|
Name |
Accession |
Description |
Interval |
E-value |
| TET3 |
cd18897 |
oxygenase domain of ten-eleven translocation (TET)3 methylcytosine dioxygenase and similar ... |
828-1105 |
0e+00 |
|
oxygenase domain of ten-eleven translocation (TET)3 methylcytosine dioxygenase and similar proteins; TET3 is involved in DNA demethylation through iteratively oxidizing 5-methylcytosine (5mC) into 5-hydroxymethylcytosine (5hmC), 5-formylcytosine (5fC) and 5-carboxylcytosine (5caC). TET proteins contain a C-terminal catalytic domain which consists of a cysteine-rich region and a double-stranded beta-helix (DSBH) fold. TET3 serves as a tumor suppressor; it acts as a suppressor of ovarian cancer by demethylating the miR-30d precursor gene promoter to block TGF-beta1 induced epithelial-mesenchymal transition (EMT). TET3 (and TET2) promoters are silenced in melanoma cells by mechanisms triggered by TGF-beta and mediated by DNA methyltransferase 3 alpha (DNMT3A), which play a functional role in the EMT process and metastasis. In addition, TET3 (and TET2) may be guardians of regulatory T cell stability and immune homeostasis. TET3 has been shown to prevent terminal differentiation of adult neural stem cells by a mechanism involving direct binding and repression of TET3 to the imprinted gene Snrpn. TET3 has also been shown to mediate the activation of hepatic stellate cells via modulation of the long non-coding RNA HIF1A-AS1 expression. TET1 belongs to the TET/JBP family of dioxygenases that require Fe2+ and alpha-ketoglutarate (also known as 2-oxoglutarate) for activity.
Pssm-ID: 380676 Cd Length: 452 Bit Score: 585.80 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370476990 828 CDCVEQIVEKDEGPYYTHLGSGPTVASIRELMEERYGEKGKAIRIEKVIYTGKEGKSSRGCPIAKWVIRRHTLEEKLLCL 907
Cdd:cd18897 1 CDCVEQILEKDEGPYYTHLGSGPTVASIRELMEERYGEKGKAIRIEKVIYTGKEGKSSRGCPIAKWVIRRSSEEEKLLCL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370476990 908 VRHRAGHHCQNAVIVILILAWEGIPRSLGDTLYQELTDTLRKYGNPTSRRCGLNDDRTCACQGKDPNTCGASFSFGCSWS 987
Cdd:cd18897 81 VRHRAGHHCQNAVIVILILAWEGIPRALGDKLYQELTETLTKYGNPTSRRCGLNDDRTCACQGKDPNTCGASFSFGCSWS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370476990 988 MYFNGCKYARSKTPRKFRLAGDNPKEEEVLRKSFQDLATEVAPLYKRLAPQAYQNQlgplsqktsllqskgkVTNEEIAI 1067
Cdd:cd18897 161 MYFNGCKYARSKTPRKFRLIGDNPKEEENLRDNFQDLATEVAPLYKRLAPQAYQNQ----------------VTNEDIAI 224
|
250 260 270
....*....|....*....|....*....|....*...
gi 1370476990 1068 DCRLGLKEGRPFAGVTACMDFCAHAHKDQHNLYNGCTV 1105
Cdd:cd18897 225 DCRLGLKEGRPFSGVTACMDFCAHAHKDQHNLYNGCTV 262
|
|
| Tet_JBP |
pfam12851 |
Oxygenase domain of the 2OGFeDO superfamily; A double-stranded beta helix (DSBH) fold domain ... |
985-1105 |
6.05e-34 |
|
Oxygenase domain of the 2OGFeDO superfamily; A double-stranded beta helix (DSBH) fold domain of the 2-oxoglutarate (2OG)-Fe(II)-dependent dioxygenase (2OGFeDO) superfamily found in various eukaryotes, bacteria and bacteriophages. Members of this family catalyze nucleic acid modifications, such as thymidine hydroxylation during base J synthesis in kinetoplastids, and the conversion of 5 methyl-cytosine (5-mC) to 5-hydroxymethyl-cytosine (hmC), or further oxidation to 5-formylcytosine (5fC) and 5-carboxylcytosine (5caC). Metazoan TET proteins contain a cysteine-rich region inserted into the core of the DSBH fold. Vertebrate TET proteins are oncogenes that are mutated in various myeloid cancers. Fungal and algal versions of this family are linked to a predicted transposase and show lineage-specific expansions.
Pssm-ID: 372343 Cd Length: 166 Bit Score: 128.27 E-value: 6.05e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370476990 985 SWSMYFNGCKYARSKTPRKFRLAGDNPKEEEVLRKSFQDLATEVAPLYKRLAPQAYQNQlgplsqktsllqskgkVTNEE 1064
Cdd:pfam12851 1 SWSMYYDGCKFPGPRKPRKFSFTPRNPKEEIKLEDELQELAALLGAIYKQIAPDLYENQ----------------IEYEQ 64
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1370476990 1065 IAIDCRLGLKEGRPFAGVTACMDFCAHAHKDQHNLYNGCTV 1105
Cdd:pfam12851 65 DAAICRLGRKWGRPFSGVTVNLNFETISHRDLGNFRNGSTL 105
|
|
| zf-CXXC |
pfam02008 |
CXXC zinc finger domain; This domain contains eight conserved cysteine residues that bind to ... |
50-89 |
1.15e-12 |
|
CXXC zinc finger domain; This domain contains eight conserved cysteine residues that bind to two zinc ions. The CXXC domain is found in a variety of chromatin-associated proteins. This domain binds to nonmethyl-CpG dinucleotides. The domain is characterized by two repeats, and shows a peculiar internal duplication in which the second unit is inserted into the first one. Each of these units is characterized by four conserved cysteines, displaying a CXXCXXCX(n)C motif that chelate a Zn+2 ion. The DNA binding interface has been identified by NMR. In eukaryotes, the CXXC domain is found in stramenopiles, plants and metazoans. Plants possess a mono-CXXC domain that is present in distinct chromatin proteins. Structural comparisons show that the mono-CXXC is homologous to the structural-zinc binding domain of medium chain dehydrogenases.
Pssm-ID: 366873 Cd Length: 48 Bit Score: 63.14 E-value: 1.15e-12
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1370476990 50 GRKKRKRCGTCEPCRRLENCGACTSCTNR-------RTHQICKLRKC 89
Cdd:pfam02008 2 NRRKRRRCGVCEGCQRPEDCGQCSFCLDMpkfggpgKKKQKCRLRRC 48
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
383-752 |
1.19e-10 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 66.12 E-value: 1.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370476990 383 PLPEALSPPAPFRS--PQSYLRAPSWPVVPPEEHSSFAPDSSAFP--PATPRTEFP-EAWGTDTPPATPRSSWPMPRPSP 457
Cdd:PHA03247 2554 PLPPAAPPAAPDRSvpPPRPAPRPSEPAVTSRARRPDAPPQSARPraPVDDRGDPRgPAPPSPLPPDTHAPDPPPPSPSP 2633
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370476990 458 DPMAeleqlLGSASDYIQSVFKRPEALPTKPKVKVEAPSSSPAPAPSPVLQREAPTPSSEPDTHQKAQTALQQHLHHKRS 537
Cdd:PHA03247 2634 AANE-----PDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSPPQRPRRRAARPTVGSLTSLADPPPPPPTP 2708
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370476990 538 LFLEQVHDTSFPAPSEPSAPGWWPPPSS---------PVPRLPDRPPKEKKKKLPTPAGGPVGTEKAAPGIKPSVRKPIQ 608
Cdd:PHA03247 2709 EPAPHALVSATPLPPGPAAARQASPALPaapappavpAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAV 2788
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370476990 609 IKKSRPREAQPLfPPVRQIVLEGLRSPASQEVQAHPPAPLPASQGSAVPLPPEPSLALFAPSPSRDSLLPPTQEMRSPSP 688
Cdd:PHA03247 2789 ASLSESRESLPS-PWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSVAPGGDVRRRPP 2867
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1370476990 689 MtalQPGSTGPLPPADDKLEELIRQFEAEFGDSFGLPGPPSVPIQDPENQQTCLPAPESPFATR 752
Cdd:PHA03247 2868 S---RSPAAKPAAPARPPVRRLARPAVSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQ 2928
|
|
| Atrophin-1 |
pfam03154 |
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ... |
326-745 |
7.47e-04 |
|
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: 43.60 E-value: 7.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370476990 326 SEVPQI-SPQEGLPLSQSAlsiaKEKNISLQTAIAIEALTQLSSALPQPSHSTPQASCPLPEALSPPAPFRSPQSYLRAP 404
Cdd:pfam03154 143 STSPSIpSPQDNESDSDSS----AQQQILQTQPPVLQAQSGAASPPSPPPPGTTQAATAGPTPSAPSVPPQGSPATSQPP 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370476990 405 SWPVVPPEEHSSFAPDSSAFPPATPRTEFPEAWGTDTPPATPRSSWPMPRPS-PDPMAELEQLLGSASDYIqsvfkrPEA 483
Cdd:pfam03154 219 NQTQSTAAPHTLIQQTPTLHPQRLPSPHPPLQPMTQPPPPSQVSPQPLPQPSlHGQMPPMPHSLQTGPSHM------QHP 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370476990 484 LPTKPkvkveapssspAPAPSPVLQREAPTPSSEPDTHQKAQTalqQHLHHKRSLFLEQVHDTSFPAPSEPSAPGWWPPP 563
Cdd:pfam03154 293 VPPQP-----------FPLTPQSSQSQVPPGPSPAAPGQSQQR---IHTPPSQSQLQSQQPPREQPLPPAPLSMPHIKPP 358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370476990 564 SSPVPRLPDRPPKEKKKKLPTpagGPVGTEKAAPGIKPSVRKPI-QIKKSRPREAQP----LFPPVRQIVLEGLRSPASQ 638
Cdd:pfam03154 359 PTTPIPQLPNPQSHKHPPHLS---GPSPFQMNSNLPPPPALKPLsSLSTHHPPSAHPpplqLMPQSQQLPPPPAQPPVLT 435
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370476990 639 EVQAHPP----APLPASQGSAVPLPPEPSLAlFAPSPSRDSLLPPTQEMRSPSPMTALQP------GSTGPLPPADDKLE 708
Cdd:pfam03154 436 QSQSLPPpaasHPPTSGLHQVPSQSPFPQHP-FVPGGPPPITPPSGPPTSTSSAMPGIQPpssasvSSSGPVPAAVSCPL 514
|
410 420 430
....*....|....*....|....*....|....*..
gi 1370476990 709 ELIrQFEAEFGDSFGLPGPPSVPIQDPENQQTCLPAP 745
Cdd:pfam03154 515 PPV-QIKEEALDEAEEPESPPPPPRSPSPEPTVVNTP 550
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| TET3 |
cd18897 |
oxygenase domain of ten-eleven translocation (TET)3 methylcytosine dioxygenase and similar ... |
828-1105 |
0e+00 |
|
oxygenase domain of ten-eleven translocation (TET)3 methylcytosine dioxygenase and similar proteins; TET3 is involved in DNA demethylation through iteratively oxidizing 5-methylcytosine (5mC) into 5-hydroxymethylcytosine (5hmC), 5-formylcytosine (5fC) and 5-carboxylcytosine (5caC). TET proteins contain a C-terminal catalytic domain which consists of a cysteine-rich region and a double-stranded beta-helix (DSBH) fold. TET3 serves as a tumor suppressor; it acts as a suppressor of ovarian cancer by demethylating the miR-30d precursor gene promoter to block TGF-beta1 induced epithelial-mesenchymal transition (EMT). TET3 (and TET2) promoters are silenced in melanoma cells by mechanisms triggered by TGF-beta and mediated by DNA methyltransferase 3 alpha (DNMT3A), which play a functional role in the EMT process and metastasis. In addition, TET3 (and TET2) may be guardians of regulatory T cell stability and immune homeostasis. TET3 has been shown to prevent terminal differentiation of adult neural stem cells by a mechanism involving direct binding and repression of TET3 to the imprinted gene Snrpn. TET3 has also been shown to mediate the activation of hepatic stellate cells via modulation of the long non-coding RNA HIF1A-AS1 expression. TET1 belongs to the TET/JBP family of dioxygenases that require Fe2+ and alpha-ketoglutarate (also known as 2-oxoglutarate) for activity.
Pssm-ID: 380676 Cd Length: 452 Bit Score: 585.80 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370476990 828 CDCVEQIVEKDEGPYYTHLGSGPTVASIRELMEERYGEKGKAIRIEKVIYTGKEGKSSRGCPIAKWVIRRHTLEEKLLCL 907
Cdd:cd18897 1 CDCVEQILEKDEGPYYTHLGSGPTVASIRELMEERYGEKGKAIRIEKVIYTGKEGKSSRGCPIAKWVIRRSSEEEKLLCL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370476990 908 VRHRAGHHCQNAVIVILILAWEGIPRSLGDTLYQELTDTLRKYGNPTSRRCGLNDDRTCACQGKDPNTCGASFSFGCSWS 987
Cdd:cd18897 81 VRHRAGHHCQNAVIVILILAWEGIPRALGDKLYQELTETLTKYGNPTSRRCGLNDDRTCACQGKDPNTCGASFSFGCSWS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370476990 988 MYFNGCKYARSKTPRKFRLAGDNPKEEEVLRKSFQDLATEVAPLYKRLAPQAYQNQlgplsqktsllqskgkVTNEEIAI 1067
Cdd:cd18897 161 MYFNGCKYARSKTPRKFRLIGDNPKEEENLRDNFQDLATEVAPLYKRLAPQAYQNQ----------------VTNEDIAI 224
|
250 260 270
....*....|....*....|....*....|....*...
gi 1370476990 1068 DCRLGLKEGRPFAGVTACMDFCAHAHKDQHNLYNGCTV 1105
Cdd:cd18897 225 DCRLGLKEGRPFSGVTACMDFCAHAHKDQHNLYNGCTV 262
|
|
| TET |
cd18892 |
oxygenase domain of ten-eleven translocation (TET)1, TET2, and TET3 methylcytosine ... |
828-1105 |
0e+00 |
|
oxygenase domain of ten-eleven translocation (TET)1, TET2, and TET3 methylcytosine dioxygenases and similar proteins; TET proteins are involved in DNA demethylation through iteratively oxidizing 5-methylcytosine (5mC) into 5-hydroxymethylcytosine (5hmC), 5-formylcytosine (5fC) and 5-carboxylcytosine (5caC). TET proteins contain a C-terminal catalytic domain which consists of a cysteine-rich region and a double-stranded beta-helix (DSBH) fold. Alterations in TET protein function have been linked to cancer, and TETs influence many cell differentiation processes. TET family genes have been implicated as tumor suppressors, for example mutations/deletions of the TET2 gene frequently occur in multiple spectra of myeloid malignancies. TET3 acts as a suppressor of ovarian cancer by demethylating the miR-30d precursor gene promoter to block TGF-beta1 induced epithelial-mesenchymal transition (EMT). TET3 (and TET2) promoters are silenced in melanoma cells by mechanisms triggered by TGF-beta and mediated by DNA methyltransferase 3 alpha (DNMT3A). TET genes are downregulated in endometriosis. TET proteins belong to the TET/JBP family of dioxygenases that require Fe2+ and alpha-ketoglutarate (also known as 2-oxoglutarate) for activity.
Pssm-ID: 380671 Cd Length: 398 Bit Score: 551.90 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370476990 828 CDCVEQIV-EKDEGPYYTHLGSGPTVASIRELMEERYGEKGKAIRIEKVIYTGKEGKSSRGCPIAKWVIRRHTLEEKLLC 906
Cdd:cd18892 1 CGCFPPDEsPPEPGPYYTHLGAGPSLAALRELLEKRTGVTGKAIRIEKVIYTGKEGKTSQGCPIAKWIIRRSSLEEKYLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370476990 907 LVRHRAGHHCQNAVIVILILAWEGIPRSLGDTLYQELTDTLRKYGNPTSRRCGLNDDRTCACQGKDPNTCGASFSFGCSW 986
Cdd:cd18892 81 LVKHRPGHFCHSAFIVICIVAWEGVPQSNADELYSLLTDKLNKFGLPTKRRCGTNEERTCACQGLDPETCGASFSFGCSW 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370476990 987 SMYFNGCKYARSKTPRKFRLAGdnPKEEEVLRKSFQDLATEVAPLYKRLAPQAYQNQlgplsqktsllqskgkVTNEEIA 1066
Cdd:cd18892 161 SMYYNGCKFARSKTVRKFRLSD--KSEEEELEDKLQNLATHLAPLYKSLAPDSYKNQ----------------VQFEEEA 222
|
250 260 270
....*....|....*....|....*....|....*....
gi 1370476990 1067 IDCRLGLKEGRPFAGVTACMDFCAHAHKDQHNLYNGCTV 1105
Cdd:cd18892 223 LDCRLGLKPGRPFSGVTACVDFCAHAHKDLHNMNNGCTV 261
|
|
| TET1 |
cd18895 |
oxygenase domain of ten-eleven translocation (TET)1 methylcytosine dioxygenase and similar ... |
828-1105 |
1.02e-165 |
|
oxygenase domain of ten-eleven translocation (TET)1 methylcytosine dioxygenase and similar proteins; TET1 is involved in DNA demethylation through iteratively oxidizing 5-methylcytosine (5mC) into 5-hydroxymethylcytosine (5hmC), 5-formylcytosine (5fC) and 5-carboxylcytosine (5caC). Human TET1 (and TET2) are more active on 5mC-DNA than 5hmC/5fC-DNA substrates. TET proteins contain a C-terminal catalytic domain which consists of a cysteine-rich region and a double-stranded beta-helix (DSBH) fold. TET1 plays multiple roles in in tumor development and progression. TET1 serves as a tumor suppressor gene; loss of TET1 is associated with tumorigenesis and can be used as a potential biomarker for cancer therapy. In addition to its dioxygenase activity, it can induce epithelial-mesenchymal transition and act as a coactivator to regulate gene transcription. The regulation of TET1 is also correlated with microRNA in a posttranscriptional modification process. TET1 belongs to the TET/JBP family of dioxygenases that require Fe2+ and alpha-ketoglutarate (also known as 2-oxoglutarate) for activity.
Pssm-ID: 380674 Cd Length: 410 Bit Score: 494.82 E-value: 1.02e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370476990 828 CDCVEQIVEKDEGPYYTHLGSGPTVASIRELMEERYGEKGKAIRIEKVIYTGKEGKSSRGCPIAKWVIRRHTLEEKLLCL 907
Cdd:cd18895 1 CDCVEQIIEKDEGPYYTHLGAGPSVAAVREIMENRYGEKGNAIRIEVVVYTGKEGKSSQGCPIAKWVIRRSSDEEKLLCL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370476990 908 VRHRAGHHCQNAVIVILILAWEGIPRSLGDTLYQELTDTLRKYGNPTSRRCGLNDDRTCACQGKDPNTCGASFSFGCSWS 987
Cdd:cd18895 81 VRQRAGHHCQTAVIVILILAWEGIPRLLADRLYQELTQTLKKYGSPTSRRCALNEDRTCACQGLDPETCGASFSFGCSWS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370476990 988 MYFNGCKYARSKTPRKFRLAGDNPKEEEVLRKSFQDLATEVAPLYKRLAPQAYQNQlgplsqktsllqskgkVTNEEIAI 1067
Cdd:cd18895 161 MYFNGCKFARSKYPRKFRLLTDDPKEEENLESNLQNLATDVAPVYKKLAPEAFQNQ----------------VENENVAP 224
|
250 260 270
....*....|....*....|....*....|....*...
gi 1370476990 1068 DCRLGLKEGRPFAGVTACMDFCAHAHKDQHNLYNGCTV 1105
Cdd:cd18895 225 DCRLGSKEGRPFSGVTACIDFCAHAHKDTHNMHNGSTV 262
|
|
| TET2 |
cd18896 |
oxygenase domain of ten-eleven translocation (TET)2 methylcytosine dioxygenase and similar ... |
824-1105 |
2.24e-155 |
|
oxygenase domain of ten-eleven translocation (TET)2 methylcytosine dioxygenase and similar proteins; TET2 is involved in DNA demethylation through iteratively oxidizing 5-methylcytosine (5mC) into 5-hydroxymethylcytosine (5hmC), 5-formylcytosine (5fC) and 5-carboxylcytosine (5caC). Human TET2 (and TET1) have been shown to be more active on 5mC-DNA than 5hmC/5fC-DNA substrates. TET proteins contain a C-terminal catalytic domain which consists of a cysteine-rich region and a double-stranded beta-helix (DSBH) fold. TET2 acts as a tumor suppressor in hematopoiesis; mutations/deletions of the TET2 gene frequently occur in multiple spectra of myeloid malignancies. TET2 (and TET3) promoters are silenced in melanoma cells by mechanisms triggered by TGF-beta and mediated by DNA methyltransferase 3 alpha (DNMT3A), which play a functional role in the epithelial-mesenchymal transition process and metastasis. In addition, TET2 (and TET3) may be guardians of regulatory T cell stability and immune homeostasis. TET2 belongs to the TET/JBP family of dioxygenases that require Fe2+ and alpha-ketoglutarate (also known as 2-oxoglutarate) for activity.
Pssm-ID: 380675 Cd Length: 434 Bit Score: 469.07 E-value: 2.24e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370476990 824 EFPTCDCVEQIVEKDEGPYYTHLGSGPTVASIRELMEERYGEKGKAIRIEKVIYTGKEGKSSRGCPIAKWVIRRHTLEEK 903
Cdd:cd18896 1 DFPSCSCVEQIIEKDEGPYYTHLGAGPNVAAIREIMEERFGQKGKAIRIERVIYTGKEGKSSQGCPIAKWVIRRSSEEEK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370476990 904 LLCLVRHRAGHHCQNAVIVILILAWEGIPRSLGDTLYQELTDTLRKYGNPTSRRCGLNDDRTCACQGKDPNTCGASFSFG 983
Cdd:cd18896 81 LLCLVRERAGHSCETAVIVILILVWEGIPISLADKLYSELTDTLRKYGTLTNRRCALNEERTCACQGLDPETCGASFSFG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370476990 984 CSWSMYFNGCKYARSKTPRKFRLAGDNPKEEEVLRKSFQDLATEVAPLYKRLAPQAYQNQlgplsqktsllqskgkVTNE 1063
Cdd:cd18896 161 CSWSMYYNGCKFARSKIPRKFKLLGDDPKEEEKLESNLQNLSTLMAPTYKKLAPDAYNNQ----------------IEYE 224
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1370476990 1064 EIAIDCRLGLKEGRPFAGVTACMDFCAHAHKDQHNLYNGCTV 1105
Cdd:cd18896 225 HRAPDCRLGLKEGRPFSGVTACLDFCAHAHRDLHNMQNGSTL 266
|
|
| Tet_JBP |
cd14946 |
oxygenase domain of ten-eleven translocation (TET) enzymes, J-binding proteins (JBPs), and ... |
855-1105 |
6.77e-47 |
|
oxygenase domain of ten-eleven translocation (TET) enzymes, J-binding proteins (JBPs), and similar proteins; TET proteins are involved in DNA demethylation through iteratively oxidizing 5-methylcytosine (5mC) into 5-hydroxymethylcytosine (5hmC), 5-formylcytosine (5fC) and 5-carboxylcytosine (5caC). TET proteins contain a C-terminal catalytic domain which consists of a cysteine-rich region and a double-stranded beta-helix (DSBH) fold. Alterations in TET protein function have been linked to cancer, and TETs influence many cell differentiation processes. J binding protein (JBP) 1 and JBP2 are thymidine hydroxylases that catalyze the first step of base J biosynthesis: the hydroxylation of thymine in DNA to form 5-hydroxymethyluracil (hmU). Base J (beta-d-glucopyranosyloxymethyluracil) is a hyper-modified DNA base found in the DNA of kinetoplastids (Trypanosoma brucei, Trypanosoma cruzi, and Leishmania). JBP1 and JBP2 each contain a J-DNA binding domain and a thymidine hydroxylase domain. Members of this TET/JBP family of dioxygenases require Fe2+ and alpha-ketoglutarate (also known as 2-oxoglutarate) for activity.
Pssm-ID: 380670 Cd Length: 264 Bit Score: 169.10 E-value: 6.77e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370476990 855 IRELMEERYG-EKGKAIRIEKVIYTGKEGKSsRGCPIAKWVIRRhtleEKLLCLVRHRAGhhcqnavIVILILAWEGIPR 933
Cdd:cd14946 1 LLENMLSKCGtQQSFANANITLKYEGKEGKS-QGCPKALKNVRT----SKLAYFVCDHDG-------SVILAYVPEVLPK 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370476990 934 SLGDTLYQELTDTLRKYGNptsrrcglnddrtcacqgKDPNTCGASFSFGCSWSMYFNGCKyarsktprkfRLAGDNPKE 1013
Cdd:cd14946 69 ELVEEFTEKLESIQTKRGT------------------LDPETKGDTGYSGILDNSMPFNYV----------TADLSQELG 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370476990 1014 EEVLRKSFQDLATEVAPLYKRLAPQAYQNQlgplsqktsllqskgkVTNEEIAIDCRLGLKEGRPFAGVTACMD-FCAHA 1092
Cdd:cd14946 121 QYLSEIVNPQISYYISKLLTCVSPRTINYL----------------VEYEHRSLNDSYYALNNCLYPSTAFNSLkRIRKP 184
|
250
....*....|...
gi 1370476990 1093 HKDQHNLYNGCTV 1105
Cdd:cd14946 185 HKDNLDIQNGPSS 197
|
|
| Tet_JBP |
pfam12851 |
Oxygenase domain of the 2OGFeDO superfamily; A double-stranded beta helix (DSBH) fold domain ... |
985-1105 |
6.05e-34 |
|
Oxygenase domain of the 2OGFeDO superfamily; A double-stranded beta helix (DSBH) fold domain of the 2-oxoglutarate (2OG)-Fe(II)-dependent dioxygenase (2OGFeDO) superfamily found in various eukaryotes, bacteria and bacteriophages. Members of this family catalyze nucleic acid modifications, such as thymidine hydroxylation during base J synthesis in kinetoplastids, and the conversion of 5 methyl-cytosine (5-mC) to 5-hydroxymethyl-cytosine (hmC), or further oxidation to 5-formylcytosine (5fC) and 5-carboxylcytosine (5caC). Metazoan TET proteins contain a cysteine-rich region inserted into the core of the DSBH fold. Vertebrate TET proteins are oncogenes that are mutated in various myeloid cancers. Fungal and algal versions of this family are linked to a predicted transposase and show lineage-specific expansions.
Pssm-ID: 372343 Cd Length: 166 Bit Score: 128.27 E-value: 6.05e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370476990 985 SWSMYFNGCKYARSKTPRKFRLAGDNPKEEEVLRKSFQDLATEVAPLYKRLAPQAYQNQlgplsqktsllqskgkVTNEE 1064
Cdd:pfam12851 1 SWSMYYDGCKFPGPRKPRKFSFTPRNPKEEIKLEDELQELAALLGAIYKQIAPDLYENQ----------------IEYEQ 64
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1370476990 1065 IAIDCRLGLKEGRPFAGVTACMDFCAHAHKDQHNLYNGCTV 1105
Cdd:pfam12851 65 DAAICRLGRKWGRPFSGVTVNLNFETISHRDLGNFRNGSTL 105
|
|
| zf-CXXC |
pfam02008 |
CXXC zinc finger domain; This domain contains eight conserved cysteine residues that bind to ... |
50-89 |
1.15e-12 |
|
CXXC zinc finger domain; This domain contains eight conserved cysteine residues that bind to two zinc ions. The CXXC domain is found in a variety of chromatin-associated proteins. This domain binds to nonmethyl-CpG dinucleotides. The domain is characterized by two repeats, and shows a peculiar internal duplication in which the second unit is inserted into the first one. Each of these units is characterized by four conserved cysteines, displaying a CXXCXXCX(n)C motif that chelate a Zn+2 ion. The DNA binding interface has been identified by NMR. In eukaryotes, the CXXC domain is found in stramenopiles, plants and metazoans. Plants possess a mono-CXXC domain that is present in distinct chromatin proteins. Structural comparisons show that the mono-CXXC is homologous to the structural-zinc binding domain of medium chain dehydrogenases.
Pssm-ID: 366873 Cd Length: 48 Bit Score: 63.14 E-value: 1.15e-12
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1370476990 50 GRKKRKRCGTCEPCRRLENCGACTSCTNR-------RTHQICKLRKC 89
Cdd:pfam02008 2 NRRKRRRCGVCEGCQRPEDCGQCSFCLDMpkfggpgKKKQKCRLRRC 48
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
383-752 |
1.19e-10 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 66.12 E-value: 1.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370476990 383 PLPEALSPPAPFRS--PQSYLRAPSWPVVPPEEHSSFAPDSSAFP--PATPRTEFP-EAWGTDTPPATPRSSWPMPRPSP 457
Cdd:PHA03247 2554 PLPPAAPPAAPDRSvpPPRPAPRPSEPAVTSRARRPDAPPQSARPraPVDDRGDPRgPAPPSPLPPDTHAPDPPPPSPSP 2633
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370476990 458 DPMAeleqlLGSASDYIQSVFKRPEALPTKPKVKVEAPSSSPAPAPSPVLQREAPTPSSEPDTHQKAQTALQQHLHHKRS 537
Cdd:PHA03247 2634 AANE-----PDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSPPQRPRRRAARPTVGSLTSLADPPPPPPTP 2708
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370476990 538 LFLEQVHDTSFPAPSEPSAPGWWPPPSS---------PVPRLPDRPPKEKKKKLPTPAGGPVGTEKAAPGIKPSVRKPIQ 608
Cdd:PHA03247 2709 EPAPHALVSATPLPPGPAAARQASPALPaapappavpAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAV 2788
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370476990 609 IKKSRPREAQPLfPPVRQIVLEGLRSPASQEVQAHPPAPLPASQGSAVPLPPEPSLALFAPSPSRDSLLPPTQEMRSPSP 688
Cdd:PHA03247 2789 ASLSESRESLPS-PWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSVAPGGDVRRRPP 2867
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1370476990 689 MtalQPGSTGPLPPADDKLEELIRQFEAEFGDSFGLPGPPSVPIQDPENQQTCLPAPESPFATR 752
Cdd:PHA03247 2868 S---RSPAAKPAAPARPPVRRLARPAVSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQ 2928
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
359-734 |
2.72e-07 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 55.33 E-value: 2.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370476990 359 AIEALTQLSSALPQPSHSTPQASCPLPEALSPPAPFRSPQSYLRAPSWPVVPPEEHSSFAPDSSAFPPATPRTEFPEAwg 438
Cdd:PHA03247 2691 TVGSLTSLADPPPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPA-- 2768
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370476990 439 tDTPPATPRSSWP--MPRPSPDPMAELEQLLGSASDYIQSVFKRPEALPTKPKVKVEAPSsspapapspvlqrEAPTPSS 516
Cdd:PHA03247 2769 -PAPPAAPAAGPPrrLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGP-------------LPPPTSA 2834
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370476990 517 EPdthqkaqtalqqhlhhkrslfleqvhdTSFPAPSEPSAPGWWPPPSSPVprlpdrppkekkkklptpaGGPV---GTE 593
Cdd:PHA03247 2835 QP---------------------------TAPPPPPGPPPPSLPLGGSVAP-------------------GGDVrrrPPS 2868
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370476990 594 KAAPGI-----KPSVRKPIQIKKSRPREAQPLFPPvrqivleglrspaSQEVQAHPPAPLPASQGSAVPLPPEPSLALFA 668
Cdd:PHA03247 2869 RSPAAKpaapaRPPVRRLARPAVSRSTESFALPPD-------------QPERPPQPQAPPPPQPQPQPPPPPQPQPPPPP 2935
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1370476990 669 PSPSRDSLLPPTQEMRSPSPMTALQPGSTGPLPPADdklEELIRQFEAEFGDSFGLPGPPSVPIQD 734
Cdd:PHA03247 2936 PPRPQPPLAPTTDPAGAGEPSGAVPQPWLGALVPGR---VAVPRFRVPQPAPSREAPASSTPPLTG 2998
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
385-803 |
2.24e-06 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 52.25 E-value: 2.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370476990 385 PEALSPPAPFRSPQSYLRAPSWPVVPPEEHS---SFAPDSSAFPPATPRT----------------EFPEAWGTDTPPAT 445
Cdd:PHA03247 2484 AEARFPFAAGAAPDPGGGGPPDPDAPPAPSRlapAILPDEPVGEPVHPRMltwirgleelasddagDPPPPLPPAAPPAA 2563
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370476990 446 PRSSWPMPRPSPDPmaeleqllgsASDYIQSVFKRPEALP--TKPKVKVEAPSSSPapapspvlqREAPTPSSEPDTHQK 523
Cdd:PHA03247 2564 PDRSVPPPRPAPRP----------SEPAVTSRARRPDAPPqsARPRAPVDDRGDPR---------GPAPPSPLPPDTHAP 2624
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370476990 524 AqtalqqhlhhkrslfleqvhdtsfPAPSEPSApgwwppPSSPVPRLPDRPPKEKKKKLPTPAGGPVGTEKAAPGIKPSV 603
Cdd:PHA03247 2625 D------------------------PPPPSPSP------AANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAA 2674
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370476990 604 RKPIQIKKSRPREAQPLFPPvrqivlegLRSPASQEVQAHPPAPLPASQGSAVPLPPEPSLALFAPSPSRDSLLPPtqem 683
Cdd:PHA03247 2675 QASSPPQRPRRRAARPTVGS--------LTSLADPPPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPP---- 2742
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370476990 684 rsPSPMTALQPGstGPLPPADDKLEElirqfeaefgdSFGLPGPPSVPIQDPENQQT---CLPAPESPFATRSPKQIKIE 760
Cdd:PHA03247 2743 --AVPAGPATPG--GPARPARPPTTA-----------GPPAPAPPAAPAAGPPRRLTrpaVASLSESRESLPSPWDPADP 2807
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 1370476990 761 SSGAVTVLSTTCFHSEEGGQEATPTKAENPLTPTLSGFLESPL 803
Cdd:PHA03247 2808 PAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSL 2850
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
313-701 |
4.00e-05 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 48.01 E-value: 4.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370476990 313 AGLPAPSTRP----LLSSEVPQISPQEGLPLSQSALSIAKEKNISLQTAIAIEALTQLSSALPQPSHSTPQASCPLPEAL 388
Cdd:PHA03247 2609 RGPAPPSPLPpdthAPDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSPPQRPRRRAA 2688
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370476990 389 SPPApfrSPQSYLRAPSWPVVPPEehssfaPDSSAFPPATPRTEFPEAWGTDTPPATprsSWPMPRPSPDpmaeleqllG 468
Cdd:PHA03247 2689 RPTV---GSLTSLADPPPPPPTPE------PAPHALVSATPLPPGPAAARQASPALP---AAPAPPAVPA---------G 2747
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370476990 469 SASDYIQSVFKRPEAL-----PTKPKVKVEAPSSSPAPAPSPVLQREAPTPSSEPDTHQKAQTALQQHlhhkrslflEQV 543
Cdd:PHA03247 2748 PATPGGPARPARPPTTagppaPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPA---------AAL 2818
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370476990 544 HDTSFPAPSEPSAPGWWPPPSSPVPRLPDRPPKEkkkklptpaGGPVgtekaAPGIKPSVRKPIQIKKSRPreAQPLFPP 623
Cdd:PHA03247 2819 PPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPL---------GGSV-----APGGDVRRRPPSRSPAAKP--AAPARPP 2882
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370476990 624 VRQIVLEGL-RSPASQEVQAHPPAPLPASQGSAVPLPPEPSLALFAPSPsrdsllPPTQEMRSPSPM-----TALQPGST 697
Cdd:PHA03247 2883 VRRLARPAVsRSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQP------PPPPPPRPQPPLapttdPAGAGEPS 2956
|
....
gi 1370476990 698 GPLP 701
Cdd:PHA03247 2957 GAVP 2960
|
|
| PRK14950 |
PRK14950 |
DNA polymerase III subunits gamma and tau; Provisional |
344-484 |
3.45e-04 |
|
DNA polymerase III subunits gamma and tau; Provisional
Pssm-ID: 237864 [Multi-domain] Cd Length: 585 Bit Score: 44.80 E-value: 3.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370476990 344 LSIAKEKNISLQTAIaIEALTqlsSALPQPSHSTPQASCPLPeALSPPAPFRSPQSYLRAPSwPVVPPEEHSSFAPDSSA 423
Cdd:PRK14950 341 LRTTSYGQLPLELAV-IEALL---VPVPAPQPAKPTAAAPSP-VRPTPAPSTRPKAAAAANI-PPKEPVRETATPPPVPP 414
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1370476990 424 FPPATPRTEFPEAWGTDTP-----PATPRSSWPMPRPSPD-----PMAELEQLLGSASDYIQSVFKRPEAL 484
Cdd:PRK14950 415 RPVAPPVPHTPESAPKLTRaaipvDEKPKYTPPAPPKEEEkaliaDGDVLEQLEAIWKQILRDVPPRSPAV 485
|
|
| PRK12323 |
PRK12323 |
DNA polymerase III subunit gamma/tau; |
589-753 |
5.76e-04 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 237057 [Multi-domain] Cd Length: 700 Bit Score: 44.10 E-value: 5.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370476990 589 PVGTEKAAPGIKPSVRKPIQIKKSRPREAQPLfPPVRQIVLEGlRSPASQEVQAHPPAPLPASQGSAVPLPPEPSLALFA 668
Cdd:PRK12323 402 PPAAPAAAPAAAAAARAVAAAPARRSPAPEAL-AAARQASARG-PGGAPAPAPAPAAAPAAAARPAAAGPRPVAAAAAAA 479
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370476990 669 PSPSR--------DSLLPPTQEMRSPSPMTALQPGSTGPLP-PADDKLEELIRQFEAEFGDSfgLPGPPSVPIQDPENQQ 739
Cdd:PRK12323 480 PARAApaaapapaDDDPPPWEELPPEFASPAPAQPDAAPAGwVAESIPDPATADPDDAFETL--APAPAAAPAPRAAAAT 557
|
170
....*....|....
gi 1370476990 740 TCLPAPESPFATRS 753
Cdd:PRK12323 558 EPVVAPRPPRASAS 571
|
|
| PTZ00449 |
PTZ00449 |
104 kDa microneme/rhoptry antigen; Provisional |
589-824 |
6.31e-04 |
|
104 kDa microneme/rhoptry antigen; Provisional
Pssm-ID: 185628 [Multi-domain] Cd Length: 943 Bit Score: 43.91 E-value: 6.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370476990 589 PVGTEKAAPGIKP-SVRKPIQIKKS-RPREAQ-PLFP--PVRQIVLEGLRSPASQEVQAHPPAPLPASQGSAvPLPPEPS 663
Cdd:PTZ00449 573 PTLSKKPEFPKDPkHPKDPEEPKKPkRPRSAQrPTRPksPKLPELLDIPKSPKRPESPKSPKRPPPPQRPSS-PERPEGP 651
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370476990 664 LALFAPSPSRDSLLP--PT--QEMRSPSPMTALQPGSTGPLPPADDKLEELIRQFEAEF-GDSFGLPGP----------- 727
Cdd:PTZ00449 652 KIIKSPKPPKSPKPPfdPKfkEKFYDDYLDAAAKSKETKTTVVLDESFESILKETLPETpGTPFTTPRPlppklprdeef 731
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370476990 728 PSVPIQDPENQQtclPAPESPFATRSPKQIKIESSGAVTVLSTTCfhSEEGGQEATPTKAENPLTPTLSGflESPLKYLD 807
Cdd:PTZ00449 732 PFEPIGDPDAEQ---PDDIEFFTPPEEERTFFHETPADTPLPDIL--AEEFKEEDIHAETGEPDEAMKRP--DSPSEHED 804
|
250
....*....|....*..
gi 1370476990 808 TPTKSLLDTPAKRAQAE 824
Cdd:PTZ00449 805 KPPGDHPSLPKKRHRLD 821
|
|
| Atrophin-1 |
pfam03154 |
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ... |
326-745 |
7.47e-04 |
|
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: 43.60 E-value: 7.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370476990 326 SEVPQI-SPQEGLPLSQSAlsiaKEKNISLQTAIAIEALTQLSSALPQPSHSTPQASCPLPEALSPPAPFRSPQSYLRAP 404
Cdd:pfam03154 143 STSPSIpSPQDNESDSDSS----AQQQILQTQPPVLQAQSGAASPPSPPPPGTTQAATAGPTPSAPSVPPQGSPATSQPP 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370476990 405 SWPVVPPEEHSSFAPDSSAFPPATPRTEFPEAWGTDTPPATPRSSWPMPRPS-PDPMAELEQLLGSASDYIqsvfkrPEA 483
Cdd:pfam03154 219 NQTQSTAAPHTLIQQTPTLHPQRLPSPHPPLQPMTQPPPPSQVSPQPLPQPSlHGQMPPMPHSLQTGPSHM------QHP 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370476990 484 LPTKPkvkveapssspAPAPSPVLQREAPTPSSEPDTHQKAQTalqQHLHHKRSLFLEQVHDTSFPAPSEPSAPGWWPPP 563
Cdd:pfam03154 293 VPPQP-----------FPLTPQSSQSQVPPGPSPAAPGQSQQR---IHTPPSQSQLQSQQPPREQPLPPAPLSMPHIKPP 358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370476990 564 SSPVPRLPDRPPKEKKKKLPTpagGPVGTEKAAPGIKPSVRKPI-QIKKSRPREAQP----LFPPVRQIVLEGLRSPASQ 638
Cdd:pfam03154 359 PTTPIPQLPNPQSHKHPPHLS---GPSPFQMNSNLPPPPALKPLsSLSTHHPPSAHPpplqLMPQSQQLPPPPAQPPVLT 435
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370476990 639 EVQAHPP----APLPASQGSAVPLPPEPSLAlFAPSPSRDSLLPPTQEMRSPSPMTALQP------GSTGPLPPADDKLE 708
Cdd:pfam03154 436 QSQSLPPpaasHPPTSGLHQVPSQSPFPQHP-FVPGGPPPITPPSGPPTSTSSAMPGIQPpssasvSSSGPVPAAVSCPL 514
|
410 420 430
....*....|....*....|....*....|....*..
gi 1370476990 709 ELIrQFEAEFGDSFGLPGPPSVPIQDPENQQTCLPAP 745
Cdd:pfam03154 515 PPV-QIKEEALDEAEEPESPPPPPRSPSPEPTVVNTP 550
|
|
| TALPID3 |
pfam15324 |
Hedgehog signalling target; TALPID3 is a family of eukaryotic proteins that are targets for ... |
364-459 |
1.75e-03 |
|
Hedgehog signalling target; TALPID3 is a family of eukaryotic proteins that are targets for Hedgehog signalling. Mutations in this gene noticed first in chickens lead to multiple abnormalities of development.
Pssm-ID: 434634 [Multi-domain] Cd Length: 1288 Bit Score: 42.57 E-value: 1.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370476990 364 TQLSSALPQPSHSTPQASCPLPEALSP-PAPFRSPQ-SYLRAPSWPVVPPEEHSSFAPDSSAF--PPATPRTEFPEAwGT 439
Cdd:pfam15324 982 TLLPTPVPTPQPTPPCSPPSPLKEPSPvKTPDSSPCvSEHDFFPVKEIPPEKGADTGPAVSLVitPTVTPIATPPPA-AT 1060
|
90 100
....*....|....*....|
gi 1370476990 440 DTPPATPRSSWPMPRPSPDP 459
Cdd:pfam15324 1061 PTPPLSENSIDKLKSPSPEL 1080
|
|
| PRK12323 |
PRK12323 |
DNA polymerase III subunit gamma/tau; |
312-462 |
1.86e-03 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 237057 [Multi-domain] Cd Length: 700 Bit Score: 42.17 E-value: 1.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370476990 312 EAGLPAPSTRPLLSSEVPQISPQEGLPLSQSALSIAKEKNISLQTAIAIEALTQLSSALPQPSHSTPQASCPLPEALSPP 391
Cdd:PRK12323 399 PAAPPAAPAAAPAAAAAARAVAAAPARRSPAPEALAAARQASARGPGGAPAPAPAPAAAPAAAARPAAAGPRPVAAAAAA 478
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1370476990 392 APFRSPQSYLRAPSWPVVPPEEH-----SSFAPDSSAFPPATPRTEFPEAWGTDTPPATPRSSWPMPRPSPDPMAE 462
Cdd:PRK12323 479 APARAAPAAAPAPADDDPPPWEElppefASPAPAQPDAAPAGWVAESIPDPATADPDDAFETLAPAPAAAPAPRAA 554
|
|
| PRK07764 |
PRK07764 |
DNA polymerase III subunits gamma and tau; Validated |
367-756 |
3.20e-03 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 41.51 E-value: 3.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370476990 367 SSALPQPSHSTPQAscPLPEALSPPAPFRSPQSYLRAPSWPVVP-PEEHSSFAPDSSAFPPATPRTEFPEAWGTDTPPAT 445
Cdd:PRK07764 419 AAAAPAPAAAPQPA--PAPAPAPAPPSPAGNAPAGGAPSPPPAAaPSAQPAPAPAAAPEPTAAPAPAPPAAPAPAAAPAA 496
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370476990 446 PRSswPMPRPSPDPMAELE----QLLGSASDYIQSVFkrpEALPTKPKVkveapssspAPAPSPVLQREAPTPS-----S 516
Cdd:PRK07764 497 PAA--PAAPAGADDAATLRerwpEILAAVPKRSRKTW---AILLPEATV---------LGVRGDTLVLGFSTGGlarrfA 562
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370476990 517 EPDTHQKAQTALQQHLHhkRSLFLEQVHDTSFPAPSEPSAPGWWPPPSSPVPRLPDRPPKEKKKKLPTPAGGPVGTEKAA 596
Cdd:PRK07764 563 SPGNAEVLVTALAEELG--GDWQVEAVVGPAPGAAGGEGPPAPASSGPPEEAARPAAPAAPAAPAAPAPAGAAAAPAEAS 640
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370476990 597 PGIKPSVRKPIQIKKSRPREAQPLFPPVRQIVLEGLRSPASQEVQAHPPAPLPASQGSAVPLPPEPslalfAPSPSRDSL 676
Cdd:PRK07764 641 AAPAPGVAAPEHHPKHVAVPDASDGGDGWPAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPA-----ATPPAGQAD 715
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370476990 677 LPPTQEMRSPSPMTALQPGSTGPLPPADdkleelirqfEAEFGDSFGLPGPPSVPIQDPENQQTclPAPESPFATRSPKQ 756
Cdd:PRK07764 716 DPAAQPPQAAQGASAPSPAADDPVPLPP----------EPDDPPDPAGAPAQPPPPPAPAPAAA--PAAAPPPSPPSEEE 783
|
|
| Atrophin-1 |
pfam03154 |
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ... |
589-754 |
3.32e-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: 41.68 E-value: 3.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370476990 589 PVGTEKAAPGIKPSVRKPIQIKKSRPREAQPlfpPVRQIVLEGLRSPASQEVQAHP---PAPLPASQGSAVPLPPEPSLA 665
Cdd:pfam03154 187 PPPGTTQAATAGPTPSAPSVPPQGSPATSQP---PNQTQSTAAPHTLIQQTPTLHPqrlPSPHPPLQPMTQPPPPSQVSP 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370476990 666 LFAPSPSRDSLLPPTqemrsPSPMTALQPGSTGPLPPADDKLEELIRQFEaefgdsfgLPGPPSVPIQDPENQQTCLPAP 745
Cdd:pfam03154 264 QPLPQPSLHGQMPPM-----PHSLQTGPSHMQHPVPPQPFPLTPQSSQSQ--------VPPGPSPAAPGQSQQRIHTPPS 330
|
....*....
gi 1370476990 746 ESPFATRSP 754
Cdd:pfam03154 331 QSQLQSQQP 339
|
|
| GGN |
pfam15685 |
Gametogenetin; GGN is a family of proteins largely found in mammals. It reacts with POG in the ... |
588-753 |
4.08e-03 |
|
Gametogenetin; GGN is a family of proteins largely found in mammals. It reacts with POG in the maturation of sperm and is expressed virtually only in the testis. It is found to be associated with the intracellular membrane, binds with GGNBP1 and may be involved in vesicular trafficking.
Pssm-ID: 434857 [Multi-domain] Cd Length: 668 Bit Score: 41.29 E-value: 4.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370476990 588 GPVGTEKAAPGIKPSVRKPIQIKKSRPREAQPLFPPVRQIVLEGLRSPASQEVQAHPPAPLPASQGSAVPlPPEPSLALF 667
Cdd:pfam15685 388 GPWGSPPPPPGKAHPIPGPRRPAPALLAPPMFIFPAPTNGEPVRPGPPAPQALLPRPPPPTPPATPPPVP-PPIPQLPAL 466
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370476990 668 APSPsRDSLLPPTQEMRSPSPMTALQPGSTGPLPPAddkleELIRQFEAEFGDSFGLPGPPSVPIqdpenqqTCLPAPES 747
Cdd:pfam15685 467 QPMP-LAAARPPTPRPCPGHGESALAPAPTAPLPPA-----LAADQAPAPALAAAPAPSPAPAPA-------TADPLPPA 533
|
....*.
gi 1370476990 748 PFATRS 753
Cdd:pfam15685 534 PAPIKA 539
|
|
| PRK14951 |
PRK14951 |
DNA polymerase III subunits gamma and tau; Provisional |
347-464 |
4.70e-03 |
|
DNA polymerase III subunits gamma and tau; Provisional
Pssm-ID: 237865 [Multi-domain] Cd Length: 618 Bit Score: 40.85 E-value: 4.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370476990 347 AKEKNISLQTAIAIEALTQLSSALPQPSHSTPQASCPLPEALSP----PAPFRSPQSYLRAPSWPVVPPEEH--SSFAPD 420
Cdd:PRK14951 369 AAEAAAPAEKKTPARPEAAAPAAAPVAQAAAAPAPAAAPAAAASapaaPPAAAPPAPVAAPAAAAPAAAPAAapAAVALA 448
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1370476990 421 SSAFPPATPRTEFPEAWGTDTPPATPRSSWPMPRPSPDPMAELE 464
Cdd:PRK14951 449 PAPPAQAAPETVAIPVRVAPEPAVASAAPAPAAAPAAARLTPTE 492
|
|
| PRK14951 |
PRK14951 |
DNA polymerase III subunits gamma and tau; Provisional |
586-703 |
5.62e-03 |
|
DNA polymerase III subunits gamma and tau; Provisional
Pssm-ID: 237865 [Multi-domain] Cd Length: 618 Bit Score: 40.85 E-value: 5.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370476990 586 AGGPVGTEKAAPgIKPSVRKPiqikkSRPREAQPLFPPVRQIVLEGLRSPASQEVQAHPPAPLPASQGSAVPLPPEPSLA 665
Cdd:PRK14951 370 AEAAAPAEKKTP-ARPEAAAP-----AAAPVAQAAAAPAPAAAPAAAASAPAAPPAAAPPAPVAAPAAAAPAAAPAAAPA 443
|
90 100 110
....*....|....*....|....*....|....*...
gi 1370476990 666 LFAPSPSrdSLLPPTQEMRSPSPMTALQPGSTGPLPPA 703
Cdd:PRK14951 444 AVALAPA--PPAQAAPETVAIPVRVAPEPAVASAAPAP 479
|
|
|