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Conserved domains on  [gi|1207143484|ref|XP_021323870|]
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PR domain zinc finger protein 1 isoform X1 [Danio rerio]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PR-SET_PRDM1 cd19187
PR-SET domain found in PR domain zinc finger protein 1 (PRDM1) and similar proteins; PRDM1 ...
 42-168 1.08e-71

PR-SET domain found in PR domain zinc finger protein 1 (PRDM1) and similar proteins; PRDM1 (also termed BLIMP-1, beta-interferon gene positive regulatory domain I-binding factor, PR domain-containing protein 1, positive regulatory domain I-binding factor 1, PRDI-BF1, or PRDI-binding factor 1) acts as a transcription factor that mediates a transcriptional program in various innate and adaptive immune tissue-resident lymphocyte T cell types such as tissue-resident memory T (Trm), natural killer (trNK) and natural killer T (NKT) cells and negatively regulates gene expression of proteins that promote the egress of tissue-resident T-cell populations from non-lymphoid organs.


:

Pssm-ID: 380964 [Multi-domain]  Cd Length: 128  Bit Score: 227.59  E-value: 1.08e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207143484  42 TSIPRNLSFQYNRDQ-QVTGVFSKEYIPQGTRFGPLQGVVYTKENVPLHTNRKYFWRIYSGGQLQHFIDGYDVRLSNWMR 120
Cdd:cd19187     1 ASLPRNLTLKYSSVGrEVLGVWSSDYIPRGTRFGPLVGEIYTNDPVPKGANRKYFWRIYSNGEFYHYIDGFDPSKSNWMR 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1207143484 121 YVNPARSLAEQNLVACQNGPDIFFYTLRPLEPKQELLVWYSPEFSQRL 168
Cdd:cd19187    81 YVNPAHSLQEQNLVACQIGMNIYFYTVKPIPPNQELLVWYCREFARRL 128
zf-H2C2_2 pfam13465
Zinc-finger double domain;
449-474 4.80e-05

Zinc-finger double domain;


:

Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 40.43  E-value: 4.80e-05
                          10        20
                  ....*....|....*....|....*.
gi 1207143484 449 NLKVHLRVHSGERPFQCNLCKKSFTQ 474
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
477-502 5.35e-05

Zinc-finger double domain;


:

Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 40.43  E-value: 5.35e-05
                          10        20
                  ....*....|....*....|....*.
gi 1207143484 477 HLQKHHLVHTGEKPHECQVCHKRFSS 502
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
505-530 5.40e-05

Zinc-finger double domain;


:

Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 40.43  E-value: 5.40e-05
                          10        20
                  ....*....|....*....|....*.
gi 1207143484 505 NLKTHLRLHSGEKPYQCKLCGVKFTQ 530
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
203-524 7.59e-05

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


:

Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 45.84  E-value: 7.59e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207143484 203 PSNPQNHPCDTNKDDEEPEE----KIDIERDTPPDTPDEQIMDFSKK-IHKSEPMHEKTNIYPSLSPPQDVPLHLHSLYG 277
Cdd:COG5048    28 SNAPRPDSCPNCTDSFSRLEhltrHIRSHTGEKPSQCSYSGCDKSFSrPLELSRHLRTHHNNPSDLNSKSLPLSNSKASS 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207143484 278 HREGLISSYPSIRSPYPLLPQYNPHYQHMLIPPYSPPFTSMLPTKPAHRYGFMNPdgLSYPSIPQSGLLPVSLPYPNTLH 357
Cdd:COG5048   108 SSLSSSSSNSNDNNLLSSHSLPPSSRDPQLPDLLSISNLRNNPLPGNNSSSVNTP--QSNSLHPPLPANSLSKDPSSNLS 185

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207143484 358 GGLNERGHNTPPRGAPATPELSPQTSPCQTHYSECEEA-INLSLTTPKSTPPPSASPAMipgYKSLPYPLKKQNGKIKYE 436
Cdd:COG5048   186 LLISSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSsSSLPLTTNSQLSPKSLLSQS---PSSLSSSDSSSSASESPR 262

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207143484 437 CNVCMKTFGQLSNLKVHLRVHSGER-PFQCNLCKKSFTQLAHLQKH--HLVHTGE--KPHEC--QVCHKRFSSTSNLKTH 509
Cdd:COG5048   263 SSLPTASSQSSSPNESDSSSEKGFSlPIKSKQCNISFSRSSPLTRHlrSVNHSGEslKPFSCpySLCGKLFSRNDALKRH 342

                         330
                  ....*....|....*
gi 1207143484 510 LRLHSGEKPYQCKLC 524
Cdd:COG5048   343 ILLHTSISPAKEKLL 357
ATP-synt_Fo_b super family cl21478
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ...
 581-637 2.79e-03

F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex of FoF1-ATP synthase. The F-type ATP synthases (FoF1-ATPase) consist of two structural domains: the F1 (assembly factor one) complex containing the soluble catalytic core, and the Fo (oligomycin sensitive factor) complex containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. F1 is composed of alpha (or A), beta (B), gamma (C), delta (D) and epsilon (E) subunits with a stoichiometry of 3:3:1:1:1, while Fo consists of the three subunits a, b, and c (1:2:10-14). An oligomeric ring of 10-14 c subunits (c-ring) make up the Fo rotor. The flux of protons through the ATPase channel (Fo) drives the rotation of the c-ring, which in turn is coupled to the rotation of the F1 complex gamma subunit rotor due to the permanent binding between the gamma and epsilon subunits of F1 and the c-ring of Fo. The F-ATP synthases are primarily found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts or in the plasma membranes of bacteria. The F-ATP synthases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. This group also includes F-ATP synthase that has also been found in the archaea Candidatus Methanoperedens.


The actual alignment was detected with superfamily member PRK14475:

Pssm-ID: 473877 [Multi-domain]  Cd Length: 167  Bit Score: 39.15  E-value: 2.79e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207143484 581 ETLRRAAELLERFDASAEAEALPE---SAAEPQVDAAlEEWLARSLQSGEEDGLLRACTG 637
Cdd:PRK14475  102 EQIKRRAEMAERKIAQAEAQAAADvkaAAVDLAAQAA-ETVLAARLAGAKSDPLVDAAIG 160
 
Name Accession Description Interval E-value
PR-SET_PRDM1 cd19187
PR-SET domain found in PR domain zinc finger protein 1 (PRDM1) and similar proteins; PRDM1 ...
 42-168 1.08e-71

PR-SET domain found in PR domain zinc finger protein 1 (PRDM1) and similar proteins; PRDM1 (also termed BLIMP-1, beta-interferon gene positive regulatory domain I-binding factor, PR domain-containing protein 1, positive regulatory domain I-binding factor 1, PRDI-BF1, or PRDI-binding factor 1) acts as a transcription factor that mediates a transcriptional program in various innate and adaptive immune tissue-resident lymphocyte T cell types such as tissue-resident memory T (Trm), natural killer (trNK) and natural killer T (NKT) cells and negatively regulates gene expression of proteins that promote the egress of tissue-resident T-cell populations from non-lymphoid organs.


Pssm-ID: 380964 [Multi-domain]  Cd Length: 128  Bit Score: 227.59  E-value: 1.08e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207143484  42 TSIPRNLSFQYNRDQ-QVTGVFSKEYIPQGTRFGPLQGVVYTKENVPLHTNRKYFWRIYSGGQLQHFIDGYDVRLSNWMR 120
Cdd:cd19187     1 ASLPRNLTLKYSSVGrEVLGVWSSDYIPRGTRFGPLVGEIYTNDPVPKGANRKYFWRIYSNGEFYHYIDGFDPSKSNWMR 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1207143484 121 YVNPARSLAEQNLVACQNGPDIFFYTLRPLEPKQELLVWYSPEFSQRL 168
Cdd:cd19187    81 YVNPAHSLQEQNLVACQIGMNIYFYTVKPIPPNQELLVWYCREFARRL 128
SET smart00317
SET (Su(var)3-9, Enhancer-of-zeste, Trithorax) domain; Putative methyl transferase, based on ...
 52-165 1.21e-16

SET (Su(var)3-9, Enhancer-of-zeste, Trithorax) domain; Putative methyl transferase, based on outlier plant homologues


Pssm-ID: 214614 [Multi-domain]  Cd Length: 124  Bit Score: 76.60  E-value: 1.21e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207143484   52 YNRDQQVTGVFSKEYIPQGTRFGPLQGVVYTKENVP--------LHTNRKYFWRIYSGgqlqHFIDGYdvRLSNWMRYVN 123
Cdd:smart00317   6 FKSPGKGWGVRATEDIPKGEFIGEYVGEIITSEEAEerpkaydtDGAKAFYLFDIDSD----LCIDAR--RKGNLARFIN 79

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 1207143484  124 PARSLAEQNLVACQNGPD-IFFYTLRPLEPKQELLVWYSPEFS 165
Cdd:smart00317  80 HSCEPNCELLFVEVNGDDrIVIFALRDIKPGEELTIDYGSDYA 122
SET pfam00856
SET domain; SET domains are protein lysine methyltransferase enzymes. SET domains appear to be ...
 60-160 2.58e-10

SET domain; SET domains are protein lysine methyltransferase enzymes. SET domains appear to be protein-protein interaction domains. It has been demonstrated that SET domains mediate interactions with a family of proteins that display similarity with dual-specificity phosphatases (dsPTPases). A subset of SET domains have been called PR domains. These domains are divergent in sequence from other SET domains, but also appear to mediate protein-protein interaction. The SET domain consists of two regions known as SET-N and SET-C. SET-C forms an unusual and conserved knot-like structure of probably functional importance. Additionally to SET-N and SET-C, an insert region (SET-I) and flanking regions of high structural variability form part of the overall structure.


Pssm-ID: 459965 [Multi-domain]  Cd Length: 115  Bit Score: 58.30  E-value: 2.58e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207143484  60 GVFSKEYIPQGTRFGPLQGV-VYTKENVPLHTNRKY------FWRIYS---GGQLQHFIDGYDVRLSNWMRYVNPARSL- 128
Cdd:pfam00856   3 GLFATEDIPKGEFIGEYVEVlLITKEEADKRELLYYdklelrLWGPYLftlDEDSEYCIDARALYYGNWARFINHSCDPn 82

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1207143484 129 AEQNLVACQNGPDIFFYTLRPLEPKQELLVWY 160
Cdd:pfam00856  83 CEVRVVYVNGGPRIVIFALRDIKPGEELTIDY 114
zf-H2C2_2 pfam13465
Zinc-finger double domain;
449-474 4.80e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 40.43  E-value: 4.80e-05
                          10        20
                  ....*....|....*....|....*.
gi 1207143484 449 NLKVHLRVHSGERPFQCNLCKKSFTQ 474
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
477-502 5.35e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 40.43  E-value: 5.35e-05
                          10        20
                  ....*....|....*....|....*.
gi 1207143484 477 HLQKHHLVHTGEKPHECQVCHKRFSS 502
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
505-530 5.40e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 40.43  E-value: 5.40e-05
                          10        20
                  ....*....|....*....|....*.
gi 1207143484 505 NLKTHLRLHSGEKPYQCKLCGVKFTQ 530
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
203-524 7.59e-05

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 45.84  E-value: 7.59e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207143484 203 PSNPQNHPCDTNKDDEEPEE----KIDIERDTPPDTPDEQIMDFSKK-IHKSEPMHEKTNIYPSLSPPQDVPLHLHSLYG 277
Cdd:COG5048    28 SNAPRPDSCPNCTDSFSRLEhltrHIRSHTGEKPSQCSYSGCDKSFSrPLELSRHLRTHHNNPSDLNSKSLPLSNSKASS 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207143484 278 HREGLISSYPSIRSPYPLLPQYNPHYQHMLIPPYSPPFTSMLPTKPAHRYGFMNPdgLSYPSIPQSGLLPVSLPYPNTLH 357
Cdd:COG5048   108 SSLSSSSSNSNDNNLLSSHSLPPSSRDPQLPDLLSISNLRNNPLPGNNSSSVNTP--QSNSLHPPLPANSLSKDPSSNLS 185

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207143484 358 GGLNERGHNTPPRGAPATPELSPQTSPCQTHYSECEEA-INLSLTTPKSTPPPSASPAMipgYKSLPYPLKKQNGKIKYE 436
Cdd:COG5048   186 LLISSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSsSSLPLTTNSQLSPKSLLSQS---PSSLSSSDSSSSASESPR 262

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207143484 437 CNVCMKTFGQLSNLKVHLRVHSGER-PFQCNLCKKSFTQLAHLQKH--HLVHTGE--KPHEC--QVCHKRFSSTSNLKTH 509
Cdd:COG5048   263 SSLPTASSQSSSPNESDSSSEKGFSlPIKSKQCNISFSRSSPLTRHlrSVNHSGEslKPFSCpySLCGKLFSRNDALKRH 342

                         330
                  ....*....|....*
gi 1207143484 510 LRLHSGEKPYQCKLC 524
Cdd:COG5048   343 ILLHTSISPAKEKLL 357
PHA03247 PHA03247
large tegument protein UL36; Provisional
 190-418 1.27e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 42.23  E-value: 1.27e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207143484  190 KPPLPQYTYYPKHPSNP--QNHPcDTNKDDEEPEEKIDIERDTPPDTPDEQIMDFSKKIHKSEPMHEKTNIYPSLSPPQD 267
Cdd:PHA03247  2576 RPSEPAVTSRARRPDAPpqSARP-RAPVDDRGDPRGPAPPSPLPPDTHAPDPPPPSPSPAANEPDPHPPPTVPPPERPRD 2654

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207143484  268 VP------LHLHSLYGHREGLISSYP------SIRSPY-PLLPQYNPHYQHMLIPPYSPPFTSMLPTKPAHRYGfmnpdG 334
Cdd:PHA03247  2655 DPapgrvsRPRRARRLGRAAQASSPPqrprrrAARPTVgSLTSLADPPPPPPTPEPAPHALVSATPLPPGPAAA-----R 2729

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207143484  335 LSYPSIPqsgLLPVSLPYPNT--LHGGLNERGHNTPPRGAPA-TPELSPQTSPCQTHYSECEEAINLSLTTPKSTPPPSA 411
Cdd:PHA03247  2730 QASPALP---AAPAPPAVPAGpaTPGGPARPARPPTTAGPPApAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPAD 2806


                   ....*..
gi 1207143484  412 SPAMIPG 418
Cdd:PHA03247  2807 PPAAVLA 2813
PRK14475 PRK14475
F0F1 ATP synthase subunit B; Provisional
 581-637 2.79e-03

F0F1 ATP synthase subunit B; Provisional


Pssm-ID: 184697 [Multi-domain]  Cd Length: 167  Bit Score: 39.15  E-value: 2.79e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207143484 581 ETLRRAAELLERFDASAEAEALPE---SAAEPQVDAAlEEWLARSLQSGEEDGLLRACTG 637
Cdd:PRK14475  102 EQIKRRAEMAERKIAQAEAQAAADvkaAAVDLAAQAA-ETVLAARLAGAKSDPLVDAAIG 160
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 189-423 5.94e-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: 39.75  E-value: 5.94e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207143484 189 QKPPLPQYTYYPKHPSNPQNHPCDTNKDDEEPEEKIDI--------ERDTPPDTPDEQIMDFSKKIHKSEPMHEKTNIYP 260
Cdd:pfam03154 308 QVPPGPSPAAPGQSQQRIHTPPSQSQLQSQQPPREQPLppaplsmpHIKPPPTTPIPQLPNPQSHKHPPHLSGPSPFQMN 387

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207143484 261 SLSPPQDVPLHLHSLYGHreglissYPSIRSPYPLlpQYNPHYQHMLIPPYSPPFTSMLPTKPAHRYGFMNPDGL----S 336
Cdd:pfam03154 388 SNLPPPPALKPLSSLSTH-------HPPSAHPPPL--QLMPQSQQLPPPPAQPPVLTQSQSLPPPAASHPPTSGLhqvpS 458

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207143484 337 YPSIPQ--------SGLLPVSLPYPNTLHGGlneRGHNTPPRGAPATPELSPQTSPCQTHYSECEEAINLSLTTPKSTPP 408
Cdd:pfam03154 459 QSPFPQhpfvpggpPPITPPSGPPTSTSSAM---PGIQPPSSASVSSSGPVPAAVSCPLPPVQIKEEALDEAEEPESPPP 535

                         250
                  ....*....|....*
gi 1207143484 409 PSASPAMIPGYKSLP 423
Cdd:pfam03154 536 PPRSPSPEPTVVNTP 550
 
Name Accession Description Interval E-value
PR-SET_PRDM1 cd19187
PR-SET domain found in PR domain zinc finger protein 1 (PRDM1) and similar proteins; PRDM1 ...
 42-168 1.08e-71

PR-SET domain found in PR domain zinc finger protein 1 (PRDM1) and similar proteins; PRDM1 (also termed BLIMP-1, beta-interferon gene positive regulatory domain I-binding factor, PR domain-containing protein 1, positive regulatory domain I-binding factor 1, PRDI-BF1, or PRDI-binding factor 1) acts as a transcription factor that mediates a transcriptional program in various innate and adaptive immune tissue-resident lymphocyte T cell types such as tissue-resident memory T (Trm), natural killer (trNK) and natural killer T (NKT) cells and negatively regulates gene expression of proteins that promote the egress of tissue-resident T-cell populations from non-lymphoid organs.


Pssm-ID: 380964 [Multi-domain]  Cd Length: 128  Bit Score: 227.59  E-value: 1.08e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207143484  42 TSIPRNLSFQYNRDQ-QVTGVFSKEYIPQGTRFGPLQGVVYTKENVPLHTNRKYFWRIYSGGQLQHFIDGYDVRLSNWMR 120
Cdd:cd19187     1 ASLPRNLTLKYSSVGrEVLGVWSSDYIPRGTRFGPLVGEIYTNDPVPKGANRKYFWRIYSNGEFYHYIDGFDPSKSNWMR 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1207143484 121 YVNPARSLAEQNLVACQNGPDIFFYTLRPLEPKQELLVWYSPEFSQRL 168
Cdd:cd19187    81 YVNPAHSLQEQNLVACQIGMNIYFYTVKPIPPNQELLVWYCREFARRL 128
PR-SET_PRDM7_9 cd19193
PR-SET domain found in PR domain zinc finger protein 7 (PRDM7) and 9 (PRDM9) and similar ...
 60-168 1.36e-33

PR-SET domain found in PR domain zinc finger protein 7 (PRDM7) and 9 (PRDM9) and similar proteins; PRDM7 (also termed PR domain-containing protein 7) is a primate-specific histone methyltransferase that is the result of a recent gene duplication of PRDM9. It selectively catalyzes the trimethylation of H3 lysine 4 (H3K4me3). PRDM9 (also termed PR domain-containing protein 9) is a histone methyltransferase that specifically trimethylates 'Lys-4' of histone H3 (H3K4me3) during meiotic prophase and is essential for proper meiotic progression. It also efficiently mono-, di-, and trimethylates H3K36. Aberrant PRDM9 expression is assciated with with genome instability in cancer.


Pssm-ID: 380970 [Multi-domain]  Cd Length: 129  Bit Score: 125.04  E-value: 1.36e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207143484  60 GVFSKEYIPQGTRFGPLQGVVyTKENVPLHTNrkYFWRIYSGGQLQHFIDGYDVRLSNWMRYVNPARSLAEQNLVACQNG 139
Cdd:cd19193    21 GVWAEAPIPKGMVFGPYEGEI-VEDEEAADSG--YSWQIYKGGKLSHYIDAKDESKSNWMRYVNCARNEEEQNLVAFQYR 97

                          90       100
                  ....*....|....*....|....*....
gi 1207143484 140 PDIFFYTLRPLEPKQELLVWYSPEFSQRL 168
Cdd:cd19193    98 GKIYYRTCKDIAPGTELLVWYGDEYAKEL 126
PR-SET_PRDM4 cd19189
PR-SET domain found in PR domain zinc finger protein 4 (PRDM4) and similar proteins; PRDM4 ...
 39-168 1.69e-29

PR-SET domain found in PR domain zinc finger protein 4 (PRDM4) and similar proteins; PRDM4 (also termed PR domain-containing protein 4, or PFM1) may function as a transcription factor involved in cell differentiation.


Pssm-ID: 380966  Cd Length: 133  Bit Score: 113.33  E-value: 1.69e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207143484  39 RAMTSIPRNLSFQYNRDQQVTGVFSKEYIPQGTRFGPLQGVVYTKENVPLHTNRK--YFWRIYSGGQLQHFIDGYDVRLS 116
Cdd:cd19189     1 RARLSLPRQLYLRQSETGAEVGVWTKETIPVRTCFGPLIGQQSHSAEVADWTDKAapHIWKIYHNDVLEFCIITTDENEC 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1207143484 117 NWMRYVNPARSLAEQNLVACQNGPDIFFYTLRPLEPKQELLVWYSPEFSQRL 168
Cdd:cd19189    81 NWMMFVRKARTREEQNLVAYPHDGKIYFCTSRDIPPDQELLFYYSRDYARQL 132
PR-SET_PRDM14 cd19198
PR-SET domain found in PR domain zinc finger protein 14 (PRDM14) and similar proteins; PRDM14 ...
 60-160 2.09e-29

PR-SET domain found in PR domain zinc finger protein 14 (PRDM14) and similar proteins; PRDM14 (also termed PR domain-containing protein 14) acts as a transcription factor that has both positive and negative roles on transcription. It acts on regulating epigenetic modifications in the cells, playing a key role in the regulation of cell pluripotency, epigenetic reprogramming, differentiation and development. Aberrant PRDM14 expression is associated with tumorigenesis, cell migration and cell chemotherapeutic drugs resistance.


Pssm-ID: 380975  Cd Length: 133  Bit Score: 113.26  E-value: 2.09e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207143484  60 GVFSKEYIPQGTRFGPLQG-VVYTKEnVPLHTNRKYFWRIYSGGQLQHFIDGYDVRlSNWMRYVNPARSLAEQNLVACQN 138
Cdd:cd19198    21 GVFCKKTIPKGTRFGPFRGrVVNTSE-IKTYDDNSFMWEIFEDGKLSHFIDGRGST-GNWMSYVNCARYAEEQNLIAIQC 98

                          90       100
                  ....*....|....*....|..
gi 1207143484 139 GPDIFFYTLRPLEPKQELLVWY 160
Cdd:cd19198    99 QGQIFYESCKEILQGQELLVWY 120
PR-SET_PRDM-like cd10534
PR-SET domain found in PRDM (PRDI-BF1 and RIZ homology domain) family of proteins; PRDM family ...
 44-161 3.90e-29

PR-SET domain found in PRDM (PRDI-BF1 and RIZ homology domain) family of proteins; PRDM family of proteins is defined based on the conserved N-terminal PR domain, which is closely related to the Su(var)3-9, enhancer of zeste, and trithorax (SET) domains of histone methyltransferases, and is specifically called PR-SET domain. The family consists of 17 members in primates. PRDMs play diverse roles in cell-cycle regulation, differentiation, and meiotic recombination. The family also contains zinc finger protein ZFPM1 and ZFPM2. ZFPM1 (also termed friend of GATA protein 1, FOG-1, friend of GATA 1, zinc finger protein 89A, or zinc finger protein multitype 1) functions as a transcription regulator that plays an essential role in erythroid and megakaryocytic cell differentiation. ZFPM2 (also termed friend of GATA protein 2, FOG-2, friend of GATA 2, zinc finger protein 89B, or zinc finger protein multitype 2) functions as a transcription regulator that plays a central role in heart morphogenesis and development of coronary vessels from epicardium, by regulating genes that are essential during cardiogenesis.


Pssm-ID: 380932  Cd Length: 83  Bit Score: 110.75  E-value: 3.90e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207143484  44 IPRNLSF-QYNRDQQVTGVFSKEYIPQGTRFGPLQGVVytkenvplhtnrkyfwriysggqlqhfidgydvrlsNWMRYV 122
Cdd:cd10534     1 LPAGLELvLSSIPEGGLGVFARRTIPAGTRFGPLEGVV------------------------------------NWMRFV 44

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1207143484 123 NPARSLAEQNLVACQNGPDIFFYTLRPLEPKQELLVWYS 161
Cdd:cd10534    45 RPARNEEEQNLVAYQHGGQIYFRTTRDIPPGEELLVWYS 83
PR-SET_PRDM10 cd19194
PR-SET domain found in PR domain zinc finger protein 10 (PRDM10) and similar proteins; PRDM10 ...
 39-168 1.96e-27

PR-SET domain found in PR domain zinc finger protein 10 (PRDM10) and similar proteins; PRDM10 (also termed PR domain-containing protein 10, or tristanin) may be involved in transcriptional regulation.


Pssm-ID: 380971  Cd Length: 128  Bit Score: 107.44  E-value: 1.96e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207143484  39 RAMTSIPRNLSFQYNRDQQVtGVFSKEYIPQGTRFGPLQGVVYTKEnvPLHTNRKYFWRIYSGGQLQHFIDGYDVRLSNW 118
Cdd:cd19194     1 RARASLPLILQIFRFGETLG-GVFAKRRIPKRTQFGPLEGPLVKKS--ELKDNKIHPLELEEDDGEDLYFDLSDENKCNW 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1207143484 119 MRYVNPARSLAEQNLVACQNGPDIFFYTLRPLEPKQELLVWYSPEFSQRL 168
Cdd:cd19194    78 MMFVRPAQNHLEQNLVAYQYGQEIYFTTIKNIEPKQELKVWYAASYAEFL 127
PR-SET_PRDM12 cd19196
PR-SET domain found in PR domain zinc finger protein 12 (PRDM12) and similar proteins; PRDM12 ...
 59-168 2.74e-27

PR-SET domain found in PR domain zinc finger protein 12 (PRDM12) and similar proteins; PRDM12 (also termed PR domain-containing protein 12) acts as a transcription factor that is involved in the positive regulation of histone H3-K9 dimethylation.


Pssm-ID: 380973 [Multi-domain]  Cd Length: 130  Bit Score: 107.06  E-value: 2.74e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207143484  59 TGVFSKEYIPQGTRFGPLQGVVYTKENVPLHTNRKYFWRIY-SGGQLQHFIDGYDVRLSNWMRYVNPARSLAEQNLVACQ 137
Cdd:cd19196    17 LGVFSKTWIKEGTEMGPYTGRIVSPEDVDPCKNNNLMWEVFnEDGTVSHFIDASQENHRSWMTFVNCARNEQEQNLEVVQ 96

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1207143484 138 NGPDIFFYTLRPLEPKQELLVWYSPEFSQRL 168
Cdd:cd19196    97 IGESIYYRAIKDIPPDQELLVWYGNSYNTFL 127
PR-SET_PRDM6 cd19191
PR-SET domain found in PR domain zinc finger protein 6 (PRDM6) and similar proteins; PRDM6 ...
 60-166 3.62e-27

PR-SET domain found in PR domain zinc finger protein 6 (PRDM6) and similar proteins; PRDM6 (also termed PR domain-containing protein 6) is a putative histone-lysine N-methyltransferase that acts as a transcriptional repressor of smooth muscle gene expression. It may specifically methylate 'Lys-20' of histone H4 when associated with other proteins and in vitro.


Pssm-ID: 380968  Cd Length: 128  Bit Score: 106.79  E-value: 3.62e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207143484  60 GVFSKEYIPQGTRFGPLQGVVYTKENV-PLHTNRKYFWRIYSG-GQLQHFIDGYDVRLSNWMRYVNPARSLAEQNLVACQ 137
Cdd:cd19191    18 GICAAQRIPQGTWIGPFEGVLVSPEKQiGAVRNTQHLWEIYDQeGTLQHFIDGGDPSKSSWMRYIRCARHCGEQNLTVVQ 97

                          90       100
                  ....*....|....*....|....*....
gi 1207143484 138 NGPDIFFYTLRPLEPKQELLVWYSPEFSQ 166
Cdd:cd19191    98 YRGCIFYRACRDIPRGTELLVWYDDSYTS 126
PR-SET_PRDM2 cd19188
PR-SET domain found in PR domain zinc finger protein 2 (PRDM2) and similar proteins; PRDM2 ...
 44-163 5.62e-25

PR-SET domain found in PR domain zinc finger protein 2 (PRDM2) and similar proteins; PRDM2 (also termed GATA-3-binding protein G3B, lysine N-methyltransferase 8, MTB-or MTE-binding protein, PR domain-containing protein 2, retinoblastoma protein-interacting zinc finger protein, or zinc finger protein RIZ) is S-adenosyl-L-methionine-dependent histone methyltransferase that specifically methylates 'Lys-9' of histone H3. It may function as a DNA-binding transcription factor.


Pssm-ID: 380965  Cd Length: 123  Bit Score: 100.21  E-value: 5.62e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207143484  44 IPRNLSF-QYNRDQQVTGVFSKEYIPQGTRFGPLQGvvyTKENVPLHTNRKYFWRIYSGGQLQHFIDGYDVRLSNWMRYV 122
Cdd:cd19188     4 LPEELELkPSAVDKTRIGVWAKKSIPKGRKFGPFVG---EKKKRSQVKNNVYMWEIYGPKRGWMCVDASDPTKGNWLRYV 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1207143484 123 NPARSLAEQNLVACQNGPDIFFYTLRPLEPKQELLVWYSPE 163
Cdd:cd19188    81 NWARSGEEQNLFPLQINRAIYYKTLKPIAPGEELLCWYNGE 121
PR-SET_PRDM15 cd19199
PR-SET domain found in PR domain zinc finger protein 15 (PRDM15) and similar proteins; PRDM15 ...
 38-168 1.92e-22

PR-SET domain found in PR domain zinc finger protein 15 (PRDM15) and similar proteins; PRDM15 (also termed PR domain-containing protein 15, or zinc finger protein 298 (ZNF298)) may be involved in transcriptional regulation. It plays an essential role as a chromatin factor that modulates the transcription of upstream regulators of WNT and MAPK-ERK signaling to safeguard naive pluripotency.


Pssm-ID: 380976  Cd Length: 126  Bit Score: 93.25  E-value: 1.92e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207143484  38 PRAMTSIPRNLSFQYNRDQQvTGVFSKEYIPQGTRFGPL--QGVVYTKENVPlhtnrKYFWRIYSGGQLQHFiDGYDVRL 115
Cdd:cd19199     1 SRARSSLPDNLEIRQLEDGS-EGVFALVPLVKRTQFGPFeaKRVARLDGFAV-----FPLKVFEKDGSVVYL-DTSNEDD 73

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1207143484 116 SNWMRYVNPARSLAEQNLVACQNGPDIFFYTLRPLEPKQELLVWYSPEFSQRL 168
Cdd:cd19199    74 CNWMMFVRPATDVEHQNLTAYQQGEDIYFTTSRDIQPGAELRVWYAAFYAKKM 126
PR-SET_PRDM11 cd19195
PR-SET domain found in PR domain zinc finger protein 11 (PRDM11) and similar proteins; PRDM11 ...
 65-168 4.09e-18

PR-SET domain found in PR domain zinc finger protein 11 (PRDM11) and similar proteins; PRDM11 (also termed PR domain-containing protein 11) may be involved in transcription regulation.


Pssm-ID: 380972  Cd Length: 127  Bit Score: 80.67  E-value: 4.09e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207143484  65 EYIPQGTRFGPLQGVVYTKENvplhTNRKYFWRIYSGGQLQHFIDGYDVRLSNWMRYVNPARSLAEQNLVACQNGPDIFF 144
Cdd:cd19195    26 EVIPKGHIFGPYEGQICTQDK----SSGFFSWLIVDKNNRYKSIDGSDETKANWMRYVVISREEREQNLLAFQHSEQIYF 101

                          90       100
                  ....*....|....*....|....
gi 1207143484 145 YTLRPLEPKQELLVWYSPEFSQRL 168
Cdd:cd19195   102 RACRDIRPGEKLRVWYSEDYMKRL 125
SET smart00317
SET (Su(var)3-9, Enhancer-of-zeste, Trithorax) domain; Putative methyl transferase, based on ...
 52-165 1.21e-16

SET (Su(var)3-9, Enhancer-of-zeste, Trithorax) domain; Putative methyl transferase, based on outlier plant homologues


Pssm-ID: 214614 [Multi-domain]  Cd Length: 124  Bit Score: 76.60  E-value: 1.21e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207143484   52 YNRDQQVTGVFSKEYIPQGTRFGPLQGVVYTKENVP--------LHTNRKYFWRIYSGgqlqHFIDGYdvRLSNWMRYVN 123
Cdd:smart00317   6 FKSPGKGWGVRATEDIPKGEFIGEYVGEIITSEEAEerpkaydtDGAKAFYLFDIDSD----LCIDAR--RKGNLARFIN 79

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 1207143484  124 PARSLAEQNLVACQNGPD-IFFYTLRPLEPKQELLVWYSPEFS 165
Cdd:smart00317  80 HSCEPNCELLFVEVNGDDrIVIFALRDIKPGEELTIDYGSDYA 122
PR-SET_PRDM16_PRDM3 cd19200
PR-SET domain found in PR domain zinc finger protein 16 (PRDM16), MDS1 and EVI1 complex locus ...
 60-164 1.24e-16

PR-SET domain found in PR domain zinc finger protein 16 (PRDM16), MDS1 and EVI1 complex locus protein and similar proteins; PRDM16 (also termed PR domain-containing protein 16, transcription factor MEL1, or MDS1/EVI1-like gene 1) functions as a transcriptional regulator. PRDM16 is preferentially expressed by hematopoietic and neuronal stem cells. It is closely related to paralog of PRDM3 (also termed MDS1 and EVI1 complex locus protein, ecotropic virus integration site 1 protein, EVI-1, myelodysplasia syndrome 1 protein, myelodysplasia syndrome-associated protein 1, or MECOM) which is a nuclear transcription factor essential for the proliferation/maintenance of hematopoietic stem cells (HSCs). PRDM3 and PRDM16 are both directly linked to various aspects of oncogenic transformation.


Pssm-ID: 380977  Cd Length: 135  Bit Score: 77.02  E-value: 1.24e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207143484  60 GVFSKEYIPQGTRFGPLQGVVYTKENVPLhtnrkYFWRIY-SGGQLQHFIDGYDVRLSNWMRYVNPARSLAEQNLVACQN 138
Cdd:cd19200    27 GVWTKVRIEVGEKFGPFVGVQRSSVKDPT-----YAWEIVdEFGKVKFWIDASEPGTGNWMKYIRSAPSCEQQNLMACQI 101

                          90       100
                  ....*....|....*....|....*.
gi 1207143484 139 GPDIFFYTLRPLEPKQELLVWYSPEF 164
Cdd:cd19200   102 DEQIYYKVVRDIQPGEELLLYMKAAV 127
PR-SET_ZFPM cd19201
PR-SET domain found in zinc finger protein ZFPM1, ZFPM2 and similar proteins; ZFPM1 (also ...
 43-165 6.46e-16

PR-SET domain found in zinc finger protein ZFPM1, ZFPM2 and similar proteins; ZFPM1 (also termed friend of GATA protein 1, FOG-1, friend of GATA 1, zinc finger protein 89A, or zinc finger protein multitype 1) functions as a transcription regulator that plays an essential role in erythroid and megakaryocytic cell differentiation. ZFPM2 (also termed friend of GATA protein 2, FOG-2, friend of GATA 2, zinc finger protein 89B, or zinc finger protein multitype 2) functions as a transcription regulator that plays a central role in heart morphogenesis and development of coronary vessels from epicardium, by regulating genes that are essential during cardiogenesis.


Pssm-ID: 380978  Cd Length: 122  Bit Score: 74.30  E-value: 6.46e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207143484  43 SIPRNLSFQyNRDQQVT---GVFSKEYIPQGTRFGPLQGVVYTKenvplHTNRKYFWRIYS-GGQLQHFIDGYDVRLSNW 118
Cdd:cd19201     2 SLPGELELR-KPSQDAGrsgGVWAKQPLPEGTRFGPYPGKLVKE-----PLDPSYEWKVEAqGSKGGEGLLLLTEDSGTW 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1207143484 119 MRYVNPARSLAEQNLVACQNGPDIFFYTLRPLEPKQELLVWYSPEFS 165
Cdd:cd19201    76 LKLVRSADDEDEANLILYFKGGQIWCEVTKDIPPGEELILVLREPLL 122
PR-SET_PRDM5 cd19190
PR-SET domain found in PR domain zinc finger protein 5 (PRDM5) and similar proteins; PRDM5 ...
 44-160 1.31e-14

PR-SET domain found in PR domain zinc finger protein 5 (PRDM5) and similar proteins; PRDM5 (also termed PR domain-containing protein 5) is a sequence-specific DNA-binding transcription factor that represses transcription at least in part by recruitment of the histone methyltransferase EHMT2/G9A and histone deacetylases such as HDAC1.


Pssm-ID: 380967  Cd Length: 127  Bit Score: 70.78  E-value: 1.31e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207143484  44 IPRNLSFQYNRDQQVTGVFSKEYIPQGTRFGPLQGVVYTKENVPLHTNRKYFWRIY-SGGQLQHFIDGYDVRLSNWMRYV 122
Cdd:cd19190     5 VPDRFSLKSSKVQDGMGLYTARRVKKGEKFGPFAGEKRMPNELDESMDPRLMWEVRgSKGEVLYILDASNPRHSNWLRFV 84

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1207143484 123 NPARSLAEQNLVACQNGPDIFFYTLRPLEPKQELLVWY 160
Cdd:cd19190    85 HEAPSQEQKNLAAIQEGENIFYLAVDDIETDTELLIGY 122
PR-SET_PRDM13 cd19197
PR-SET domain found in PR domain zinc finger protein 13 (PRDM13) and similar proteins; PRDM13 ...
 67-166 3.52e-14

PR-SET domain found in PR domain zinc finger protein 13 (PRDM13) and similar proteins; PRDM13 (also termed PR domain-containing protein 13) may be involved in transcriptional regulation. It mediates the balance of inhibitory and excitatory neurons in somatosensory circuits.


Pssm-ID: 380974  Cd Length: 103  Bit Score: 68.69  E-value: 3.52e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207143484  67 IPQGTRFGPLQGVVYTKENVPLHT---NRKYFWRiysgGQLQHFIDGYDVRLSNWMRYVNPARSLAEQNLVACQNGPD-- 141
Cdd:cd19197     1 IPAGLRLGPVPGIFKLGKYLSDRKepgNKKKVRR----VRGDYLVDESGSPATEWIGLVRAARNNQEQNLEAIADLPGgq 76

                          90       100
                  ....*....|....*....|....*
gi 1207143484 142 IFFYTLRPLEPKQELLVWYSPEFSQ 166
Cdd:cd19197    77 IFYRALRDIQPGEELTVWYSNSLAQ 101
PR-SET_PRDM8 cd19192
PR-SET domain found in PR domain zinc finger protein 8 (PRDM8) and similar proteins; PRDM8 ...
 59-168 2.54e-11

PR-SET domain found in PR domain zinc finger protein 8 (PRDM8) and similar proteins; PRDM8 (also termed PR domain-containing protein 8) may function as histone methyltransferase, preferentially acting on 'Lys-9' of histone H3.


Pssm-ID: 380969  Cd Length: 131  Bit Score: 61.68  E-value: 2.54e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207143484  59 TGVFSKEYIPQGTRFGPLQG---VVYTKENVPLHT----NRKYFWRIYSGgqlqhfIDGYDVRLSNWMRYVNPARSLAEQ 131
Cdd:cd19192    20 TSVVTTTDIPAGTIFGPCVLsftLGYDIADIALKTtdkrVVPYIFRVDTG------ACNGSSEPSDWLRLVQPARDRHEQ 93

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1207143484 132 NLVA-CQNGPDIFFYTLRPLEPKQELLVWYSPEFSQRL 168
Cdd:cd19192    94 NLEAfRKNEGQVYFRTLRRIRKGEELLVWYSDELAELL 131
SET pfam00856
SET domain; SET domains are protein lysine methyltransferase enzymes. SET domains appear to be ...
 60-160 2.58e-10

SET domain; SET domains are protein lysine methyltransferase enzymes. SET domains appear to be protein-protein interaction domains. It has been demonstrated that SET domains mediate interactions with a family of proteins that display similarity with dual-specificity phosphatases (dsPTPases). A subset of SET domains have been called PR domains. These domains are divergent in sequence from other SET domains, but also appear to mediate protein-protein interaction. The SET domain consists of two regions known as SET-N and SET-C. SET-C forms an unusual and conserved knot-like structure of probably functional importance. Additionally to SET-N and SET-C, an insert region (SET-I) and flanking regions of high structural variability form part of the overall structure.


Pssm-ID: 459965 [Multi-domain]  Cd Length: 115  Bit Score: 58.30  E-value: 2.58e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207143484  60 GVFSKEYIPQGTRFGPLQGV-VYTKENVPLHTNRKY------FWRIYS---GGQLQHFIDGYDVRLSNWMRYVNPARSL- 128
Cdd:pfam00856   3 GLFATEDIPKGEFIGEYVEVlLITKEEADKRELLYYdklelrLWGPYLftlDEDSEYCIDARALYYGNWARFINHSCDPn 82

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1207143484 129 AEQNLVACQNGPDIFFYTLRPLEPKQELLVWY 160
Cdd:pfam00856  83 CEVRVVYVNGGPRIVIFALRDIKPGEELTIDY 114
PR-SET_PRDM3 cd19214
PR-SET domain found in MDS1 and EVI1 complex locus protein and similar proteins; PRDM3 (also ...
 60-166 5.51e-09

PR-SET domain found in MDS1 and EVI1 complex locus protein and similar proteins; PRDM3 (also termed MDS1 and EVI1 complex locus protein, ecotropic virus integration site 1 protein, EVI-1, myelodysplasia syndrome 1 protein, myelodysplasia syndrome-associated protein 1, or MECOM) is a nuclear transcription factor, which is essential for the proliferation/maintenance of hematopoietic stem cells (HSCs). It is closely related to paralog PRDM16, both o fwhich are directly linked to various aspects of oncogenic transformation.


Pssm-ID: 380991  Cd Length: 158  Bit Score: 55.71  E-value: 5.51e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207143484  60 GVFSKEYIPQGTRFGPLQGvvytkENVPLHTNRKYFWRIYSG-GQLQHFIDGYDVRLSNWMRYVNPARSLAEQNLVACQN 138
Cdd:cd19214    47 GIWTKRKIEVGEKFGPYVG-----EQRSNLKDPSYGWEVLDEfGNVKFCIDASQPDVGSWLKYIRFAGCYDQHNLVACQI 121

                          90       100
                  ....*....|....*....|....*....
gi 1207143484 139 GPDIFFYTLRPLEPKQELLVWY-SPEFSQ 166
Cdd:cd19214   122 NDQIFYRAVADIDPGEELLLFMkSEDYSH 150
PR-SET_PRDM16 cd19213
PR-SET domain found in PR domain zinc finger protein 16 (PRDM16) and similar proteins; PRDM16, ...
 60-159 1.62e-08

PR-SET domain found in PR domain zinc finger protein 16 (PRDM16) and similar proteins; PRDM16, also termed PR domain-containing protein 16, or transcription factor MEL1, or MDS1/EVI1-like gene 1, functions as a transcriptional regulator. PRDM16 is preferentially expressed by hematopoietic and neuronal stem cells and is closely related to paralog of PRDM3, both of which are directly linked to various aspects of oncogenic transformation.


Pssm-ID: 380990  Cd Length: 162  Bit Score: 54.11  E-value: 1.62e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207143484  60 GVFSKEYIPQGTRFGPLQGVVYTK------------ENVPLHTNRKYFWRIYSG-GQLQHFIDGYDVRLSNWMRYVNPAR 126
Cdd:cd19213    37 GVWAKRKIEAGERFGPYTGVQRSTlkdtnfgweqilNDVEVSSQEGCITKIVDDlGNEKFCVDAGQAGAGSWLKYIRVAC 116

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1207143484 127 SLAEQNLVACQNGPDIFFYTLRPLEPKQELLVW 159
Cdd:cd19213   117 SCDEQNLTACQINEQIYYKVIKDIEPGEELLVY 149
PR-SET_PRDM17 cd10520
PR-SET domain found in PR domain zinc finger protein 17 (PRDM17) and similar proteins; PRDM17 ...
 67-163 9.98e-06

PR-SET domain found in PR domain zinc finger protein 17 (PRDM17) and similar proteins; PRDM17 (also termed zinc finger protein 408 (ZNF408)) may be involved in transcriptional regulation.


Pssm-ID: 380918  Cd Length: 121  Bit Score: 45.10  E-value: 9.98e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207143484  67 IPQGTRFGPLQGvvytKENVPLHTNRKYFwRIYSGGQLQHFIDGYDVrlSNWMRYVNPARSLAEQNLVACQNGPDIFFYT 146
Cdd:cd10520    30 LQKGTFLGPLEE----ELESHDLTEGGSP-RQEESGQSGDVLACEQS--SKWMRFACRARSEEESNVAVVRLSGRLHLRV 102

                          90
                  ....*....|....*..
gi 1207143484 147 LRPLEPKQELLVWYSPE 163
Cdd:cd10520   103 CKDIEPGSELLLWPEEN 119
SET_LegAS4-like cd10522
SET domain found in Legionella pneumophila type IV secretion system effector LegAS4 and ...
 60-164 1.44e-05

SET domain found in Legionella pneumophila type IV secretion system effector LegAS4 and similar proteins; LegAS4 is a type IV secretion system effector of Legionella pneumophila. It contains a SET domain that is involved in the modification of Lys4 of histone H3 (H3K4) in the nucleolus of the host cell, thereby enhancing heterochromatic rDNA transcription. It also contains an ankyrin repeat domain of unknown function at its C-terminal region.


Pssm-ID: 380920 [Multi-domain]  Cd Length: 122  Bit Score: 44.64  E-value: 1.44e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207143484  60 GVFSKEYIPQGTRFGPLQGVVYTkenvPLHTNRKYFWRIYSGGQLQHFIDGYDV---RLSNWMRYVNparSLAEQNL--- 133
Cdd:cd10522    16 GLFAAETIAKGEFVGEYTGEVLD----RWEEDRDSVYHYDPLYPFDLNGDILVIdagKKGNLTRFIN---HSDQPNLeli 88

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1207143484 134 VACQNG-PDIFFYTLRPLEPKQELLVWYSPEF 164
Cdd:cd10522    89 VRTLKGeQHIGFVAIRDIKPGEELFISYGPKY 120
zf-H2C2_2 pfam13465
Zinc-finger double domain;
449-474 4.80e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 40.43  E-value: 4.80e-05
                          10        20
                  ....*....|....*....|....*.
gi 1207143484 449 NLKVHLRVHSGERPFQCNLCKKSFTQ 474
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
477-502 5.35e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 40.43  E-value: 5.35e-05
                          10        20
                  ....*....|....*....|....*.
gi 1207143484 477 HLQKHHLVHTGEKPHECQVCHKRFSS 502
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
505-530 5.40e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 40.43  E-value: 5.40e-05
                          10        20
                  ....*....|....*....|....*.
gi 1207143484 505 NLKTHLRLHSGEKPYQCKLCGVKFTQ 530
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
203-524 7.59e-05

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 45.84  E-value: 7.59e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207143484 203 PSNPQNHPCDTNKDDEEPEE----KIDIERDTPPDTPDEQIMDFSKK-IHKSEPMHEKTNIYPSLSPPQDVPLHLHSLYG 277
Cdd:COG5048    28 SNAPRPDSCPNCTDSFSRLEhltrHIRSHTGEKPSQCSYSGCDKSFSrPLELSRHLRTHHNNPSDLNSKSLPLSNSKASS 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207143484 278 HREGLISSYPSIRSPYPLLPQYNPHYQHMLIPPYSPPFTSMLPTKPAHRYGFMNPdgLSYPSIPQSGLLPVSLPYPNTLH 357
Cdd:COG5048   108 SSLSSSSSNSNDNNLLSSHSLPPSSRDPQLPDLLSISNLRNNPLPGNNSSSVNTP--QSNSLHPPLPANSLSKDPSSNLS 185

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207143484 358 GGLNERGHNTPPRGAPATPELSPQTSPCQTHYSECEEA-INLSLTTPKSTPPPSASPAMipgYKSLPYPLKKQNGKIKYE 436
Cdd:COG5048   186 LLISSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSsSSLPLTTNSQLSPKSLLSQS---PSSLSSSDSSSSASESPR 262

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207143484 437 CNVCMKTFGQLSNLKVHLRVHSGER-PFQCNLCKKSFTQLAHLQKH--HLVHTGE--KPHEC--QVCHKRFSSTSNLKTH 509
Cdd:COG5048   263 SSLPTASSQSSSPNESDSSSEKGFSlPIKSKQCNISFSRSSPLTRHlrSVNHSGEslKPFSCpySLCGKLFSRNDALKRH 342

                         330
                  ....*....|....*
gi 1207143484 510 LRLHSGEKPYQCKLC 524
Cdd:COG5048   343 ILLHTSISPAKEKLL 357
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 463-485 9.26e-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: 36.89  E-value: 9.26e-04
                          10        20
                  ....*....|....*....|...
gi 1207143484 463 FQCNLCKKSFTQLAHLQKHHLVH 485
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 491-513 9.72e-04

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


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 36.89  E-value: 9.72e-04
                          10        20
                  ....*....|....*....|...
gi 1207143484 491 HECQVCHKRFSSTSNLKTHLRLH 513
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
PHA03247 PHA03247
large tegument protein UL36; Provisional
 190-418 1.27e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 42.23  E-value: 1.27e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207143484  190 KPPLPQYTYYPKHPSNP--QNHPcDTNKDDEEPEEKIDIERDTPPDTPDEQIMDFSKKIHKSEPMHEKTNIYPSLSPPQD 267
Cdd:PHA03247  2576 RPSEPAVTSRARRPDAPpqSARP-RAPVDDRGDPRGPAPPSPLPPDTHAPDPPPPSPSPAANEPDPHPPPTVPPPERPRD 2654

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207143484  268 VP------LHLHSLYGHREGLISSYP------SIRSPY-PLLPQYNPHYQHMLIPPYSPPFTSMLPTKPAHRYGfmnpdG 334
Cdd:PHA03247  2655 DPapgrvsRPRRARRLGRAAQASSPPqrprrrAARPTVgSLTSLADPPPPPPTPEPAPHALVSATPLPPGPAAA-----R 2729

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207143484  335 LSYPSIPqsgLLPVSLPYPNT--LHGGLNERGHNTPPRGAPA-TPELSPQTSPCQTHYSECEEAINLSLTTPKSTPPPSA 411
Cdd:PHA03247  2730 QASPALP---AAPAPPAVPAGpaTPGGPARPARPPTTAGPPApAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPAD 2806


                   ....*..
gi 1207143484  412 SPAMIPG 418
Cdd:PHA03247  2807 PPAAVLA 2813
PRK14475 PRK14475
F0F1 ATP synthase subunit B; Provisional
 581-637 2.79e-03

F0F1 ATP synthase subunit B; Provisional


Pssm-ID: 184697 [Multi-domain]  Cd Length: 167  Bit Score: 39.15  E-value: 2.79e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207143484 581 ETLRRAAELLERFDASAEAEALPE---SAAEPQVDAAlEEWLARSLQSGEEDGLLRACTG 637
Cdd:PRK14475  102 EQIKRRAEMAERKIAQAEAQAAADvkaAAVDLAAQAA-ETVLAARLAGAKSDPLVDAAIG 160
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 189-423 5.94e-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: 39.75  E-value: 5.94e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207143484 189 QKPPLPQYTYYPKHPSNPQNHPCDTNKDDEEPEEKIDI--------ERDTPPDTPDEQIMDFSKKIHKSEPMHEKTNIYP 260
Cdd:pfam03154 308 QVPPGPSPAAPGQSQQRIHTPPSQSQLQSQQPPREQPLppaplsmpHIKPPPTTPIPQLPNPQSHKHPPHLSGPSPFQMN 387

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207143484 261 SLSPPQDVPLHLHSLYGHreglissYPSIRSPYPLlpQYNPHYQHMLIPPYSPPFTSMLPTKPAHRYGFMNPDGL----S 336
Cdd:pfam03154 388 SNLPPPPALKPLSSLSTH-------HPPSAHPPPL--QLMPQSQQLPPPPAQPPVLTQSQSLPPPAASHPPTSGLhqvpS 458

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207143484 337 YPSIPQ--------SGLLPVSLPYPNTLHGGlneRGHNTPPRGAPATPELSPQTSPCQTHYSECEEAINLSLTTPKSTPP 408
Cdd:pfam03154 459 QSPFPQhpfvpggpPPITPPSGPPTSTSSAM---PGIQPPSSASVSSSGPVPAAVSCPLPPVQIKEEALDEAEEPESPPP 535

                         250
                  ....*....|....*
gi 1207143484 409 PSASPAMIPGYKSLP 423
Cdd:pfam03154 536 PPRSPSPEPTVVNTP 550
SSL1 COG5151
RNA polymerase II transcription initiation/nucleotide excision repair factor TFIIH, subunit ...
 435-553 6.40e-03

RNA polymerase II transcription initiation/nucleotide excision repair factor TFIIH, subunit SSL1 [Transcription / DNA replication, recombination, and repair];


Pssm-ID: 227480 [Multi-domain]  Cd Length: 421  Bit Score: 39.60  E-value: 6.40e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207143484 435 YECNVCmktfgqlsnlkvHLRVHSgeRPFQCNLCKKSFTQLAHLQK--HHL--------VHTGEKPH--ECQVCHKRFSS 502
Cdd:COG5151   309 YECPVC------------KTKVCS--LPISCPICSLQLILSTHLARsyHHLyplkpfveKPEGTNPKstHCFVCQGPFPK 374

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1207143484 503 TSNLKTHLRLHSGEkpYQCKLCGVKFTQYIHLKLHrrlhssrERLHSCAAC 553
Cdd:COG5151   375 PPVSPFDESTSSGR--YQCELCKSTFCSDCDVFIH-------ETLHFCIGC 416
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 189-415 8.43e-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: 39.37  E-value: 8.43e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207143484 189 QKPPLPQY----TYYPKHPSNPQNHPCDTNKDDEE----PEEKIDIERDTPPDTPDEQIMDFSKKIHKSEPMHEKTNIYP 260
Cdd:pfam03154 274 QMPPMPHSlqtgPSHMQHPVPPQPFPLTPQSSQSQvppgPSPAAPGQSQQRIHTPPSQSQLQSQQPPREQPLPPAPLSMP 353

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207143484 261 SLSPPQDVPL-HLHSLYGHREGlissyPSIRSPYPLLPQYNphyqhmlIPPysPPFTSMLPTKPAHRYGFMNPDGLSYps 339
Cdd:pfam03154 354 HIKPPPTTPIpQLPNPQSHKHP-----PHLSGPSPFQMNSN-------LPP--PPALKPLSSLSTHHPPSAHPPPLQL-- 417

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1207143484 340 IPQSGLLPVSLPYPNTLhgglnERGHNTPPRGAPATPELSPQTSPCQTHYSECEEAINLS-LTTPKSTPPPSASPAM 415
Cdd:pfam03154 418 MPQSQQLPPPPAQPPVL-----TQSQSLPPPAASHPPTSGLHQVPSQSPFPQHPFVPGGPpPITPPSGPPTSTSSAM 489
PHA03377 PHA03377
EBNA-3C; Provisional
 192-427 8.60e-03

EBNA-3C; Provisional


Pssm-ID: 177614 [Multi-domain]  Cd Length: 1000  Bit Score: 39.27  E-value: 8.60e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207143484  192 PLPQYTYYPKHPSNPQNHpcDTNKDDEEPEEKIDIERDTPPDTPDEQIMDFSKKihkSEPMHEKTNiYPSL--SPPQDVP 269
Cdd:PHA03377   700 PSEESHLSSMSPTQPISH--EEQPRYEDPDDPLDLSLHPDQAPPPSHQAPYSGH---EEPQAQQAP-YPGYwePRPPQAP 773

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207143484  270 LHLHSLYGHREGLISSYPSIRSPYPLLPQYnPHYQHMLI-----PPYSPPFTSMLPTKPahrygfmnpdglsYPSipqsg 344
Cdd:PHA03377   774 YLGYQEPQAQGVQVSSYPGYAGPWGLRAQH-PRYRHSWAywsqyPGHGHPQGPWAPRPP-------------HLP----- 834

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207143484  345 llPVSLPYPNTLHGGLNERGHNTPPRGaPATPELS--PQTSPCQTHYSeceeainlSLTTPKSTPPPSASPAMIPG-YKS 421
Cdd:PHA03377   835 --PQWDGSAGHGQDQVSQFPHLQSETG-PPRLQLSqvPQLPYSQTLVS--------SSAPSWSSPQPRAPIRPIPTrFPP 903


                   ....*.
gi 1207143484  422 LPYPLK 427
Cdd:PHA03377   904 PPMPLQ 909
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 200-417 9.50e-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: 39.37  E-value: 9.50e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207143484 200 PKHPSnPQNHPCDTNKDDEEP---EEKIDIERDTPPDTPDEQIMDFSKKIHKSEPMHEKTNIYPSLSPPQDVPLHLHSLY 276
Cdd:pfam03154 146 PSIPS-PQDNESDSDSSAQQQilqTQPPVLQAQSGAASPPSPPPPGTTQAATAGPTPSAPSVPPQGSPATSQPPNQTQST 224

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207143484 277 GHREGLISSYPSIRSPYplLPQYNPHYQHMLIPPySPPFTSMLPTKPAHRYGFMNPdglsypsipqsgllpvslpYPNTL 356
Cdd:pfam03154 225 AAPHTLIQQTPTLHPQR--LPSPHPPLQPMTQPP-PPSQVSPQPLPQPSLHGQMPP-------------------MPHSL 282

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1207143484 357 HGGLNERGHNTPPRGAPatpeLSPQTSPCQTHYSECEEAINLSLTTPKSTPPPSASPAMIP 417
Cdd:pfam03154 283 QTGPSHMQHPVPPQPFP----LTPQSSQSQVPPGPSPAAPGQSQQRIHTPPSQSQLQSQQP 339
 
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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