 657
Cdd:COG5048   425 SKSFNRHYNLIPHKKIHTNHAPLLCSILKSFRRDLD 460
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
421-664 2.33e-05

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 47.38  E-value: 2.33e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789702 421 KPYKCNKCTKAFGCSSRLIRHQRTHTGEKPFKC--EECGKGFVQGSHLIQHQRIHTGEKPYVCDDCGKafSQSSSLIYHQ 498
Cdd:COG5048    32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCsySGCDKSFSRPLELSRHLRTHHNNPSDLNSKSLP--LSNSKASSSS 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789702 499 RIHKGEKPYECIQC---GKAFSMSTQLTSHQRIHTGERPYKCSECGKAF--SQNSTLFQHQIIHAGVKPYECSECGKAFS 573
Cdd:COG5048   110 LSSSSSNSNDNNLLsshSLPPSSRDPQLPDLLSISNLRNNPLPGNNSSSvnTPQSNSLHPPLPANSLSKDPSSNLSLLIS 189

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789702 574 ---RSSYLIEHQRIHTRAQWYYEFGNTTESS------------TFLNHKKVNPVKKLHQCDD--------------CDKI 624
Cdd:COG5048   190 snvSTSIPSSSENSPLSSSYSIPSSSSDQNLensssslplttnSQLSPKSLLSQSPSSLSSSdssssasesprsslPTAS 269

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1958789702 625 FRWRSHLVIHQRIHTG-EKPYRCNACGKAFNRSSRLTQHQK 664
Cdd:COG5048   270 SQSSSPNESDSSSEKGfSLPIKSKQCNISFSRSSPLTRHLR 310
zf-H2C2_2 pfam13465
Zinc-finger double domain;
331-355 9.36e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 39.66  E-value: 9.36e-05
                          10        20
                  ....*....|....*....|....*
gi 1958789702 331 LVRHQRTHTGERPYPCQECGKAFSQ 355
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
437-462 1.13e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 39.66  E-value: 1.13e-04
                          10        20
                  ....*....|....*....|....*.
gi 1958789702 437 RLIRHQRTHTGEKPFKCEECGKGFVQ 462
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
465-490 1.50e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 39.28  E-value: 1.50e-04
                          10        20
                  ....*....|....*....|....*.
gi 1958789702 465 HLIQHQRIHTGEKPYVCDDCGKAFSQ 490
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
522-546 1.90e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.89  E-value: 1.90e-04
                          10        20
                  ....*....|....*....|....*
gi 1958789702 522 LTSHQRIHTGERPYKCSECGKAFSQ 546
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
630-655 4.20e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 37.74  E-value: 4.20e-04
                          10        20
                  ....*....|....*....|....*.
gi 1958789702 630 HLVIHQRIHTGEKPYRCNACGKAFNR 655
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
275-297 4.77e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 37.74  E-value: 4.77e-04
                          10        20
                  ....*....|....*....|...
gi 1958789702 275 LIQHQRIHTGEKPYRCEECGKTF 297
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSF 24
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 316-338 6.32e-04

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


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 37.28  E-value: 6.32e-04
                          10        20
                  ....*....|....*....|...
gi 1958789702 316 YSCQECGKSFSQQSQLVRHQRTH 338
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
493-517 1.56e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.20  E-value: 1.56e-03
                          10        20
                  ....*....|....*....|....*
gi 1958789702 493 SLIYHQRIHKGEKPYECIQCGKAFS 517
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFK 25
SUF4-like cd20908
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
 258-310 1.69e-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: 1.69e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1958789702 258 KPFkCVDCGKGFRLSSKLIQHQRIHTgekpYRCEECGKTFGQSSSL-IHHQRIH 310
Cdd:cd20908     1 KPW-CYYCDREFDDEKILIQHQKAKH----FKCHICHKKLYTAGGLaVHCLQVH 49
zf-H2C2_2 pfam13465
Zinc-finger double domain;
306-327 1.71e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.20  E-value: 1.71e-03
                          10        20
                  ....*....|....*....|..
gi 1958789702 306 HQRIHTGERPYSCQECGKSFSQ 327
Cdd:pfam13465   5 HMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
409-432 2.04e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.81  E-value: 2.04e-03
                          10        20
                  ....*....|....*....|....
gi 1958789702 409 RLNQHQLIHTGEKPYKCNKCTKAF 432
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSF 24
SFP1 COG5189
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ...
 419-497 3.13e-03

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


Pssm-ID: 227516 [Multi-domain]  Cd Length: 423  Bit Score: 40.47  E-value: 3.13e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789702 419 GEKPYKCN--KCTKAFGCSSRLIRHqRTHTGEKPFKCEECGKgfvqgshlIQHQRIHTGEKPYVCDDCGKAFSQSSSLIY 496
Cdd:COG5189   346 DGKPYKCPveGCNKKYKNQNGLKYH-MLHGHQNQKLHENPSP--------EKMNIFSAKDKPYRCEVCDKRYKNLNGLKY 416


                  .
gi 1958789702 497 H 497
Cdd:COG5189   417 H 417
SFP1 COG5189
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ...
 475-553 3.38e-03

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


Pssm-ID: 227516 [Multi-domain]  Cd Length: 423  Bit Score: 40.47  E-value: 3.38e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789702 475 GEKPYVCD--DCGKAFSQSSSLIYHqRIHKgekpyeciQCGKAFSMSTQLTSHQRIHTGERPYKCSECGKAFSQNSTLFQ 552
Cdd:COG5189   346 DGKPYKCPveGCNKKYKNQNGLKYH-MLHG--------HQNQKLHENPSPEKMNIFSAKDKPYRCEVCDKRYKNLNGLKY 416


                  .
gi 1958789702 553 H 553
Cdd:COG5189   417 H 417
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 563-585 3.45e-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: 3.45e-03
                          10        20
                  ....*....|....*....|...
gi 1958789702 563 YECSECGKAFSRSSYLIEHQRIH 585
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 288-310 3.77e-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: 3.77e-03
                          10        20
                  ....*....|....*....|...
gi 1958789702 288 YRCEECGKTFGQSSSLIHHQRIH 310
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 479-501 5.11e-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: 5.11e-03
                          10        20
                  ....*....|....*....|...
gi 1958789702 479 YVCDDCGKAFSQSSSLIYHQRIH 501
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
247-269 7.10e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 34.27  E-value: 7.10e-03
                          10        20
                  ....*....|....*....|...
gi 1958789702 247 LNQHQRIHTGEKPFKCVDCGKGF 269
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSF 24
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 344-366 9.03e-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: 34.20  E-value: 9.03e-03
                          10        20
                  ....*....|....*....|...
gi 1958789702 344 YPCQECGKAFSQSSTLAQHQRMH 366
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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