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Conserved domains on  [gi|1884012931|gb|KAF6087206|]
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zinc finger protein 777 [Phyllostomus discolor]

Protein Classification

KRAB domain-containing zinc finger protein( domain architecture ID 12204699)

KRAB (Kruppel-associated box) domain-containing zinc finger protein (KRAB-ZFP) plays important roles in cell differentiation and organ development and in regulating viral replication and transcription; similar to Homo sapiens zinc finger protein 2 that may be involved in transcriptional regulation

Gene Ontology:  GO:0003677|GO:0008270|GO:0003700
PubMed:  8183940|14519192|22803940

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
KRAB smart00349
krueppel associated box;
364-422 1.55e-24

krueppel associated box;


:

Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 97.28  E-value: 1.55e-24
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1884012931  364 VTFDDVAVHFSEQEWGNLSEWQKELYKNVMRGNYESLVSMDYAISKPDLMSQMERGERP 422
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQVPKPDLISQLEQGEEP 59
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
718-904 6.82e-11

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


:

Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 65.49  E-value: 6.82e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1884012931 718 ECDSSFSHKSSLTKHQITHtgerPYTCPECKKSFRLHISLVIHQR--VHAGKHEVSFIC--SLCGKSFSRPSHLLRHQRT 793
Cdd:COG5048   270 SQSSSPNESDSSSEKGFSL----PIKSKQCNISFSRSSPLTRHLRsvNHSGESLKPFSCpySLCGKLFSRNDALKRHILL 345

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1884012931 794 HTGERPFKCPECEKSFSEKSKLTNHCRVHSRERPHACP---------ECGKSFIRKHHLLEHRRIHTGERPYHC--AECG 862
Cdd:COG5048   346 HTSISPAKEKLLNSSSKFSPLLNNEPPQSLQQYKDLKNdkksetlsnSCIRNFKRDSNLSLHIITHLSFRPYNCknPPCS 425

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1884012931 863 KRFTQKHHLLEHQRAHTgERPYPCTHCAKCFRYKQSLKYHLR 904
Cdd:COG5048   426 KSFNRHYNLIPHKKIHT-NHAPLLCSILKSFRRDLDLSNHGK 466
PHA03247 super family cl33720
large tegument protein UL36; Provisional
 49-275 2.55e-07

large tegument protein UL36; Provisional


The actual alignment was detected with superfamily member PHA03247:

Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 54.94  E-value: 2.55e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1884012931   49 RRPGcallfllcAPASRSRPRVPGR-RGPQVQQLdmeaqRSSPLPfPSILPEESPQQAPAGPPREALF-QSRVLPPKEIP 126
Cdd:PHA03247  2587 RRPD--------APPQSARPRAPVDdRGDPRGPA-----PPSPLP-PDTHAPDPPPPSPSPAANEPDPhPPPTVPPPERP 2652

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1884012931  127 SLSPSVPR--------QGSRPLTPKQETSGRMPPALQKGPSLLYSAASEPemplqgpltSQEETPYPAPAAAERDMPLLS 198
Cdd:PHA03247  2653 RDDPAPGRvsrprrarRLGRAAQASSPPQRPRRRAARPTVGSLTSLADPP---------PPPPTPEPAPHALVSATPLPP 2723

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1884012931  199 HSARHQEAPLHSPEVPEKDPLTLSPTVPEADMDPllQSPVSQKETPFHVSSAAQKDTPLPTAeiTRLAVWAAVQAVE 275
Cdd:PHA03247  2724 GPAAARQASPALPAAPAPPAVPAGPATPGGPARP--ARPPTTAGPPAPAPPAAPAAGPPRRL--TRPAVASLSESRE 2796
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 625-647 3.95e-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: 3.95e-03
                          10        20
                  ....*....|....*....|...
gi 1884012931 625 FTCMECGKSFRLKINLIIHQRNH 647
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 653-675 6.58e-03

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


:

Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 34.97  E-value: 6.58e-03
                          10        20
                  ....*....|....*....|...
gi 1884012931 653 YECAECEISFRHKQQLTLHQRIH 675
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
 
Name Accession Description Interval E-value
KRAB smart00349
krueppel associated box;
364-422 1.55e-24

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 97.28  E-value: 1.55e-24
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1884012931  364 VTFDDVAVHFSEQEWGNLSEWQKELYKNVMRGNYESLVSMDYAISKPDLMSQMERGERP 422
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQVPKPDLISQLEQGEEP 59
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
 363-404 9.23e-19

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: 80.21  E-value: 9.23e-19
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1884012931 363 PVTFDDVAVHFSEQEWGNLSEWQKELYKNVMRGNYESLVSMD 404
Cdd:pfam01352   1 SVTFEDVAVDFTQEEWALLDPAQRNLYRDVMLENYRNLVSLG 42
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
 364-403 1.76e-18

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: 79.52  E-value: 1.76e-18
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1884012931 364 VTFDDVAVHFSEQEWGNLSEWQKELYKNVMRGNYESLVSM 403
Cdd:cd07765     1 VTFEDVAVYFSQEEWELLDPAQRDLYRDVMLENYENLVSL 40
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
718-904 6.82e-11

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 65.49  E-value: 6.82e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1884012931 718 ECDSSFSHKSSLTKHQITHtgerPYTCPECKKSFRLHISLVIHQR--VHAGKHEVSFIC--SLCGKSFSRPSHLLRHQRT 793
Cdd:COG5048   270 SQSSSPNESDSSSEKGFSL----PIKSKQCNISFSRSSPLTRHLRsvNHSGESLKPFSCpySLCGKLFSRNDALKRHILL 345

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1884012931 794 HTGERPFKCPECEKSFSEKSKLTNHCRVHSRERPHACP---------ECGKSFIRKHHLLEHRRIHTGERPYHC--AECG 862
Cdd:COG5048   346 HTSISPAKEKLLNSSSKFSPLLNNEPPQSLQQYKDLKNdkksetlsnSCIRNFKRDSNLSLHIITHLSFRPYNCknPPCS 425

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1884012931 863 KRFTQKHHLLEHQRAHTgERPYPCTHCAKCFRYKQSLKYHLR 904
Cdd:COG5048   426 KSFNRHYNLIPHKKIHT-NHAPLLCSILKSFRRDLDLSNHGK 466
PHA03247 PHA03247
large tegument protein UL36; Provisional
 49-275 2.55e-07

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 54.94  E-value: 2.55e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1884012931   49 RRPGcallfllcAPASRSRPRVPGR-RGPQVQQLdmeaqRSSPLPfPSILPEESPQQAPAGPPREALF-QSRVLPPKEIP 126
Cdd:PHA03247  2587 RRPD--------APPQSARPRAPVDdRGDPRGPA-----PPSPLP-PDTHAPDPPPPSPSPAANEPDPhPPPTVPPPERP 2652

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1884012931  127 SLSPSVPR--------QGSRPLTPKQETSGRMPPALQKGPSLLYSAASEPemplqgpltSQEETPYPAPAAAERDMPLLS 198
Cdd:PHA03247  2653 RDDPAPGRvsrprrarRLGRAAQASSPPQRPRRRAARPTVGSLTSLADPP---------PPPPTPEPAPHALVSATPLPP 2723

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1884012931  199 HSARHQEAPLHSPEVPEKDPLTLSPTVPEADMDPllQSPVSQKETPFHVSSAAQKDTPLPTAeiTRLAVWAAVQAVE 275
Cdd:PHA03247  2724 GPAAARQASPALPAAPAPPAVPAGPATPGGPARP--ARPPTTAGPPAPAPPAAPAAGPPRRL--TRPAVASLSESRE 2796
zf-H2C2_2 pfam13465
Zinc-finger double domain;
786-810 8.15e-07

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 45.83  E-value: 8.15e-07
                          10        20
                  ....*....|....*....|....*
gi 1884012931 786 HLLRHQRTHTGERPFKCPECEKSFS 810
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFK 25
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 66-261 1.06e-05

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 49.38  E-value: 1.06e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1884012931  66 SRPRVPGRRGPQVQQlDMEAQRSSPLPFPSILPEESPQQAPAGPPREALFQSRVLPPkeiPSLSPSVPRQGSRPLT-PKQ 144
Cdd:pfam03154 144 TSPSIPSPQDNESDS-DSSAQQQILQTQPPVLQAQSGAASPPSPPPPGTTQAATAGP---TPSAPSVPPQGSPATSqPPN 219

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1884012931 145 ETSGRMPP--ALQKGPSLLYSAASEPEMPLQG---PLTSQEETPYPAPAAA-ERDMPLLSHSARHQEAPLHSPEVPEKDP 218
Cdd:pfam03154 220 QTQSTAAPhtLIQQTPTLHPQRLPSPHPPLQPmtqPPPPSQVSPQPLPQPSlHGQMPPMPHSLQTGPSHMQHPVPPQPFP 299

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1884012931 219 LTLSPTVPEADMDPLLQSPVSQKETPFHVSSAAQKDTPLPTAE 261
Cdd:pfam03154 300 LTPQSSQSQVPPGPSPAAPGQSQQRIHTPPSQSQLQSQQPPRE 342
SUF4-like cd20908
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
 774-831 5.46e-05

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: 42.54  E-value: 5.46e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1884012931 774 CSLCGKSFSRPSHLLRHQRTHTgerpFKCPECEKSFSEKSKLTNHC-RVHSRER---PHACP 831
Cdd:cd20908     4 CYYCDREFDDEKILIQHQKAKH----FKCHICHKKLYTAGGLAVHClQVHKETLtkvPNALP 61
transpos_ISL3 NF033550
ISL3 family transposase;
820-868 1.02e-03

ISL3 family transposase;


Pssm-ID: 468079 [Multi-domain]  Cd Length: 369  Bit Score: 42.57  E-value: 1.02e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1884012931 820 RVHSRERPHACPECGKS--FIRKHHlleHRRIH---TGERP---------YHCAECGKRFTQK 868
Cdd:NF033550    3 EAELTRGDATCPECGKPsrRVHDTG---KRRIRhlpIFGRPvylelrvrrFKCPECGKTFTEE 62
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 625-647 3.95e-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: 3.95e-03
                          10        20
                  ....*....|....*....|...
gi 1884012931 625 FTCMECGKSFRLKINLIIHQRNH 647
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
ZnF_C2H2 smart00355
zinc finger;
772-794 6.22e-03

zinc finger;


Pssm-ID: 197676  Cd Length: 23  Bit Score: 35.13  E-value: 6.22e-03
                           10        20
                   ....*....|....*....|...
gi 1884012931  772 FICSLCGKSFSRPSHLLRHQRTH 794
Cdd:smart00355   1 YRCPECGKVFKSKSALREHMRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 653-675 6.58e-03

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


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 34.97  E-value: 6.58e-03
                          10        20
                  ....*....|....*....|...
gi 1884012931 653 YECAECEISFRHKQQLTLHQRIH 675
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
 
Name Accession Description Interval E-value
KRAB smart00349
krueppel associated box;
364-422 1.55e-24

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 97.28  E-value: 1.55e-24
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1884012931  364 VTFDDVAVHFSEQEWGNLSEWQKELYKNVMRGNYESLVSMDYAISKPDLMSQMERGERP 422
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQVPKPDLISQLEQGEEP 59
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
 363-404 9.23e-19

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: 80.21  E-value: 9.23e-19
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1884012931 363 PVTFDDVAVHFSEQEWGNLSEWQKELYKNVMRGNYESLVSMD 404
Cdd:pfam01352   1 SVTFEDVAVDFTQEEWALLDPAQRNLYRDVMLENYRNLVSLG 42
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
 364-403 1.76e-18

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: 79.52  E-value: 1.76e-18
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1884012931 364 VTFDDVAVHFSEQEWGNLSEWQKELYKNVMRGNYESLVSM 403
Cdd:cd07765     1 VTFEDVAVYFSQEEWELLDPAQRDLYRDVMLENYENLVSL 40
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
718-904 6.82e-11

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 65.49  E-value: 6.82e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1884012931 718 ECDSSFSHKSSLTKHQITHtgerPYTCPECKKSFRLHISLVIHQR--VHAGKHEVSFIC--SLCGKSFSRPSHLLRHQRT 793
Cdd:COG5048   270 SQSSSPNESDSSSEKGFSL----PIKSKQCNISFSRSSPLTRHLRsvNHSGESLKPFSCpySLCGKLFSRNDALKRHILL 345

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1884012931 794 HTGERPFKCPECEKSFSEKSKLTNHCRVHSRERPHACP---------ECGKSFIRKHHLLEHRRIHTGERPYHC--AECG 862
Cdd:COG5048   346 HTSISPAKEKLLNSSSKFSPLLNNEPPQSLQQYKDLKNdkksetlsnSCIRNFKRDSNLSLHIITHLSFRPYNCknPPCS 425

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1884012931 863 KRFTQKHHLLEHQRAHTgERPYPCTHCAKCFRYKQSLKYHLR 904
Cdd:COG5048   426 KSFNRHYNLIPHKKIHT-NHAPLLCSILKSFRRDLDLSNHGK 466
PHA03247 PHA03247
large tegument protein UL36; Provisional
 49-275 2.55e-07

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 54.94  E-value: 2.55e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1884012931   49 RRPGcallfllcAPASRSRPRVPGR-RGPQVQQLdmeaqRSSPLPfPSILPEESPQQAPAGPPREALF-QSRVLPPKEIP 126
Cdd:PHA03247  2587 RRPD--------APPQSARPRAPVDdRGDPRGPA-----PPSPLP-PDTHAPDPPPPSPSPAANEPDPhPPPTVPPPERP 2652

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1884012931  127 SLSPSVPR--------QGSRPLTPKQETSGRMPPALQKGPSLLYSAASEPemplqgpltSQEETPYPAPAAAERDMPLLS 198
Cdd:PHA03247  2653 RDDPAPGRvsrprrarRLGRAAQASSPPQRPRRRAARPTVGSLTSLADPP---------PPPPTPEPAPHALVSATPLPP 2723

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1884012931  199 HSARHQEAPLHSPEVPEKDPLTLSPTVPEADMDPllQSPVSQKETPFHVSSAAQKDTPLPTAeiTRLAVWAAVQAVE 275
Cdd:PHA03247  2724 GPAAARQASPALPAAPAPPAVPAGPATPGGPARP--ARPPTTAGPPAPAPPAAPAAGPPRRL--TRPAVASLSESRE 2796
PRK10263 PRK10263
DNA translocase FtsK; Provisional
 88-233 6.58e-07

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 53.55  E-value: 6.58e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1884012931   88 SSPLPFPSILPEESPQQAPAGPPREALFQSRVLPPK--EIPSLSPSVPRQGSRPLTPKQETSGRMPPALQKGPSLLYsaa 165
Cdd:PRK10263   741 HEPLFTPIVEPVQQPQQPVAPQQQYQQPQQPVAPQPqyQQPQQPVAPQPQYQQPQQPVAPQPQYQQPQQPVAPQPQY--- 817

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1884012931  166 SEPEMPLQGPLTSQEETPYPAPAAAERDM-PLLSHSARHQeaPLHSPEVPEKDPLTLSPtvPEADMDPL 233
Cdd:PRK10263   818 QQPQQPVAPQPQYQQPQQPVAPQPQDTLLhPLLMRNGDSR--PLHKPTTPLPSLDLLTP--PPSEVEPV 882
zf-H2C2_2 pfam13465
Zinc-finger double domain;
786-810 8.15e-07

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 45.83  E-value: 8.15e-07
                          10        20
                  ....*....|....*....|....*
gi 1884012931 786 HLLRHQRTHTGERPFKCPECEKSFS 810
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFK 25
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
617-907 5.19e-06

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 50.08  E-value: 5.19e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1884012931 617 RNRRGERPFTCM--ECGKSFRLKINLIIHQRNH-----------IKEGPYECAECEISF--------------------R 663
Cdd:COG5048    54 RSHTGEKPSQCSysGCDKSFSRPLELSRHLRTHhnnpsdlnsksLPLSNSKASSSSLSSsssnsndnnllsshslppssR 133

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1884012931 664 HKQQLTLHQRIHRV----RGGYGSPERGPSFTSKHVLKPRPKSPSSGSGGGPKP--------YKCPECDSSFSHKSSLTK 731
Cdd:COG5048   134 DPQLPDLLSISNLRnnplPGNNSSSVNTPQSNSLHPPLPANSLSKDPSSNLSLLissnvstsIPSSSENSPLSSSYSIPS 213

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1884012931 732 HQITHTGERPYTCPEC-KKSFRLHISLVIHQRVHAGKHE------VSFICSLCGKSFSRPSHLLRHQRTHTGER-PFKCP 803
Cdd:COG5048   214 SSSDQNLENSSSSLPLtTNSQLSPKSLLSQSPSSLSSSDssssasESPRSSLPTASSQSSSPNESDSSSEKGFSlPIKSK 293

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1884012931 804 ECEKSFSEKSKLTNH--CRVHSRE--RPHACPE--CGKSFIRKHHLLEHRRIHTGERPYHC------------------- 858
Cdd:COG5048   294 QCNISFSRSSPLTRHlrSVNHSGEslKPFSCPYslCGKLFSRNDALKRHILLHTSISPAKEkllnssskfspllnneppq 373

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1884012931 859 ------------------AECGKRFTQKHHLLEHQRAHTGERP--YPCTHCAKCFRYKQSLKYHLRTHT 907
Cdd:COG5048   374 slqqykdlkndkksetlsNSCIRNFKRDSNLSLHIITHLSFRPynCKNPPCSKSFNRHYNLIPHKKIHT 442
PHA03247 PHA03247
large tegument protein UL36; Provisional
 20-260 6.32e-06

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 50.32  E-value: 6.32e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1884012931   20 FERVLGLRGAGDPAGEGCRSqssrlqtPPRRPGCAllfllcAPASRSRPRVPGRRGPQVQQldmeaqrsSPLPFPSILPE 99
Cdd:PHA03247  2846 PPPSLPLGGSVAPGGDVRRR-------PPSRSPAA------KPAAPARPPVRRLARPAVSR--------STESFALPPDQ 2904

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1884012931  100 ESPQQAPAGPPREAlfQSRVLPPKEIPSLSPSVPRQGSRPLTPKQETSGRMPPAlQKGPSLLYSAASEPEMPLQGPLTSQ 179
Cdd:PHA03247  2905 PERPPQPQAPPPPQ--PQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGAGEPS-GAVPQPWLGALVPGRVAVPRFRVPQ 2981

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1884012931  180 EETPYPAPAAAE---RDMPLLSHSARHQEAPLH----SPEVPEKDPLTLSPTVPEADMDPLLQSPVSQKET--------P 244
Cdd:PHA03247  2982 PAPSREAPASSTpplTGHSLSRVSSWASSLALHeetdPPPVSLKQTLWPPDDTEDSDADSLFDSDSERSDLealdplppE 3061

                          250
                   ....*....|....*.
gi 1884012931  245 FHVSSAAQKDTPLPTA 260
Cdd:PHA03247  3062 PHDPFAHEPDPATPEA 3077
zf-H2C2_2 pfam13465
Zinc-finger double domain;
842-867 8.98e-06

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 43.13  E-value: 8.98e-06
                          10        20
                  ....*....|....*....|....*.
gi 1884012931 842 HLLEHRRIHTGERPYHCAECGKRFTQ 867
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 772-794 9.34e-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: 43.06  E-value: 9.34e-06
                          10        20
                  ....*....|....*....|...
gi 1884012931 772 FICSLCGKSFSRPSHLLRHQRTH 794
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 66-261 1.06e-05

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 49.38  E-value: 1.06e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1884012931  66 SRPRVPGRRGPQVQQlDMEAQRSSPLPFPSILPEESPQQAPAGPPREALFQSRVLPPkeiPSLSPSVPRQGSRPLT-PKQ 144
Cdd:pfam03154 144 TSPSIPSPQDNESDS-DSSAQQQILQTQPPVLQAQSGAASPPSPPPPGTTQAATAGP---TPSAPSVPPQGSPATSqPPN 219

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1884012931 145 ETSGRMPP--ALQKGPSLLYSAASEPEMPLQG---PLTSQEETPYPAPAAA-ERDMPLLSHSARHQEAPLHSPEVPEKDP 218
Cdd:pfam03154 220 QTQSTAAPhtLIQQTPTLHPQRLPSPHPPLQPmtqPPPPSQVSPQPLPQPSlHGQMPPMPHSLQTGPSHMQHPVPPQPFP 299

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1884012931 219 LTLSPTVPEADMDPLLQSPVSQKETPFHVSSAAQKDTPLPTAE 261
Cdd:pfam03154 300 LTPQSSQSQVPPGPSPAAPGQSQQRIHTPPSQSQLQSQQPPRE 342
PHA03247 PHA03247
large tegument protein UL36; Provisional
 47-286 1.09e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 49.55  E-value: 1.09e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1884012931   47 PPRRPGCALLFLLCAPASRSRPRVPGRRGP---------QVQQLDMEAQRSSPLPFP-SILPEESPQQAPAGPPREALFQ 116
Cdd:PHA03247  2775 PAAGPPRRLTRPAVASLSESRESLPSPWDPadppaavlaPAAALPPAASPAGPLPPPtSAQPTAPPPPPGPPPPSLPLGG 2854

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1884012931  117 S-------RVLPPKEIPSLSPSVP-----RQGSRPLTPKQETSGRMPPALQKGPsllySAASEPEMPLQGPLTSQEETPY 184
Cdd:PHA03247  2855 SvapggdvRRRPPSRSPAAKPAAParppvRRLARPAVSRSTESFALPPDQPERP----PQPQAPPPPQPQPQPPPPPQPQ 2930

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1884012931  185 PAPAAAERDMPLLSHSARHQEAPLHSPEVPEKDPLTLSPTVPEAdMDPLLQSPVSQKETPfhvssaAQKDTPLPTAEITR 264
Cdd:PHA03247  2931 PPPPPPPRPQPPLAPTTDPAGAGEPSGAVPQPWLGALVPGRVAV-PRFRVPQPAPSREAP------ASSTPPLTGHSLSR 3003

                          250       260
                   ....*....|....*....|..
gi 1884012931  265 LAVWAAVQAVERKLEAQAMRLL 286
Cdd:PHA03247  3004 VSSWASSLALHEETDPPPVSLK 3025
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
771-823 1.81e-05

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 48.15  E-value: 1.81e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1884012931 771 SFICSLCGKSFSRPSHLLRHQRTHTGERPFKC--PECEKSFSEKSKLTNHCRVHS 823
Cdd:COG5048    33 PDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCsySGCDKSFSRPLELSRHLRTHH 87
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
46-290 4.14e-05

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 47.56  E-value: 4.14e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1884012931  46 TPPRRPGCALLFLLCAPASRSRPRVPGRRGPQVQQLDMEAQRSSPLPFPSILPEESPQQAPAGPPREAlfqsrVLPPKEI 125
Cdd:PRK12323  398 APAAPPAAPAAAPAAAAAARAVAAAPARRSPAPEALAAARQASARGPGGAPAPAPAPAAAPAAAARPA-----AAGPRPV 472

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1884012931 126 PSLSPSVPRQGSRPLTPKQETSGrmPPALQKGPSLLYSAASEPEMPLQGPLTSqEETPYPAPAAAERDMPLLSHSArhqe 205
Cdd:PRK12323  473 AAAAAAAPARAAPAAAPAPADDD--PPPWEELPPEFASPAPAQPDAAPAGWVA-ESIPDPATADPDDAFETLAPAP---- 545

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1884012931 206 APLHSPEVPEKDPLTLSPTVPEADMDPLlqSPVSQKETPfhvSSAAQkdtpLP----TAEITRLAVWAAVQAVERKLEAq 281
Cdd:PRK12323  546 AAAPAPRAAAATEPVVAPRPPRASASGL--PDMFDGDWP---ALAAR----LPvrglAQQLARQSELAGVEGDTVRLRV- 615


                  ....*....
gi 1884012931 282 AMRLLTLEG 290
Cdd:PRK12323  616 PVPALAEAE 624
PHA03247 PHA03247
large tegument protein UL36; Provisional
 27-271 5.45e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 47.24  E-value: 5.45e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1884012931   27 RGAGDPAGEGcrSQSSRLQTPPRRPGCALLfllcaPASRSRPRVPGRRGPQVQQLDMEAQRSS---PLPFPSILPEESPQ 103
Cdd:PHA03247  2493 GAAPDPGGGG--PPDPDAPPAPSRLAPAIL-----PDEPVGEPVHPRMLTWIRGLEELASDDAgdpPPPLPPAAPPAAPD 2565

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1884012931  104 QA-----PAGPPREALFQSRvlppkeipSLSPSVPRQGSRPLTPKQEtsgRMPPALQKGPSLLYSAASEPEMPLQGPLTS 178
Cdd:PHA03247  2566 RSvppprPAPRPSEPAVTSR--------ARRPDAPPQSARPRAPVDD---RGDPRGPAPPSPLPPDTHAPDPPPPSPSPA 2634

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1884012931  179 QEETPYPAPAAA-----ERDMPLLSHSARHQEA-----------PLHSPEVPEKDPLTLS------PTVPEADMDPLLQS 236
Cdd:PHA03247  2635 ANEPDPHPPPTVppperPRDDPAPGRVSRPRRArrlgraaqassPPQRPRRRAARPTVGSltsladPPPPPPTPEPAPHA 2714

                          250       260       270
                   ....*....|....*....|....*....|....*
gi 1884012931  237 PVSQKETPFHVSSAAQKDTPLPTAEITRLAVWAAV 271
Cdd:PHA03247  2715 LVSATPLPPGPAAARQASPALPAAPAPPAVPAGPA 2749
SUF4-like cd20908
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
 774-831 5.46e-05

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: 42.54  E-value: 5.46e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1884012931 774 CSLCGKSFSRPSHLLRHQRTHTgerpFKCPECEKSFSEKSKLTNHC-RVHSRER---PHACP 831
Cdd:cd20908     4 CYYCDREFDDEKILIQHQKAKH----FKCHICHKKLYTAGGLAVHClQVHKETLtkvPNALP 61
zf-H2C2_2 pfam13465
Zinc-finger double domain;
728-751 1.62e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 39.28  E-value: 1.62e-04
                          10        20
                  ....*....|....*....|....
gi 1884012931 728 SLTKHQITHTGERPYTCPECKKSF 751
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSF 24
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 714-736 1.87e-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: 39.21  E-value: 1.87e-04
                          10        20
                  ....*....|....*....|...
gi 1884012931 714 YKCPECDSSFSHKSSLTKHQITH 736
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
61-292 2.49e-04

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 44.87  E-value: 2.49e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1884012931  61 APASRSRPRVPGRRGPQVQQLDMEAQRSSPLPFPSILPEESPQQAPAG-------PPREALFQSRVLPPKEIPSLSPSVP 133
Cdd:PRK12323  373 GPATAAAAPVAQPAPAAAAPAAAAPAPAAPPAAPAAAPAAAAAARAVAaaparrsPAPEALAAARQASARGPGGAPAPAP 452

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1884012931 134 RQGSRPL--TPKQETSGRMPPALQKGPSLLYSAASEPEMPLQGPLTSQEETP-YPAPAAAERDMPLLSHSARHQEAPLHS 210
Cdd:PRK12323  453 APAAAPAaaARPAAAGPRPVAAAAAAAPARAAPAAAPAPADDDPPPWEELPPeFASPAPAQPDAAPAGWVAESIPDPATA 532

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1884012931 211 PEVPEKDPLTLSPTVPEAdmdPLLQSPVSQKETPFHVSSAAQKDTPLPTAEITRLAVWAAVQAVERKLEAQAmRLLTLEG 290
Cdd:PRK12323  533 DPDDAFETLAPAPAAAPA---PRAAAATEPVVAPRPPRASASGLPDMFDGDWPALAARLPVRGLAQQLARQS-ELAGVEG 608


                  ..
gi 1884012931 291 RT 292
Cdd:PRK12323  609 DT 610
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 828-850 2.53e-04

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


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 38.82  E-value: 2.53e-04
                          10        20
                  ....*....|....*....|...
gi 1884012931 828 HACPECGKSFIRKHHLLEHRRIH 850
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
PRK08691 PRK08691
DNA polymerase III subunits gamma and tau; Validated
 74-283 3.77e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236333 [Multi-domain]  Cd Length: 709  Bit Score: 44.31  E-value: 3.77e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1884012931  74 RGPQVQQLDMEAQRSSPLPFPSILPEESPQQAP--AGPPREAlfqsRVLPPKEIPSLSPSVPRQGSrPlTPKQETSGRMP 151
Cdd:PRK08691  378 QSPSAQTAEKETAAKKPQPRPEAETAQTPVQTAsaAAMPSEG----KTAGPVSNQENNDVPPWEDA-P-DEAQTAAGTAQ 451

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1884012931 152 PalqkgPSLLYSAASEPEMPLQGPLTSQE-----------ETPYPAPA-AAERDMPLLSHSARHQ--EAPLHSPEVPEKD 217
Cdd:PRK08691  452 T-----SAKSIQTASEAETPPENQVSKNKaadnetdaplsEVPSENPIqATPNDEAVETETFAHEapAEPFYGYGFPDND 526

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1884012931 218 -PLTLSPTVPEADMDPLLQSPVSQKETPFHVSSAAQKDTPLPTAEITRLAV--WAA-VQAVERKLEAQAM 283
Cdd:PRK08691  527 cPPEDGAEIPPPDWEHAAPADTAGGGADEEAEAGGIGGNNTPSAPPPEFSTenWAAiVRHFARKLGAAQM 596
PHA03321 PHA03321
tegument protein VP11/12; Provisional
 19-218 4.29e-04

tegument protein VP11/12; Provisional


Pssm-ID: 223041 [Multi-domain]  Cd Length: 694  Bit Score: 44.18  E-value: 4.29e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1884012931  19 RFERVLGLRGAGDPAGEGCRSQSSRLQTPPR-RPGcallfllCAPASRSRPRVPGRRGPQVQQLDMEAQrSSPLPFPSil 97
Cdd:PHA03321  417 HYEASLRLLSSRQPPGAPAPRRDNDPPPPPRaRPG-------STPACARRARAQRARDAGPEYVDPLGA-LRRLPAGA-- 486

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1884012931  98 peeSPQQAPAGPPREALFQSRVlppkeipslspsvprQGSRPLTPKQetsGRMPPALQK--GPsllySAASEPEmplqgp 175
Cdd:PHA03321  487 ---APPPEPAAAPSPATYYTRM---------------GGGPPRLPPR---NRATETLRPdwGP----PAAAPPE------ 535

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1884012931 176 ltsQEETPYPAP---AAAERDMPLLSHSARHQEAPlhspeVPEKDP 218
Cdd:PHA03321  536 ---QMEDPYLEPdddRFDRRDGAAAAATSHPREAP-----APDDDP 573
zf-H2C2_5 pfam13909
C2H2-type zinc-finger domain;
714-738 5.27e-04

C2H2-type zinc-finger domain;


Pssm-ID: 404746 [Multi-domain]  Cd Length: 25  Bit Score: 37.92  E-value: 5.27e-04
                          10        20
                  ....*....|....*....|....*
gi 1884012931 714 YKCPECDSSFSHKSSLTKHQITHTG 738
Cdd:pfam13909   1 YKCSQCDYSTAWKSNLKRHLRKHTG 25
zf-H2C2_2 pfam13465
Zinc-finger double domain;
815-839 5.47e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.12  E-value: 5.47e-04
                          10        20
                  ....*....|....*....|....*
gi 1884012931 815 LTNHCRVHSRERPHACPECGKSFIR 839
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 26
PLN03209 PLN03209
translocon at the inner envelope of chloroplast subunit 62; Provisional
 88-257 5.64e-04

translocon at the inner envelope of chloroplast subunit 62; Provisional


Pssm-ID: 178748 [Multi-domain]  Cd Length: 576  Bit Score: 43.76  E-value: 5.64e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1884012931  88 SSPLPF-PSILPEESPQQAPAGPPREALFQSRVLPPKEIPSLSP-SVPRQGSRPLTP-------KQETSGRMPPALQKGP 158
Cdd:PLN03209  384 TSPIPTpPSSSPASSKSVDAVAKPAEPDVVPSPGSASNVPEVEPaQVEAKKTRPLSPyaryedlKPPTSPSPTAPTGVSP 463

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1884012931 159 SLLySAASEPEMPLQGPLTSQEETPYPAPAaaeRDMPLLSHSARHQEAPLHSPEVPEKDPLTLSPTVPEADMDPLLQSPV 238
Cdd:PLN03209  464 SVS-STSSVPAVPDTAPATAATDAAAPPPA---NMRPLSPYAVYDDLKPPTSPSPAAPVGKVAPSSTNEVVKVGNSAPPT 539

                         170
                  ....*....|....*....
gi 1884012931 239 SQKETPFHvssAAQKDTPL 257
Cdd:PLN03209  540 ALADEQHH---AQPKPRPL 555
PHA03379 PHA03379
EBNA-3A; Provisional
 26-251 8.26e-04

EBNA-3A; Provisional


Pssm-ID: 223066 [Multi-domain]  Cd Length: 935  Bit Score: 43.12  E-value: 8.26e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1884012931  26 LRGAGDPAGEGCRSQSSR----LQTPPRRPgcALLFLLCAPAsRSRPRVPGRRGP---QVQQLDMeAQRSSPLPFPSILP 98
Cdd:PHA03379  554 MQGPGETSGIVRVRERWRpapwTPNPPRSP--SQMSVRDRLA-RLRAEAQPYQASvevQPPQLTQ-VSPQQPMEYPLEPE 629

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1884012931  99 EESPQQAPAGPPREALFQSRVlPPKEIPSLSPSV--PRQGSRPLTPKQETSGRMPPALQKGPSLLYSAASE--------- 167
Cdd:PHA03379  630 QQMFPGSPFSQVADVMRAGGV-PAMQPQYFDLPLqqPISQGAPLAPLRASMGPVPPVPATQPQYFDIPLTEpinqgasaa 708

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1884012931 168 ---PEMPLQGPLTSqEETPYPAPAAAERDMPLLSHS-------------------ARHQeAPLHSPEVPEKDPLTLSPTV 225
Cdd:PHA03379  709 hflPQQPMEGPLVP-ERWMFQGATLSQSVRPGVAQSqyfdlpltqpinhgapaahFLHQ-PPMEGPWVPEQWMFQGAPPS 786

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1884012931 226 PEAD-----MDPLLQS---------PVSQKETPFHVSSAA 251
Cdd:PHA03379  787 QGTDvvqhqLDALGYVlhvlnhpgvPVSPAVNQYHVSQAA 826
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 856-878 8.47e-04

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


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 37.28  E-value: 8.47e-04
                          10        20
                  ....*....|....*....|...
gi 1884012931 856 YHCAECGKRFTQKHHLLEHQRAH 878
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 61-286 8.61e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 43.05  E-value: 8.61e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1884012931  61 APASRSRPRVPGRRGPQVQQldmeAQRSSPLPfpsilPEESPQQAPAGPPREALFQSRVLPPKEIPSLSPSVPRQGSRPL 140
Cdd:PRK07764  593 GAAGGEGPPAPASSGPPEEA----ARPAAPAA-----PAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDAS 663

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1884012931 141 TPKQETSGRMPPALQKGPSLlySAASEPEMPLQGPLTSQEETPYPAPAAAERDMPLLSHSARHQEAPLHSPEVPEKD-PL 219
Cdd:PRK07764  664 DGGDGWPAKAGGAAPAAPPP--APAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQPPQAAQGASAPSPAADDPvPL 741

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1884012931 220 TLSPTVPEADMDPLLQSPvsQKETPFHVSSAAQKDTPLPTAEITRLAVWAAVQAVERKL---EAQAMRLL 286
Cdd:PRK07764  742 PPEPDDPPDPAGAPAQPP--PPPAPAPAAAPAAAPPPSPPSEEEEMAEDDAPSMDDEDRrdaEEVAMELL 809
PRK10263 PRK10263
DNA translocase FtsK; Provisional
 61-266 9.23e-04

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 43.15  E-value: 9.23e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1884012931   61 APASRSRPRVPGRRGPQVQQLDMEAQRSSPLPFPSILPEESPQQAP---AGPPREALFQSRVLPPKEIPSLSPSVPRQGS 137
Cdd:PRK10263   374 APAPEGYPQQSQYAQPAVQYNEPLQQPVQPQQPYYAPAAEQPAQQPyyaPAPEQPAQQPYYAPAPEQPVAGNAWQAEEQQ 453

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1884012931  138 RPLTPK---QETSGRMPPALQkgPSLLYSAASEPEMPLQGPLTSQEET-PYPAPAAAERDMPLLSHSARHQEAPLHSPeV 213
Cdd:PRK10263   454 STFAPQstyQTEQTYQQPAAQ--EPLYQQPQPVEQQPVVEPEPVVEETkPARPPLYYFEEVEEKRAREREQLAAWYQP-I 530

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1884012931  214 PE--KDPLTLSPTVPEadMDPLLQSPVSQKETPFHVSSAAQKDTPLPTAEITRLA 266
Cdd:PRK10263   531 PEpvKEPEPIKSSLKA--PSVAAVPPVEAAAAVSPLASGVKKATLATGAAATVAA 583
transpos_ISL3 NF033550
ISL3 family transposase;
820-868 1.02e-03

ISL3 family transposase;


Pssm-ID: 468079 [Multi-domain]  Cd Length: 369  Bit Score: 42.57  E-value: 1.02e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1884012931 820 RVHSRERPHACPECGKS--FIRKHHlleHRRIH---TGERP---------YHCAECGKRFTQK 868
Cdd:NF033550    3 EAELTRGDATCPECGKPsrRVHDTG---KRRIRhlpIFGRPvylelrvrrFKCPECGKTFTEE 62
PHA03247 PHA03247
large tegument protein UL36; Provisional
 17-250 1.50e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 42.62  E-value: 1.50e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1884012931   17 ERRFERVLGLRGAGD-------PAGEGCRSQSSRLQTPPRRPgcallfllcaPASRSRPRVPGRRGPQVQQLDMEAqrsS 89
Cdd:PHA03247   239 ERRVVISHPLRGDIAapapppvVGEGADRAPETARGATGPPP----------PPEAAAPNGAAAPPDGVWGAALAG---A 305

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1884012931   90 PLPFPSilPEESPQQAPAGPPREALFQSRVLP-----PKEIPSLSPSVPRQGSRPLTPKQE----TSGRMPPALQKGPSL 160
Cdd:PHA03247   306 PLALPA--PPDPPPPAPAGDAEEEDDEDGAMEvvsplPRPRQHYPLGFPKRRRPTWTPPSSledlSAGRHHPKRASLPTR 383

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1884012931  161 LYSAASEPEMPL----QGPLTSQEETPYPAPAAAERDMPLLSHSARHQEAPLHSPEVPEKDpltlSPTVPEADMDPLLQS 236
Cdd:PHA03247   384 KRRSARHAATPFargpGGDDQTRPAAPVPASVPTPAPTPVPASAPPPPATPLPSAEPGSDD----GPAPPPERQPPAPAT 459

                          250
                   ....*....|....
gi 1884012931  237 PVSQKETPFHVSSA 250
Cdd:PHA03247   460 EPAPDDPDDATRKA 473
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 30-262 2.03e-03

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 42.06  E-value: 2.03e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1884012931  30 GDPAGEGCRSQSSRLQTPPRRPGCAllfllcAPASRSRPRVPGrrgPQVQQLDMEAQRSSPLPfPSILPEESPQQAPAGP 109
Cdd:pfam03154 293 VPPQPFPLTPQSSQSQVPPGPSPAA------PGQSQQRIHTPP---SQSQLQSQQPPREQPLP-PAPLSMPHIKPPPTTP 362

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1884012931 110 -PREALFQSRVLPPKEIPSLSPSVPRQGSRP--LTPKQETSGRMPPALQKGPSLLYSAASE-PEMPLQGPLTSQEETpYP 185
Cdd:pfam03154 363 iPQLPNPQSHKHPPHLSGPSPFQMNSNLPPPpaLKPLSSLSTHHPPSAHPPPLQLMPQSQQlPPPPAQPPVLTQSQS-LP 441

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1884012931 186 APAAAERDMPLLSHSARHQEAPLHsPEVPEKDPLTLSPTVPEADMDPLLqsPVSQKETPFHVSSA----AQKDTPLPTAE 261
Cdd:pfam03154 442 PPAASHPPTSGLHQVPSQSPFPQH-PFVPGGPPPITPPSGPPTSTSSAM--PGIQPPSSASVSSSgpvpAAVSCPLPPVQ 518


                  .
gi 1884012931 262 I 262
Cdd:pfam03154 519 I 519
PHA03247 PHA03247
large tegument protein UL36; Provisional
 30-270 2.93e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 41.46  E-value: 2.93e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1884012931   30 GDPAGEGCRSQSSRLQTPPRRPgcallfllcAPASRSRPRVPGRRGPQVQ---------------QLDMEAQRSSPLPFP 94
Cdd:PHA03247  2606 GDPRGPAPPSPLPPDTHAPDPP---------PPSPSPAANEPDPHPPPTVppperprddpapgrvSRPRRARRLGRAAQA 2676

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1884012931   95 SIlPEESPQQAPAGPPREALFQSRVLPPKEIPSLSPSVPRQGSRPLTPKQETSGR---------MPPALQKGPSLLYSAA 165
Cdd:PHA03247  2677 SS-PPQRPRRRAARPTVGSLTSLADPPPPPPTPEPAPHALVSATPLPPGPAAARQaspalpaapAPPAVPAGPATPGGPA 2755

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1884012931  166 SEPEMPLQGPLTSQEETPYPAPAAAERDMPLLSHSARHQEAPLHSPEVPEKDPltlSPTVPEADMDPLLQSPVSQKETPF 245
Cdd:PHA03247  2756 RPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPP---AAVLAPAAALPPAASPAGPLPPPT 2832

                          250       260
                   ....*....|....*....|....*
gi 1884012931  246 HVSSAAQKDTPLPTAEITRLAVWAA 270
Cdd:PHA03247  2833 SAQPTAPPPPPGPPPPSLPLGGSVA 2857
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 884-906 3.03e-03

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


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 35.74  E-value: 3.03e-03
                          10        20
                  ....*....|....*....|...
gi 1884012931 884 YPCTHCAKCFRYKQSLKYHLRTH 906
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 625-647 3.95e-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: 3.95e-03
                          10        20
                  ....*....|....*....|...
gi 1884012931 625 FTCMECGKSFRLKINLIIHQRNH 647
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
CpXC pfam14353
CpXC protein; This presumed domain is functionally uncharacterized. This domain is found in ...
 715-762 4.40e-03

CpXC protein; This presumed domain is functionally uncharacterized. This domain is found in bacteria and archaea, and is typically between 122 and 134 amino acids in length. It contains four conserved cysteines forming two CpXC motifs.


Pssm-ID: 433895  Cd Length: 121  Bit Score: 38.09  E-value: 4.40e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1884012931 715 KCPECDSSFSHksslTKHQITHTGERP-------------YTCPECKKSFRLHISLVIHQR 762
Cdd:pfam14353   2 TCPKCGKEFEA----EVWTSINADEDPelkekvldgslfsFTCPKCGASFRLEYPLLYHDP 58
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
688-889 5.03e-03

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 40.45  E-value: 5.03e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1884012931 688 PSFTSKHVLKPRPKSPSSGSGGGPKPYKCPECDSSFSHKSSLTKHQITHTGERPYTC--PECKKSFRLHISLVIHQRvHA 765
Cdd:COG5048     8 SSSSNNSVLSSTPKSTLKSLSNAPRPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCsySGCDKSFSRPLELSRHLR-TH 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1884012931 766 GKHEVSFICSLCGKSFSRPSHLLRHQRTHTGERPFKCPECEKSFSEKSKLTNHCRVHSRERPHACPECGKSFI------R 839
Cdd:COG5048    87 HNNPSDLNSKSLPLSNSKASSSSLSSSSSNSNDNNLLSSHSLPPSSRDPQLPDLLSISNLRNNPLPGNNSSSVntpqsnS 166

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1884012931 840 KHHLLE----------------HRRIHTGERPYHCAECGKRFTQKHHLLEHQRAHTGERPYPCTHC 889
Cdd:COG5048   167 LHPPLPanslskdpssnlslliSSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTN 232
zf-H2C2_2 pfam13465
Zinc-finger double domain;
870-895 5.34e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.04  E-value: 5.34e-03
                          10        20
                  ....*....|....*....|....*.
gi 1884012931 870 HLLEHQRAHTGERPYPCTHCAKCFRY 895
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
ZnF_C2H2 smart00355
zinc finger;
772-794 6.22e-03

zinc finger;


Pssm-ID: 197676  Cd Length: 23  Bit Score: 35.13  E-value: 6.22e-03
                           10        20
                   ....*....|....*....|...
gi 1884012931  772 FICSLCGKSFSRPSHLLRHQRTH 794
Cdd:smart00355   1 YRCPECGKVFKSKSALREHMRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 653-675 6.58e-03

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


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 34.97  E-value: 6.58e-03
                          10        20
                  ....*....|....*....|...
gi 1884012931 653 YECAECEISFRHKQQLTLHQRIH 675
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
101-294 7.04e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 40.24  E-value: 7.04e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1884012931 101 SPQQAPAGPPREALFQSR-VLPPKEIPSLSPSVPRQGSRPLTPKQETSGRMPPALQKGPSLLYSAASEPemplqGPLTSQ 179
Cdd:PRK12323  376 TAAAAPVAQPAPAAAAPAaAAPAPAAPPAAPAAAPAAAAAARAVAAAPARRSPAPEALAAARQASARGP-----GGAPAP 450

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1884012931 180 EETPYPAPAAAER-------DMPLLSHSARHQEAPLHSPEVPEKDPL---TLSPTVPEADMDPLLQSPVSQKETPFHVSS 249
Cdd:PRK12323  451 APAPAAAPAAAARpaaagprPVAAAAAAAPARAAPAAAPAPADDDPPpweELPPEFASPAPAQPDAAPAGWVAESIPDPA 530

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1884012931 250 AAQKDTPLPTAEITRLAVWAAVQAVERKLEAQAMRLLTLEGRTGT 294
Cdd:PRK12323  531 TADPDDAFETLAPAPAAAPAPRAAAATEPVVAPRPPRASASGLPD 575
PHA03377 PHA03377
EBNA-3C; Provisional
 38-259 7.64e-03

EBNA-3C; Provisional


Pssm-ID: 177614 [Multi-domain]  Cd Length: 1000  Bit Score: 40.04  E-value: 7.64e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1884012931   38 RSQSSRLQTPPRRPGCALLFLLCA-PASRSRPRVPGRRGPQ--VQQLDMEAQRSSPLPFPSILPEESPQQAPAgPPREAL 114
Cdd:PHA03377   669 RRQPATQSTPPRPSWLPSVFVLPSvDAGRAQPSEESHLSSMspTQPISHEEQPRYEDPDDPLDLSLHPDQAPP-PSHQAP 747

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1884012931  115 FQSRVLP--------------PKEIPSLSPSVPRQGSRPLTPKQETSGRMPPALQKgPSLLYSAASEPEMPLQGPLTS-- 178
Cdd:PHA03377   748 YSGHEEPqaqqapypgyweprPPQAPYLGYQEPQAQGVQVSSYPGYAGPWGLRAQH-PRYRHSWAYWSQYPGHGHPQGpw 826

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1884012931  179 QEETPYPAPAAAERDMPllSHSARHQEAPLHSPEVPEKDPLTLSPTVPEAdmdpllQSPVSQKETPFHVSSAAQKDTPLP 258
Cdd:PHA03377   827 APRPPHLPPQWDGSAGH--GQDQVSQFPHLQSETGPPRLQLSQVPQLPYS------QTLVSSSAPSWSSPQPRAPIRPIP 898


                   .
gi 1884012931  259 T 259
Cdd:PHA03377   899 T 899
ZnF_C2H2 smart00355
zinc finger;
714-736 8.52e-03

zinc finger;


Pssm-ID: 197676  Cd Length: 23  Bit Score: 34.75  E-value: 8.52e-03
                           10        20
                   ....*....|....*....|...
gi 1884012931  714 YKCPECDSSFSHKSSLTKHQITH 736
Cdd:smart00355   1 YRCPECGKVFKSKSALREHMRTH 23
zf-C2H2_4 pfam13894
C2H2-type zinc finger; This family contains a number of divergent C2H2 type zinc fingers.
 772-794 9.46e-03

C2H2-type zinc finger; This family contains a number of divergent C2H2 type zinc fingers.


Pssm-ID: 464025  Cd Length: 24  Bit Score: 34.54  E-value: 9.46e-03
                          10        20
                  ....*....|....*....|...
gi 1884012931 772 FICSLCGKSFSRPSHLLRHQRTH 794
Cdd:pfam13894   1 FKCPICGKSFSSKKSLKRHLKTH 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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