NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1168812000|ref|NP_001336736|]
View 

zinc finger protein 7 isoform 7 [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;
4-64 3.37e-32

krueppel associated box;


:

Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 118.46  E-value: 3.37e-32
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1168812000    4 VTFGDVAVHFSREEWQCLDPGQRALYREVMLENHSSVAGLGFLVFKPELISRLEQGEEPWV 64
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQVPKPDLISQLEQGEEPWI 61
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
217-674 4.34e-20

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


:

Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 93.99  E-value: 4.34e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168812000 217 NTQKISRCQECQKKLSDCLQGKHTNNCHGEKPYECAECGKVFRLCSQLNQHQRIHTGEKPFKCT--ECGKAFRLSSKLIQ 294
Cdd:COG5048     2 TLTSSQSSSSNNSVLSSTPKSTLKSLSNAPRPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSysGCDKSFSRPLELSR 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168812000 295 HQRIHTGEKPYRCE--ECGKAFGQSSSLIHHQrIHTGERPYGCRECGKAFSQQSQLVRHQRTHTGERPYPCKECGKAF-- 370
Cdd:COG5048    82 HLRTHHNNPSDLNSksLPLSNSKASSSSLSSS-SSNSNDNNLLSSHSLPPSSRDPQLPDLLSISNLRNNPLPGNNSSSvn 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168812000 371 SQSSTLAQHQRMHTGEKAQILKASDSPSlvaHQRIHAVEKPFKCDECGKAFRWISRLSQHQLIHTGEKPYKCNKCTKAFG 450
Cdd:COG5048   161 TPQSNSLHPPLPANSLSKDPSSNLSLLI---SSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSP 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168812000 451 CSSRLIRHQRTHTGEKPFKCDECGKGFVQGSHLIQHQRIHTGE-------KPYVCNDCGKAFSQSSSLIYHQR--IHKGE 521
Cdd:COG5048   238 KSLLSQSPSSLSSSDSSSSASESPRSSLPTASSQSSSPNESDSssekgfsLPIKSKQCNISFSRSSPLTRHLRsvNHSGE 317

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168812000 522 --KPYEC--LQCGKAFSMSTQLTIHQRVHTGERPYKC--NECGKAFSQNST-----LFQHQIIHAGVKPYEC--SECGKA 588
Cdd:COG5048   318 slKPFSCpySLCGKLFSRNDALKRHILLHTSISPAKEklLNSSSKFSPLLNneppqSLQQYKDLKNDKKSETlsNSCIRN 397

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168812000 589 FSRSSYLIEHqRIHTRAQWFYEYGNALEGSTFVSRKKvntikklhqcedcekifrwrshLIIHQRIHTGEKPYKCNDCGK 668
Cdd:COG5048   398 FKRDSNLSLH-IITHLSFRPYNCKNPPCSKSFNRHYN----------------------LIPHKKIHTNHAPLLCSILKS 454


                  ....*.
gi 1168812000 669 AFNRSS 674
Cdd:COG5048   455 FRRDLD 460
PHA02693 super family cl28640
hypothetical protein; Provisional
 46-115 1.58e-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: 1.58e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168812000  46 LVFKPELISRLEQGEEPWVLDLQGAEGTEAPRTSKTdstiRTENEQACEDMDILKSESYGTVVRISPQDF 115
Cdd:PHA02693  113 LVYEPEVVDMVEKGRVPAVLALTCAPWTACPQLKLS----RTEIETVCRAIDPALVNEMIPKLEISPEDL 178
 
Name Accession Description Interval E-value
KRAB smart00349
krueppel associated box;
4-64 3.37e-32

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 118.46  E-value: 3.37e-32
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1168812000    4 VTFGDVAVHFSREEWQCLDPGQRALYREVMLENHSSVAGLGFLVFKPELISRLEQGEEPWV 64
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQVPKPDLISQLEQGEEPWI 61
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
 3-44 2.64e-20

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: 84.06  E-value: 2.64e-20
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1168812000   3 VVTFGDVAVHFSREEWQCLDPGQRALYREVMLENHSSVAGLG 44
Cdd:pfam01352   1 SVTFEDVAVDFTQEEWALLDPAQRNLYRDVMLENYRNLVSLG 42
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
217-674 4.34e-20

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 93.99  E-value: 4.34e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168812000 217 NTQKISRCQECQKKLSDCLQGKHTNNCHGEKPYECAECGKVFRLCSQLNQHQRIHTGEKPFKCT--ECGKAFRLSSKLIQ 294
Cdd:COG5048     2 TLTSSQSSSSNNSVLSSTPKSTLKSLSNAPRPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSysGCDKSFSRPLELSR 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168812000 295 HQRIHTGEKPYRCE--ECGKAFGQSSSLIHHQrIHTGERPYGCRECGKAFSQQSQLVRHQRTHTGERPYPCKECGKAF-- 370
Cdd:COG5048    82 HLRTHHNNPSDLNSksLPLSNSKASSSSLSSS-SSNSNDNNLLSSHSLPPSSRDPQLPDLLSISNLRNNPLPGNNSSSvn 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168812000 371 SQSSTLAQHQRMHTGEKAQILKASDSPSlvaHQRIHAVEKPFKCDECGKAFRWISRLSQHQLIHTGEKPYKCNKCTKAFG 450
Cdd:COG5048   161 TPQSNSLHPPLPANSLSKDPSSNLSLLI---SSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSP 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168812000 451 CSSRLIRHQRTHTGEKPFKCDECGKGFVQGSHLIQHQRIHTGE-------KPYVCNDCGKAFSQSSSLIYHQR--IHKGE 521
Cdd:COG5048   238 KSLLSQSPSSLSSSDSSSSASESPRSSLPTASSQSSSPNESDSssekgfsLPIKSKQCNISFSRSSPLTRHLRsvNHSGE 317

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168812000 522 --KPYEC--LQCGKAFSMSTQLTIHQRVHTGERPYKC--NECGKAFSQNST-----LFQHQIIHAGVKPYEC--SECGKA 588
Cdd:COG5048   318 slKPFSCpySLCGKLFSRNDALKRHILLHTSISPAKEklLNSSSKFSPLLNneppqSLQQYKDLKNDKKSETlsNSCIRN 397

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168812000 589 FSRSSYLIEHqRIHTRAQWFYEYGNALEGSTFVSRKKvntikklhqcedcekifrwrshLIIHQRIHTGEKPYKCNDCGK 668
Cdd:COG5048   398 FKRDSNLSLH-IITHLSFRPYNCKNPPCSKSFNRHYN----------------------LIPHKKIHTNHAPLLCSILKS 454


                  ....*.
gi 1168812000 669 AFNRSS 674
Cdd:COG5048   455 FRRDLD 460
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
 4-43 3.14e-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: 3.14e-19
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1168812000   4 VTFGDVAVHFSREEWQCLDPGQRALYREVMLENHSSVAGL 43
Cdd:cd07765     1 VTFEDVAVYFSQEEWELLDPAQRDLYRDVMLENYENLVSL 40
zf-H2C2_2 pfam13465
Zinc-finger double domain;
348-372 3.82e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 40.82  E-value: 3.82e-05
                          10        20
                  ....*....|....*....|....*
gi 1168812000 348 LVRHQRTHTGERPYPCKECGKAFSQ 372
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 26
PHA02693 PHA02693
hypothetical protein; Provisional
 46-115 1.58e-03

hypothetical protein; Provisional


Pssm-ID: 177475  Cd Length: 710  Bit Score: 41.94  E-value: 1.58e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168812000  46 LVFKPELISRLEQGEEPWVLDLQGAEGTEAPRTSKTdstiRTENEQACEDMDILKSESYGTVVRISPQDF 115
Cdd:PHA02693  113 LVYEPEVVDMVEKGRVPAVLALTCAPWTACPQLKLS----RTEIETVCRAIDPALVNEMIPKLEISPEDL 178
SUF4-like cd20908
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
 275-327 5.04e-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: 5.04e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1168812000 275 KPFkCTECGKAFRLSSKLIQHQRIHTgekpYRCEECGKAFGQSSSL-IHHQRIH 327
Cdd:cd20908     1 KPW-CYYCDREFDDEKILIQHQKAKH----FKCHICHKKLYTAGGLaVHCLQVH 49
 
Name Accession Description Interval E-value
KRAB smart00349
krueppel associated box;
4-64 3.37e-32

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 118.46  E-value: 3.37e-32
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1168812000    4 VTFGDVAVHFSREEWQCLDPGQRALYREVMLENHSSVAGLGFLVFKPELISRLEQGEEPWV 64
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQVPKPDLISQLEQGEEPWI 61
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
 3-44 2.64e-20

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: 84.06  E-value: 2.64e-20
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1168812000   3 VVTFGDVAVHFSREEWQCLDPGQRALYREVMLENHSSVAGLG 44
Cdd:pfam01352   1 SVTFEDVAVDFTQEEWALLDPAQRNLYRDVMLENYRNLVSLG 42
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
217-674 4.34e-20

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 93.99  E-value: 4.34e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168812000 217 NTQKISRCQECQKKLSDCLQGKHTNNCHGEKPYECAECGKVFRLCSQLNQHQRIHTGEKPFKCT--ECGKAFRLSSKLIQ 294
Cdd:COG5048     2 TLTSSQSSSSNNSVLSSTPKSTLKSLSNAPRPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSysGCDKSFSRPLELSR 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168812000 295 HQRIHTGEKPYRCE--ECGKAFGQSSSLIHHQrIHTGERPYGCRECGKAFSQQSQLVRHQRTHTGERPYPCKECGKAF-- 370
Cdd:COG5048    82 HLRTHHNNPSDLNSksLPLSNSKASSSSLSSS-SSNSNDNNLLSSHSLPPSSRDPQLPDLLSISNLRNNPLPGNNSSSvn 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168812000 371 SQSSTLAQHQRMHTGEKAQILKASDSPSlvaHQRIHAVEKPFKCDECGKAFRWISRLSQHQLIHTGEKPYKCNKCTKAFG 450
Cdd:COG5048   161 TPQSNSLHPPLPANSLSKDPSSNLSLLI---SSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSP 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168812000 451 CSSRLIRHQRTHTGEKPFKCDECGKGFVQGSHLIQHQRIHTGE-------KPYVCNDCGKAFSQSSSLIYHQR--IHKGE 521
Cdd:COG5048   238 KSLLSQSPSSLSSSDSSSSASESPRSSLPTASSQSSSPNESDSssekgfsLPIKSKQCNISFSRSSPLTRHLRsvNHSGE 317

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168812000 522 --KPYEC--LQCGKAFSMSTQLTIHQRVHTGERPYKC--NECGKAFSQNST-----LFQHQIIHAGVKPYEC--SECGKA 588
Cdd:COG5048   318 slKPFSCpySLCGKLFSRNDALKRHILLHTSISPAKEklLNSSSKFSPLLNneppqSLQQYKDLKNDKKSETlsNSCIRN 397

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168812000 589 FSRSSYLIEHqRIHTRAQWFYEYGNALEGSTFVSRKKvntikklhqcedcekifrwrshLIIHQRIHTGEKPYKCNDCGK 668
Cdd:COG5048   398 FKRDSNLSLH-IITHLSFRPYNCKNPPCSKSFNRHYN----------------------LIPHKKIHTNHAPLLCSILKS 454


                  ....*.
gi 1168812000 669 AFNRSS 674
Cdd:COG5048   455 FRRDLD 460
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
 4-43 3.14e-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: 3.14e-19
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1168812000   4 VTFGDVAVHFSREEWQCLDPGQRALYREVMLENHSSVAGL 43
Cdd:cd07765     1 VTFEDVAVYFSQEEWELLDPAQRDLYRDVMLENYENLVSL 40
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
331-683 9.93e-12

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 67.80  E-value: 9.93e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168812000 331 RPYGCRECGKAFSQQSQLVRHQRTHTGERPYPC--KECGKAFSQSSTLAQHQRMHTGEKAQILKASDSPSLV-------- 400
Cdd:COG5048    32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCsySGCDKSFSRPLELSRHLRTHHNNPSDLNSKSLPLSNSkassssls 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168812000 401 -----------------AHQRIHAVEKP------FKCDECGKAFRWISRLSQHQLIHtGEKPYKCNKCTKAFGCSSRLir 457
Cdd:COG5048   112 ssssnsndnnllsshslPPSSRDPQLPDllsisnLRNNPLPGNNSSSVNTPQSNSLH-PPLPANSLSKDPSSNLSLLI-- 188

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168812000 458 HQRTHTGEKPFKCDECGKGFVQGSHLIQHQRIHTGEKPYVCNDCGKAFSQSSSLIYHQRI------HKGEKPYECLQCGK 531
Cdd:COG5048   189 SSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLsssdssSSASESPRSSLPTA 268

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168812000 532 AFSMSTQLTIHQRVHTGER-PYKCNECGKAFSQNSTLFQHQ--IIH--AGVKPYECSE--CGKAFSRSSYLIEHQRIHTR 604
Cdd:COG5048   269 SSQSSSPNESDSSSEKGFSlPIKSKQCNISFSRSSPLTRHLrsVNHsgESLKPFSCPYslCGKLFSRNDALKRHILLHTS 348

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168812000 605 AQWFYEY-----------GNALEGSTFVSRKKVNTIKKLHQCEDCEKIFRWRSHLIIHQRIHT---GEKPYKCNDCGKAF 670
Cdd:COG5048   349 ISPAKEKllnssskfsplLNNEPPQSLQQYKDLKNDKKSETLSNSCIRNFKRDSNLSLHIITHlsfRPYNCKNPPCSKSF 428

                         410
                  ....*....|...
gi 1168812000 671 NRSSRLTQHQKIH 683
Cdd:COG5048   429 NRHYNLIPHKKIH 441
zf-H2C2_2 pfam13465
Zinc-finger double domain;
348-372 3.82e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 40.82  E-value: 3.82e-05
                          10        20
                  ....*....|....*....|....*
gi 1168812000 348 LVRHQRTHTGERPYPCKECGKAFSQ 372
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
454-479 4.51e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 40.82  E-value: 4.51e-05
                          10        20
                  ....*....|....*....|....*.
gi 1168812000 454 RLIRHQRTHTGEKPFKCDECGKGFVQ 479
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
264-286 6.29e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 40.43  E-value: 6.29e-05
                          10        20
                  ....*....|....*....|...
gi 1168812000 264 LNQHQRIHTGEKPFKCTECGKAF 286
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSF 24
zf-H2C2_2 pfam13465
Zinc-finger double domain;
482-507 1.33e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 39.28  E-value: 1.33e-04
                          10        20
                  ....*....|....*....|....*.
gi 1168812000 482 HLIQHQRIHTGEKPYVCNDCGKAFSQ 507
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
623-684 1.59e-04

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 44.69  E-value: 1.59e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1168812000 623 RKKVNTIKKLHQCEDCEKIFRWRSHLIIHQRIHTGEKPYKCNDCGKAFNRSSR--LTQHQKIHM 684
Cdd:COG5048    24 LKSLSNAPRPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYSGCDKSFSRPleLSRHLRTHH 87
zf-H2C2_2 pfam13465
Zinc-finger double domain;
647-672 1.68e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.89  E-value: 1.68e-04
                          10        20
                  ....*....|....*....|....*.
gi 1168812000 647 HLIIHQRIHTGEKPYKCNDCGKAFNR 672
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
292-314 1.94e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.89  E-value: 1.94e-04
                          10        20
                  ....*....|....*....|...
gi 1168812000 292 LIQHQRIHTGEKPYRCEECGKAF 314
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSF 24
SFP1 COG5189
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ...
 357-430 2.57e-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: 2.57e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1168812000 357 GERPYPCK--ECGKAFSQSSTLAQHqRMHtGEKAQILKASDSPslVAHQRIHAVEKPFKCDECGKAFRWISRLSQH 430
Cdd:COG5189   346 DGKPYKCPveGCNKKYKNQNGLKYH-MLH-GHQNQKLHENPSP--EKMNIFSAKDKPYRCEVCDKRYKNLNGLKYH 417
zf-H2C2_2 pfam13465
Zinc-finger double domain;
539-563 6.82e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 37.35  E-value: 6.82e-04
                          10        20
                  ....*....|....*....|....*
gi 1168812000 539 LTIHQRVHTGERPYKCNECGKAFSQ 563
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 26
PHA02693 PHA02693
hypothetical protein; Provisional
 46-115 1.58e-03

hypothetical protein; Provisional


Pssm-ID: 177475  Cd Length: 710  Bit Score: 41.94  E-value: 1.58e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168812000  46 LVFKPELISRLEQGEEPWVLDLQGAEGTEAPRTSKTdstiRTENEQACEDMDILKSESYGTVVRISPQDF 115
Cdd:PHA02693  113 LVYEPEVVDMVEKGRVPAVLALTCAPWTACPQLKLS----RTEIETVCRAIDPALVNEMIPKLEISPEDL 178
zf-H2C2_2 pfam13465
Zinc-finger double domain;
426-449 1.72e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.20  E-value: 1.72e-03
                          10        20
                  ....*....|....*....|....
gi 1168812000 426 RLSQHQLIHTGEKPYKCNKCTKAF 449
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSF 24
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 580-602 2.00e-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: 2.00e-03
                          10        20
                  ....*....|....*....|...
gi 1168812000 580 YECSECGKAFSRSSYLIEHQRIH 602
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 496-518 2.30e-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: 2.30e-03
                          10        20
                  ....*....|....*....|...
gi 1168812000 496 YVCNDCGKAFSQSSSLIYHQRIH 518
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
510-534 2.47e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.81  E-value: 2.47e-03
                          10        20
                  ....*....|....*....|....*
gi 1168812000 510 SLIYHQRIHKGEKPYECLQCGKAFS 534
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFK 25
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 361-383 2.93e-03

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


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 35.35  E-value: 2.93e-03
                          10        20
                  ....*....|....*....|...
gi 1168812000 361 YPCKECGKAFSQSSTLAQHQRMH 383
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 305-327 3.82e-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: 3.82e-03
                          10        20
                  ....*....|....*....|...
gi 1168812000 305 YRCEECGKAFGQSSSLIHHQRIH 327
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 661-683 4.26e-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: 4.26e-03
                          10        20
                  ....*....|....*....|...
gi 1168812000 661 YKCNDCGKAFNRSSRLTQHQKIH 683
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
398-421 4.63e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.04  E-value: 4.63e-03
                          10        20
                  ....*....|....*....|....
gi 1168812000 398 SLVAHQRIHAVEKPFKCDECGKAF 421
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSF 24
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 552-574 4.94e-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: 4.94e-03
                          10        20
                  ....*....|....*....|...
gi 1168812000 552 YKCNECGKAFSQNSTLFQHQIIH 574
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
SUF4-like cd20908
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
 275-327 5.04e-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: 5.04e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1168812000 275 KPFkCTECGKAFRLSSKLIQHQRIHTgekpYRCEECGKAFGQSSSL-IHHQRIH 327
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 ...
 335-355 6.43e-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: 34.58  E-value: 6.43e-03
                          10        20
                  ....*....|....*....|.
gi 1168812000 335 CRECGKAFSQQSQLVRHQRTH 355
Cdd:pfam00096   3 CPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
567-591 9.78e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 34.27  E-value: 9.78e-03
                          10        20
                  ....*....|....*....|....*
gi 1168812000 567 LFQHQIIHAGVKPYECSECGKAFSR 591
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