NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|767953597|ref|XP_011515595|]
View 

zinc finger protein 7 isoform X1 [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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
KRAB smart00349
krueppel associated box;
4-65 1.45e-30

krueppel associated box;


:

Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 113.84  E-value: 1.45e-30
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767953597     4 VTFGDVAVHFSREEWQCLDPGQRALYREVMLENHSSVAGLaGFLVFKPELISRLEQGEEPWV 65
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSL-GFQVPKPDLISQLEQGEEPWI 61
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
218-675 3.44e-20

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


:

Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 93.99  E-value: 3.44e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953597 218 NTQKISRCQECQKKLSDCLQGKHTNNCHGEKPYECAECGKVFRLCSQLNQHQRIHTGEKPFKCT--ECGKAFRLSSKLIQ 295
Cdd:COG5048    2 TLTSSQSSSSNNSVLSSTPKSTLKSLSNAPRPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSysGCDKSFSRPLELSR 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953597 296 HQRIHTGEKPYRCE--ECGKAFGQSSSLIHHQrIHTGERPYGCRECGKAFSQQSQLVRHQRTHTGERPYPCKECGKAF-- 371
Cdd:COG5048   82 HLRTHHNNPSDLNSksLPLSNSKASSSSLSSS-SSNSNDNNLLSSHSLPPSSRDPQLPDLLSISNLRNNPLPGNNSSSvn 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953597 372 SQSSTLAQHQRMHTGEKAQILKASDSPSlvaHQRIHAVEKPFKCDECGKAFRWISRLSQHQLIHTGEKPYKCNKCTKAFG 451
Cdd:COG5048  161 TPQSNSLHPPLPANSLSKDPSSNLSLLI---SSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSP 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953597 452 CSSRLIRHQRTHTGEKPFKCDECGKGFVQGSHLIQHQRIHTGE-------KPYVCNDCGKAFSQSSSLIYHQR--IHKGE 522
Cdd:COG5048  238 KSLLSQSPSSLSSSDSSSSASESPRSSLPTASSQSSSPNESDSssekgfsLPIKSKQCNISFSRSSPLTRHLRsvNHSGE 317

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953597 523 --KPYEC--LQCGKAFSMSTQLTIHQRVHTGERPYKC--NECGKAFSQNST-----LFQHQIIHAGVKPYEC--SECGKA 589
Cdd:COG5048  318 slKPFSCpySLCGKLFSRNDALKRHILLHTSISPAKEklLNSSSKFSPLLNneppqSLQQYKDLKNDKKSETlsNSCIRN 397

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953597 590 FSRSSYLIEHqRIHTRAQWFYEYGNALEGSTFVSRKKvntikklhqcedcekifrwrshLIIHQRIHTGEKPYKCNDCGK 669
Cdd:COG5048  398 FKRDSNLSLH-IITHLSFRPYNCKNPPCSKSFNRHYN----------------------LIPHKKIHTNHAPLLCSILKS 454


                 ....*.
gi 767953597 670 AFNRSS 675
Cdd:COG5048  455 FRRDLD 460
PHA02693 super family cl28640
hypothetical protein; Provisional
 43-116 1.34e-03

hypothetical protein; Provisional


The actual alignment was detected with superfamily member PHA02693:

Pssm-ID: 333460  Cd Length: 710  Bit Score: 41.94  E-value: 1.34e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767953597  43 LAGFLVFKPELISRLEQGEEPWVLDLQGAEGTEAPRTSKTdstiRTENEQACEDMDILKSESYGTVVRISPQDF 116
Cdd:PHA02693 109 LSAGLVYEPEVVDMVEKGRVPAVLALTCAPWTACPQLKLS----RTEIETVCRAIDPALVNEMIPKLEISPEDL 178
 
Name Accession Description Interval E-value
KRAB smart00349
krueppel associated box;
4-65 1.45e-30

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 113.84  E-value: 1.45e-30
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767953597     4 VTFGDVAVHFSREEWQCLDPGQRALYREVMLENHSSVAGLaGFLVFKPELISRLEQGEEPWV 65
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSL-GFQVPKPDLISQLEQGEEPWI 61
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
218-675 3.44e-20

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 93.99  E-value: 3.44e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953597 218 NTQKISRCQECQKKLSDCLQGKHTNNCHGEKPYECAECGKVFRLCSQLNQHQRIHTGEKPFKCT--ECGKAFRLSSKLIQ 295
Cdd:COG5048    2 TLTSSQSSSSNNSVLSSTPKSTLKSLSNAPRPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSysGCDKSFSRPLELSR 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953597 296 HQRIHTGEKPYRCE--ECGKAFGQSSSLIHHQrIHTGERPYGCRECGKAFSQQSQLVRHQRTHTGERPYPCKECGKAF-- 371
Cdd:COG5048   82 HLRTHHNNPSDLNSksLPLSNSKASSSSLSSS-SSNSNDNNLLSSHSLPPSSRDPQLPDLLSISNLRNNPLPGNNSSSvn 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953597 372 SQSSTLAQHQRMHTGEKAQILKASDSPSlvaHQRIHAVEKPFKCDECGKAFRWISRLSQHQLIHTGEKPYKCNKCTKAFG 451
Cdd:COG5048  161 TPQSNSLHPPLPANSLSKDPSSNLSLLI---SSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSP 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953597 452 CSSRLIRHQRTHTGEKPFKCDECGKGFVQGSHLIQHQRIHTGE-------KPYVCNDCGKAFSQSSSLIYHQR--IHKGE 522
Cdd:COG5048  238 KSLLSQSPSSLSSSDSSSSASESPRSSLPTASSQSSSPNESDSssekgfsLPIKSKQCNISFSRSSPLTRHLRsvNHSGE 317

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953597 523 --KPYEC--LQCGKAFSMSTQLTIHQRVHTGERPYKC--NECGKAFSQNST-----LFQHQIIHAGVKPYEC--SECGKA 589
Cdd:COG5048  318 slKPFSCpySLCGKLFSRNDALKRHILLHTSISPAKEklLNSSSKFSPLLNneppqSLQQYKDLKNDKKSETlsNSCIRN 397

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953597 590 FSRSSYLIEHqRIHTRAQWFYEYGNALEGSTFVSRKKvntikklhqcedcekifrwrshLIIHQRIHTGEKPYKCNDCGK 669
Cdd:COG5048  398 FKRDSNLSLH-IITHLSFRPYNCKNPPCSKSFNRHYN----------------------LIPHKKIHTNHAPLLCSILKS 454


                 ....*.
gi 767953597 670 AFNRSS 675
Cdd:COG5048  455 FRRDLD 460
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
 3-41 1.97e-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: 1.97e-19
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 767953597    3 VVTFGDVAVHFSREEWQCLDPGQRALYREVMLENHSSVA 41
Cdd:pfam01352   1 SVTFEDVAVDFTQEEWALLDPAQRNLYRDVMLENYRNLV 39
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
 4-43 3.15e-19

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: 81.06  E-value: 3.15e-19
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 767953597   4 VTFGDVAVHFSREEWQCLDPGQRALYREVMLENHSSVAGL 43
Cdd:cd07765    1 VTFEDVAVYFSQEEWELLDPAQRDLYRDVMLENYENLVSL 40
zf-H2C2_2 pfam13465
Zinc-finger double domain;
349-373 3.71e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 40.82  E-value: 3.71e-05
                          10        20
                  ....*....|....*....|....*
gi 767953597  349 LVRHQRTHTGERPYPCKECGKAFSQ 373
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 26
PHA02693 PHA02693
hypothetical protein; Provisional
 43-116 1.34e-03

hypothetical protein; Provisional


Pssm-ID: 177475  Cd Length: 710  Bit Score: 41.94  E-value: 1.34e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767953597  43 LAGFLVFKPELISRLEQGEEPWVLDLQGAEGTEAPRTSKTdstiRTENEQACEDMDILKSESYGTVVRISPQDF 116
Cdd:PHA02693 109 LSAGLVYEPEVVDMVEKGRVPAVLALTCAPWTACPQLKLS----RTEIETVCRAIDPALVNEMIPKLEISPEDL 178
SUF4-like cd20908
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
 276-328 4.90e-03

N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), Arabidopsis thaliana SUF4 (AtSUF4), and similar proteins; Oryza sativa SUPPRESSOR OF FRI 4 (OsSUF4) is a C2H2-type zinc finger transcription factor which interacts with the major H3K36 methyltransferase SDG725 to promote H3K36me3 (tri-methylation at H3K9) establishment. The transcription factor OsSUF4 recognizes a specific 7-bp DNA element (5'-CGGAAAT-3'), which is contained in the promoter regions of many genes throughout the rice genome. Through interaction with OsSUF4, SDG725 is recruited to the promoters of key florigen genes, RICE FLOWERING LOCUS T1 (RFT1) and Heading date 3a (Hd3a), for H3K36 deposition to promote gene activation and rice plant flowering. OsSUF4 target genes include a number of genes involved in many biological processes. Flowering plant Arabidopsis SUF4 binds to a 15bp DNA element (5'-CCAAATTTTAAGTTT-3') within the promoter of the floral repressor gene FLOWERING LOCUS C (FLC) and recruits the FRI-C transcription activator complex to the FLC promoter. Although the DNA-binding element and target genes of AtSUF4 are different from those of OsSUF4, AtSUF4 is known to interact with the Arabidopsis H3K36 methyltransferase SDG8 (also known as ASHH2/EFS/SET8), and the methylation deposition mechanism mediated by the SUF4 transcription factor and H3K36 methyltransferase may be conserved in Arabidopsis and rice. Proteins in this family have two conserved C2H2-type zinc finger motifs at the N-terminus (included in this model), and a large proline-rich domain at the C-terminus; for OsSUF4, it has been shown that the N-terminal zinc-finger domain is responsible for DNA binding, and that the C-terminal domain interacts with SDG725.


Pssm-ID: 411020 [Multi-domain]  Cd Length: 82  Bit Score: 36.38  E-value: 4.90e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 767953597 276 KPFkCTECGKAFRLSSKLIQHQRIHTgekpYRCEECGKAFGQSSSL-IHHQRIH 328
Cdd:cd20908    1 KPW-CYYCDREFDDEKILIQHQKAKH----FKCHICHKKLYTAGGLaVHCLQVH 49
 
Name Accession Description Interval E-value
KRAB smart00349
krueppel associated box;
4-65 1.45e-30

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 113.84  E-value: 1.45e-30
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767953597     4 VTFGDVAVHFSREEWQCLDPGQRALYREVMLENHSSVAGLaGFLVFKPELISRLEQGEEPWV 65
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSL-GFQVPKPDLISQLEQGEEPWI 61
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
218-675 3.44e-20

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 93.99  E-value: 3.44e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953597 218 NTQKISRCQECQKKLSDCLQGKHTNNCHGEKPYECAECGKVFRLCSQLNQHQRIHTGEKPFKCT--ECGKAFRLSSKLIQ 295
Cdd:COG5048    2 TLTSSQSSSSNNSVLSSTPKSTLKSLSNAPRPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSysGCDKSFSRPLELSR 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953597 296 HQRIHTGEKPYRCE--ECGKAFGQSSSLIHHQrIHTGERPYGCRECGKAFSQQSQLVRHQRTHTGERPYPCKECGKAF-- 371
Cdd:COG5048   82 HLRTHHNNPSDLNSksLPLSNSKASSSSLSSS-SSNSNDNNLLSSHSLPPSSRDPQLPDLLSISNLRNNPLPGNNSSSvn 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953597 372 SQSSTLAQHQRMHTGEKAQILKASDSPSlvaHQRIHAVEKPFKCDECGKAFRWISRLSQHQLIHTGEKPYKCNKCTKAFG 451
Cdd:COG5048  161 TPQSNSLHPPLPANSLSKDPSSNLSLLI---SSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSP 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953597 452 CSSRLIRHQRTHTGEKPFKCDECGKGFVQGSHLIQHQRIHTGE-------KPYVCNDCGKAFSQSSSLIYHQR--IHKGE 522
Cdd:COG5048  238 KSLLSQSPSSLSSSDSSSSASESPRSSLPTASSQSSSPNESDSssekgfsLPIKSKQCNISFSRSSPLTRHLRsvNHSGE 317

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953597 523 --KPYEC--LQCGKAFSMSTQLTIHQRVHTGERPYKC--NECGKAFSQNST-----LFQHQIIHAGVKPYEC--SECGKA 589
Cdd:COG5048  318 slKPFSCpySLCGKLFSRNDALKRHILLHTSISPAKEklLNSSSKFSPLLNneppqSLQQYKDLKNDKKSETlsNSCIRN 397

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953597 590 FSRSSYLIEHqRIHTRAQWFYEYGNALEGSTFVSRKKvntikklhqcedcekifrwrshLIIHQRIHTGEKPYKCNDCGK 669
Cdd:COG5048  398 FKRDSNLSLH-IITHLSFRPYNCKNPPCSKSFNRHYN----------------------LIPHKKIHTNHAPLLCSILKS 454


                 ....*.
gi 767953597 670 AFNRSS 675
Cdd:COG5048  455 FRRDLD 460
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
 3-41 1.97e-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: 1.97e-19
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 767953597    3 VVTFGDVAVHFSREEWQCLDPGQRALYREVMLENHSSVA 41
Cdd:pfam01352   1 SVTFEDVAVDFTQEEWALLDPAQRNLYRDVMLENYRNLV 39
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
 4-43 3.15e-19

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: 81.06  E-value: 3.15e-19
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 767953597   4 VTFGDVAVHFSREEWQCLDPGQRALYREVMLENHSSVAGL 43
Cdd:cd07765    1 VTFEDVAVYFSQEEWELLDPAQRDLYRDVMLENYENLVSL 40
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
332-684 7.93e-12

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 68.18  E-value: 7.93e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953597 332 RPYGCRECGKAFSQQSQLVRHQRTHTGERPYPC--KECGKAFSQSSTLAQHQRMHTGEKAQILKASDSPSLV-------- 401
Cdd:COG5048   32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCsySGCDKSFSRPLELSRHLRTHHNNPSDLNSKSLPLSNSkassssls 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953597 402 -----------------AHQRIHAVEKP------FKCDECGKAFRWISRLSQHQLIHtGEKPYKCNKCTKAFGCSSRLir 458
Cdd:COG5048  112 ssssnsndnnllsshslPPSSRDPQLPDllsisnLRNNPLPGNNSSSVNTPQSNSLH-PPLPANSLSKDPSSNLSLLI-- 188

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953597 459 HQRTHTGEKPFKCDECGKGFVQGSHLIQHQRIHTGEKPYVCNDCGKAFSQSSSLIYHQRI------HKGEKPYECLQCGK 532
Cdd:COG5048  189 SSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLsssdssSSASESPRSSLPTA 268

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953597 533 AFSMSTQLTIHQRVHTGER-PYKCNECGKAFSQNSTLFQHQ--IIH--AGVKPYECSE--CGKAFSRSSYLIEHQRIHTR 605
Cdd:COG5048  269 SSQSSSPNESDSSSEKGFSlPIKSKQCNISFSRSSPLTRHLrsVNHsgESLKPFSCPYslCGKLFSRNDALKRHILLHTS 348

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953597 606 AQWFYEY-----------GNALEGSTFVSRKKVNTIKKLHQCEDCEKIFRWRSHLIIHQRIHT---GEKPYKCNDCGKAF 671
Cdd:COG5048  349 ISPAKEKllnssskfsplLNNEPPQSLQQYKDLKNDKKSETLSNSCIRNFKRDSNLSLHIITHlsfRPYNCKNPPCSKSF 428

                        410
                 ....*....|...
gi 767953597 672 NRSSRLTQHQKIH 684
Cdd:COG5048  429 NRHYNLIPHKKIH 441
zf-H2C2_2 pfam13465
Zinc-finger double domain;
349-373 3.71e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 40.82  E-value: 3.71e-05
                          10        20
                  ....*....|....*....|....*
gi 767953597  349 LVRHQRTHTGERPYPCKECGKAFSQ 373
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
455-480 4.38e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 40.82  E-value: 4.38e-05
                          10        20
                  ....*....|....*....|....*.
gi 767953597  455 RLIRHQRTHTGEKPFKCDECGKGFVQ 480
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
265-287 6.12e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 40.43  E-value: 6.12e-05
                          10        20
                  ....*....|....*....|...
gi 767953597  265 LNQHQRIHTGEKPFKCTECGKAF 287
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSF 24
zf-H2C2_2 pfam13465
Zinc-finger double domain;
483-508 1.29e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 39.28  E-value: 1.29e-04
                          10        20
                  ....*....|....*....|....*.
gi 767953597  483 HLIQHQRIHTGEKPYVCNDCGKAFSQ 508
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
624-685 1.51e-04

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 44.69  E-value: 1.51e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767953597 624 RKKVNTIKKLHQCEDCEKIFRWRSHLIIHQRIHTGEKPYKCNDCGKAFNRSSR--LTQHQKIHM 685
Cdd:COG5048   24 LKSLSNAPRPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYSGCDKSFSRPleLSRHLRTHH 87
zf-H2C2_2 pfam13465
Zinc-finger double domain;
648-673 1.65e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 39.28  E-value: 1.65e-04
                          10        20
                  ....*....|....*....|....*.
gi 767953597  648 HLIIHQRIHTGEKPYKCNDCGKAFNR 673
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
293-315 1.91e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.89  E-value: 1.91e-04
                          10        20
                  ....*....|....*....|...
gi 767953597  293 LIQHQRIHTGEKPYRCEECGKAF 315
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSF 24
SFP1 COG5189
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ...
 358-431 2.51e-04

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


Pssm-ID: 227516 [Multi-domain]  Cd Length: 423  Bit Score: 43.94  E-value: 2.51e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767953597 358 GERPYPCK--ECGKAFSQSSTLAQHqRMHtGEKAQILKASDSPslVAHQRIHAVEKPFKCDECGKAFRWISRLSQH 431
Cdd:COG5189  346 DGKPYKCPveGCNKKYKNQNGLKYH-MLH-GHQNQKLHENPSP--EKMNIFSAKDKPYRCEVCDKRYKNLNGLKYH 417
zf-H2C2_2 pfam13465
Zinc-finger double domain;
540-564 6.64e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 37.35  E-value: 6.64e-04
                          10        20
                  ....*....|....*....|....*
gi 767953597  540 LTIHQRVHTGERPYKCNECGKAFSQ 564
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 26
PHA02693 PHA02693
hypothetical protein; Provisional
 43-116 1.34e-03

hypothetical protein; Provisional


Pssm-ID: 177475  Cd Length: 710  Bit Score: 41.94  E-value: 1.34e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767953597  43 LAGFLVFKPELISRLEQGEEPWVLDLQGAEGTEAPRTSKTdstiRTENEQACEDMDILKSESYGTVVRISPQDF 116
Cdd:PHA02693 109 LSAGLVYEPEVVDMVEKGRVPAVLALTCAPWTACPQLKLS----RTEIETVCRAIDPALVNEMIPKLEISPEDL 178
zf-H2C2_2 pfam13465
Zinc-finger double domain;
427-450 1.69e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.20  E-value: 1.69e-03
                          10        20
                  ....*....|....*....|....
gi 767953597  427 RLSQHQLIHTGEKPYKCNKCTKAF 450
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSF 24
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 581-603 1.95e-03

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


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 36.12  E-value: 1.95e-03
                          10        20
                  ....*....|....*....|...
gi 767953597  581 YECSECGKAFSRSSYLIEHQRIH 603
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 497-519 2.23e-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: 2.23e-03
                          10        20
                  ....*....|....*....|...
gi 767953597  497 YVCNDCGKAFSQSSSLIYHQRIH 519
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
511-535 2.40e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.81  E-value: 2.40e-03
                          10        20
                  ....*....|....*....|....*
gi 767953597  511 SLIYHQRIHKGEKPYECLQCGKAFS 535
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFK 25
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 362-384 2.85e-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: 2.85e-03
                          10        20
                  ....*....|....*....|...
gi 767953597  362 YPCKECGKAFSQSSTLAQHQRMH 384
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 306-328 3.76e-03

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


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 35.35  E-value: 3.76e-03
                          10        20
                  ....*....|....*....|...
gi 767953597  306 YRCEECGKAFGQSSSLIHHQRIH 328
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 662-684 4.14e-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: 4.14e-03
                          10        20
                  ....*....|....*....|...
gi 767953597  662 YKCNDCGKAFNRSSRLTQHQKIH 684
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
399-422 4.50e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.04  E-value: 4.50e-03
                          10        20
                  ....*....|....*....|....
gi 767953597  399 SLVAHQRIHAVEKPFKCDECGKAF 422
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSF 24
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 553-575 4.80e-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: 4.80e-03
                          10        20
                  ....*....|....*....|...
gi 767953597  553 YKCNECGKAFSQNSTLFQHQIIH 575
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
SUF4-like cd20908
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
 276-328 4.90e-03

N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), Arabidopsis thaliana SUF4 (AtSUF4), and similar proteins; Oryza sativa SUPPRESSOR OF FRI 4 (OsSUF4) is a C2H2-type zinc finger transcription factor which interacts with the major H3K36 methyltransferase SDG725 to promote H3K36me3 (tri-methylation at H3K9) establishment. The transcription factor OsSUF4 recognizes a specific 7-bp DNA element (5'-CGGAAAT-3'), which is contained in the promoter regions of many genes throughout the rice genome. Through interaction with OsSUF4, SDG725 is recruited to the promoters of key florigen genes, RICE FLOWERING LOCUS T1 (RFT1) and Heading date 3a (Hd3a), for H3K36 deposition to promote gene activation and rice plant flowering. OsSUF4 target genes include a number of genes involved in many biological processes. Flowering plant Arabidopsis SUF4 binds to a 15bp DNA element (5'-CCAAATTTTAAGTTT-3') within the promoter of the floral repressor gene FLOWERING LOCUS C (FLC) and recruits the FRI-C transcription activator complex to the FLC promoter. Although the DNA-binding element and target genes of AtSUF4 are different from those of OsSUF4, AtSUF4 is known to interact with the Arabidopsis H3K36 methyltransferase SDG8 (also known as ASHH2/EFS/SET8), and the methylation deposition mechanism mediated by the SUF4 transcription factor and H3K36 methyltransferase may be conserved in Arabidopsis and rice. Proteins in this family have two conserved C2H2-type zinc finger motifs at the N-terminus (included in this model), and a large proline-rich domain at the C-terminus; for OsSUF4, it has been shown that the N-terminal zinc-finger domain is responsible for DNA binding, and that the C-terminal domain interacts with SDG725.


Pssm-ID: 411020 [Multi-domain]  Cd Length: 82  Bit Score: 36.38  E-value: 4.90e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 767953597 276 KPFkCTECGKAFRLSSKLIQHQRIHTgekpYRCEECGKAFGQSSSL-IHHQRIH 328
Cdd:cd20908    1 KPW-CYYCDREFDDEKILIQHQKAKH----FKCHICHKKLYTAGGLaVHCLQVH 49
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 336-356 6.32e-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: 6.32e-03
                          10        20
                  ....*....|....*....|.
gi 767953597  336 CRECGKAFSQQSQLVRHQRTH 356
Cdd:pfam00096   3 CPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
568-592 9.51e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 34.27  E-value: 9.51e-03
                          10        20
                  ....*....|....*....|....*
gi 767953597  568 LFQHQIIHAGVKPYECSECGKAFSR 592
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH