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Conserved domains on  [gi|548961129|ref|NP_001271456|]
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zinc finger and SCAN domain-containing protein 32 isoform a [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SCAN super family cl42860
leucine rich region;
33-142 7.23e-47

leucine rich region;


The actual alignment was detected with superfamily member smart00431:

Pssm-ID: 128708 [Multi-domain]  Cd Length: 113  Bit Score: 161.32  E-value: 7.23e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961129    33 SEASRQRFRQFCYQEVTGPHEAFSKLWELCCQWLRPKTHSKEEILELLVLEQFLTILPEEIQTWVREQHPENGEEAVALV 112
Cdd:smart00431   1 PEIFRQRFRQFRYQETSGPREALSRLRELCRQWLRPELHTKEQILELLVLEQFLTILPGELQAWVREHHPESGEEAVTLL 80

                           90       100       110
                   ....*....|....*....|....*....|...
gi 548961129   113 EDVQRA---PGQQVLDSEKDLKVLMKEMAPLGA 142
Cdd:smart00431  81 EDLEREldePGQQVSAHVHGQEVLLEKMVPLGA 113
Myb_DNA-bind_4 pfam13837
Myb/SANT-like DNA-binding domain; This presumed domain appears to be related to other Myb ...
 253-334 2.48e-17

Myb/SANT-like DNA-binding domain; This presumed domain appears to be related to other Myb/SANT-like DNA binding domains. In particular pfam10545 seems most related. This family is greatly expanded in plants and appears in several proteins annotated as transposon proteins.


:

Pssm-ID: 463994  Cd Length: 84  Bit Score: 77.31  E-value: 2.48e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961129  253 GVPWGYEETKTLLAILSSSQfYGKLQT-CQQNSQIYRAMAEGLWEQGFLRTPEQCRTKFKSLQLSYRKVRRGRV--PEPC 329
Cdd:pfam13837   1 RNKWTEEETLALIEIWGERL-ELRFQEsKKRNKKLWEEIAEKMAELGYNRSPEQCKEKWENLKKKYRKEKEGNNgsGSSW 79


                  ....*
gi 548961129  330 IFYEE 334
Cdd:pfam13837  80 PFFEE 84
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
455-668 1.82e-11

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


:

Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 67.03  E-value: 1.82e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961129 455 LESEPTSRRQCRnSPGESEEKTPSQEKMSHQSFCARDKACtHILCGKNCSQSVHSPH--KPALKLEKVSQCPECGKTFSR 532
Cdd:COG5048  224 SSSLPLTTNSQL-SPKSLLSQSPSSLSSSDSSSSASESPR-SSLPTASSQSSSPNESdsSSEKGFSLPIKSKQCNISFSR 301

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961129 533 SSYLVRHQR--IHTGE--KPHKCSE--CGKGFSERSNLTAHLRTHTGERPYQC--GQCGKSFNQSS-----SLIVHQRTH 599
Cdd:COG5048  302 SSPLTRHLRsvNHSGEslKPFSCPYslCGKLFSRNDALKRHILLHTSISPAKEklLNSSSKFSPLLnneppQSLQQYKDL 381

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 548961129 600 TGEKPYQCIV--CGKRFNNSSQFSAHRRIHTGESPY--KCAVCGKIFNNSSHFSAHRKTHTGEKPYRCSHCER 668
Cdd:COG5048  382 KNDKKSETLSnsCIRNFKRDSNLSLHIITHLSFRPYncKNPPCSKSFNRHYNLIPHKKIHTNHAPLLCSILKS 454
KRAB super family cl42959
krueppel associated box;
218-255 4.45e-04

krueppel associated box;


The actual alignment was detected with superfamily member smart00349:

Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 38.73  E-value: 4.45e-04
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 548961129   218 AVSLCQQEWMCPGPAQRALYRGATQRKDSH-VSLATGVP 255
Cdd:smart00349   7 AVYFTQEEWEQLDPAQKNLYRDVMLENYSNlVSLGFQVP 45
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 661-683 3.23e-03

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


:

Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 35.35  E-value: 3.23e-03
                          10        20
                  ....*....|....*....|...
gi 548961129  661 YRCSHCERGFTKNSALTRHQTVH 683
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
 
Name Accession Description Interval E-value
SCAN smart00431
leucine rich region;
33-142 7.23e-47

leucine rich region;


Pssm-ID: 128708 [Multi-domain]  Cd Length: 113  Bit Score: 161.32  E-value: 7.23e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961129    33 SEASRQRFRQFCYQEVTGPHEAFSKLWELCCQWLRPKTHSKEEILELLVLEQFLTILPEEIQTWVREQHPENGEEAVALV 112
Cdd:smart00431   1 PEIFRQRFRQFRYQETSGPREALSRLRELCRQWLRPELHTKEQILELLVLEQFLTILPGELQAWVREHHPESGEEAVTLL 80

                           90       100       110
                   ....*....|....*....|....*....|...
gi 548961129   113 EDVQRA---PGQQVLDSEKDLKVLMKEMAPLGA 142
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 ...
 33-121 5.05e-42

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: 147.25  E-value: 5.05e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961129   33 SEASRQRFRQFCYQEVTGPHEAFSKLWELCCQWLRPKTHSKEEILELLVLEQFLTILPEEIQTWVREQHPENGEEAVALV 112
Cdd:pfam02023   1 PEASRQRFRQFCYQEAEGPREALSQLRELCHQWLRPEKHTKEQILELLVLEQFLTILPEEIQSWVREHHPESGEEAVALA 80


                  ....*....
gi 548961129  113 EDVQRAPGQ 121
Cdd:pfam02023  81 EDLLLERGE 89
SCAN cd07936
SCAN oligomerization domain; The SCAN domain (named after SRE-ZBP, CTfin51, AW-1 and Number 18 ...
 33-117 7.90e-31

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: 115.44  E-value: 7.90e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961129  33 SEASRQRFRQFCYQEVTGPHEAFSKLWELCCQWLRPKTHSKEEILELLVLEQFLTILPEEIQTWVREQHPENGEEAVALV 112
Cdd:cd07936    1 PETYRQRFRAFQYQEASGPREALQRLRELCRQWLRPEIHTKEQILELLVLEQFLIILPPEVQAWVRERKPESGEEAATLA 80


                 ....*
gi 548961129 113 EDVQR 117
Cdd:cd07936   81 EDLLA 85
Myb_DNA-bind_4 pfam13837
Myb/SANT-like DNA-binding domain; This presumed domain appears to be related to other Myb ...
 253-334 2.48e-17

Myb/SANT-like DNA-binding domain; This presumed domain appears to be related to other Myb/SANT-like DNA binding domains. In particular pfam10545 seems most related. This family is greatly expanded in plants and appears in several proteins annotated as transposon proteins.


Pssm-ID: 463994  Cd Length: 84  Bit Score: 77.31  E-value: 2.48e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961129  253 GVPWGYEETKTLLAILSSSQfYGKLQT-CQQNSQIYRAMAEGLWEQGFLRTPEQCRTKFKSLQLSYRKVRRGRV--PEPC 329
Cdd:pfam13837   1 RNKWTEEETLALIEIWGERL-ELRFQEsKKRNKKLWEEIAEKMAELGYNRSPEQCKEKWENLKKKYRKEKEGNNgsGSSW 79


                  ....*
gi 548961129  330 IFYEE 334
Cdd:pfam13837  80 PFFEE 84
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
455-668 1.82e-11

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 67.03  E-value: 1.82e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961129 455 LESEPTSRRQCRnSPGESEEKTPSQEKMSHQSFCARDKACtHILCGKNCSQSVHSPH--KPALKLEKVSQCPECGKTFSR 532
Cdd:COG5048  224 SSSLPLTTNSQL-SPKSLLSQSPSSLSSSDSSSSASESPR-SSLPTASSQSSSPNESdsSSEKGFSLPIKSKQCNISFSR 301

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961129 533 SSYLVRHQR--IHTGE--KPHKCSE--CGKGFSERSNLTAHLRTHTGERPYQC--GQCGKSFNQSS-----SLIVHQRTH 599
Cdd:COG5048  302 SSPLTRHLRsvNHSGEslKPFSCPYslCGKLFSRNDALKRHILLHTSISPAKEklLNSSSKFSPLLnneppQSLQQYKDL 381

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 548961129 600 TGEKPYQCIV--CGKRFNNSSQFSAHRRIHTGESPY--KCAVCGKIFNNSSHFSAHRKTHTGEKPYRCSHCER 668
Cdd:COG5048  382 KNDKKSETLSnsCIRNFKRDSNLSLHIITHLSFRPYncKNPPCSKSFNRHYNLIPHKKIHTNHAPLLCSILKS 454
zf-H2C2_2 pfam13465
Zinc-finger double domain;
535-559 4.86e-06

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 43.51  E-value: 4.86e-06
                          10        20
                  ....*....|....*....|....*
gi 548961129  535 YLVRHQRIHTGEKPHKCSECGKGFS 559
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFK 25
GT1 cd12203
GT1, myb-like, SANT family; GT-1, a myb-like protein, is one of the GT trihelix transcription ...
 256-321 7.83e-06

GT1, myb-like, SANT family; GT-1, a myb-like protein, is one of the GT trihelix transcription factors. GT-1 binds the GT cis-element of rbcS-3A, a light-induced gene, as a dimer. Arabidopsis GT-1 is a trans-activator and acts in the stabilization of components of the transcription pre-initiation complex comprised of TFIIA-TBP-TATA. The isolated GT-1 DNA-binding domain is sufficient to bind DNA. This region closely resembles the myb domain, but with longer helices. It has been proposed that GT-1 may respond to light signals via calcium-dependent phosphorylation to create a light-modulated molecular switch. These proteins are members of the SANT/myb group. SANT is named after 'SWI3, ADA2, N-CoR and TFIIIB', several factors that share this domain. The SANT domain resembles the 3 alpha-helix bundle of the DNA-binding Myb domains and is found in a diverse set of proteins.


Pssm-ID: 213402  Cd Length: 66  Bit Score: 43.81  E-value: 7.83e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 548961129 256 WGYEETKTLLAIlsSSQFYGKLQTCQQNSQIYRAMAEGLWEQGFLRTPEQCRTKFKSLQLSYRKVR 321
Cdd:cd12203    3 WPREETLSLIRL--RREMESRFQETKSKKALWEEIAAKMRELGYNRSAKQCKEKWENLNKYYKKVK 66
KRAB smart00349
krueppel associated box;
218-255 4.45e-04

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 38.73  E-value: 4.45e-04
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 548961129   218 AVSLCQQEWMCPGPAQRALYRGATQRKDSH-VSLATGVP 255
Cdd:smart00349   7 AVYFTQEEWEQLDPAQKNLYRDVMLENYSNlVSLGFQVP 45
SUF4-like cd20908
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
 575-623 9.90e-04

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: 38.31  E-value: 9.90e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 548961129 575 RPYqCGQCGKSFNQSSSLIVHQRTHTgekpYQCIVCGKRFNNSSQFSAH 623
Cdd:cd20908    1 KPW-CYYCDREFDDEKILIQHQKAKH----FKCHICHKKLYTAGGLAVH 44
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
 218-250 9.99e-04

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: 37.14  E-value: 9.99e-04
                         10        20        30
                 ....*....|....*....|....*....|....
gi 548961129 218 AVSLCQQEWMCPGPAQRALYRGATQRKDSH-VSL 250
Cdd:cd07765    7 AVYFSQEEWELLDPAQRDLYRDVMLENYENlVSL 40
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 661-683 3.23e-03

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


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 35.35  E-value: 3.23e-03
                          10        20
                  ....*....|....*....|...
gi 548961129  661 YRCSHCERGFTKNSALTRHQTVH 683
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
 
Name Accession Description Interval E-value
SCAN smart00431
leucine rich region;
33-142 7.23e-47

leucine rich region;


Pssm-ID: 128708 [Multi-domain]  Cd Length: 113  Bit Score: 161.32  E-value: 7.23e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961129    33 SEASRQRFRQFCYQEVTGPHEAFSKLWELCCQWLRPKTHSKEEILELLVLEQFLTILPEEIQTWVREQHPENGEEAVALV 112
Cdd:smart00431   1 PEIFRQRFRQFRYQETSGPREALSRLRELCRQWLRPELHTKEQILELLVLEQFLTILPGELQAWVREHHPESGEEAVTLL 80

                           90       100       110
                   ....*....|....*....|....*....|...
gi 548961129   113 EDVQRA---PGQQVLDSEKDLKVLMKEMAPLGA 142
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 ...
 33-121 5.05e-42

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: 147.25  E-value: 5.05e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961129   33 SEASRQRFRQFCYQEVTGPHEAFSKLWELCCQWLRPKTHSKEEILELLVLEQFLTILPEEIQTWVREQHPENGEEAVALV 112
Cdd:pfam02023   1 PEASRQRFRQFCYQEAEGPREALSQLRELCHQWLRPEKHTKEQILELLVLEQFLTILPEEIQSWVREHHPESGEEAVALA 80


                  ....*....
gi 548961129  113 EDVQRAPGQ 121
Cdd:pfam02023  81 EDLLLERGE 89
SCAN cd07936
SCAN oligomerization domain; The SCAN domain (named after SRE-ZBP, CTfin51, AW-1 and Number 18 ...
 33-117 7.90e-31

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: 115.44  E-value: 7.90e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961129  33 SEASRQRFRQFCYQEVTGPHEAFSKLWELCCQWLRPKTHSKEEILELLVLEQFLTILPEEIQTWVREQHPENGEEAVALV 112
Cdd:cd07936    1 PETYRQRFRAFQYQEASGPREALQRLRELCRQWLRPEIHTKEQILELLVLEQFLIILPPEVQAWVRERKPESGEEAATLA 80


                 ....*
gi 548961129 113 EDVQR 117
Cdd:cd07936   81 EDLLA 85
Myb_DNA-bind_4 pfam13837
Myb/SANT-like DNA-binding domain; This presumed domain appears to be related to other Myb ...
 253-334 2.48e-17

Myb/SANT-like DNA-binding domain; This presumed domain appears to be related to other Myb/SANT-like DNA binding domains. In particular pfam10545 seems most related. This family is greatly expanded in plants and appears in several proteins annotated as transposon proteins.


Pssm-ID: 463994  Cd Length: 84  Bit Score: 77.31  E-value: 2.48e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961129  253 GVPWGYEETKTLLAILSSSQfYGKLQT-CQQNSQIYRAMAEGLWEQGFLRTPEQCRTKFKSLQLSYRKVRRGRV--PEPC 329
Cdd:pfam13837   1 RNKWTEEETLALIEIWGERL-ELRFQEsKKRNKKLWEEIAEKMAELGYNRSPEQCKEKWENLKKKYRKEKEGNNgsGSSW 79


                  ....*
gi 548961129  330 IFYEE 334
Cdd:pfam13837  80 PFFEE 84
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
455-668 1.82e-11

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 67.03  E-value: 1.82e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961129 455 LESEPTSRRQCRnSPGESEEKTPSQEKMSHQSFCARDKACtHILCGKNCSQSVHSPH--KPALKLEKVSQCPECGKTFSR 532
Cdd:COG5048  224 SSSLPLTTNSQL-SPKSLLSQSPSSLSSSDSSSSASESPR-SSLPTASSQSSSPNESdsSSEKGFSLPIKSKQCNISFSR 301

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961129 533 SSYLVRHQR--IHTGE--KPHKCSE--CGKGFSERSNLTAHLRTHTGERPYQC--GQCGKSFNQSS-----SLIVHQRTH 599
Cdd:COG5048  302 SSPLTRHLRsvNHSGEslKPFSCPYslCGKLFSRNDALKRHILLHTSISPAKEklLNSSSKFSPLLnneppQSLQQYKDL 381

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 548961129 600 TGEKPYQCIV--CGKRFNNSSQFSAHRRIHTGESPY--KCAVCGKIFNNSSHFSAHRKTHTGEKPYRCSHCER 668
Cdd:COG5048  382 KNDKKSETLSnsCIRNFKRDSNLSLHIITHLSFRPYncKNPPCSKSFNRHYNLIPHKKIHTNHAPLLCSILKS 454
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
509-591 2.92e-08

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 56.63  E-value: 2.92e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961129 509 SPHKPALKLEKVSQCPECGKTFSRSSYLVRHQRIHTGEKPHKCS--ECGKGFSERSNLTAHLRTHTGERPYQCGQCGKSF 586
Cdd:COG5048   22 STLKSLSNAPRPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSysGCDKSFSRPLELSRHLRTHHNNPSDLNSKSLPLS 101


                 ....*
gi 548961129 587 NQSSS 591
Cdd:COG5048  102 NSKAS 106
zf-H2C2_2 pfam13465
Zinc-finger double domain;
535-559 4.86e-06

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 43.51  E-value: 4.86e-06
                          10        20
                  ....*....|....*....|....*
gi 548961129  535 YLVRHQRIHTGEKPHKCSECGKGFS 559
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFK 25
GT1 cd12203
GT1, myb-like, SANT family; GT-1, a myb-like protein, is one of the GT trihelix transcription ...
 256-321 7.83e-06

GT1, myb-like, SANT family; GT-1, a myb-like protein, is one of the GT trihelix transcription factors. GT-1 binds the GT cis-element of rbcS-3A, a light-induced gene, as a dimer. Arabidopsis GT-1 is a trans-activator and acts in the stabilization of components of the transcription pre-initiation complex comprised of TFIIA-TBP-TATA. The isolated GT-1 DNA-binding domain is sufficient to bind DNA. This region closely resembles the myb domain, but with longer helices. It has been proposed that GT-1 may respond to light signals via calcium-dependent phosphorylation to create a light-modulated molecular switch. These proteins are members of the SANT/myb group. SANT is named after 'SWI3, ADA2, N-CoR and TFIIIB', several factors that share this domain. The SANT domain resembles the 3 alpha-helix bundle of the DNA-binding Myb domains and is found in a diverse set of proteins.


Pssm-ID: 213402  Cd Length: 66  Bit Score: 43.81  E-value: 7.83e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 548961129 256 WGYEETKTLLAIlsSSQFYGKLQTCQQNSQIYRAMAEGLWEQGFLRTPEQCRTKFKSLQLSYRKVR 321
Cdd:cd12203    3 WPREETLSLIRL--RREMESRFQETKSKKALWEEIAAKMRELGYNRSAKQCKEKWENLNKYYKKVK 66
zf-H2C2_2 pfam13465
Zinc-finger double domain;
591-616 1.01e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 42.36  E-value: 1.01e-05
                          10        20
                  ....*....|....*....|....*.
gi 548961129  591 SLIVHQRTHTGEKPYQCIVCGKRFNN 616
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
448-651 1.02e-05

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 48.54  E-value: 1.02e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961129 448 HSELQKGLESEPTSRRQCRNSPGESEEKTPSQEKMSHQSFCARD-KACTHILCGKNCS-----QSVHSPHKPALKLE--- 518
Cdd:COG5048  239 SLLSQSPSSLSSSDSSSSASESPRSSLPTASSQSSSPNESDSSSeKGFSLPIKSKQCNisfsrSSPLTRHLRSVNHSges 318

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961129 519 -KVSQCPE--CGKTFSRSSYLVRHQRIHTGEKPHKCSECGKGFSERSNLTA-----------HLRTHTGERPYQCgqCGK 584
Cdd:COG5048  319 lKPFSCPYslCGKLFSRNDALKRHILLHTSISPAKEKLLNSSSKFSPLLNNeppqslqqykdLKNDKKSETLSNS--CIR 396

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 548961129 585 SFNQSSSLIVHQRTHTGEKPYQC--IVCGKRFNNSSQFSAHRRIHTGESPYKCAVCGKiFNNSSHFSAH 651
Cdd:COG5048  397 NFKRDSNLSLHIITHLSFRPYNCknPPCSKSFNRHYNLIPHKKIHTNHAPLLCSILKS-FRRDLDLSNH 464
zf-H2C2_2 pfam13465
Zinc-finger double domain;
563-588 1.61e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 41.97  E-value: 1.61e-05
                          10        20
                  ....*....|....*....|....*.
gi 548961129  563 NLTAHLRTHTGERPYQCGQCGKSFNQ 588
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 522-543 4.19e-05

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: 40.75  E-value: 4.19e-05
                          10        20
                  ....*....|....*....|..
gi 548961129  522 QCPECGKTFSRSSYLVRHQRIH 543
Cdd:pfam00096   2 KCPDCGKSFSRKSNLKRHLRTH 23
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
575-656 7.66e-05

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 45.84  E-value: 7.66e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961129 575 RPYQCGQCGKSFNQSSSLIVHQRTHTGEKPYQCIV--CGKRFNNSSQFSAHRRIHTGESPYKCAVCGKIFNNS-SHFSAH 651
Cdd:COG5048   32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYsgCDKSFSRPLELSRHLRTHHNNPSDLNSKSLPLSNSKaSSSSLS 111


                 ....*
gi 548961129 652 RKTHT 656
Cdd:COG5048  112 SSSSN 116
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 577-599 7.70e-05

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: 39.98  E-value: 7.70e-05
                          10        20
                  ....*....|....*....|...
gi 548961129  577 YQCGQCGKSFNQSSSLIVHQRTH 599
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 549-571 1.21e-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: 39.59  E-value: 1.21e-04
                          10        20
                  ....*....|....*....|...
gi 548961129  549 HKCSECGKGFSERSNLTAHLRTH 571
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
547-684 1.25e-04

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 45.07  E-value: 1.25e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961129 547 KPHKCSECGKGFSERSNLTAHLRTHTGERPYQCGQ--CGKSFNQSSSLIVHQRTHTGEKPYQCIVCGKRFNNSSQFSAHR 624
Cdd:COG5048   32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYsgCDKSFSRPLELSRHLRTHHNNPSDLNSKSLPLSNSKASSSSLS 111

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 548961129 625 RIHTgESPYKCAVCGKIFNNSSHFSAHR----KTHTGEKPYRCSHCERGFTKNSALTRHQTVHM 684
Cdd:COG5048  112 SSSS-NSNDNNLLSSHSLPPSSRDPQLPdllsISNLRNNPLPGNNSSSVNTPQSNSLHPPLPAN 174
SFP1 COG5189
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ...
 545-624 1.48e-04

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


Pssm-ID: 227516 [Multi-domain]  Cd Length: 423  Bit Score: 44.71  E-value: 1.48e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961129 545 GEKPHKCS--ECGKGFSERSNLTAHlRTHtgerpyqcGQCGKSFNQSSSLIVHQRTHTGEKPYQCIVCGKRFNNSSQFSA 622
Cdd:COG5189  346 DGKPYKCPveGCNKKYKNQNGLKYH-MLH--------GHQNQKLHENPSPEKMNIFSAKDKPYRCEVCDKRYKNLNGLKY 416


                 ..
gi 548961129 623 HR 624
Cdd:COG5189  417 HR 418
KRAB smart00349
krueppel associated box;
218-255 4.45e-04

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 38.73  E-value: 4.45e-04
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 548961129   218 AVSLCQQEWMCPGPAQRALYRGATQRKDSH-VSLATGVP 255
Cdd:smart00349   7 AVYFTQEEWEQLDPAQKNLYRDVMLENYSNlVSLGFQVP 45
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 633-655 8.26e-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: 8.26e-04
                          10        20
                  ....*....|....*....|...
gi 548961129  633 YKCAVCGKIFNNSSHFSAHRKTH 655
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
623-644 9.79e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.97  E-value: 9.79e-04
                          10        20
                  ....*....|....*....|..
gi 548961129  623 HRRIHTGESPYKCAVCGKIFNN 644
Cdd:pfam13465   5 HMRTHTGEKPYKCPECGKSFKS 26
SUF4-like cd20908
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
 575-623 9.90e-04

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: 38.31  E-value: 9.90e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 548961129 575 RPYqCGQCGKSFNQSSSLIVHQRTHTgekpYQCIVCGKRFNNSSQFSAH 623
Cdd:cd20908    1 KPW-CYYCDREFDDEKILIQHQKAKH----FKCHICHKKLYTAGGLAVH 44
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
 218-250 9.99e-04

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: 37.14  E-value: 9.99e-04
                         10        20        30
                 ....*....|....*....|....*....|....
gi 548961129 218 AVSLCQQEWMCPGPAQRALYRGATQRKDSH-VSL 250
Cdd:cd07765    7 AVYFSQEEWELLDPAQRDLYRDVMLENYENlVSL 40
zf-H2C2_2 pfam13465
Zinc-finger double domain;
651-672 2.51e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.81  E-value: 2.51e-03
                          10        20
                  ....*....|....*....|..
gi 548961129  651 HRKTHTGEKPYRCSHCERGFTK 672
Cdd:pfam13465   5 HMRTHTGEKPYKCPECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 661-683 3.23e-03

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


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 35.35  E-value: 3.23e-03
                          10        20
                  ....*....|....*....|...
gi 548961129  661 YRCSHCERGFTKNSALTRHQTVH 683
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
603-685 4.67e-03

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 40.06  E-value: 4.67e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961129 603 KPYQCIVCGKRFNNSSQFSAHRR--IHTGES--PYKC--AVCGKIFNNSSHFSAHRKTHTGEKPYRCSHCERGFTKNSAL 676
Cdd:COG5048  288 LPIKSKQCNISFSRSSPLTRHLRsvNHSGESlkPFSCpySLCGKLFSRNDALKRHILLHTSISPAKEKLLNSSSKFSPLL 367

                         90
                 ....*....|.
gi 548961129 677 T--RHQTVHMK 685
Cdd:COG5048  368 NnePPQSLQQY 378
 
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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