|
Name |
Accession |
Description |
Interval |
E-value |
| TET3 |
cd18897 |
oxygenase domain of ten-eleven translocation (TET)3 methylcytosine dioxygenase and similar ... |
836-1160 |
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: 725.63 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941150 836 CDCVEQIVEKDEGPYYTHLGSGPTVASIRELMEDRYGEKGKAIRIEKVIYTGKEGKSSRGCPIAKWVIRRHTLEEKLLCL 915
Cdd:cd18897 1 CDCVEQILEKDEGPYYTHLGSGPTVASIRELMEERYGEKGKAIRIEKVIYTGKEGKSSRGCPIAKWVIRRSSEEEKLLCL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941150 916 VRHRAGHHCQNAVIVILILAWEGIPRSLGDTLYQELTDTLRKYGNPTSRRCGLNDDRTCACQGKDPNTCGASFSFGCSWS 995
Cdd:cd18897 81 VRHRAGHHCQNAVIVILILAWEGIPRALGDKLYQELTETLTKYGNPTSRRCGLNDDRTCACQGKDPNTCGASFSFGCSWS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941150 996 MYFNGCKYARSKTPRKFRLTGDNPKEEEVLRNSFQDLATEVAPLYKRLAPQAYQNQVTNEDVAIDCRLGLKEGRPFSGVT 1075
Cdd:cd18897 161 MYFNGCKYARSKTPRKFRLIGDNPKEEENLRDNFQDLATEVAPLYKRLAPQAYQNQVTNEDIAIDCRLGLKEGRPFSGVT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941150 1076 ACMDFCAHAHKDQHNLYNGCTVVCTLTKEDNRCVGQIPEDEQLHVLPLYKMASTDEFGSEENQNAKVSSGAIQVLTAFPR 1155
Cdd:cd18897 241 ACMDFCAHAHKDQHNLYNGCTVVCTLTKEDNRTVGKIPEDEQLHVLPLYKMSTTDEFGSEENQNEKIGSGAIQVLTSFPR 320
|
....*
gi 568941150 1156 EVRRL 1160
Cdd:cd18897 321 EVREV 325
|
|
| Tet_JBP super family |
cl40427 |
oxygenase domain of ten-eleven translocation (TET) enzymes, J-binding proteins (JBPs), and ... |
1612-1774 |
3.81e-81 |
|
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.
The actual alignment was detected with superfamily member cd18897:
Pssm-ID: 394797 Cd Length: 452 Bit Score: 275.33 E-value: 3.81e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941150 1612 DPFSLEEGTAEEPPSkGVVKEEKSGPtveEDEEELWSDSEHNFLDENIGGVAVAPAHCSILIECARRELHATTPLKKPNR 1691
Cdd:cd18897 295 DEFGSEENQNEKIGS-GAIQVLTSFP---REVREVWSDSEHNFLDENIGGVAVAPAHGSILIECARRELHATTPLKKPNR 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941150 1692 CHPTRISLVFYQHKNLNQPNHGLALWEAKMKQLAERARQRQEEAARLGLgQQEAKLYGKKRKWGGAMVAEPQHKEKKGAI 1771
Cdd:cd18897 371 CHPTRISLVFYQHKNLNQPNHGLALWEAKMKLLAERARARQEEAARLGL-QQEIKPYGKKRKWGGAPAAEPQPKEKKDKI 449
|
...
gi 568941150 1772 PTR 1774
Cdd:cd18897 450 PTR 452
|
|
| zf-CXXC |
pfam02008 |
CXXC zinc finger domain; This domain contains eight conserved cysteine residues that bind to ... |
50-89 |
1.82e-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: 63.53 E-value: 1.82e-12
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 568941150 50 GRKKRKRCGTCDPCRRLENCGSCTSCTNR-------RTHQICKLRKC 89
Cdd:pfam02008 2 NRRKRRRCGVCEGCQRPEDCGQCSFCLDMpkfggpgKKKQKCRLRRC 48
|
|
| PHA03247 super family |
cl33720 |
large tegument protein UL36; Provisional |
297-760 |
1.84e-08 |
|
large tegument protein UL36; Provisional
The actual alignment was detected with superfamily member PHA03247:
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 59.95 E-value: 1.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941150 297 QGRPRLPGALPPSEAGLPAPSTRPPllSSEVPQVPPLEGLPLSQSALSiakeknislQTAIAIEALTQLSSALPQPSHST 376
Cdd:PHA03247 2595 SARPRAPVDDRGDPRGPAPPSPLPP--DTHAPDPPPPSPSPAANEPDP---------HPPPTVPPPERPRDDPAPGRVSR 2663
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941150 377 SQASCPLPEALSPSAPFRSPQ-SYLRAPSWPVV----PPEEHPSFAPDSPAFPPATPRPEFSEAWGTDTPPATPRnswPV 451
Cdd:PHA03247 2664 PRRARRLGRAAQASSPPQRPRrRAARPTVGSLTsladPPPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAA---PA 2740
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941150 452 PRPSPDpmaeleqllGSASDYIQSVFKRPEAL-----PTKPKVKVEAPSSSPAPVPSPISQREAPLLSSEPDTHQKAQTA 526
Cdd:PHA03247 2741 PPAVPA---------GPATPGGPARPARPPTTagppaPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAV 2811
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941150 527 LqqhlhhkrnlfleqAQDASFPTSTEPQAPgwwaPPGSPAPRPPDKPPKEKKKKPPTPAGGPVgaektTPGIKTSVRKPI 606
Cdd:PHA03247 2812 L--------------APAAALPPAASPAGP----LPPPTSAQPTAPPPPPGPPPPSLPLGGSV-----APGGDVRRRPPS 2868
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941150 607 QikKSRSRDMQPLFLPVRQIVleglKPQASEGQAPLP-AQLSVPPPASQGAASQSCATPLTPEPSLALFAPSPSGDSLLP 685
Cdd:PHA03247 2869 R--SPAAKPAAPARPPVRRLA----RPAVSRSTESFAlPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPP 2942
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568941150 686 PtqemrSPSPMVALQSGSTGGPLPPADDKLeelirqfeaefgdsfgLPGPPSVPIQEPENQSTCLPAPESPFATR 760
Cdd:PHA03247 2943 L-----APTTDPAGAGEPSGAVPQPWLGAL----------------VPGRVAVPRFRVPQPAPSREAPASSTPPL 2996
|
|
| PHA03247 super family |
cl33720 |
large tegument protein UL36; Provisional |
126-461 |
5.87e-06 |
|
large tegument protein UL36; Provisional
The actual alignment was detected with superfamily member PHA03247:
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 51.86 E-value: 5.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941150 126 SPVD--GPVPGQMDSGPVYHGDSRQLSTSGAPVNGAREPAGPGLLGAAGPWRVDQKPDWEAASGPTHAARLEDAHDLVAF 203
Cdd:PHA03247 2600 APVDdrGDPRGPAPPSPLPPDTHAPDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSP 2679
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941150 204 S------AVAEAVSSYGALstrlyetfnremsreAGSNGRGPRPESCSEGSEDLDTLQTALALARHGMKPPNCTCDGPEC 277
Cdd:PHA03247 2680 PqrprrrAARPTVGSLTSL---------------ADPPPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAV 2744
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941150 278 PDflewlegkikSMAMEGGQGRPRLPG--ALPPSEAGLPAPSTRPPLLSSEVPQVPPLEGLPLSQSALSIAKEKNISLQT 355
Cdd:PHA03247 2745 PA----------GPATPGGPARPARPPttAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAP 2814
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941150 356 AIAIEALTQLSSALPQPSHST----SQASCPLPEALS------PSAPFRSpqsylRAPSWPVVPPEEHPSFAPDSPAFPP 425
Cdd:PHA03247 2815 AAALPPAASPAGPLPPPTSAQptapPPPPGPPPPSLPlggsvaPGGDVRR-----RPPSRSPAAKPAAPARPPVRRLARP 2889
|
330 340 350
....*....|....*....|....*....|....*.
gi 568941150 426 ATPRPEFSEAWGTDtPPATPRNSWPVPRPSPDPMAE 461
Cdd:PHA03247 2890 AVSRSTESFALPPD-QPERPPQPQAPPPPQPQPQPP 2924
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| TET3 |
cd18897 |
oxygenase domain of ten-eleven translocation (TET)3 methylcytosine dioxygenase and similar ... |
836-1160 |
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: 725.63 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941150 836 CDCVEQIVEKDEGPYYTHLGSGPTVASIRELMEDRYGEKGKAIRIEKVIYTGKEGKSSRGCPIAKWVIRRHTLEEKLLCL 915
Cdd:cd18897 1 CDCVEQILEKDEGPYYTHLGSGPTVASIRELMEERYGEKGKAIRIEKVIYTGKEGKSSRGCPIAKWVIRRSSEEEKLLCL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941150 916 VRHRAGHHCQNAVIVILILAWEGIPRSLGDTLYQELTDTLRKYGNPTSRRCGLNDDRTCACQGKDPNTCGASFSFGCSWS 995
Cdd:cd18897 81 VRHRAGHHCQNAVIVILILAWEGIPRALGDKLYQELTETLTKYGNPTSRRCGLNDDRTCACQGKDPNTCGASFSFGCSWS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941150 996 MYFNGCKYARSKTPRKFRLTGDNPKEEEVLRNSFQDLATEVAPLYKRLAPQAYQNQVTNEDVAIDCRLGLKEGRPFSGVT 1075
Cdd:cd18897 161 MYFNGCKYARSKTPRKFRLIGDNPKEEENLRDNFQDLATEVAPLYKRLAPQAYQNQVTNEDIAIDCRLGLKEGRPFSGVT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941150 1076 ACMDFCAHAHKDQHNLYNGCTVVCTLTKEDNRCVGQIPEDEQLHVLPLYKMASTDEFGSEENQNAKVSSGAIQVLTAFPR 1155
Cdd:cd18897 241 ACMDFCAHAHKDQHNLYNGCTVVCTLTKEDNRTVGKIPEDEQLHVLPLYKMSTTDEFGSEENQNEKIGSGAIQVLTSFPR 320
|
....*
gi 568941150 1156 EVRRL 1160
Cdd:cd18897 321 EVREV 325
|
|
| TET3 |
cd18897 |
oxygenase domain of ten-eleven translocation (TET)3 methylcytosine dioxygenase and similar ... |
1612-1774 |
3.81e-81 |
|
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: 275.33 E-value: 3.81e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941150 1612 DPFSLEEGTAEEPPSkGVVKEEKSGPtveEDEEELWSDSEHNFLDENIGGVAVAPAHCSILIECARRELHATTPLKKPNR 1691
Cdd:cd18897 295 DEFGSEENQNEKIGS-GAIQVLTSFP---REVREVWSDSEHNFLDENIGGVAVAPAHGSILIECARRELHATTPLKKPNR 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941150 1692 CHPTRISLVFYQHKNLNQPNHGLALWEAKMKQLAERARQRQEEAARLGLgQQEAKLYGKKRKWGGAMVAEPQHKEKKGAI 1771
Cdd:cd18897 371 CHPTRISLVFYQHKNLNQPNHGLALWEAKMKLLAERARARQEEAARLGL-QQEIKPYGKKRKWGGAPAAEPQPKEKKDKI 449
|
...
gi 568941150 1772 PTR 1774
Cdd:cd18897 450 PTR 452
|
|
| Tet_JBP |
pfam12851 |
Oxygenase domain of the 2OGFeDO superfamily; A double-stranded beta helix (DSBH) fold domain ... |
993-1120 |
5.04e-45 |
|
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: 160.62 E-value: 5.04e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941150 993 SWSMYFNGCKYARSKTPRKFRLTGDNPKEEEVLRNSFQDLATEVAPLYKRLAPQAYQNQVTNEDVAIDCRLGLKEGRPFS 1072
Cdd:pfam12851 1 SWSMYYDGCKFPGPRKPRKFSFTPRNPKEEIKLEDELQELAALLGAIYKQIAPDLYENQIEYEQDAAICRLGRKWGRPFS 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 568941150 1073 GVTACMDFCAHAHKDQHNLYNGCTVVCTLTkedNRCVGQIPEDEQLHV 1120
Cdd:pfam12851 81 GVTVNLNFETISHRDLGNFRNGSTLLCTLT---GRYEGGRLALPQLGV 125
|
|
| zf-CXXC |
pfam02008 |
CXXC zinc finger domain; This domain contains eight conserved cysteine residues that bind to ... |
50-89 |
1.82e-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: 63.53 E-value: 1.82e-12
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 568941150 50 GRKKRKRCGTCDPCRRLENCGSCTSCTNR-------RTHQICKLRKC 89
Cdd:pfam02008 2 NRRKRRRCGVCEGCQRPEDCGQCSFCLDMpkfggpgKKKQKCRLRRC 48
|
|
| Tet_JBP |
pfam12851 |
Oxygenase domain of the 2OGFeDO superfamily; A double-stranded beta helix (DSBH) fold domain ... |
1661-1705 |
8.41e-10 |
|
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: 59.32 E-value: 8.41e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 568941150 1661 GVAVAPAHCSILIECARRELHATTPLKKPNRchPTRISLVFYQHK 1705
Cdd:pfam12851 124 GVAFAPTPGTVLIFCGKSLEHGVTPVKNPNR--WERVSLVFYWHK 166
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
297-760 |
1.84e-08 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 59.95 E-value: 1.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941150 297 QGRPRLPGALPPSEAGLPAPSTRPPllSSEVPQVPPLEGLPLSQSALSiakeknislQTAIAIEALTQLSSALPQPSHST 376
Cdd:PHA03247 2595 SARPRAPVDDRGDPRGPAPPSPLPP--DTHAPDPPPPSPSPAANEPDP---------HPPPTVPPPERPRDDPAPGRVSR 2663
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941150 377 SQASCPLPEALSPSAPFRSPQ-SYLRAPSWPVV----PPEEHPSFAPDSPAFPPATPRPEFSEAWGTDTPPATPRnswPV 451
Cdd:PHA03247 2664 PRRARRLGRAAQASSPPQRPRrRAARPTVGSLTsladPPPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAA---PA 2740
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941150 452 PRPSPDpmaeleqllGSASDYIQSVFKRPEAL-----PTKPKVKVEAPSSSPAPVPSPISQREAPLLSSEPDTHQKAQTA 526
Cdd:PHA03247 2741 PPAVPA---------GPATPGGPARPARPPTTagppaPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAV 2811
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941150 527 LqqhlhhkrnlfleqAQDASFPTSTEPQAPgwwaPPGSPAPRPPDKPPKEKKKKPPTPAGGPVgaektTPGIKTSVRKPI 606
Cdd:PHA03247 2812 L--------------APAAALPPAASPAGP----LPPPTSAQPTAPPPPPGPPPPSLPLGGSV-----APGGDVRRRPPS 2868
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941150 607 QikKSRSRDMQPLFLPVRQIVleglKPQASEGQAPLP-AQLSVPPPASQGAASQSCATPLTPEPSLALFAPSPSGDSLLP 685
Cdd:PHA03247 2869 R--SPAAKPAAPARPPVRRLA----RPAVSRSTESFAlPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPP 2942
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568941150 686 PtqemrSPSPMVALQSGSTGGPLPPADDKLeelirqfeaefgdsfgLPGPPSVPIQEPENQSTCLPAPESPFATR 760
Cdd:PHA03247 2943 L-----APTTDPAGAGEPSGAVPQPWLGAL----------------VPGRVAVPRFRVPQPAPSREAPASSTPPL 2996
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
126-461 |
5.87e-06 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 51.86 E-value: 5.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941150 126 SPVD--GPVPGQMDSGPVYHGDSRQLSTSGAPVNGAREPAGPGLLGAAGPWRVDQKPDWEAASGPTHAARLEDAHDLVAF 203
Cdd:PHA03247 2600 APVDdrGDPRGPAPPSPLPPDTHAPDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSP 2679
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941150 204 S------AVAEAVSSYGALstrlyetfnremsreAGSNGRGPRPESCSEGSEDLDTLQTALALARHGMKPPNCTCDGPEC 277
Cdd:PHA03247 2680 PqrprrrAARPTVGSLTSL---------------ADPPPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAV 2744
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941150 278 PDflewlegkikSMAMEGGQGRPRLPG--ALPPSEAGLPAPSTRPPLLSSEVPQVPPLEGLPLSQSALSIAKEKNISLQT 355
Cdd:PHA03247 2745 PA----------GPATPGGPARPARPPttAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAP 2814
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941150 356 AIAIEALTQLSSALPQPSHST----SQASCPLPEALS------PSAPFRSpqsylRAPSWPVVPPEEHPSFAPDSPAFPP 425
Cdd:PHA03247 2815 AAALPPAASPAGPLPPPTSAQptapPPPPGPPPPSLPlggsvaPGGDVRR-----RPPSRSPAAKPAAPARPPVRRLARP 2889
|
330 340 350
....*....|....*....|....*....|....*.
gi 568941150 426 ATPRPEFSEAWGTDtPPATPRNSWPVPRPSPDPMAE 461
Cdd:PHA03247 2890 AVSRSTESFALPPD-QPERPPQPQAPPPPQPQPQPP 2924
|
|
| Atrophin-1 |
pfam03154 |
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ... |
303-431 |
8.21e-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: 41.29 E-value: 8.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941150 303 PGALPPSEAGLPAPSTRPPLLSSEVPQVPPLEGLPLSQSALSIAKEKNISLQTAIAIEALTQLSSALPQPSHSTSQASCP 382
Cdd:pfam03154 414 PLQLMPQSQQLPPPPAQPPVLTQSQSLPPPAASHPPTSGLHQVPSQSPFPQHPFVPGGPPPITPPSGPPTSTSSAMPGIQ 493
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 568941150 383 LPEALSPSAPFRSPQSyLRAPSWPVVPPEEHPSFA--PDSPAFPPATPRPE 431
Cdd:pfam03154 494 PPSSASVSSSGPVPAA-VSCPLPPVQIKEEALDEAeePESPPPPPRSPSPE 543
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| TET3 |
cd18897 |
oxygenase domain of ten-eleven translocation (TET)3 methylcytosine dioxygenase and similar ... |
836-1160 |
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: 725.63 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941150 836 CDCVEQIVEKDEGPYYTHLGSGPTVASIRELMEDRYGEKGKAIRIEKVIYTGKEGKSSRGCPIAKWVIRRHTLEEKLLCL 915
Cdd:cd18897 1 CDCVEQILEKDEGPYYTHLGSGPTVASIRELMEERYGEKGKAIRIEKVIYTGKEGKSSRGCPIAKWVIRRSSEEEKLLCL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941150 916 VRHRAGHHCQNAVIVILILAWEGIPRSLGDTLYQELTDTLRKYGNPTSRRCGLNDDRTCACQGKDPNTCGASFSFGCSWS 995
Cdd:cd18897 81 VRHRAGHHCQNAVIVILILAWEGIPRALGDKLYQELTETLTKYGNPTSRRCGLNDDRTCACQGKDPNTCGASFSFGCSWS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941150 996 MYFNGCKYARSKTPRKFRLTGDNPKEEEVLRNSFQDLATEVAPLYKRLAPQAYQNQVTNEDVAIDCRLGLKEGRPFSGVT 1075
Cdd:cd18897 161 MYFNGCKYARSKTPRKFRLIGDNPKEEENLRDNFQDLATEVAPLYKRLAPQAYQNQVTNEDIAIDCRLGLKEGRPFSGVT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941150 1076 ACMDFCAHAHKDQHNLYNGCTVVCTLTKEDNRCVGQIPEDEQLHVLPLYKMASTDEFGSEENQNAKVSSGAIQVLTAFPR 1155
Cdd:cd18897 241 ACMDFCAHAHKDQHNLYNGCTVVCTLTKEDNRTVGKIPEDEQLHVLPLYKMSTTDEFGSEENQNEKIGSGAIQVLTSFPR 320
|
....*
gi 568941150 1156 EVRRL 1160
Cdd:cd18897 321 EVREV 325
|
|
| TET |
cd18892 |
oxygenase domain of ten-eleven translocation (TET)1, TET2, and TET3 methylcytosine ... |
836-1170 |
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: 660.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941150 836 CDCVEQIV-EKDEGPYYTHLGSGPTVASIRELMEDRYGEKGKAIRIEKVIYTGKEGKSSRGCPIAKWVIRRHTLEEKLLC 914
Cdd:cd18892 1 CGCFPPDEsPPEPGPYYTHLGAGPSLAALRELLEKRTGVTGKAIRIEKVIYTGKEGKTSQGCPIAKWIIRRSSLEEKYLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941150 915 LVRHRAGHHCQNAVIVILILAWEGIPRSLGDTLYQELTDTLRKYGNPTSRRCGLNDDRTCACQGKDPNTCGASFSFGCSW 994
Cdd:cd18892 81 LVKHRPGHFCHSAFIVICIVAWEGVPQSNADELYSLLTDKLNKFGLPTKRRCGTNEERTCACQGLDPETCGASFSFGCSW 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941150 995 SMYFNGCKYARSKTPRKFRLTGdnPKEEEVLRNSFQDLATEVAPLYKRLAPQAYQNQVTNEDVAIDCRLGLKEGRPFSGV 1074
Cdd:cd18892 161 SMYYNGCKFARSKTVRKFRLSD--KSEEEELEDKLQNLATHLAPLYKSLAPDSYKNQVQFEEEALDCRLGLKPGRPFSGV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941150 1075 TACMDFCAHAHKDQHNLYNGCTVVCTLTKEDNRCvGQIPEDEQLHVLPLYKMASTDEFGSEENQNAKVSSGAIQVLTAFP 1154
Cdd:cd18892 239 TACVDFCAHAHKDLHNMNNGCTVVVTLTKHRNLT-KPEPEQLHVLPLYLYDMTDEDEFGSVEGQEEKVRNGSIEVLTKYP 317
|
330
....*....|....*.
gi 568941150 1155 REVRRLPEPAKSCRQR 1170
Cdd:cd18892 318 CEVREYWSDSEECFLD 333
|
|
| TET1 |
cd18895 |
oxygenase domain of ten-eleven translocation (TET)1 methylcytosine dioxygenase and similar ... |
836-1160 |
0e+00 |
|
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: 621.16 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941150 836 CDCVEQIVEKDEGPYYTHLGSGPTVASIRELMEDRYGEKGKAIRIEKVIYTGKEGKSSRGCPIAKWVIRRHTLEEKLLCL 915
Cdd:cd18895 1 CDCVEQIIEKDEGPYYTHLGAGPSVAAVREIMENRYGEKGNAIRIEVVVYTGKEGKSSQGCPIAKWVIRRSSDEEKLLCL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941150 916 VRHRAGHHCQNAVIVILILAWEGIPRSLGDTLYQELTDTLRKYGNPTSRRCGLNDDRTCACQGKDPNTCGASFSFGCSWS 995
Cdd:cd18895 81 VRQRAGHHCQTAVIVILILAWEGIPRLLADRLYQELTQTLKKYGSPTSRRCALNEDRTCACQGLDPETCGASFSFGCSWS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941150 996 MYFNGCKYARSKTPRKFRLTGDNPKEEEVLRNSFQDLATEVAPLYKRLAPQAYQNQVTNEDVAIDCRLGLKEGRPFSGVT 1075
Cdd:cd18895 161 MYFNGCKFARSKYPRKFRLLTDDPKEEENLESNLQNLATDVAPVYKKLAPEAFQNQVENENVAPDCRLGSKEGRPFSGVT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941150 1076 ACMDFCAHAHKDQHNLYNGCTVVCTLTKEDNRCVGQIPEDEQLHVLPLYKMASTDEFGSEENQNAKVSSGAIQVLTAFPR 1155
Cdd:cd18895 241 ACIDFCAHAHKDTHNMHNGSTVVCTLTKEDNRSVGVIPEDEQLHVLPLYKISDTDEFGSEEGQEAKIKNGAIQVLSAFPR 320
|
....*
gi 568941150 1156 EVRRL 1160
Cdd:cd18895 321 EVREV 325
|
|
| TET2 |
cd18896 |
oxygenase domain of ten-eleven translocation (TET)2 methylcytosine dioxygenase and similar ... |
832-1172 |
0e+00 |
|
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: 613.13 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941150 832 EFPTCDCVEQIVEKDEGPYYTHLGSGPTVASIRELMEDRYGEKGKAIRIEKVIYTGKEGKSSRGCPIAKWVIRRHTLEEK 911
Cdd:cd18896 1 DFPSCSCVEQIIEKDEGPYYTHLGAGPNVAAIREIMEERFGQKGKAIRIERVIYTGKEGKSSQGCPIAKWVIRRSSEEEK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941150 912 LLCLVRHRAGHHCQNAVIVILILAWEGIPRSLGDTLYQELTDTLRKYGNPTSRRCGLNDDRTCACQGKDPNTCGASFSFG 991
Cdd:cd18896 81 LLCLVRERAGHSCETAVIVILILVWEGIPISLADKLYSELTDTLRKYGTLTNRRCALNEERTCACQGLDPETCGASFSFG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941150 992 CSWSMYFNGCKYARSKTPRKFRLTGDNPKEEEVLRNSFQDLATEVAPLYKRLAPQAYQNQVTNEDVAIDCRLGLKEGRPF 1071
Cdd:cd18896 161 CSWSMYYNGCKFARSKIPRKFKLLGDDPKEEEKLESNLQNLSTLMAPTYKKLAPDAYNNQIEYEHRAPDCRLGLKEGRPF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941150 1072 SGVTACMDFCAHAHKDQHNLYNGCTVVCTLTKEDNRCVGQIPEDEQLHVLPLYKMASTDEFGSEENQNAKVSSGAIQVLT 1151
Cdd:cd18896 241 SGVTACLDFCAHAHRDLHNMQNGSTLVCTLTREDNREIGKIPEDEQLHVLPLYKVSDVDEFGSTEAQEEKKRNGAIQVLS 320
|
330 340
....*....|....*....|.
gi 568941150 1152 AFPREVRRLPEPAKSCRQRQL 1172
Cdd:cd18896 321 SFRRKVRMLAEPVKTCRQRKL 341
|
|
| TET3 |
cd18897 |
oxygenase domain of ten-eleven translocation (TET)3 methylcytosine dioxygenase and similar ... |
1612-1774 |
3.81e-81 |
|
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: 275.33 E-value: 3.81e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941150 1612 DPFSLEEGTAEEPPSkGVVKEEKSGPtveEDEEELWSDSEHNFLDENIGGVAVAPAHCSILIECARRELHATTPLKKPNR 1691
Cdd:cd18897 295 DEFGSEENQNEKIGS-GAIQVLTSFP---REVREVWSDSEHNFLDENIGGVAVAPAHGSILIECARRELHATTPLKKPNR 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941150 1692 CHPTRISLVFYQHKNLNQPNHGLALWEAKMKQLAERARQRQEEAARLGLgQQEAKLYGKKRKWGGAMVAEPQHKEKKGAI 1771
Cdd:cd18897 371 CHPTRISLVFYQHKNLNQPNHGLALWEAKMKLLAERARARQEEAARLGL-QQEIKPYGKKRKWGGAPAAEPQPKEKKDKI 449
|
...
gi 568941150 1772 PTR 1774
Cdd:cd18897 450 PTR 452
|
|
| Tet_JBP |
cd14946 |
oxygenase domain of ten-eleven translocation (TET) enzymes, J-binding proteins (JBPs), and ... |
863-1125 |
2.94e-58 |
|
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: 202.61 E-value: 2.94e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941150 863 IRELMEDRYG-EKGKAIRIEKVIYTGKEGKSsRGCPIAKWVIRRhtleEKLLCLVRHRAGhhcqnavIVILILAWEGIPR 941
Cdd:cd14946 1 LLENMLSKCGtQQSFANANITLKYEGKEGKS-QGCPKALKNVRT----SKLAYFVCDHDG-------SVILAYVPEVLPK 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941150 942 SLGDTLYQELTDTLRKYGNptsrrcglnddrtcacqgKDPNTCGASFSFGCSWSMYFNGCKyarsktprkfRLTGDNPKE 1021
Cdd:cd14946 69 ELVEEFTEKLESIQTKRGT------------------LDPETKGDTGYSGILDNSMPFNYV----------TADLSQELG 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941150 1022 EEVLRNSFQDLATEVAPLYKRLAPQAYQNQVTNEDVAIDCRLGLKEGRPFSGVTACMD-FCAHAHKDQHNLYNGCTVVCT 1100
Cdd:cd14946 121 QYLSEIVNPQISYYISKLLTCVSPRTINYLVEYEHRSLNDSYYALNNCLYPSTAFNSLkRIRKPHKDNLDIQNGPSSLFY 200
|
250 260
....*....|....*....|....*
gi 568941150 1101 LTKEDNrcvgqipeDEQLHVLPLYK 1125
Cdd:cd14946 201 FGNFQN--------TEGYLELTLKK 217
|
|
| TET2 |
cd18896 |
oxygenase domain of ten-eleven translocation (TET)2 methylcytosine dioxygenase and similar ... |
1643-1738 |
1.31e-47 |
|
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: 177.47 E-value: 1.31e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941150 1643 EEELWSDSEHNFLDENIGGVAVAPAHCSILIECARRELHATTPLKKPNRCHPTRISLVFYQHKNLNQPNHGLALWEAKMk 1722
Cdd:cd18896 342 EDEVWSDSEQSFLDPDIGGVAVAPSHGSILIECAKRELHATTPLKNPNRNHPTRISLVFYQHKSMNEPKHGLALWEAKM- 420
|
90
....*....|....*.
gi 568941150 1723 qlAERARQRQEEAARL 1738
Cdd:cd18896 421 --AEKAREKEEECEKY 434
|
|
| TET1 |
cd18895 |
oxygenase domain of ten-eleven translocation (TET)1 methylcytosine dioxygenase and similar ... |
1612-1734 |
2.76e-46 |
|
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: 172.79 E-value: 2.76e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941150 1612 DPFSLEEGTaEEPPSKGVVKEEKSGPtveEDEEELWSDSEHNFLDENIGGVAVAPAHCSILIECARRELHATTPLKKPNR 1691
Cdd:cd18895 295 DEFGSEEGQ-EAKIKNGAIQVLSAFP---REVREVWSDSEHNFLDEDIGGVAVAPSHGSILIECARRELHATTPIKKPNR 370
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 568941150 1692 CHPTRISLVFYQHKNLNQPNHGLALWEAKMkqlAERARQRQEE 1734
Cdd:cd18895 371 NHPTRISLVFYQHKNLNEPKHGLALWEAKM---AEKAKEKEKE 410
|
|
| Tet_JBP |
pfam12851 |
Oxygenase domain of the 2OGFeDO superfamily; A double-stranded beta helix (DSBH) fold domain ... |
993-1120 |
5.04e-45 |
|
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: 160.62 E-value: 5.04e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941150 993 SWSMYFNGCKYARSKTPRKFRLTGDNPKEEEVLRNSFQDLATEVAPLYKRLAPQAYQNQVTNEDVAIDCRLGLKEGRPFS 1072
Cdd:pfam12851 1 SWSMYYDGCKFPGPRKPRKFSFTPRNPKEEIKLEDELQELAALLGAIYKQIAPDLYENQIEYEQDAAICRLGRKWGRPFS 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 568941150 1073 GVTACMDFCAHAHKDQHNLYNGCTVVCTLTkedNRCVGQIPEDEQLHV 1120
Cdd:pfam12851 81 GVTVNLNFETISHRDLGNFRNGSTLLCTLT---GRYEGGRLALPQLGV 125
|
|
| TET |
cd18892 |
oxygenase domain of ten-eleven translocation (TET)1, TET2, and TET3 methylcytosine ... |
1645-1721 |
2.84e-39 |
|
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: 152.06 E-value: 2.84e-39
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568941150 1645 ELWSDSEHNFLDENIGGVAVAPAHCSILIECARRELHATTPLKKPNRCHPTRISLVFYQHKNLNQPNHGLALWEAKM 1721
Cdd:cd18892 322 EYWSDSEECFLDPDIGGVAIALSHGSVLFECAKRELHATTPLKNPNRQHPTRISLVFYQHKNLNYSRHGLAEYEAKM 398
|
|
| zf-CXXC |
pfam02008 |
CXXC zinc finger domain; This domain contains eight conserved cysteine residues that bind to ... |
50-89 |
1.82e-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: 63.53 E-value: 1.82e-12
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 568941150 50 GRKKRKRCGTCDPCRRLENCGSCTSCTNR-------RTHQICKLRKC 89
Cdd:pfam02008 2 NRRKRRRCGVCEGCQRPEDCGQCSFCLDMpkfggpgKKKQKCRLRRC 48
|
|
| Tet_JBP |
cd14946 |
oxygenase domain of ten-eleven translocation (TET) enzymes, J-binding proteins (JBPs), and ... |
1659-1705 |
1.30e-11 |
|
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: 67.02 E-value: 1.30e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 568941150 1659 IGGVAVAPAHCSILIECARRELHATTPLKKPNRcHPTRISLVFYQHK 1705
Cdd:cd14946 219 IGNCAVFVQPGDVLFFKGNEYKHVVTNITNPNN-HGWRISLVYYAHK 264
|
|
| Tet_JBP |
pfam12851 |
Oxygenase domain of the 2OGFeDO superfamily; A double-stranded beta helix (DSBH) fold domain ... |
1661-1705 |
8.41e-10 |
|
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: 59.32 E-value: 8.41e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 568941150 1661 GVAVAPAHCSILIECARRELHATTPLKKPNRchPTRISLVFYQHK 1705
Cdd:pfam12851 124 GVAFAPTPGTVLIFCGKSLEHGVTPVKNPNR--WERVSLVFYWHK 166
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
297-760 |
1.84e-08 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 59.95 E-value: 1.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941150 297 QGRPRLPGALPPSEAGLPAPSTRPPllSSEVPQVPPLEGLPLSQSALSiakeknislQTAIAIEALTQLSSALPQPSHST 376
Cdd:PHA03247 2595 SARPRAPVDDRGDPRGPAPPSPLPP--DTHAPDPPPPSPSPAANEPDP---------HPPPTVPPPERPRDDPAPGRVSR 2663
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941150 377 SQASCPLPEALSPSAPFRSPQ-SYLRAPSWPVV----PPEEHPSFAPDSPAFPPATPRPEFSEAWGTDTPPATPRnswPV 451
Cdd:PHA03247 2664 PRRARRLGRAAQASSPPQRPRrRAARPTVGSLTsladPPPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAA---PA 2740
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941150 452 PRPSPDpmaeleqllGSASDYIQSVFKRPEAL-----PTKPKVKVEAPSSSPAPVPSPISQREAPLLSSEPDTHQKAQTA 526
Cdd:PHA03247 2741 PPAVPA---------GPATPGGPARPARPPTTagppaPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAV 2811
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941150 527 LqqhlhhkrnlfleqAQDASFPTSTEPQAPgwwaPPGSPAPRPPDKPPKEKKKKPPTPAGGPVgaektTPGIKTSVRKPI 606
Cdd:PHA03247 2812 L--------------APAAALPPAASPAGP----LPPPTSAQPTAPPPPPGPPPPSLPLGGSV-----APGGDVRRRPPS 2868
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941150 607 QikKSRSRDMQPLFLPVRQIVleglKPQASEGQAPLP-AQLSVPPPASQGAASQSCATPLTPEPSLALFAPSPSGDSLLP 685
Cdd:PHA03247 2869 R--SPAAKPAAPARPPVRRLA----RPAVSRSTESFAlPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPP 2942
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568941150 686 PtqemrSPSPMVALQSGSTGGPLPPADDKLeelirqfeaefgdsfgLPGPPSVPIQEPENQSTCLPAPESPFATR 760
Cdd:PHA03247 2943 L-----APTTDPAGAGEPSGAVPQPWLGAL----------------VPGRVAVPRFRVPQPAPSREAPASSTPPL 2996
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
384-835 |
1.53e-06 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 53.79 E-value: 1.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941150 384 PEALSPSAPFRSPQSYLRAPSWPVVPP---EEHPSFAPDSPAFPPATPRpefSEAW-------------------GTDTP 441
Cdd:PHA03247 2484 AEARFPFAAGAAPDPGGGGPPDPDAPPapsRLAPAILPDEPVGEPVHPR---MLTWirgleelasddagdpppplPPAAP 2560
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941150 442 PATPRNSWPVPRPSPDPmaeleqllgsASDYIQSVFKRPEALP--TKPKVKVEapssspapvPSPISQREAPLLSSEPDT 519
Cdd:PHA03247 2561 PAAPDRSVPPPRPAPRP----------SEPAVTSRARRPDAPPqsARPRAPVD---------DRGDPRGPAPPSPLPPDT 2621
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941150 520 HQkaqtalqqhlhhkrnlfLEQAQDASFPTSTEPQAPGWWAPPGSPAPRPPDKPPKEKKKKPPTPAGGPVGAEKTTPGIK 599
Cdd:PHA03247 2622 HA-----------------PDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSPPQRPR 2684
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941150 600 TSVRKPIQIKKSRSRD-------MQPLFLPVRQIVLEGLKPQASEGQAPLPAQLSVPPPASQGAASQ-SCATPLTPEPSL 671
Cdd:PHA03247 2685 RRAARPTVGSLTSLADpppppptPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPgGPARPARPPTTA 2764
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941150 672 ALFAPSPSGDSLLPPTQemRSPSPMVALQSGSTGGPLPPADDKLEELIRQFEAEFGDSFGLPGPPSVPiqEPENQSTCLP 751
Cdd:PHA03247 2765 GPPAPAPPAAPAAGPPR--RLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPP--PTSAQPTAPP 2840
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941150 752 APESPFATRSPKKIKIESSGAVtvlsttcfhSEEGGQEATPTKAENPLTPTLSGFLESPLKYLDTPTKSLLDTPAKKAQS 831
Cdd:PHA03247 2841 PPPGPPPPSLPLGGSVAPGGDV---------RRRPPSRSPAAKPAAPARPPVRRLARPAVSRSTESFALPPDQPERPPQP 2911
|
....
gi 568941150 832 EFPT 835
Cdd:PHA03247 2912 QAPP 2915
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
126-461 |
5.87e-06 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 51.86 E-value: 5.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941150 126 SPVD--GPVPGQMDSGPVYHGDSRQLSTSGAPVNGAREPAGPGLLGAAGPWRVDQKPDWEAASGPTHAARLEDAHDLVAF 203
Cdd:PHA03247 2600 APVDdrGDPRGPAPPSPLPPDTHAPDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSP 2679
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941150 204 S------AVAEAVSSYGALstrlyetfnremsreAGSNGRGPRPESCSEGSEDLDTLQTALALARHGMKPPNCTCDGPEC 277
Cdd:PHA03247 2680 PqrprrrAARPTVGSLTSL---------------ADPPPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAV 2744
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941150 278 PDflewlegkikSMAMEGGQGRPRLPG--ALPPSEAGLPAPSTRPPLLSSEVPQVPPLEGLPLSQSALSIAKEKNISLQT 355
Cdd:PHA03247 2745 PA----------GPATPGGPARPARPPttAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAP 2814
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941150 356 AIAIEALTQLSSALPQPSHST----SQASCPLPEALS------PSAPFRSpqsylRAPSWPVVPPEEHPSFAPDSPAFPP 425
Cdd:PHA03247 2815 AAALPPAASPAGPLPPPTSAQptapPPPPGPPPPSLPlggsvaPGGDVRR-----RPPSRSPAAKPAAPARPPVRRLARP 2889
|
330 340 350
....*....|....*....|....*....|....*.
gi 568941150 426 ATPRPEFSEAWGTDtPPATPRNSWPVPRPSPDPMAE 461
Cdd:PHA03247 2890 AVSRSTESFALPPD-QPERPPQPQAPPPPQPQPQPP 2924
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
298-760 |
1.64e-05 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 50.32 E-value: 1.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941150 298 GRPRLPGALPPSEAGLPAPSTRPPLLSSEVP---QVPP--------LEGL----------PLSQSALSIAKEKNISLqta 356
Cdd:PHA03247 2494 AAPDPGGGGPPDPDAPPAPSRLAPAILPDEPvgePVHPrmltwirgLEELasddagdpppPLPPAAPPAAPDRSVPP--- 2570
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941150 357 iaiealtqlSSALPQPSHSTSQAscplpEALSPSAPfrsPQSYL-RAPSWPVVPPEEHPSFAPDSPAF-----PPATPRP 430
Cdd:PHA03247 2571 ---------PRPAPRPSEPAVTS-----RARRPDAP---PQSARpRAPVDDRGDPRGPAPPSPLPPDThapdpPPPSPSP 2633
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941150 431 EFSEAWGTDT----PPATPRNSWPVPRPSPDPMAELEQLLGSASDYIQSvfKRPEALPtkPKVKVEAPSSSPAPVPSPIS 506
Cdd:PHA03247 2634 AANEPDPHPPptvpPPERPRDDPAPGRVSRPRRARRLGRAAQASSPPQR--PRRRAAR--PTVGSLTSLADPPPPPPTPE 2709
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941150 507 QREAPLLSSEPDTHQKAqtalqqhlhhkrnlfleQAQDASFPTSTEPQAPgwwAPPGSPAPRPPDKPPKEKKKKPPTPAG 586
Cdd:PHA03247 2710 PAPHALVSATPLPPGPA-----------------AARQASPALPAAPAPP---AVPAGPATPGGPARPARPPTTAGPPAP 2769
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941150 587 GPVGAEKTTPGIKTSVrkPIQIKKSRSRDMQPLFLPVRQIVLEGLKPQASEGQAPLPAQLSVPPPASQGAASQSCATPlt 666
Cdd:PHA03247 2770 APPAAPAAGPPRRLTR--PAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGP-- 2845
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941150 667 PEPSLALF-APSPSGD-SLLPPTqemRSPSPMvalqsgstggPLPPADDKLEELIRQFEAEFGDSFGLPGPPSVPIQEPE 744
Cdd:PHA03247 2846 PPPSLPLGgSVAPGGDvRRRPPS---RSPAAK----------PAAPARPPVRRLARPAVSRSTESFALPPDQPERPPQPQ 2912
|
490
....*....|....*.
gi 568941150 745 NQSTCLPAPESPFATR 760
Cdd:PHA03247 2913 APPPPQPQPQPPPPPQ 2928
|
|
| PRK14950 |
PRK14950 |
DNA polymerase III subunits gamma and tau; Provisional |
343-483 |
3.48e-05 |
|
DNA polymerase III subunits gamma and tau; Provisional
Pssm-ID: 237864 [Multi-domain] Cd Length: 585 Bit Score: 48.65 E-value: 3.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941150 343 LSIAKEKNISLQTAIaIEALTQLSSAlPQPSHSTSQASCPLPEALSPSAPFRSPQSyLRAPSWPVVPPEEHPsfaPDSPA 422
Cdd:PRK14950 341 LRTTSYGQLPLELAV-IEALLVPVPA-PQPAKPTAAAPSPVRPTPAPSTRPKAAAA-ANIPPKEPVRETATP---PPVPP 414
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568941150 423 FPPATPRPEFSEAWGTDTPPATPRNSWPVPRPSPDP----------MAELEQLLGSASDYIQSVFKRPEAL 483
Cdd:PRK14950 415 RPVAPPVPHTPESAPKLTRAAIPVDEKPKYTPPAPPkeeekaliadGDVLEQLEAIWKQILRDVPPRSPAV 485
|
|
| PRK12323 |
PRK12323 |
DNA polymerase III subunit gamma/tau; |
588-761 |
5.49e-04 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 237057 [Multi-domain] Cd Length: 700 Bit Score: 44.87 E-value: 5.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941150 588 PVGAEKTTPGIKTSVRKPIQIKKSRSRDMQPLfLPVRQIVLEGLKPQASEGQAPLPAQLSVPPPASQGAASQSCATPLTP 667
Cdd:PRK12323 402 PPAAPAAAPAAAAAARAVAAAPARRSPAPEAL-AAARQASARGPGGAPAPAPAPAAAPAAAARPAAAGPRPVAAAAAAAP 480
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941150 668 EPSLALFAPSPSgDSLLPPTQEMRSPSPMVALQSGSTGGPLPPADDKLEELIRQFEAEFGDSfgLPGPPSVPIQEPENQS 747
Cdd:PRK12323 481 ARAAPAAAPAPA-DDDPPPWEELPPEFASPAPAQPDAAPAGWVAESIPDPATADPDDAFETL--APAPAAAPAPRAAAAT 557
|
170
....*....|....
gi 568941150 748 TCLPAPESPFATRS 761
Cdd:PRK12323 558 EPVVAPRPPRASAS 571
|
|
| PRK12323 |
PRK12323 |
DNA polymerase III subunit gamma/tau; |
295-514 |
2.80e-03 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 237057 [Multi-domain] Cd Length: 700 Bit Score: 42.56 E-value: 2.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941150 295 GGQGRPRLPGALPPSEaglPAPSTRPPLLSSEVPQVPPLEGLPLSQSALSIAKEKNISLQTAIAIEALtqlssalpqPSH 374
Cdd:PRK12323 369 GGGAGPATAAAAPVAQ---PAPAAAAPAAAAPAPAAPPAAPAAAPAAAAAARAVAAAPARRSPAPEAL---------AAA 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941150 375 STSQASCPLPEALSPSAPFRSPQSYLRAPSWPVVPPeehpsfaPDSPAFPPATPRPEFSEAWGTDTPPATPRNSWPVPRP 454
Cdd:PRK12323 437 RQASARGPGGAPAPAPAPAAAPAAAARPAAAGPRPV-------AAAAAAAPARAAPAAAPAPADDDPPPWEELPPEFASP 509
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941150 455 SPDPMAELEQLLGSASDYIQSVFKRPEALPTKPKVKVEAPSSSPAPVPSPISQREAPLLS 514
Cdd:PRK12323 510 APAQPDAAPAGWVAESIPDPATADPDDAFETLAPAPAAAPAPRAAAATEPVVAPRPPRAS 569
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
278-711 |
3.27e-03 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 42.47 E-value: 3.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941150 278 PDFLEWLEgkiksMAMEGGQGRPRlpgalPPSEAGLPAPStrppLLSSEVPQVPPLEGlplsqsalsiAKEKNISLQTAI 357
Cdd:PHA03307 5 PDLYDLIE-----AAAEGGEFFPR-----PPATPGDAADD----LLSGSQGQLVSDSA----------ELAAVTVVAGAA 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941150 358 AIEALTQLSSALPQPSH--STSQASCPLPEALSPSAPFRSPQSYLRAPSWPVVPPEEHPSFAPDSPAFPPATPRPEF--- 432
Cdd:PHA03307 61 ACDRFEPPTGPPPGPGTeaPANESRSTPTWSLSTLAPASPAREGSPTPPGPSSPDPPPPTPPPASPPPSPAPDLSEMlrp 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941150 433 ---SEAWGTDTPPATPRNSWPVPRPSPDPmaeleqllGSASDYIQSVfkrPEALPTKPKVKVEAPSSSPAPVPSPISQRE 509
Cdd:PHA03307 141 vgsPGPPPAASPPAAGASPAAVASDAASS--------RQAALPLSSP---EETARAPSSPPAEPPPSTPPAAASPRPPRR 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941150 510 APLLSSEPDTHQKAQTalqqhlhhkRNLFLEQAQDASFPTSTEPQAPGWWAPPGSPAPRPPDKPPKEKKKKPPTPAGGPV 589
Cdd:PHA03307 210 SSPISASASSPAPAPG---------RSAADDAGASSSDSSSSESSGCGWGPENECPLPRPAPITLPTRIWEASGWNGPSS 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941150 590 GAEKTTPGIKTSVRKPiqiKKSRSRDMQPLFLPVRQIVLEGLKPQASegqaplpaqlSVPPPASQGAASQSCATPLTPEP 669
Cdd:PHA03307 281 RPGPASSSSSPRERSP---SPSPSSPGSGPAPSSPRASSSSSSSRES----------SSSSTSSSSESSRGAAVSPGPSP 347
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 568941150 670 SLALFAPSPSGDSLLPPTQEMRSPSPMVALQSGSTGGPLPPA 711
Cdd:PHA03307 348 SRSPSPSRPPPPADPSSPRKRPRPSRAPSSPAASAGRPTRRR 389
|
|
| dnaA |
PRK14086 |
chromosomal replication initiator protein DnaA; |
298-461 |
4.05e-03 |
|
chromosomal replication initiator protein DnaA;
Pssm-ID: 237605 [Multi-domain] Cd Length: 617 Bit Score: 42.12 E-value: 4.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941150 298 GRP-RLPGALPPSeAGLPAPSTRPPLLSSEvPQVP-----PLEGLPLSQ-SALSIAKEKNISLQTAI-AIEALTQLSSAL 369
Cdd:PRK14086 79 GRPiRIAITVDPS-AGEPAPPPPHARRTSE-PELPrpgrrPYEGYGGPRaDDRPPGLPRQDQLPTARpAYPAYQQRPEPG 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941150 370 PQPSHSTSQASCPLPEALSPSAPFRSPQSYLRAPSwpvvppeehpsfaPDSPafPPATPRPEFSEAWG---TDTPPATPR 446
Cdd:PRK14086 157 AWPRAADDYGWQQQRLGFPPRAPYASPASYAPEQE-------------RDRE--PYDAGRPEYDQRRRdydHPRPDWDRP 221
|
170
....*....|....*
gi 568941150 447 NSWPVPRPSPDPMAE 461
Cdd:PRK14086 222 RRDRTDRPEPPPGAG 236
|
|
| Atrophin-1 |
pfam03154 |
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ... |
303-431 |
8.21e-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: 41.29 E-value: 8.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941150 303 PGALPPSEAGLPAPSTRPPLLSSEVPQVPPLEGLPLSQSALSIAKEKNISLQTAIAIEALTQLSSALPQPSHSTSQASCP 382
Cdd:pfam03154 414 PLQLMPQSQQLPPPPAQPPVLTQSQSLPPPAASHPPTSGLHQVPSQSPFPQHPFVPGGPPPITPPSGPPTSTSSAMPGIQ 493
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 568941150 383 LPEALSPSAPFRSPQSyLRAPSWPVVPPEEHPSFA--PDSPAFPPATPRPE 431
Cdd:pfam03154 494 PPSSASVSSSGPVPAA-VSCPLPPVQIKEEALDEAeePESPPPPPRSPSPE 543
|
|
| |
