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Conserved domains on  [gi|568982068|ref|XP_006516852|]
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zinc finger protein with KRAB and SCAN domains 3 isoform X1 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SCAN smart00431
leucine rich region;
47-159 6.35e-58

leucine rich region;


:

Pssm-ID: 128708 [Multi-domain]  Cd Length: 113  Bit Score: 188.67  E-value: 6.35e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568982068    47 PDRSRQRFRAFRYPEAAGPRQALSRLRELCRQWLRPDMHSKEQILELLVLEQFLTILPGELQAWVREQHPDSGEEVVALL 126
Cdd:smart00431   1 PEIFRQRFRQFRYQETSGPREALSRLRELCRQWLRPELHTKEQILELLVLEQFLTILPGELQAWVREHHPESGEEAVTLL 80

                           90       100       110
                   ....*....|....*....|....*....|...
gi 568982068   127 EYLDRQLDDTPPQVPDDDDGQELLCSKAVLLTS 159
Cdd:smart00431  81 EDLERELDEPGQQVSAHVHGQEVLLEKMVPLGA 113
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
367-514 2.92e-09

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


:

Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 59.32  E-value: 2.92e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568982068 367 KPYECEECGKAFSHSSDLIKHQRT--HTGE--KPYECD--DCGKTFTQSCSLLEHHRIHTGEKPYQCNM--CPKAFRRSS 438
Cdd:COG5048  288 LPIKSKQCNISFSRSSPLTRHLRSvnHSGEslKPFSCPysLCGKLFSRNDALKRHILLHTSISPAKEKLlnSSSKFSPLL 367

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568982068 439 HLLRHQRTHTGDKDFFVPEPYWESQSRVESHWENIETPVSYQCNDCER-----------SFSRITSLIEHQKVHTGEKPF 507
Cdd:COG5048  368 NNEPPQSLQQYKDLKNDKKSETLSNSCIRNFKRDSNLSLHIITHLSFRpyncknppcskSFNRHYNLIPHKKIHTNHAPL 447


                 ....*..
gi 568982068 508 ECQTCGK 514
Cdd:COG5048  448 LCSILKS 454
KRAB super family cl42959
krueppel associated box;
213-267 2.50e-07

krueppel associated box;


The actual alignment was detected with superfamily member smart00349:

Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 47.59  E-value: 2.50e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 568982068   213 LKMEDVAPVLSP-RWTEQDSSQMNLYKDGMQEHSGSLVSLDQDMQTK--VRDLPRAEE 267
Cdd:smart00349   1 VTFEDVAVYFTQeEWEQLDPAQKNLYRDVMLENYSNLVSLGFQVPKPdlISQLEQGEE 58
zf-H2C2_2 pfam13465
Zinc-finger double domain;
328-350 2.70e-05

Zinc-finger double domain;


:

Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 41.20  E-value: 2.70e-05
                          10        20
                  ....*....|....*....|...
gi 568982068  328 LSKHKRIHTGLKPYECEECGKAF 350
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSF 24
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 507-529 1.93e-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: 38.44  E-value: 1.93e-04
                          10        20
                  ....*....|....*....|...
gi 568982068  507 FECQTCGKGFTRPSYLIQHQRRH 529
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 313-335 9.01e-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: 36.89  E-value: 9.01e-04
                          10        20
                  ....*....|....*....|...
gi 568982068  313 FYCRECGKSFAQSSGLSKHKRIH 335
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 341-363 1.23e-03

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


:

Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 36.51  E-value: 1.23e-03
                          10        20
                  ....*....|....*....|...
gi 568982068  341 YECEECGKAFIGSSALIIHQRVH 363
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
 
Name Accession Description Interval E-value
SCAN smart00431
leucine rich region;
47-159 6.35e-58

leucine rich region;


Pssm-ID: 128708 [Multi-domain]  Cd Length: 113  Bit Score: 188.67  E-value: 6.35e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568982068    47 PDRSRQRFRAFRYPEAAGPRQALSRLRELCRQWLRPDMHSKEQILELLVLEQFLTILPGELQAWVREQHPDSGEEVVALL 126
Cdd:smart00431   1 PEIFRQRFRQFRYQETSGPREALSRLRELCRQWLRPELHTKEQILELLVLEQFLTILPGELQAWVREHHPESGEEAVTLL 80

                           90       100       110
                   ....*....|....*....|....*....|...
gi 568982068   127 EYLDRQLDDTPPQVPDDDDGQELLCSKAVLLTS 159
Cdd:smart00431  81 EDLERELDEPGQQVSAHVHGQEVLLEKMVPLGA 113
SCAN pfam02023
SCAN domain; The SCAN domain (named after SRE-ZBP, CTfin51, AW-1 and Number 18 cDNA) is found ...
 47-135 4.18e-49

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: 164.58  E-value: 4.18e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568982068   47 PDRSRQRFRAFRYPEAAGPRQALSRLRELCRQWLRPDMHSKEQILELLVLEQFLTILPGELQAWVREQHPDSGEEVVALL 126
Cdd:pfam02023   1 PEASRQRFRQFCYQEAEGPREALSQLRELCHQWLRPEKHTKEQILELLVLEQFLTILPEEIQSWVREHHPESGEEAVALA 80


                  ....*....
gi 568982068  127 EYLDRQLDD 135
Cdd:pfam02023  81 EDLLLERGE 89
SCAN cd07936
SCAN oligomerization domain; The SCAN domain (named after SRE-ZBP, CTfin51, AW-1 and Number 18 ...
 47-127 1.44e-39

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: 138.93  E-value: 1.44e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568982068  47 PDRSRQRFRAFRYPEAAGPRQALSRLRELCRQWLRPDMHSKEQILELLVLEQFLTILPGELQAWVREQHPDSGEEVVALL 126
Cdd:cd07936    1 PETYRQRFRAFQYQEASGPREALQRLRELCRQWLRPEIHTKEQILELLVLEQFLIILPPEVQAWVRERKPESGEEAATLA 80


                 .
gi 568982068 127 E 127
Cdd:cd07936   81 E 81
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
367-514 2.92e-09

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 59.32  E-value: 2.92e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568982068 367 KPYECEECGKAFSHSSDLIKHQRT--HTGE--KPYECD--DCGKTFTQSCSLLEHHRIHTGEKPYQCNM--CPKAFRRSS 438
Cdd:COG5048  288 LPIKSKQCNISFSRSSPLTRHLRSvnHSGEslKPFSCPysLCGKLFSRNDALKRHILLHTSISPAKEKLlnSSSKFSPLL 367

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568982068 439 HLLRHQRTHTGDKDFFVPEPYWESQSRVESHWENIETPVSYQCNDCER-----------SFSRITSLIEHQKVHTGEKPF 507
Cdd:COG5048  368 NNEPPQSLQQYKDLKNDKKSETLSNSCIRNFKRDSNLSLHIITHLSFRpyncknppcskSFNRHYNLIPHKKIHTNHAPL 447


                 ....*..
gi 568982068 508 ECQTCGK 514
Cdd:COG5048  448 LCSILKS 454
KRAB smart00349
krueppel associated box;
213-267 2.50e-07

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 47.59  E-value: 2.50e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 568982068   213 LKMEDVAPVLSP-RWTEQDSSQMNLYKDGMQEHSGSLVSLDQDMQTK--VRDLPRAEE 267
Cdd:smart00349   1 VTFEDVAVYFTQeEWEQLDPAQKNLYRDVMLENYSNLVSLGFQVPKPdlISQLEQGEE 58
zf-H2C2_2 pfam13465
Zinc-finger double domain;
383-408 4.36e-06

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 43.13  E-value: 4.36e-06
                          10        20
                  ....*....|....*....|....*.
gi 568982068  383 DLIKHQRTHTGEKPYECDDCGKTFTQ 408
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
328-350 2.70e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 41.20  E-value: 2.70e-05
                          10        20
                  ....*....|....*....|...
gi 568982068  328 LSKHKRIHTGLKPYECEECGKAF 350
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSF 24
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
 213-251 5.10e-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: 40.61  E-value: 5.10e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 568982068 213 LKMEDVAPVLSPR-WTEQDSSQMNLYKDGMQEHSGSLVSL 251
Cdd:cd07765    1 VTFEDVAVYFSQEeWELLDPAQRDLYRDVMLENYENLVSL 40
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 507-529 1.93e-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: 38.44  E-value: 1.93e-04
                          10        20
                  ....*....|....*....|...
gi 568982068  507 FECQTCGKGFTRPSYLIQHQRRH 529
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 313-335 9.01e-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: 36.89  E-value: 9.01e-04
                          10        20
                  ....*....|....*....|...
gi 568982068  313 FYCRECGKSFAQSSGLSKHKRIH 335
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
 216-252 9.11e-04

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: 37.07  E-value: 9.11e-04
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 568982068  216 EDVAPVLSPRWTEQ-DSSQMNLYKDGMQEHSGSLVSLD 252
Cdd:pfam01352   5 EDVAVDFTQEEWALlDPAQRNLYRDVMLENYRNLVSLG 42
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 341-363 1.23e-03

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


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 36.51  E-value: 1.23e-03
                          10        20
                  ....*....|....*....|...
gi 568982068  341 YECEECGKAFIGSSALIIHQRVH 363
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
SUF4-like cd20908
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
 481-529 3.03e-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: 36.77  E-value: 3.03e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 568982068 481 CNDCERSFSRITSLIEHQKvhtgEKPFECQTCGKGFTRPSYLIQH-QRRH 529
Cdd:cd20908    4 CYYCDREFDDEKILIQHQK----AKHFKCHICHKKLYTAGGLAVHcLQVH 49
PHA00733 PHA00733
hypothetical protein
 368-415 4.64e-03

hypothetical protein


Pssm-ID: 177301  Cd Length: 128  Bit Score: 37.55  E-value: 4.64e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 568982068 368 PYECEECGKAFSHSSDLIKHQR--THTGEKPYecddCGKTFTQSCSLLEH 415
Cdd:PHA00733  73 PYVCPLCLMPFSSSVSLKQHIRytEHSKVCPV----CGKEFRNTDSTLDH 118
ZnF_C2H2 smart00355
zinc finger;
369-391 4.93e-03

zinc finger;


Pssm-ID: 197676  Cd Length: 23  Bit Score: 34.75  E-value: 4.93e-03
                           10        20
                   ....*....|....*....|...
gi 568982068   369 YECEECGKAFSHSSDLIKHQRTH 391
Cdd:smart00355   1 YRCPECGKVFKSKSALREHMRTH 23
 
Name Accession Description Interval E-value
SCAN smart00431
leucine rich region;
47-159 6.35e-58

leucine rich region;


Pssm-ID: 128708 [Multi-domain]  Cd Length: 113  Bit Score: 188.67  E-value: 6.35e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568982068    47 PDRSRQRFRAFRYPEAAGPRQALSRLRELCRQWLRPDMHSKEQILELLVLEQFLTILPGELQAWVREQHPDSGEEVVALL 126
Cdd:smart00431   1 PEIFRQRFRQFRYQETSGPREALSRLRELCRQWLRPELHTKEQILELLVLEQFLTILPGELQAWVREHHPESGEEAVTLL 80

                           90       100       110
                   ....*....|....*....|....*....|...
gi 568982068   127 EYLDRQLDDTPPQVPDDDDGQELLCSKAVLLTS 159
Cdd:smart00431  81 EDLERELDEPGQQVSAHVHGQEVLLEKMVPLGA 113
SCAN pfam02023
SCAN domain; The SCAN domain (named after SRE-ZBP, CTfin51, AW-1 and Number 18 cDNA) is found ...
 47-135 4.18e-49

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: 164.58  E-value: 4.18e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568982068   47 PDRSRQRFRAFRYPEAAGPRQALSRLRELCRQWLRPDMHSKEQILELLVLEQFLTILPGELQAWVREQHPDSGEEVVALL 126
Cdd:pfam02023   1 PEASRQRFRQFCYQEAEGPREALSQLRELCHQWLRPEKHTKEQILELLVLEQFLTILPEEIQSWVREHHPESGEEAVALA 80


                  ....*....
gi 568982068  127 EYLDRQLDD 135
Cdd:pfam02023  81 EDLLLERGE 89
SCAN cd07936
SCAN oligomerization domain; The SCAN domain (named after SRE-ZBP, CTfin51, AW-1 and Number 18 ...
 47-127 1.44e-39

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: 138.93  E-value: 1.44e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568982068  47 PDRSRQRFRAFRYPEAAGPRQALSRLRELCRQWLRPDMHSKEQILELLVLEQFLTILPGELQAWVREQHPDSGEEVVALL 126
Cdd:cd07936    1 PETYRQRFRAFQYQEASGPREALQRLRELCRQWLRPEIHTKEQILELLVLEQFLIILPPEVQAWVRERKPESGEEAATLA 80


                 .
gi 568982068 127 E 127
Cdd:cd07936   81 E 81
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
367-514 2.92e-09

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 59.32  E-value: 2.92e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568982068 367 KPYECEECGKAFSHSSDLIKHQRT--HTGE--KPYECD--DCGKTFTQSCSLLEHHRIHTGEKPYQCNM--CPKAFRRSS 438
Cdd:COG5048  288 LPIKSKQCNISFSRSSPLTRHLRSvnHSGEslKPFSCPysLCGKLFSRNDALKRHILLHTSISPAKEKLlnSSSKFSPLL 367

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568982068 439 HLLRHQRTHTGDKDFFVPEPYWESQSRVESHWENIETPVSYQCNDCER-----------SFSRITSLIEHQKVHTGEKPF 507
Cdd:COG5048  368 NNEPPQSLQQYKDLKNDKKSETLSNSCIRNFKRDSNLSLHIITHLSFRpyncknppcskSFNRHYNLIPHKKIHTNHAPL 447


                 ....*..
gi 568982068 508 ECQTCGK 514
Cdd:COG5048  448 LCSILKS 454
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
395-530 1.21e-07

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 54.32  E-value: 1.21e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568982068 395 KPYECDDCGKTFTQSCSLLEH--HRIHTGE--KPYQC--NMCPKAFRRSSHLLRHQRTHTGDKDF---FVPEPYWES--- 462
Cdd:COG5048  288 LPIKSKQCNISFSRSSPLTRHlrSVNHSGEslKPFSCpySLCGKLFSRNDALKRHILLHTSISPAkekLLNSSSKFSpll 367

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568982068 463 -----QSRVESHWENIETPVSYQCNDCERSFSRITSLIEHQKVHTGEKP--FECQTCGKGFTRPSYLIQHQRRHT 530
Cdd:COG5048  368 nneppQSLQQYKDLKNDKKSETLSNSCIRNFKRDSNLSLHIITHLSFRPynCKNPPCSKSFNRHYNLIPHKKIHT 442
KRAB smart00349
krueppel associated box;
213-267 2.50e-07

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 47.59  E-value: 2.50e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 568982068   213 LKMEDVAPVLSP-RWTEQDSSQMNLYKDGMQEHSGSLVSLDQDMQTK--VRDLPRAEE 267
Cdd:smart00349   1 VTFEDVAVYFTQeEWEQLDPAQKNLYRDVMLENYSNLVSLGFQVPKPdlISQLEQGEE 58
zf-H2C2_2 pfam13465
Zinc-finger double domain;
383-408 4.36e-06

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 43.13  E-value: 4.36e-06
                          10        20
                  ....*....|....*....|....*.
gi 568982068  383 DLIKHQRTHTGEKPYECDDCGKTFTQ 408
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
324-546 6.15e-06

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 48.92  E-value: 6.15e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568982068 324 QSSGLSKHKRIHTGL----KPYECEECGKAFIGSSALIIHQRVHTGEKPYEC--EECGKAFSHSSDLIKHQRTHTGEKPY 397
Cdd:COG5048   13 NSVLSSTPKSTLKSLsnapRPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCsySGCDKSFSRPLELSRHLRTHHNNPSD 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568982068 398 ECDDCGKTFTQSCSLLEHHRIHT----GEKPYQCNMCPKAFRRSSHLLRH--------------------QRTHTG-DKD 452
Cdd:COG5048   93 LNSKSLPLSNSKASSSSLSSSSSnsndNNLLSSHSLPPSSRDPQLPDLLSisnlrnnplpgnnsssvntpQSNSLHpPLP 172

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568982068 453 FFVPEPYWESQSRVESHWENIETPVSYQCNDCERSFSRITSLIEHQKVHTGEKPFECQTCGKGFTRPSylIQHQRRHTGK 532
Cdd:COG5048  173 ANSLSKDPSSNLSLLISSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSL--LSQSPSSLSS 250

                        250
                 ....*....|....
gi 568982068 533 KTSVTVTPAVHSEV 546
Cdd:COG5048  251 SDSSSSASESPRSS 264
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 425-447 8.09e-06

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: 42.67  E-value: 8.09e-06
                          10        20
                  ....*....|....*....|...
gi 568982068  425 YQCNMCPKAFRRSSHLLRHQRTH 447
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 369-391 8.84e-06

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: 42.29  E-value: 8.84e-06
                          10        20
                  ....*....|....*....|...
gi 568982068  369 YECEECGKAFSHSSDLIKHQRTH 391
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
313-533 2.06e-05

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 47.00  E-value: 2.06e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568982068 313 FYCRECGKSFAQSSGLSKHKRIHTGLKPYEC--EECGKAFIGSSALIIHQRVHTGEKPYECE------------------ 372
Cdd:COG5048   34 DSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCsySGCDKSFSRPLELSRHLRTHHNNPSDLNSkslplsnskasssslsss 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568982068 373 --------------------------------------------------------------ECGKAFSHSSDLIKHQRT 390
Cdd:COG5048  114 ssnsndnnllsshslppssrdpqlpdllsisnlrnnplpgnnsssvntpqsnslhpplpansLSKDPSSNLSLLISSNVS 193

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568982068 391 HTGEKPYECDDCGKTFTQScSLLEHHRIHTGEKPYQCNMCpkAFRRSSHLLRHQRTHTGDKDF------FVPEPYWESQS 464
Cdd:COG5048  194 TSIPSSSENSPLSSSYSIP-SSSSDQNLENSSSSLPLTTN--SQLSPKSLLSQSPSSLSSSDSsssaseSPRSSLPTASS 270

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568982068 465 RVESHWENIETPV-----SYQCNDCERSFSRITSLIEHQ--KVHTGE--KPFEC--QTCGKGFTRPSYLIQHQRRHTGKK 533
Cdd:COG5048  271 QSSSPNESDSSSEkgfslPIKSKQCNISFSRSSPLTRHLrsVNHSGEslKPFSCpySLCGKLFSRNDALKRHILLHTSIS 350
zf-H2C2_2 pfam13465
Zinc-finger double domain;
355-380 2.09e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 41.20  E-value: 2.09e-05
                          10        20
                  ....*....|....*....|....*.
gi 568982068  355 ALIIHQRVHTGEKPYECEECGKAFSH 380
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
328-350 2.70e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 41.20  E-value: 2.70e-05
                          10        20
                  ....*....|....*....|...
gi 568982068  328 LSKHKRIHTGLKPYECEECGKAF 350
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSF 24
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
 213-251 5.10e-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: 40.61  E-value: 5.10e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 568982068 213 LKMEDVAPVLSPR-WTEQDSSQMNLYKDGMQEHSGSLVSL 251
Cdd:cd07765    1 VTFEDVAVYFSQEeWELLDPAQRDLYRDVMLENYENLVSL 40
zf-H2C2_2 pfam13465
Zinc-finger double domain;
411-436 7.93e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 39.66  E-value: 7.93e-05
                          10        20
                  ....*....|....*....|....*.
gi 568982068  411 SLLEHHRIHTGEKPYQCNMCPKAFRR 436
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
493-518 1.26e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 39.28  E-value: 1.26e-04
                          10        20
                  ....*....|....*....|....*.
gi 568982068  493 SLIEHQKVHTGEKPFECQTCGKGFTR 518
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 507-529 1.93e-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: 38.44  E-value: 1.93e-04
                          10        20
                  ....*....|....*....|...
gi 568982068  507 FECQTCGKGFTRPSYLIQHQRRH 529
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 397-419 6.33e-04

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


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 37.28  E-value: 6.33e-04
                          10        20
                  ....*....|....*....|...
gi 568982068  397 YECDDCGKTFTQSCSLLEHHRIH 419
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 313-335 9.01e-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: 36.89  E-value: 9.01e-04
                          10        20
                  ....*....|....*....|...
gi 568982068  313 FYCRECGKSFAQSSGLSKHKRIH 335
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
 216-252 9.11e-04

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: 37.07  E-value: 9.11e-04
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 568982068  216 EDVAPVLSPRWTEQ-DSSQMNLYKDGMQEHSGSLVSLD 252
Cdd:pfam01352   5 EDVAVDFTQEEWALlDPAQRNLYRDVMLENYRNLVSLG 42
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 341-363 1.23e-03

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


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 36.51  E-value: 1.23e-03
                          10        20
                  ....*....|....*....|...
gi 568982068  341 YECEECGKAFIGSSALIIHQRVH 363
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 479-501 2.68e-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: 2.68e-03
                          10        20
                  ....*....|....*....|...
gi 568982068  479 YQCNDCERSFSRITSLIEHQKVH 501
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
SUF4-like cd20908
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
 481-529 3.03e-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: 36.77  E-value: 3.03e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 568982068 481 CNDCERSFSRITSLIEHQKvhtgEKPFECQTCGKGFTRPSYLIQH-QRRH 529
Cdd:cd20908    4 CYYCDREFDDEKILIQHQK----AKHFKCHICHKKLYTAGGLAVHcLQVH 49
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
318-443 3.21e-03

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 40.06  E-value: 3.21e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568982068 318 CGKSFAQSSGLSKHKRIHTGLKPYEC--EECGKAFIGSS-----ALIIHQRVHTGEKPYECE--ECGKAFSHSSDLIKHQ 388
Cdd:COG5048  329 CGKLFSRNDALKRHILLHTSISPAKEklLNSSSKFSPLLnneppQSLQQYKDLKNDKKSETLsnSCIRNFKRDSNLSLHI 408

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 568982068 389 RTHTGEKPYECDD--CGKTFTQSCSLLEHHRIHTGEKPYQCNMCPKaFRRSSHLLRH 443
Cdd:COG5048  409 ITHLSFRPYNCKNppCSKSFNRHYNLIPHKKIHTNHAPLLCSILKS-FRRDLDLSNH 464
PHA00733 PHA00733
hypothetical protein
 368-415 4.64e-03

hypothetical protein


Pssm-ID: 177301  Cd Length: 128  Bit Score: 37.55  E-value: 4.64e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 568982068 368 PYECEECGKAFSHSSDLIKHQR--THTGEKPYecddCGKTFTQSCSLLEH 415
Cdd:PHA00733  73 PYVCPLCLMPFSSSVSLKQHIRytEHSKVCPV----CGKEFRNTDSTLDH 118
ZnF_C2H2 smart00355
zinc finger;
369-391 4.93e-03

zinc finger;


Pssm-ID: 197676  Cd Length: 23  Bit Score: 34.75  E-value: 4.93e-03
                           10        20
                   ....*....|....*....|...
gi 568982068   369 YECEECGKAFSHSSDLIKHQRTH 391
Cdd:smart00355   1 YRCPECGKVFKSKSALREHMRTH 23
ZnF_C2H2 smart00355
zinc finger;
425-447 7.68e-03

zinc finger;


Pssm-ID: 197676  Cd Length: 23  Bit Score: 33.98  E-value: 7.68e-03
                           10        20
                   ....*....|....*....|...
gi 568982068   425 YQCNMCPKAFRRSSHLLRHQRTH 447
Cdd:smart00355   1 YRCPECGKVFKSKSALREHMRTH 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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