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Conserved domains on  [gi|1631970668|ref|NP_001357144|]
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endothelial zinc finger protein induced by tumor necrosis factor alpha isoform 2 [Homo sapiens]

Protein Classification

KRAB domain-containing zinc finger protein( domain architecture ID 12016853)

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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
13-54 9.61e-26

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: 99.47  E-value: 9.61e-26
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1631970668  13 SVTFRDVTVDFTQEEWQQLEPAQKDLYRDVMLENYRNLVSLD 54
Cdd:pfam01352   1 SVTFEDVAVDFTQEEWALLDPAQRNLYRDVMLENYRNLVSLG 42
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
170-544 6.46e-16

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


:

Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 80.12  E-value: 6.46e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970668 170 NFSSTSDLSKPPMPC-----EEKKTYDCSECGKAFSRSSSLIKHQRIHTGEKPFEC--DTCGKHFIERSSLTIHQRVHTG 242
Cdd:COG5048     9 SSSNNSVLSSTPKSTlkslsNAPRPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCsySGCDKSFSRPLELSRHLRTHHN 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970668 243 ------------EKPYACGD----CGKAFS---------------QRMNLTVHQRTHTGEKPY----------------- 274
Cdd:COG5048    89 npsdlnskslplSNSKASSSslssSSSNSNdnnllsshslppssrDPQLPDLLSISNLRNNPLpgnnsssvntpqsnslh 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970668 275 ----VCDVCGKAFRKTSSLTQHERIHTGEKPYACGDCGKAFSQNMHLIVHQRTHTgEKPYVCPECGRAFSQnmHLTEHQR 350
Cdd:COG5048   169 pplpANSLSKDPSSNLSLLISSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENS-SSSLPLTTNSQLSPK--SLLSQSP 245
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970668 351 THTGEKPYA--CKECGKAFNKSSSLTLHQRNHTGE-------KPYVCGECGKAFSQSSYLIQHQR--FHIG--VKPFECS 417
Cdd:COG5048   246 SSLSSSDSSssASESPRSSLPTASSQSSSPNESDSssekgfsLPIKSKQCNISFSRSSPLTRHLRsvNHSGesLKPFSCP 325
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970668 418 E--CGKAFSKNSSLTQHQRIHTGEKPYECYI--CKKHFTGRS-----SLIVHQIVHTGEKPYVC--GECGKAFSQSAYLI 486
Cdd:COG5048   326 YslCGKLFSRNDALKRHILLHTSISPAKEKLlnSSSKFSPLLnneppQSLQQYKDLKNDKKSETlsNSCIRNFKRDSNLS 405
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970668 487 EHQRIHTGEKPY--RCGQCGKSFIKNSSLTVHQRIHTGEKPYRCgeCGKTFSRNTNLTRH 544
Cdd:COG5048   406 LHIITHLSFRPYncKNPPCSKSFNRHYNLIPHKKIHTNHAPLLC--SILKSFRRDLDLSN 463
 
Name Accession Description Interval E-value
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
13-54 9.61e-26

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: 99.47  E-value: 9.61e-26
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1631970668  13 SVTFRDVTVDFTQEEWQQLEPAQKDLYRDVMLENYRNLVSLD 54
Cdd:pfam01352   1 SVTFEDVAVDFTQEEWALLDPAQRNLYRDVMLENYRNLVSLG 42
KRAB smart00349
krueppel associated box;
14-61 2.32e-24

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 96.12  E-value: 2.32e-24
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 1631970668   14 VTFRDVTVDFTQEEWQQLEPAQKDLYRDVMLENYRNLVSLDWE-TRPEM 61
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQvPKPDL 49
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
14-53 1.08e-22

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: 90.69  E-value: 1.08e-22
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1631970668  14 VTFRDVTVDFTQEEWQQLEPAQKDLYRDVMLENYRNLVSL 53
Cdd:cd07765     1 VTFEDVAVYFSQEEWELLDPAQRDLYRDVMLENYENLVSL 40
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
170-544 6.46e-16

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 80.12  E-value: 6.46e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970668 170 NFSSTSDLSKPPMPC-----EEKKTYDCSECGKAFSRSSSLIKHQRIHTGEKPFEC--DTCGKHFIERSSLTIHQRVHTG 242
Cdd:COG5048     9 SSSNNSVLSSTPKSTlkslsNAPRPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCsySGCDKSFSRPLELSRHLRTHHN 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970668 243 ------------EKPYACGD----CGKAFS---------------QRMNLTVHQRTHTGEKPY----------------- 274
Cdd:COG5048    89 npsdlnskslplSNSKASSSslssSSSNSNdnnllsshslppssrDPQLPDLLSISNLRNNPLpgnnsssvntpqsnslh 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970668 275 ----VCDVCGKAFRKTSSLTQHERIHTGEKPYACGDCGKAFSQNMHLIVHQRTHTgEKPYVCPECGRAFSQnmHLTEHQR 350
Cdd:COG5048   169 pplpANSLSKDPSSNLSLLISSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENS-SSSLPLTTNSQLSPK--SLLSQSP 245
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970668 351 THTGEKPYA--CKECGKAFNKSSSLTLHQRNHTGE-------KPYVCGECGKAFSQSSYLIQHQR--FHIG--VKPFECS 417
Cdd:COG5048   246 SSLSSSDSSssASESPRSSLPTASSQSSSPNESDSssekgfsLPIKSKQCNISFSRSSPLTRHLRsvNHSGesLKPFSCP 325
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970668 418 E--CGKAFSKNSSLTQHQRIHTGEKPYECYI--CKKHFTGRS-----SLIVHQIVHTGEKPYVC--GECGKAFSQSAYLI 486
Cdd:COG5048   326 YslCGKLFSRNDALKRHILLHTSISPAKEKLlnSSSKFSPLLnneppQSLQQYKDLKNDKKSETlsNSCIRNFKRDSNLS 405
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970668 487 EHQRIHTGEKPY--RCGQCGKSFIKNSSLTVHQRIHTGEKPYRCgeCGKTFSRNTNLTRH 544
Cdd:COG5048   406 LHIITHLSFRPYncKNPPCSKSFNRHYNLIPHKKIHTNHAPLLC--SILKSFRRDLDLSN 463
zf-H2C2_2 pfam13465
Zinc-finger double domain;
344-369 3.53e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 40.82  E-value: 3.53e-05
                          10        20
                  ....*....|....*....|....*.
gi 1631970668 344 HLTEHQRTHTGEKPYACKECGKAFNK 369
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
PHA00733 PHA00733
hypothetical protein
385-450 4.25e-04

hypothetical protein


Pssm-ID: 177301  Cd Length: 128  Bit Score: 40.63  E-value: 4.25e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1631970668 385 PYVCGECGKAFSQSSYLIQHQRFHIGVKpfECSECGKAFSKNSSLTQHqrihtgekpyecyICKKH 450
Cdd:PHA00733   73 PYVCPLCLMPFSSSVSLKQHIRYTEHSK--VCPVCGKEFRNTDSTLDH-------------VCKKH 123
SUF4-like cd20908
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
192-240 5.25e-03

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


Pssm-ID: 411020 [Multi-domain]  Cd Length: 82  Bit Score: 36.00  E-value: 5.25e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1631970668 192 CSECGKAFSRSSSLIKHQRIHTgekpFECDTCGKHFIERSSLTIH-QRVH 240
Cdd:cd20908     4 CYYCDREFDDEKILIQHQKAKH----FKCHICHKKLYTAGGLAVHcLQVH 49
 
Name Accession Description Interval E-value
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
13-54 9.61e-26

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: 99.47  E-value: 9.61e-26
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1631970668  13 SVTFRDVTVDFTQEEWQQLEPAQKDLYRDVMLENYRNLVSLD 54
Cdd:pfam01352   1 SVTFEDVAVDFTQEEWALLDPAQRNLYRDVMLENYRNLVSLG 42
KRAB smart00349
krueppel associated box;
14-61 2.32e-24

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 96.12  E-value: 2.32e-24
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 1631970668   14 VTFRDVTVDFTQEEWQQLEPAQKDLYRDVMLENYRNLVSLDWE-TRPEM 61
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQvPKPDL 49
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
14-53 1.08e-22

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: 90.69  E-value: 1.08e-22
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1631970668  14 VTFRDVTVDFTQEEWQQLEPAQKDLYRDVMLENYRNLVSL 53
Cdd:cd07765     1 VTFEDVAVYFSQEEWELLDPAQRDLYRDVMLENYENLVSL 40
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
170-544 6.46e-16

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 80.12  E-value: 6.46e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970668 170 NFSSTSDLSKPPMPC-----EEKKTYDCSECGKAFSRSSSLIKHQRIHTGEKPFEC--DTCGKHFIERSSLTIHQRVHTG 242
Cdd:COG5048     9 SSSNNSVLSSTPKSTlkslsNAPRPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCsySGCDKSFSRPLELSRHLRTHHN 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970668 243 ------------EKPYACGD----CGKAFS---------------QRMNLTVHQRTHTGEKPY----------------- 274
Cdd:COG5048    89 npsdlnskslplSNSKASSSslssSSSNSNdnnllsshslppssrDPQLPDLLSISNLRNNPLpgnnsssvntpqsnslh 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970668 275 ----VCDVCGKAFRKTSSLTQHERIHTGEKPYACGDCGKAFSQNMHLIVHQRTHTgEKPYVCPECGRAFSQnmHLTEHQR 350
Cdd:COG5048   169 pplpANSLSKDPSSNLSLLISSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENS-SSSLPLTTNSQLSPK--SLLSQSP 245
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970668 351 THTGEKPYA--CKECGKAFNKSSSLTLHQRNHTGE-------KPYVCGECGKAFSQSSYLIQHQR--FHIG--VKPFECS 417
Cdd:COG5048   246 SSLSSSDSSssASESPRSSLPTASSQSSSPNESDSssekgfsLPIKSKQCNISFSRSSPLTRHLRsvNHSGesLKPFSCP 325
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970668 418 E--CGKAFSKNSSLTQHQRIHTGEKPYECYI--CKKHFTGRS-----SLIVHQIVHTGEKPYVC--GECGKAFSQSAYLI 486
Cdd:COG5048   326 YslCGKLFSRNDALKRHILLHTSISPAKEKLlnSSSKFSPLLnneppQSLQQYKDLKNDKKSETlsNSCIRNFKRDSNLS 405
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970668 487 EHQRIHTGEKPY--RCGQCGKSFIKNSSLTVHQRIHTGEKPYRCgeCGKTFSRNTNLTRH 544
Cdd:COG5048   406 LHIITHLSFRPYncKNPPCSKSFNRHYNLIPHKKIHTNHAPLLC--SILKSFRRDLDLSN 463
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
200-460 1.52e-12

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 69.72  E-value: 1.52e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970668 200 SRSSSLIKHQRIHTGEKPFECDTCGKHFIERSSLTIHQRVHTGEKPYACGDCGKAFSQrmNLTVHQRTHTGEK--PYVCD 277
Cdd:COG5048   181 SSNLSLLISSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPK--SLLSQSPSSLSSSdsSSSAS 258
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970668 278 VCGKAFRKTSSLTQHERIHTGE-------KPYACGDCGKAFSQNMHLIVHQRT--HTGE--KPYVCPE--CGRAFSQNMH 344
Cdd:COG5048   259 ESPRSSLPTASSQSSSPNESDSssekgfsLPIKSKQCNISFSRSSPLTRHLRSvnHSGEslKPFSCPYslCGKLFSRNDA 338
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970668 345 LTEHQRTHTGEKPYACKEC-------GKAFNKSSSLTLHQRNHTGEKPYVC--GECGKAFSQSSYLIQHQRFHIGVKP-- 413
Cdd:COG5048   339 LKRHILLHTSISPAKEKLLnssskfsPLLNNEPPQSLQQYKDLKNDKKSETlsNSCIRNFKRDSNLSLHIITHLSFRPyn 418
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1631970668 414 FECSECGKAFSKNSSLTQHQRIHTgEKPYECYICKKHFTGRSSLIVH 460
Cdd:COG5048   419 CKNPPCSKSFNRHYNLIPHKKIHT-NHAPLLCSILKSFRRDLDLSNH 464
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
202-548 1.99e-11

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 66.26  E-value: 1.99e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970668 202 SSSLIKHQRIHTGE----KPFECDTCGKHFIERSSLTIHQRVHTGEKPYACGD--CGKAFSQRMNLTVHQRTHTGEKPYV 275
Cdd:COG5048    14 SVLSSTPKSTLKSLsnapRPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYsgCDKSFSRPLELSRHLRTHHNNPSDL 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970668 276 C-DVCGKAFRKTSSLTQHERIHTGEKPYACGDCGKAFSQN--MHLIVHQRTHTGEKPYvcPECGRAFSQNM--------- 343
Cdd:COG5048    94 NsKSLPLSNSKASSSSLSSSSSNSNDNNLLSSHSLPPSSRdpQLPDLLSISNLRNNPL--PGNNSSSVNTPqsnslhppl 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970668 344 -------------HLTEHQRTHTGEKPYACKECGKAFNKSSSLTLHQRNHTGEKPYVCGECGKAFSQSSYLIQHQRFHIG 410
Cdd:COG5048   172 panslskdpssnlSLLISSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLSSS 251
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970668 411 VKPFECSECGKAFSKNSSLTQHQRIHtgekpyecyickKHFTGRSSLIvhqivhtgeKPYVCGECGKAFSQSAYLIEHQR 490
Cdd:COG5048   252 DSSSSASESPRSSLPTASSQSSSPNE------------SDSSSEKGFS---------LPIKSKQCNISFSRSSPLTRHLR 310
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1631970668 491 --IHTGE--KPYRCG--QCGKSFIKNSSLTVHQRIHTGEKPYRC--GECGKTFSRNTNLTRHLRIH 548
Cdd:COG5048   311 svNHSGEslKPFSCPysLCGKLFSRNDALKRHILLHTSISPAKEklLNSSSKFSPLLNNEPPQSLQ 376
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
244-549 2.76e-09

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 59.32  E-value: 2.76e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970668 244 KPYACGDCGKAFSQRMNLTVHQRTHTGEKPYVCDV--CGKAFRKTSSLTQHERIHTGEKPYACGDCG------KAFSQNM 315
Cdd:COG5048    32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYsgCDKSFSRPLELSRHLRTHHNNPSDLNSKSLplsnskASSSSLS 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970668 316 HLIVHQRTHTGEKPYVCPEcgrAFSQNMHLTEHQRTHTGEKP-YACKECGKAFNKSSSLTL-HQRNHTGEKPYVCGECG- 392
Cdd:COG5048   112 SSSSNSNDNNLLSSHSLPP---SSRDPQLPDLLSISNLRNNPlPGNNSSSVNTPQSNSLHPpLPANSLSKDPSSNLSLLi 188
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970668 393 ---KAFSQSSYLIQHQRFHIGVKPFECSECGKaFSKNSSLTQHQRIHTGEKPYECYIcKKHFTGRSSLIVHQIVHTGEKP 469
Cdd:COG5048   189 ssnVSTSIPSSSENSPLSSSYSIPSSSSDQNL-ENSSSSLPLTTNSQLSPKSLLSQS-PSSLSSSDSSSSASESPRSSLP 266
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970668 470 YVcGECGKAFSQSaYLIEHQRIHTgekPYRCGQCGKSFIKNSSLTVHQR--IHTGE--KPYRCGE--CGKTFSRNTNLTR 543
Cdd:COG5048   267 TA-SSQSSSPNES-DSSSEKGFSL---PIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCPYslCGKLFSRNDALKR 341

                  ....*.
gi 1631970668 544 HLRIHT 549
Cdd:COG5048   342 HILLHT 347
zf-H2C2_2 pfam13465
Zinc-finger double domain;
344-369 3.53e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 40.82  E-value: 3.53e-05
                          10        20
                  ....*....|....*....|....*.
gi 1631970668 344 HLTEHQRTHTGEKPYACKECGKAFNK 369
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
SFP1 COG5189
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ...
270-353 3.85e-05

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


Pssm-ID: 227516 [Multi-domain]  Cd Length: 423  Bit Score: 46.25  E-value: 3.85e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970668 270 GEKPYVCDV--CGKAFRKTSSLTQHeRIHtgekpyacGDCGKAFSQNMHLIVHQRTHTGEKPYVCPECGRAFSQNMHLTE 347
Cdd:COG5189   346 DGKPYKCPVegCNKKYKNQNGLKYH-MLH--------GHQNQKLHENPSPEKMNIFSAKDKPYRCEVCDKRYKNLNGLKY 416

                  ....*.
gi 1631970668 348 HqRTHT 353
Cdd:COG5189   417 H-RKHS 421
zf-H2C2_2 pfam13465
Zinc-finger double domain;
316-341 6.80e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 40.05  E-value: 6.80e-05
                          10        20
                  ....*....|....*....|....*.
gi 1631970668 316 HLIVHQRTHTGEKPYVCPECGRAFSQ 341
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
260-283 8.60e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 39.66  E-value: 8.60e-05
                          10        20
                  ....*....|....*....|....
gi 1631970668 260 NLTVHQRTHTGEKPYVCDVCGKAF 283
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSF 24
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
526-548 1.47e-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: 38.82  E-value: 1.47e-04
                          10        20
                  ....*....|....*....|...
gi 1631970668 526 YRCGECGKTFSRNTNLTRHLRIH 548
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
SFP1 COG5189
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ...
354-432 1.56e-04

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


Pssm-ID: 227516 [Multi-domain]  Cd Length: 423  Bit Score: 44.32  E-value: 1.56e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970668 354 GEKPYACK--ECGKAFNKSSSLTLHQRNhtgekpyvcGECGKAFSQSSYLIQHQRFHIGVKPFECSECGKAFSKNSSLTQ 431
Cdd:COG5189   346 DGKPYKCPveGCNKKYKNQNGLKYHMLH---------GHQNQKLHENPSPEKMNIFSAKDKPYRCEVCDKRYKNLNGLKY 416

                  .
gi 1631970668 432 H 432
Cdd:COG5189   417 H 417
zf-H2C2_2 pfam13465
Zinc-finger double domain;
288-313 1.60e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.89  E-value: 1.60e-04
                          10        20
                  ....*....|....*....|....*.
gi 1631970668 288 SLTQHERIHTGEKPYACGDCGKAFSQ 313
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
512-537 1.87e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.51  E-value: 1.87e-04
                          10        20
                  ....*....|....*....|....*.
gi 1631970668 512 SLTVHQRIHTGEKPYRCGECGKTFSR 537
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
484-507 2.53e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.12  E-value: 2.53e-04
                          10        20
                  ....*....|....*....|....
gi 1631970668 484 YLIEHQRIHTGEKPYRCGQCGKSF 507
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSF 24
PHA00733 PHA00733
hypothetical protein
385-450 4.25e-04

hypothetical protein


Pssm-ID: 177301  Cd Length: 128  Bit Score: 40.63  E-value: 4.25e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1631970668 385 PYVCGECGKAFSQSSYLIQHQRFHIGVKpfECSECGKAFSKNSSLTQHqrihtgekpyecyICKKH 450
Cdd:PHA00733   73 PYVCPLCLMPFSSSVSLKQHIRYTEHSK--VCPVCGKEFRNTDSTLDH-------------VCKKH 123
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
190-212 5.12e-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: 5.12e-04
                          10        20
                  ....*....|....*....|...
gi 1631970668 190 YDCSECGKAFSRSSSLIKHQRIH 212
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
372-397 5.44e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 37.35  E-value: 5.44e-04
                          10        20
                  ....*....|....*....|....*.
gi 1631970668 372 SLTLHQRNHTGEKPYVCGECGKAFSQ 397
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
204-227 5.66e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 37.35  E-value: 5.66e-04
                          10        20
                  ....*....|....*....|....
gi 1631970668 204 SLIKHQRIHTGEKPFECDTCGKHF 227
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSF 24
zf-H2C2_2 pfam13465
Zinc-finger double domain;
428-452 9.06e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.58  E-value: 9.06e-04
                          10        20
                  ....*....|....*....|....*
gi 1631970668 428 SLTQHQRIHTGEKPYECYICKKHFT 452
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFK 25
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
330-352 1.04e-03

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


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 36.51  E-value: 1.04e-03
                          10        20
                  ....*....|....*....|...
gi 1631970668 330 YVCPECGRAFSQNMHLTEHQRTH 352
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
400-425 1.07e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.58  E-value: 1.07e-03
                          10        20
                  ....*....|....*....|....*.
gi 1631970668 400 YLIQHQRFHIGVKPFECSECGKAFSK 425
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
414-436 1.14e-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: 36.51  E-value: 1.14e-03
                          10        20
                  ....*....|....*....|...
gi 1631970668 414 FECSECGKAFSKNSSLTQHQRIH 436
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
SFP1 COG5189
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ...
466-544 1.50e-03

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


Pssm-ID: 227516 [Multi-domain]  Cd Length: 423  Bit Score: 41.24  E-value: 1.50e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970668 466 GEKPYVCG--ECGKAFSQSAYLIEHqRIHtgekpyrcGQCGKSFIKNSSLTVHQRIHTGEKPYRCGECGKTFSRNTNLTR 543
Cdd:COG5189   346 DGKPYKCPveGCNKKYKNQNGLKYH-MLH--------GHQNQKLHENPSPEKMNIFSAKDKPYRCEVCDKRYKNLNGLKY 416

                  .
gi 1631970668 544 H 544
Cdd:COG5189   417 H 417
zf-H2C2_2 pfam13465
Zinc-finger double domain;
232-257 1.62e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.20  E-value: 1.62e-03
                          10        20
                  ....*....|....*....|....*.
gi 1631970668 232 SLTIHQRVHTGEKPYACGDCGKAFSQ 257
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
246-268 2.14e-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: 35.74  E-value: 2.14e-03
                          10        20
                  ....*....|....*....|...
gi 1631970668 246 YACGDCGKAFSQRMNLTVHQRTH 268
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
498-520 2.58e-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: 2.58e-03
                          10        20
                  ....*....|....*....|...
gi 1631970668 498 YRCGQCGKSFIKNSSLTVHQRIH 520
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
302-324 2.96e-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: 2.96e-03
                          10        20
                  ....*....|....*....|...
gi 1631970668 302 YACGDCGKAFSQNMHLIVHQRTH 324
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
PHA00733 PHA00733
hypothetical protein
245-292 3.20e-03

hypothetical protein


Pssm-ID: 177301  Cd Length: 128  Bit Score: 37.93  E-value: 3.20e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1631970668 245 PYACGDCGKAFSQRMNLTVHQRTHTGEKpyVCDVCGKAFRKTSSLTQH 292
Cdd:PHA00733   73 PYVCPLCLMPFSSSVSLKQHIRYTEHSK--VCPVCGKEFRNTDSTLDH 118
PHA00733 PHA00733
hypothetical protein
329-376 4.03e-03

hypothetical protein


Pssm-ID: 177301  Cd Length: 128  Bit Score: 37.55  E-value: 4.03e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1631970668 329 PYVCPECGRAFSQNMHLTEHQRTHTGEKpyACKECGKAFNKSSSLTLH 376
Cdd:PHA00733   73 PYVCPLCLMPFSSSVSLKQHIRYTEHSK--VCPVCGKEFRNTDSTLDH 118
zf-H2C2_2 pfam13465
Zinc-finger double domain;
456-481 4.03e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.04  E-value: 4.03e-03
                          10        20
                  ....*....|....*....|....*.
gi 1631970668 456 SLIVHQIVHTGEKPYVCGECGKAFSQ 481
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
386-408 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 1631970668 386 YVCGECGKAFSQSSYLIQHQRFH 408
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
SUF4-like cd20908
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
192-240 5.25e-03

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


Pssm-ID: 411020 [Multi-domain]  Cd Length: 82  Bit Score: 36.00  E-value: 5.25e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1631970668 192 CSECGKAFSRSSSLIKHQRIHTgekpFECDTCGKHFIERSSLTIH-QRVH 240
Cdd:cd20908     4 CYYCDREFDDEKILIQHQKAKH----FKCHICHKKLYTAGGLAVHcLQVH 49
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
470-492 6.18e-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: 6.18e-03
                          10        20
                  ....*....|....*....|...
gi 1631970668 470 YVCGECGKAFSQSAYLIEHQRIH 492
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
358-380 8.14e-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: 33.81  E-value: 8.14e-03
                          10        20
                  ....*....|....*....|...
gi 1631970668 358 YACKECGKAFNKSSSLTLHQRNH 380
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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