NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|564370656|ref|XP_006245893|]
View 

zinc finger protein 263 isoform X1 [Rattus norvegicus]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
SCAN super family cl42860
leucine rich region;
41-133 2.14e-49

leucine rich region;


The actual alignment was detected with superfamily member smart00431:

Pssm-ID: 128708 [Multi-domain]  Cd Length: 113  Bit Score: 166.71  E-value: 2.14e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564370656    41 ASHLRFRRFRFQDASGPREALNQLQELCRGWLRPEMRTKEQILELLVLEQFLTILPQEIQSRVQELRPESGEEAVTLVER 120
Cdd:smart00431   3 IFRQRFRQFRYQETSGPREALSRLRELCRQWLRPELHTKEQILELLVLEQFLTILPGELQAWVREHHPESGEEAVTLLED 82

                           90
                   ....*....|...
gi 564370656   121 MQKELGKLRQQLP 133
Cdd:smart00431  83 LERELDEPGQQVS 95
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
375-561 1.10e-11

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


:

Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 67.41  E-value: 1.10e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564370656 375 KPFQCNVCGKSFSCNSNLNRHQRT--HTGE--KPYKCPE--CGEIFAHSSNLLRHQRIHTGERPYRC--SECGKSFSRSS 446
Cdd:COG5048  288 LPIKSKQCNISFSRSSPLTRHLRSvnHSGEslKPFSCPYslCGKLFSRNDALKRHILLHTSISPAKEklLNSSSKFSPLL 367

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564370656 447 HLVIHERTHEKERLDP-LPECGQGINDSAPFLTNHRVEKklfecstcgksfrqgmHLTRH--QRTHtgekPYKCILCGEN 523
Cdd:COG5048  368 NNEPPQSLQQYKDLKNdKKSETLSNSCIRNFKRDSNLSL----------------HIITHlsFRPY----NCKNPPCSKS 427

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 564370656 524 FSHRSNLIRHQRIHTGEKPYTCHECGDSFS--HSSNRIRH 561
Cdd:COG5048  428 FNRHYNLIPHKKIHTNHAPLLCSILKSFRRdlDLSNHGKD 467
KRAB_A-box super family cl02581
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
 134-172 1.14e-05

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.


The actual alignment was detected with superfamily member cd07765:

Pssm-ID: 470626  Cd Length: 40  Bit Score: 42.54  E-value: 1.14e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 564370656 134 ESLEDMAMYISQ-EWDHQDHSKRAPSRDMVQDSYENVGTL 172
Cdd:cd07765    1 VTFEDVAVYFSQeEWELLDPAQRDLYRDVMLENYENLVSL 40
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
282-446 3.91e-05

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


:

Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 46.61  E-value: 3.91e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564370656 282 LVQAKEQPKKLHLCALCGKNFSNNSNLIRHQRI------HAAEKLCMDVECGEVFGGHPHFLSLHRTHVGEEAHKC--LE 353
Cdd:COG5048  279 DSSSEKGFSLPIKSKQCNISFSRSSPLTRHLRSvnhsgeSLKPFSCPYSLCGKLFSRNDALKRHILLHTSISPAKEklLN 358

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564370656 354 CGKCFSQNTH-----LTRHQRTHTGEKPFQCNV--CGKSFSCNSNLNRHQRTHTGEKPY--KCPECGEIFAHSSNLLRHQ 424
Cdd:COG5048  359 SSSKFSPLLNneppqSLQQYKDLKNDKKSETLSnsCIRNFKRDSNLSLHIITHLSFRPYncKNPPCSKSFNRHYNLIPHK 438

                        170       180
                 ....*....|....*....|..
gi 564370656 425 RIHTGERPYRCSECGKSFSRSS 446
Cdd:COG5048  439 KIHTNHAPLLCSILKSFRRDLD 460
zf-H2C2_2 pfam13465
Zinc-finger double domain;
560-582 1.06e-04

Zinc-finger double domain;


:

Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 39.66  E-value: 1.06e-04
                          10        20
                  ....*....|....*....|...
gi 564370656  560 RHLRTHTGERPYKCSECGESFSR 582
Cdd:pfam13465   4 RHMRTHTGEKPYKCPECGKSFKS 26
 
Name Accession Description Interval E-value
SCAN smart00431
leucine rich region;
41-133 2.14e-49

leucine rich region;


Pssm-ID: 128708 [Multi-domain]  Cd Length: 113  Bit Score: 166.71  E-value: 2.14e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564370656    41 ASHLRFRRFRFQDASGPREALNQLQELCRGWLRPEMRTKEQILELLVLEQFLTILPQEIQSRVQELRPESGEEAVTLVER 120
Cdd:smart00431   3 IFRQRFRQFRYQETSGPREALSRLRELCRQWLRPELHTKEQILELLVLEQFLTILPGELQAWVREHHPESGEEAVTLLED 82

                           90
                   ....*....|...
gi 564370656   121 MQKELGKLRQQLP 133
Cdd:smart00431  83 LERELDEPGQQVS 95
SCAN pfam02023
SCAN domain; The SCAN domain (named after SRE-ZBP, CTfin51, AW-1 and Number 18 cDNA) is found ...
 41-127 6.10e-44

SCAN domain; The SCAN domain (named after SRE-ZBP, CTfin51, AW-1 and Number 18 cDNA) is found in several pfam00096 proteins. The domain has been shown to be able to mediate homo- and hetero-oligomerization.


Pssm-ID: 460417 [Multi-domain]  Cd Length: 89  Bit Score: 151.49  E-value: 6.10e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564370656   41 ASHLRFRRFRFQDASGPREALNQLQELCRGWLRPEMRTKEQILELLVLEQFLTILPQEIQSRVQELRPESGEEAVTLVER 120
Cdd:pfam02023   3 ASRQRFRQFCYQEAEGPREALSQLRELCHQWLRPEKHTKEQILELLVLEQFLTILPEEIQSWVREHHPESGEEAVALAED 82


                  ....*..
gi 564370656  121 MQKELGK 127
Cdd:pfam02023  83 LLLERGE 89
SCAN cd07936
SCAN oligomerization domain; The SCAN domain (named after SRE-ZBP, CTfin51, AW-1 and Number 18 ...
 41-122 3.95e-36

SCAN oligomerization domain; The SCAN domain (named after SRE-ZBP, CTfin51, AW-1 and Number 18 cDNA) is found in several vertebrate proteins that contain C2H2 zinc finger motifs, many of which may be transcription factors playing roles in cell survival and differentiation. This protein-interaction domain is able to mediate homo- and hetero-oligomerization of SCAN-containing proteins. Some SCAN-containing proteins, including those of lower vertebrates, do not contain zinc finger motifs. It has been noted that the SCAN domain resembles a domain-swapped version of the C-terminal domain of the HIV capsid protein. This domain model features elements common to the three general groups of SCAN domains (SCAN-A1, SCAN-A2, and SCAN-B). The SCAND1 protein is truncated at the C-terminus with respect to this model, the SCAND2 protein appears to have a truncated central helix.


Pssm-ID: 153421  Cd Length: 85  Bit Score: 130.07  E-value: 3.95e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564370656  41 ASHLRFRRFRFQDASGPREALNQLQELCRGWLRPEMRTKEQILELLVLEQFLTILPQEIQSRVQELRPESGEEAVTLVER 120
Cdd:cd07936    3 TYRQRFRAFQYQEASGPREALQRLRELCRQWLRPEIHTKEQILELLVLEQFLIILPPEVQAWVRERKPESGEEAATLAED 82


                 ..
gi 564370656 121 MQ 122
Cdd:cd07936   83 LL 84
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
375-561 1.10e-11

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 67.41  E-value: 1.10e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564370656 375 KPFQCNVCGKSFSCNSNLNRHQRT--HTGE--KPYKCPE--CGEIFAHSSNLLRHQRIHTGERPYRC--SECGKSFSRSS 446
Cdd:COG5048  288 LPIKSKQCNISFSRSSPLTRHLRSvnHSGEslKPFSCPYslCGKLFSRNDALKRHILLHTSISPAKEklLNSSSKFSPLL 367

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564370656 447 HLVIHERTHEKERLDP-LPECGQGINDSAPFLTNHRVEKklfecstcgksfrqgmHLTRH--QRTHtgekPYKCILCGEN 523
Cdd:COG5048  368 NNEPPQSLQQYKDLKNdKKSETLSNSCIRNFKRDSNLSL----------------HIITHlsFRPY----NCKNPPCSKS 427

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 564370656 524 FSHRSNLIRHQRIHTGEKPYTCHECGDSFS--HSSNRIRH 561
Cdd:COG5048  428 FNRHYNLIPHKKIHTNHAPLLCSILKSFRRdlDLSNHGKD 467
zf-H2C2_2 pfam13465
Zinc-finger double domain;
391-416 6.47e-06

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 42.74  E-value: 6.47e-06
                          10        20
                  ....*....|....*....|....*.
gi 564370656  391 NLNRHQRTHTGEKPYKCPECGEIFAH 416
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
 134-172 1.14e-05

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: 42.54  E-value: 1.14e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 564370656 134 ESLEDMAMYISQ-EWDHQDHSKRAPSRDMVQDSYENVGTL 172
Cdd:cd07765    1 VTFEDVAVYFSQeEWELLDPAQRDLYRDVMLENYENLVSL 40
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
282-446 3.91e-05

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 46.61  E-value: 3.91e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564370656 282 LVQAKEQPKKLHLCALCGKNFSNNSNLIRHQRI------HAAEKLCMDVECGEVFGGHPHFLSLHRTHVGEEAHKC--LE 353
Cdd:COG5048  279 DSSSEKGFSLPIKSKQCNISFSRSSPLTRHLRSvnhsgeSLKPFSCPYSLCGKLFSRNDALKRHILLHTSISPAKEklLN 358

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564370656 354 CGKCFSQNTH-----LTRHQRTHTGEKPFQCNV--CGKSFSCNSNLNRHQRTHTGEKPY--KCPECGEIFAHSSNLLRHQ 424
Cdd:COG5048  359 SSSKFSPLLNneppqSLQQYKDLKNDKKSETLSnsCIRNFKRDSNLSLHIITHLSFRPYncKNPPCSKSFNRHYNLIPHK 438

                        170       180
                 ....*....|....*....|..
gi 564370656 425 RIHTGERPYRCSECGKSFSRSS 446
Cdd:COG5048  439 KIHTNHAPLLCSILKSFRRDLD 460
zf-H2C2_2 pfam13465
Zinc-finger double domain;
560-582 1.06e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 39.66  E-value: 1.06e-04
                          10        20
                  ....*....|....*....|...
gi 564370656  560 RHLRTHTGERPYKCSECGESFSR 582
Cdd:pfam13465   4 RHMRTHTGEKPYKCPECGKSFKS 26
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
541-594 1.46e-04

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 44.69  E-value: 1.46e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 564370656 541 KPYTCHECGDSFSHSSNRIRHLRTHTGERPYKCS--ECGESFSRSSRLTSHQRTHT 594
Cdd:COG5048   32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSysGCDKSFSRPLELSRHLRTHH 87
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 349-371 2.73e-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: 38.44  E-value: 2.73e-04
                          10        20
                  ....*....|....*....|...
gi 564370656  349 HKCLECGKCFSQNTHLTRHQRTH 371
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
SUF4-like cd20908
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
 403-475 9.34e-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: 35.61  E-value: 9.34e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564370656 403 KPYkCPECGEIFAHSSNLLRHQRIHTgerpYRCSECGKSFSRSSHLVIHERTHEKERLDPLPECGQGINDSAP 475
Cdd:cd20908    1 KPW-CYYCDREFDDEKILIQHQKAKH----FKCHICHKKLYTAGGLAVHCLQVHKETLTKVPNALPGRDDPEI 68
 
Name Accession Description Interval E-value
SCAN smart00431
leucine rich region;
41-133 2.14e-49

leucine rich region;


Pssm-ID: 128708 [Multi-domain]  Cd Length: 113  Bit Score: 166.71  E-value: 2.14e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564370656    41 ASHLRFRRFRFQDASGPREALNQLQELCRGWLRPEMRTKEQILELLVLEQFLTILPQEIQSRVQELRPESGEEAVTLVER 120
Cdd:smart00431   3 IFRQRFRQFRYQETSGPREALSRLRELCRQWLRPELHTKEQILELLVLEQFLTILPGELQAWVREHHPESGEEAVTLLED 82

                           90
                   ....*....|...
gi 564370656   121 MQKELGKLRQQLP 133
Cdd:smart00431  83 LERELDEPGQQVS 95
SCAN pfam02023
SCAN domain; The SCAN domain (named after SRE-ZBP, CTfin51, AW-1 and Number 18 cDNA) is found ...
 41-127 6.10e-44

SCAN domain; The SCAN domain (named after SRE-ZBP, CTfin51, AW-1 and Number 18 cDNA) is found in several pfam00096 proteins. The domain has been shown to be able to mediate homo- and hetero-oligomerization.


Pssm-ID: 460417 [Multi-domain]  Cd Length: 89  Bit Score: 151.49  E-value: 6.10e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564370656   41 ASHLRFRRFRFQDASGPREALNQLQELCRGWLRPEMRTKEQILELLVLEQFLTILPQEIQSRVQELRPESGEEAVTLVER 120
Cdd:pfam02023   3 ASRQRFRQFCYQEAEGPREALSQLRELCHQWLRPEKHTKEQILELLVLEQFLTILPEEIQSWVREHHPESGEEAVALAED 82


                  ....*..
gi 564370656  121 MQKELGK 127
Cdd:pfam02023  83 LLLERGE 89
SCAN cd07936
SCAN oligomerization domain; The SCAN domain (named after SRE-ZBP, CTfin51, AW-1 and Number 18 ...
 41-122 3.95e-36

SCAN oligomerization domain; The SCAN domain (named after SRE-ZBP, CTfin51, AW-1 and Number 18 cDNA) is found in several vertebrate proteins that contain C2H2 zinc finger motifs, many of which may be transcription factors playing roles in cell survival and differentiation. This protein-interaction domain is able to mediate homo- and hetero-oligomerization of SCAN-containing proteins. Some SCAN-containing proteins, including those of lower vertebrates, do not contain zinc finger motifs. It has been noted that the SCAN domain resembles a domain-swapped version of the C-terminal domain of the HIV capsid protein. This domain model features elements common to the three general groups of SCAN domains (SCAN-A1, SCAN-A2, and SCAN-B). The SCAND1 protein is truncated at the C-terminus with respect to this model, the SCAND2 protein appears to have a truncated central helix.


Pssm-ID: 153421  Cd Length: 85  Bit Score: 130.07  E-value: 3.95e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564370656  41 ASHLRFRRFRFQDASGPREALNQLQELCRGWLRPEMRTKEQILELLVLEQFLTILPQEIQSRVQELRPESGEEAVTLVER 120
Cdd:cd07936    3 TYRQRFRAFQYQEASGPREALQRLRELCRQWLRPEIHTKEQILELLVLEQFLIILPPEVQAWVRERKPESGEEAATLAED 82


                 ..
gi 564370656 121 MQ 122
Cdd:cd07936   83 LL 84
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
375-561 1.10e-11

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 67.41  E-value: 1.10e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564370656 375 KPFQCNVCGKSFSCNSNLNRHQRT--HTGE--KPYKCPE--CGEIFAHSSNLLRHQRIHTGERPYRC--SECGKSFSRSS 446
Cdd:COG5048  288 LPIKSKQCNISFSRSSPLTRHLRSvnHSGEslKPFSCPYslCGKLFSRNDALKRHILLHTSISPAKEklLNSSSKFSPLL 367

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564370656 447 HLVIHERTHEKERLDP-LPECGQGINDSAPFLTNHRVEKklfecstcgksfrqgmHLTRH--QRTHtgekPYKCILCGEN 523
Cdd:COG5048  368 NNEPPQSLQQYKDLKNdKKSETLSNSCIRNFKRDSNLSL----------------HIITHlsFRPY----NCKNPPCSKS 427

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 564370656 524 FSHRSNLIRHQRIHTGEKPYTCHECGDSFS--HSSNRIRH 561
Cdd:COG5048  428 FNRHYNLIPHKKIHTNHAPLLCSILKSFRRdlDLSNHGKD 467
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
349-590 2.72e-10

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 62.79  E-value: 2.72e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564370656 349 HKCLECGKCFSQNTHLTRHQRTHTGEKPFQCNV--CGKSFSCNSNLNRHQRTHTGEKPYKC--PECGEIFAHSSNLLRHQ 424
Cdd:COG5048   34 DSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYsgCDKSFSRPLELSRHLRTHHNNPSDLNskSLPLSNSKASSSSLSSS 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564370656 425 rIHTGERPYRCSECGKSFSRSSHLVIHERTHEKERLDPLPEC-GQGINDSAPFLTNHRVEKKLFecstcGKSFRQGMHLT 503
Cdd:COG5048  114 -SSNSNDNNLLSSHSLPPSSRDPQLPDLLSISNLRNNPLPGNnSSSVNTPQSNSLHPPLPANSL-----SKDPSSNLSLL 187

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564370656 504 RHQRTHTGEKPYKCILCGENFSHRSNLIRHQRIHTGEKPYTCHECGDSFSHSSNRIRHLRTHTGERPYKCSECGESFSRS 583
Cdd:COG5048  188 ISSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLSSSDSSSSASESPRSSLPT 267


                 ....*..
gi 564370656 584 SRLTSHQ 590
Cdd:COG5048  268 ASSQSSS 274
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
359-594 3.13e-09

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 59.32  E-value: 3.13e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564370656 359 SQNTHLTRHQRTHTGEKPFQCNVCGKSFSCNSNLNRHQRTHTGEKPYKCPECGEIFAHSSNLLRHQRIHTGERPYRCSEC 438
Cdd:COG5048  181 SSNLSLLISSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLSSSDSSSSASES 260

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564370656 439 G------KSFSRSSHLVIHERTHEKERLDPL-PECGQGINDSAPFLTNHRVEKKLFEC--------STCGKSFRQGMHLT 503
Cdd:COG5048  261 PrsslptASSQSSSPNESDSSSEKGFSLPIKsKQCNISFSRSSPLTRHLRSVNHSGESlkpfscpySLCGKLFSRNDALK 340

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564370656 504 RHQRTHTGEKPYKCILCGENFSHRSNL-------IRHQRIHTGEKPYTC--HECGDSFSHSSNRIRHLRTHTGERP--YK 572
Cdd:COG5048  341 RHILLHTSISPAKEKLLNSSSKFSPLLnneppqsLQQYKDLKNDKKSETlsNSCIRNFKRDSNLSLHIITHLSFRPynCK 420

                        250       260
                 ....*....|....*....|..
gi 564370656 573 CSECGESFSRSSRLTSHQRTHT 594
Cdd:COG5048  421 NPPCSKSFNRHYNLIPHKKIHT 442
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
284-588 8.60e-08

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 55.09  E-value: 8.60e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564370656 284 QAKEQPKKLHLCALCGKNFSNNSNLIRHQRIHAAEKL--CMDVECGEVFG----GHPHFLSLHRTHVGEEAHKCL----- 352
Cdd:COG5048   25 KSLSNAPRPDSCPNCTDSFSRLEHLTRHIRSHTGEKPsqCSYSGCDKSFSrpleLSRHLRTHHNNPSDLNSKSLPlsnsk 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564370656 353 -------ECGKCFSQNTHLTRHQRTHTGEKPFQCNVcgkSFSCNSNLNRHQRTHTGEKPYKCP-----------ECGEIF 414
Cdd:COG5048  105 asssslsSSSSNSNDNNLLSSHSLPPSSRDPQLPDL---LSISNLRNNPLPGNNSSSVNTPQSnslhpplpansLSKDPS 181

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564370656 415 AHSSNLLRHQRIHTGERPYRCSECGKSFSRSSHLVIHERTHEKERLdPLPECGQGINDSAPFL--------TNHRVEKKL 486
Cdd:COG5048  182 SNLSLLISSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSL-PLTTNSQLSPKSLLSQspsslsssDSSSSASES 260

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564370656 487 FECSTCGKSFRQGMHLTRHQRTHTG-EKPYKCILCGENFSHRSNLIRHQR--IHTGE--KPYTCHE--CGDSFSHSSNRI 559
Cdd:COG5048  261 PRSSLPTASSQSSSPNESDSSSEKGfSLPIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCPYslCGKLFSRNDALK 340

                        330       340
                 ....*....|....*....|....*....
gi 564370656 560 RHLRTHTGERPYKCSECGESFSRSSRLTS 588
Cdd:COG5048  341 RHILLHTSISPAKEKLLNSSSKFSPLLNN 369
zf-H2C2_2 pfam13465
Zinc-finger double domain;
391-416 6.47e-06

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 42.74  E-value: 6.47e-06
                          10        20
                  ....*....|....*....|....*.
gi 564370656  391 NLNRHQRTHTGEKPYKCPECGEIFAH 416
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
363-388 8.19e-06

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 42.74  E-value: 8.19e-06
                          10        20
                  ....*....|....*....|....*.
gi 564370656  363 HLTRHQRTHTGEKPFQCNVCGKSFSC 388
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
419-444 9.67e-06

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 42.36  E-value: 9.67e-06
                          10        20
                  ....*....|....*....|....*.
gi 564370656  419 NLLRHQRIHTGERPYRCSECGKSFSR 444
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
 134-172 1.14e-05

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: 42.54  E-value: 1.14e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 564370656 134 ESLEDMAMYISQ-EWDHQDHSKRAPSRDMVQDSYENVGTL 172
Cdd:cd07765    1 VTFEDVAVYFSQeEWELLDPAQRDLYRDVMLENYENLVSL 40
zf-H2C2_2 pfam13465
Zinc-finger double domain;
529-554 3.36e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 40.82  E-value: 3.36e-05
                          10        20
                  ....*....|....*....|....*.
gi 564370656  529 NLIRHQRIHTGEKPYTCHECGDSFSH 554
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
282-446 3.91e-05

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 46.61  E-value: 3.91e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564370656 282 LVQAKEQPKKLHLCALCGKNFSNNSNLIRHQRI------HAAEKLCMDVECGEVFGGHPHFLSLHRTHVGEEAHKC--LE 353
Cdd:COG5048  279 DSSSEKGFSLPIKSKQCNISFSRSSPLTRHLRSvnhsgeSLKPFSCPYSLCGKLFSRNDALKRHILLHTSISPAKEklLN 358

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564370656 354 CGKCFSQNTH-----LTRHQRTHTGEKPFQCNV--CGKSFSCNSNLNRHQRTHTGEKPY--KCPECGEIFAHSSNLLRHQ 424
Cdd:COG5048  359 SSSKFSPLLNneppqSLQQYKDLKNDKKSETLSnsCIRNFKRDSNLSLHIITHLSFRPYncKNPPCSKSFNRHYNLIPHK 438

                        170       180
                 ....*....|....*....|..
gi 564370656 425 RIHTGERPYRCSECGKSFSRSS 446
Cdd:COG5048  439 KIHTNHAPLLCSILKSFRRDLD 460
zf-H2C2_2 pfam13465
Zinc-finger double domain;
501-526 9.58e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 39.66  E-value: 9.58e-05
                          10        20
                  ....*....|....*....|....*.
gi 564370656  501 HLTRHQRTHTGEKPYKCILCGENFSH 526
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
560-582 1.06e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 39.66  E-value: 1.06e-04
                          10        20
                  ....*....|....*....|...
gi 564370656  560 RHLRTHTGERPYKCSECGESFSR 582
Cdd:pfam13465   4 RHMRTHTGEKPYKCPECGKSFKS 26
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
541-594 1.46e-04

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 44.69  E-value: 1.46e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 564370656 541 KPYTCHECGDSFSHSSNRIRHLRTHTGERPYKCS--ECGESFSRSSRLTSHQRTHT 594
Cdd:COG5048   32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSysGCDKSFSRPLELSRHLRTHH 87
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
385-455 1.59e-04

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 44.30  E-value: 1.59e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564370656 385 SFSCNSNLN-RHQRTHTGE----KPYKCPECGEIFAHSSNLLRHQRIHTGERPYRCS--ECGKSFSRSSHLVIHERTH 455
Cdd:COG5048    9 SSSNNSVLSsTPKSTLKSLsnapRPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSysGCDKSFSRPLELSRHLRTH 86
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 349-371 2.73e-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: 38.44  E-value: 2.73e-04
                          10        20
                  ....*....|....*....|...
gi 564370656  349 HKCLECGKCFSQNTHLTRHQRTH 371
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 433-455 3.93e-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: 37.66  E-value: 3.93e-04
                          10        20
                  ....*....|....*....|...
gi 564370656  433 YRCSECGKSFSRSSHLVIHERTH 455
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 405-427 5.81e-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: 5.81e-04
                          10        20
                  ....*....|....*....|...
gi 564370656  405 YKCPECGEIFAHSSNLLRHQRIH 427
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 571-593 1.24e-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: 1.24e-03
                          10        20
                  ....*....|....*....|...
gi 564370656  571 YKCSECGESFSRSSRLTSHQRTH 593
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 377-399 1.49e-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: 1.49e-03
                          10        20
                  ....*....|....*....|...
gi 564370656  377 FQCNVCGKSFSCNSNLNRHQRTH 399
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
SFP1 COG5189
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ...
 373-455 3.04e-03

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


Pssm-ID: 227516 [Multi-domain]  Cd Length: 423  Bit Score: 40.47  E-value: 3.04e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564370656 373 GEKPFQCNV--CGKSFScNSNLNRHQRTHTGEKPYKCPECGEIfahssnllRHQRIHTGERPYRCSECGKSFSRSSHLVI 450
Cdd:COG5189  346 DGKPYKCPVegCNKKYK-NQNGLKYHMLHGHQNQKLHENPSPE--------KMNIFSAKDKPYRCEVCDKRYKNLNGLKY 416


                 ....*
gi 564370656 451 HeRTH 455
Cdd:COG5189  417 H-RKH 420
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 487-509 3.20e-03

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


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 35.35  E-value: 3.20e-03
                          10        20
                  ....*....|....*....|...
gi 564370656  487 FECSTCGKSFRQGMHLTRHQRTH 509
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 295-315 7.16e-03

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


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 34.20  E-value: 7.16e-03
                          10        20
                  ....*....|....*....|.
gi 564370656  295 CALCGKNFSNNSNLIRHQRIH 315
Cdd:pfam00096   3 CPDCGKSFSRKSNLKRHLRTH 23
SUF4-like cd20908
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
 403-475 9.34e-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: 35.61  E-value: 9.34e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564370656 403 KPYkCPECGEIFAHSSNLLRHQRIHTgerpYRCSECGKSFSRSSHLVIHERTHEKERLDPLPECGQGINDSAP 475
Cdd:cd20908    1 KPW-CYYCDREFDDEKILIQHQKAKH----FKCHICHKKLYTAGGLAVHCLQVHKETLTKVPNALPGRDDPEI 68
 
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