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Conserved domains on  [gi|1034612339|ref|XP_016859055|]
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methylcytosine dioxygenase TET3 isoform X1 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
TET3 cd18897
oxygenase domain of ten-eleven translocation (TET)3 methylcytosine dioxygenase and similar ...
 828-1168 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: 719.46  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034612339  828 CDCVEQIVEKDEGPYYTHLGSGPTVASIRELMEERYGEKGKAIRIEKVIYTGKEGKSSRGCPIAKWVIRRHTLEEKLLCL 907
Cdd:cd18897      1 CDCVEQILEKDEGPYYTHLGSGPTVASIRELMEERYGEKGKAIRIEKVIYTGKEGKSSRGCPIAKWVIRRSSEEEKLLCL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034612339  908 VRHRAGHHCQNAVIVILILAWEGIPRSLGDTLYQELTDTLRKYGNPTSRRCGLNDDRTCACQGKDPNTCGASFSFGCSWS 987
Cdd:cd18897     81 VRHRAGHHCQNAVIVILILAWEGIPRALGDKLYQELTETLTKYGNPTSRRCGLNDDRTCACQGKDPNTCGASFSFGCSWS 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034612339  988 MYFNGCKYARSKTPRKFRLAGDNPKEEEVLRKSFQDLATEVAPLYKRLAPQAYQNQlgplsqktsllqskgkVTNEEIAI 1067
Cdd:cd18897    161 MYFNGCKYARSKTPRKFRLIGDNPKEEENLRDNFQDLATEVAPLYKRLAPQAYQNQ----------------VTNEDIAI 224

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034612339 1068 DCRLGLKEGRPFAGVTACMDFCAHAHKDQHNLYNGCTVVCTLTKEDNRCVGKIPEDEQLHVLPLYKMANTDEFGSEENQN 1147
Cdd:cd18897    225 DCRLGLKEGRPFSGVTACMDFCAHAHKDQHNLYNGCTVVCTLTKEDNRTVGKIPEDEQLHVLPLYKMSTTDEFGSEENQN 304

                          330       340
                   ....*....|....*....|.
gi 1034612339 1148 AKVGSGAIQVLTAFPREVRRL 1168
Cdd:cd18897    305 EKIGSGAIQVLTSFPREVREV 325
Tet_JBP super family cl40427
oxygenase domain of ten-eleven translocation (TET) enzymes, J-binding proteins (JBPs), and ...
 1654-1782 3.68e-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: 275.71  E-value: 3.68e-81
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034612339 1654 LWSDSEHNFLDENIGGVAVAPAHGSILIECARRELHATTPLKKPNRCHPTRISLVFYQHKNLNQPNHGLALWEAKMKQLA 1733
Cdd:cd18897    325 VWSDSEHNFLDENIGGVAVAPAHGSILIECARRELHATTPLKKPNRCHPTRISLVFYQHKNLNQPNHGLALWEAKMKLLA 404

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 1034612339 1734 ERARARQEEAARLGLgQQEAKLYGKKRKWGGTVVAEPQQKEKKGVVPTR 1782
Cdd:cd18897    405 ERARARQEEAARLGL-QQEIKPYGKKRKWGGAPAAEPQPKEKKDKIPTR 452
zf-CXXC pfam02008
CXXC zinc finger domain; This domain contains eight conserved cysteine residues that bind to ...
 50-89 2.22e-13

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: 65.84  E-value: 2.22e-13
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1034612339   50 GRKKRKRCGTCEPCRRLENCGACTSCTNR-------RTHQICKLRKC 89
Cdd:pfam02008    2 NRRKRRRCGVCEGCQRPEDCGQCSFCLDMpkfggpgKKKQKCRLRRC 48
PHA03247 super family cl33720
large tegument protein UL36; Provisional
 383-752 6.54e-11

large tegument protein UL36; Provisional


The actual alignment was detected with superfamily member PHA03247:

Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 68.04  E-value: 6.54e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034612339  383 PLPEALSPPAPFRS--PQSYLRAPSWPVVPPEEHSSFAPDSSAFP--PATPRTEFP-EAWGTDTPPATPRSSWPMPRPSP 457
Cdd:PHA03247  2554 PLPPAAPPAAPDRSvpPPRPAPRPSEPAVTSRARRPDAPPQSARPraPVDDRGDPRgPAPPSPLPPDTHAPDPPPPSPSP 2633

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034612339  458 DPMAeleqlLGSASDYIQSVFKRPEALPTKPKVKVEAPSSSPAPAPSPVLQREAPTPSSEPDTHQKAQTALQQHLHHKRS 537
Cdd:PHA03247  2634 AANE-----PDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSPPQRPRRRAARPTVGSLTSLADPPPPPPTP 2708

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034612339  538 LFLEQVHDTSFPAPSEPSAPGWWPPPSS---------PVPRLPDRPPKEKKKKLPTPAGGPVGTEKAAPGIKPSVRKPIQ 608
Cdd:PHA03247  2709 EPAPHALVSATPLPPGPAAARQASPALPaapappavpAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAV 2788

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034612339  609 IKKSRPREAQPLfPPVRQIVLEGLRSPASQEVQAHPPAPLPASQGSAVPLPPEPSLALFAPSPSRDSLLPPTQEMRSPSP 688
Cdd:PHA03247  2789 ASLSESRESLPS-PWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSVAPGGDVRRRPP 2867

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034612339  689 MtalQPGSTGPLPPADDKLEELIRQFEAEFGDSFGLPGPPSVPIQDPENQQTCLPAPESPFATR 752
Cdd:PHA03247  2868 S---RSPAAKPAAPARPPVRRLARPAVSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQ 2928
 
Name Accession Description Interval E-value
TET3 cd18897
oxygenase domain of ten-eleven translocation (TET)3 methylcytosine dioxygenase and similar ...
 828-1168 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: 719.46  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034612339  828 CDCVEQIVEKDEGPYYTHLGSGPTVASIRELMEERYGEKGKAIRIEKVIYTGKEGKSSRGCPIAKWVIRRHTLEEKLLCL 907
Cdd:cd18897      1 CDCVEQILEKDEGPYYTHLGSGPTVASIRELMEERYGEKGKAIRIEKVIYTGKEGKSSRGCPIAKWVIRRSSEEEKLLCL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034612339  908 VRHRAGHHCQNAVIVILILAWEGIPRSLGDTLYQELTDTLRKYGNPTSRRCGLNDDRTCACQGKDPNTCGASFSFGCSWS 987
Cdd:cd18897     81 VRHRAGHHCQNAVIVILILAWEGIPRALGDKLYQELTETLTKYGNPTSRRCGLNDDRTCACQGKDPNTCGASFSFGCSWS 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034612339  988 MYFNGCKYARSKTPRKFRLAGDNPKEEEVLRKSFQDLATEVAPLYKRLAPQAYQNQlgplsqktsllqskgkVTNEEIAI 1067
Cdd:cd18897    161 MYFNGCKYARSKTPRKFRLIGDNPKEEENLRDNFQDLATEVAPLYKRLAPQAYQNQ----------------VTNEDIAI 224

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034612339 1068 DCRLGLKEGRPFAGVTACMDFCAHAHKDQHNLYNGCTVVCTLTKEDNRCVGKIPEDEQLHVLPLYKMANTDEFGSEENQN 1147
Cdd:cd18897    225 DCRLGLKEGRPFSGVTACMDFCAHAHKDQHNLYNGCTVVCTLTKEDNRTVGKIPEDEQLHVLPLYKMSTTDEFGSEENQN 304

                          330       340
                   ....*....|....*....|.
gi 1034612339 1148 AKVGSGAIQVLTAFPREVRRL 1168
Cdd:cd18897    305 EKIGSGAIQVLTSFPREVREV 325
TET3 cd18897
oxygenase domain of ten-eleven translocation (TET)3 methylcytosine dioxygenase and similar ...
 1654-1782 3.68e-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: 275.71  E-value: 3.68e-81
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034612339 1654 LWSDSEHNFLDENIGGVAVAPAHGSILIECARRELHATTPLKKPNRCHPTRISLVFYQHKNLNQPNHGLALWEAKMKQLA 1733
Cdd:cd18897    325 VWSDSEHNFLDENIGGVAVAPAHGSILIECARRELHATTPLKKPNRCHPTRISLVFYQHKNLNQPNHGLALWEAKMKLLA 404

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 1034612339 1734 ERARARQEEAARLGLgQQEAKLYGKKRKWGGTVVAEPQQKEKKGVVPTR 1782
Cdd:cd18897    405 ERARARQEEAARLGL-QQEIKPYGKKRKWGGAPAAEPQPKEKKDKIPTR 452
Tet_JBP pfam12851
Oxygenase domain of the 2OGFeDO superfamily; A double-stranded beta helix (DSBH) fold domain ...
 985-1128 1.43e-39

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: 144.83  E-value: 1.43e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034612339  985 SWSMYFNGCKYARSKTPRKFRLAGDNPKEEEVLRKSFQDLATEVAPLYKRLAPQAYQNQlgplsqktsllqskgkVTNEE 1064
Cdd:pfam12851    1 SWSMYYDGCKFPGPRKPRKFSFTPRNPKEEIKLEDELQELAALLGAIYKQIAPDLYENQ----------------IEYEQ 64

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034612339 1065 IAIDCRLGLKEGRPFAGVTACMDFCAHAHKDQHNLYNGCTVVCTLTkedNRCVGKIPEDEQLHV 1128
Cdd:pfam12851   65 DAAICRLGRKWGRPFSGVTVNLNFETISHRDLGNFRNGSTLLCTLT---GRYEGGRLALPQLGV 125
zf-CXXC pfam02008
CXXC zinc finger domain; This domain contains eight conserved cysteine residues that bind to ...
 50-89 2.22e-13

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: 65.84  E-value: 2.22e-13
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1034612339   50 GRKKRKRCGTCEPCRRLENCGACTSCTNR-------RTHQICKLRKC 89
Cdd:pfam02008    2 NRRKRRRCGVCEGCQRPEDCGQCSFCLDMpkfggpgKKKQKCRLRRC 48
Tet_JBP pfam12851
Oxygenase domain of the 2OGFeDO superfamily; A double-stranded beta helix (DSBH) fold domain ...
 1669-1713 3.31e-11

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: 63.55  E-value: 3.31e-11
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 1034612339 1669 GVAVAPAHGSILIECARRELHATTPLKKPNRchPTRISLVFYQHK 1713
Cdd:pfam12851  124 GVAFAPTPGTVLIFCGKSLEHGVTPVKNPNR--WERVSLVFYWHK 166
PHA03247 PHA03247
large tegument protein UL36; Provisional
 383-752 6.54e-11

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 68.04  E-value: 6.54e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034612339  383 PLPEALSPPAPFRS--PQSYLRAPSWPVVPPEEHSSFAPDSSAFP--PATPRTEFP-EAWGTDTPPATPRSSWPMPRPSP 457
Cdd:PHA03247  2554 PLPPAAPPAAPDRSvpPPRPAPRPSEPAVTSRARRPDAPPQSARPraPVDDRGDPRgPAPPSPLPPDTHAPDPPPPSPSP 2633

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034612339  458 DPMAeleqlLGSASDYIQSVFKRPEALPTKPKVKVEAPSSSPAPAPSPVLQREAPTPSSEPDTHQKAQTALQQHLHHKRS 537
Cdd:PHA03247  2634 AANE-----PDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSPPQRPRRRAARPTVGSLTSLADPPPPPPTP 2708

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034612339  538 LFLEQVHDTSFPAPSEPSAPGWWPPPSS---------PVPRLPDRPPKEKKKKLPTPAGGPVGTEKAAPGIKPSVRKPIQ 608
Cdd:PHA03247  2709 EPAPHALVSATPLPPGPAAARQASPALPaapappavpAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAV 2788

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034612339  609 IKKSRPREAQPLfPPVRQIVLEGLRSPASQEVQAHPPAPLPASQGSAVPLPPEPSLALFAPSPSRDSLLPPTQEMRSPSP 688
Cdd:PHA03247  2789 ASLSESRESLPS-PWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSVAPGGDVRRRPP 2867

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034612339  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 2.12e-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: 46.30  E-value: 2.12e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034612339  326 SEVPQI-SPQEGLPLSQSAlsiaKEKNISLQTAIAIEALTQLSSALPQPSHSTPQASCPLPEALSPPAPFRSPQSYLRAP 404
Cdd:pfam03154  143 STSPSIpSPQDNESDSDSS----AQQQILQTQPPVLQAQSGAASPPSPPPPGTTQAATAGPTPSAPSVPPQGSPATSQPP 218

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034612339  405 SWPVVPPEEHSSFAPDSSAFPPATPRTEFPEAWGTDTPPATPRSSWPMPRPS-PDPMAELEQLLGSASDYIqsvfkrPEA 483
Cdd:pfam03154  219 NQTQSTAAPHTLIQQTPTLHPQRLPSPHPPLQPMTQPPPPSQVSPQPLPQPSlHGQMPPMPHSLQTGPSHM------QHP 292

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034612339  484 LPTKPkvkveapssspAPAPSPVLQREAPTPSSEPDTHQKAQTalqQHLHHKRSLFLEQVHDTSFPAPSEPSAPGWWPPP 563
Cdd:pfam03154  293 VPPQP-----------FPLTPQSSQSQVPPGPSPAAPGQSQQR---IHTPPSQSQLQSQQPPREQPLPPAPLSMPHIKPP 358

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034612339  564 SSPVPRLPDRPPKEKKKKLPTpagGPVGTEKAAPGIKPSVRKPI-QIKKSRPREAQP----LFPPVRQIVLEGLRSPASQ 638
Cdd:pfam03154  359 PTTPIPQLPNPQSHKHPPHLS---GPSPFQMNSNLPPPPALKPLsSLSTHHPPSAHPpplqLMPQSQQLPPPPAQPPVLT 435

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034612339  639 EVQAHPP----APLPASQGSAVPLPPEPSLAlFAPSPSRDSLLPPTQEMRSPSPMTALQP------GSTGPLPPADDKLE 708
Cdd:pfam03154  436 QSQSLPPpaasHPPTSGLHQVPSQSPFPQHP-FVPGGPPPITPPSGPPTSTSSAMPGIQPpssasvSSSGPVPAAVSCPL 514

                          410       420       430
                   ....*....|....*....|....*....|....*..
gi 1034612339  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 ...
 828-1168 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: 719.46  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034612339  828 CDCVEQIVEKDEGPYYTHLGSGPTVASIRELMEERYGEKGKAIRIEKVIYTGKEGKSSRGCPIAKWVIRRHTLEEKLLCL 907
Cdd:cd18897      1 CDCVEQILEKDEGPYYTHLGSGPTVASIRELMEERYGEKGKAIRIEKVIYTGKEGKSSRGCPIAKWVIRRSSEEEKLLCL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034612339  908 VRHRAGHHCQNAVIVILILAWEGIPRSLGDTLYQELTDTLRKYGNPTSRRCGLNDDRTCACQGKDPNTCGASFSFGCSWS 987
Cdd:cd18897     81 VRHRAGHHCQNAVIVILILAWEGIPRALGDKLYQELTETLTKYGNPTSRRCGLNDDRTCACQGKDPNTCGASFSFGCSWS 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034612339  988 MYFNGCKYARSKTPRKFRLAGDNPKEEEVLRKSFQDLATEVAPLYKRLAPQAYQNQlgplsqktsllqskgkVTNEEIAI 1067
Cdd:cd18897    161 MYFNGCKYARSKTPRKFRLIGDNPKEEENLRDNFQDLATEVAPLYKRLAPQAYQNQ----------------VTNEDIAI 224

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034612339 1068 DCRLGLKEGRPFAGVTACMDFCAHAHKDQHNLYNGCTVVCTLTKEDNRCVGKIPEDEQLHVLPLYKMANTDEFGSEENQN 1147
Cdd:cd18897    225 DCRLGLKEGRPFSGVTACMDFCAHAHKDQHNLYNGCTVVCTLTKEDNRTVGKIPEDEQLHVLPLYKMSTTDEFGSEENQN 304

                          330       340
                   ....*....|....*....|.
gi 1034612339 1148 AKVGSGAIQVLTAFPREVRRL 1168
Cdd:cd18897    305 EKIGSGAIQVLTSFPREVREV 325
TET cd18892
oxygenase domain of ten-eleven translocation (TET)1, TET2, and TET3 methylcytosine ...
 828-1178 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: 653.59  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034612339  828 CDCVEQIV-EKDEGPYYTHLGSGPTVASIRELMEERYGEKGKAIRIEKVIYTGKEGKSSRGCPIAKWVIRRHTLEEKLLC 906
Cdd:cd18892      1 CGCFPPDEsPPEPGPYYTHLGAGPSLAALRELLEKRTGVTGKAIRIEKVIYTGKEGKTSQGCPIAKWIIRRSSLEEKYLV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034612339  907 LVRHRAGHHCQNAVIVILILAWEGIPRSLGDTLYQELTDTLRKYGNPTSRRCGLNDDRTCACQGKDPNTCGASFSFGCSW 986
Cdd:cd18892     81 LVKHRPGHFCHSAFIVICIVAWEGVPQSNADELYSLLTDKLNKFGLPTKRRCGTNEERTCACQGLDPETCGASFSFGCSW 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034612339  987 SMYFNGCKYARSKTPRKFRLAGdnPKEEEVLRKSFQDLATEVAPLYKRLAPQAYQNQlgplsqktsllqskgkVTNEEIA 1066
Cdd:cd18892    161 SMYYNGCKFARSKTVRKFRLSD--KSEEEELEDKLQNLATHLAPLYKSLAPDSYKNQ----------------VQFEEEA 222

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034612339 1067 IDCRLGLKEGRPFAGVTACMDFCAHAHKDQHNLYNGCTVVCTLTKEDNRCvGKIPEDEQLHVLPLYKMANTDEFGSEENQ 1146
Cdd:cd18892    223 LDCRLGLKPGRPFSGVTACVDFCAHAHKDLHNMNNGCTVVVTLTKHRNLT-KPEPEQLHVLPLYLYDMTDEDEFGSVEGQ 301

                          330       340       350
                   ....*....|....*....|....*....|..
gi 1034612339 1147 NAKVGSGAIQVLTAFPREVRRLPEPAKSCRQR 1178
Cdd:cd18892    302 EEKVRNGSIEVLTKYPCEVREYWSDSEECFLD 333
TET1 cd18895
oxygenase domain of ten-eleven translocation (TET)1 methylcytosine dioxygenase and similar ...
 828-1168 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: 607.30  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034612339  828 CDCVEQIVEKDEGPYYTHLGSGPTVASIRELMEERYGEKGKAIRIEKVIYTGKEGKSSRGCPIAKWVIRRHTLEEKLLCL 907
Cdd:cd18895      1 CDCVEQIIEKDEGPYYTHLGAGPSVAAVREIMENRYGEKGNAIRIEVVVYTGKEGKSSQGCPIAKWVIRRSSDEEKLLCL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034612339  908 VRHRAGHHCQNAVIVILILAWEGIPRSLGDTLYQELTDTLRKYGNPTSRRCGLNDDRTCACQGKDPNTCGASFSFGCSWS 987
Cdd:cd18895     81 VRQRAGHHCQTAVIVILILAWEGIPRLLADRLYQELTQTLKKYGSPTSRRCALNEDRTCACQGLDPETCGASFSFGCSWS 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034612339  988 MYFNGCKYARSKTPRKFRLAGDNPKEEEVLRKSFQDLATEVAPLYKRLAPQAYQNQlgplsqktsllqskgkVTNEEIAI 1067
Cdd:cd18895    161 MYFNGCKFARSKYPRKFRLLTDDPKEEENLESNLQNLATDVAPVYKKLAPEAFQNQ----------------VENENVAP 224

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034612339 1068 DCRLGLKEGRPFAGVTACMDFCAHAHKDQHNLYNGCTVVCTLTKEDNRCVGKIPEDEQLHVLPLYKMANTDEFGSEENQN 1147
Cdd:cd18895    225 DCRLGSKEGRPFSGVTACIDFCAHAHKDTHNMHNGSTVVCTLTKEDNRSVGVIPEDEQLHVLPLYKISDTDEFGSEEGQE 304

                          330       340
                   ....*....|....*....|.
gi 1034612339 1148 AKVGSGAIQVLTAFPREVRRL 1168
Cdd:cd18895    305 AKIKNGAIQVLSAFPREVREV 325
TET2 cd18896
oxygenase domain of ten-eleven translocation (TET)2 methylcytosine dioxygenase and similar ...
 824-1180 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: 602.73  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034612339  824 EFPTCDCVEQIVEKDEGPYYTHLGSGPTVASIRELMEERYGEKGKAIRIEKVIYTGKEGKSSRGCPIAKWVIRRHTLEEK 903
Cdd:cd18896      1 DFPSCSCVEQIIEKDEGPYYTHLGAGPNVAAIREIMEERFGQKGKAIRIERVIYTGKEGKSSQGCPIAKWVIRRSSEEEK 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034612339  904 LLCLVRHRAGHHCQNAVIVILILAWEGIPRSLGDTLYQELTDTLRKYGNPTSRRCGLNDDRTCACQGKDPNTCGASFSFG 983
Cdd:cd18896     81 LLCLVRERAGHSCETAVIVILILVWEGIPISLADKLYSELTDTLRKYGTLTNRRCALNEERTCACQGLDPETCGASFSFG 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034612339  984 CSWSMYFNGCKYARSKTPRKFRLAGDNPKEEEVLRKSFQDLATEVAPLYKRLAPQAYQNQlgplsqktsllqskgkVTNE 1063
Cdd:cd18896    161 CSWSMYYNGCKFARSKIPRKFKLLGDDPKEEEKLESNLQNLSTLMAPTYKKLAPDAYNNQ----------------IEYE 224

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034612339 1064 EIAIDCRLGLKEGRPFAGVTACMDFCAHAHKDQHNLYNGCTVVCTLTKEDNRCVGKIPEDEQLHVLPLYKMANTDEFGSE 1143
Cdd:cd18896    225 HRAPDCRLGLKEGRPFSGVTACLDFCAHAHRDLHNMQNGSTLVCTLTREDNREIGKIPEDEQLHVLPLYKVSDVDEFGST 304

                          330       340       350
                   ....*....|....*....|....*....|....*..
gi 1034612339 1144 ENQNAKVGSGAIQVLTAFPREVRRLPEPAKSCRQRQL 1180
Cdd:cd18896    305 EAQEEKKRNGAIQVLSSFRRKVRMLAEPVKTCRQRKL 341
TET3 cd18897
oxygenase domain of ten-eleven translocation (TET)3 methylcytosine dioxygenase and similar ...
 1654-1782 3.68e-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: 275.71  E-value: 3.68e-81
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034612339 1654 LWSDSEHNFLDENIGGVAVAPAHGSILIECARRELHATTPLKKPNRCHPTRISLVFYQHKNLNQPNHGLALWEAKMKQLA 1733
Cdd:cd18897    325 VWSDSEHNFLDENIGGVAVAPAHGSILIECARRELHATTPLKKPNRCHPTRISLVFYQHKNLNQPNHGLALWEAKMKLLA 404

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 1034612339 1734 ERARARQEEAARLGLgQQEAKLYGKKRKWGGTVVAEPQQKEKKGVVPTR 1782
Cdd:cd18897    405 ERARARQEEAARLGL-QQEIKPYGKKRKWGGAPAAEPQPKEKKDKIPTR 452
Tet_JBP cd14946
oxygenase domain of ten-eleven translocation (TET) enzymes, J-binding proteins (JBPs), and ...
 855-1133 4.35e-54

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: 190.67  E-value: 4.35e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034612339  855 IRELMEERYG-EKGKAIRIEKVIYTGKEGKSsRGCPIAKWVIRRhtleEKLLCLVRHRAGhhcqnavIVILILAWEGIPR 933
Cdd:cd14946      1 LLENMLSKCGtQQSFANANITLKYEGKEGKS-QGCPKALKNVRT----SKLAYFVCDHDG-------SVILAYVPEVLPK 68

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034612339  934 SLGDTLYQELTDTLRKYGNptsrrcglnddrtcacqgKDPNTCGASFSFGCSWSMYFNGCKyarsktprkfRLAGDNPKE 1013
Cdd:cd14946     69 ELVEEFTEKLESIQTKRGT------------------LDPETKGDTGYSGILDNSMPFNYV----------TADLSQELG 120

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034612339 1014 EEVLRKSFQDLATEVAPLYKRLAPQAYQNQlgplsqktsllqskgkVTNEEIAIDCRLGLKEGRPFAGVTACMD-FCAHA 1092
Cdd:cd14946    121 QYLSEIVNPQISYYISKLLTCVSPRTINYL----------------VEYEHRSLNDSYYALNNCLYPSTAFNSLkRIRKP 184

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|.
gi 1034612339 1093 HKDQHNLYNGCTVVCTLTKEDNrcvgkipeDEQLHVLPLYK 1133
Cdd:cd14946    185 HKDNLDIQNGPSSLFYFGNFQN--------TEGYLELTLKK 217
TET2 cd18896
oxygenase domain of ten-eleven translocation (TET)2 methylcytosine dioxygenase and similar ...
 1654-1746 9.50e-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: 174.77  E-value: 9.50e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034612339 1654 LWSDSEHNFLDENIGGVAVAPAHGSILIECARRELHATTPLKKPNRCHPTRISLVFYQHKNLNQPNHGLALWEAKMkqlA 1733
Cdd:cd18896    345 VWSDSEQSFLDPDIGGVAVAPSHGSILIECAKRELHATTPLKNPNRNHPTRISLVFYQHKSMNEPKHGLALWEAKM---A 421

                           90
                   ....*....|...
gi 1034612339 1734 ERARARQEEAARL 1746
Cdd:cd18896    422 EKAREKEEECEKY 434
TET1 cd18895
oxygenase domain of ten-eleven translocation (TET)1 methylcytosine dioxygenase and similar ...
 1654-1742 2.60e-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: 2.60e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034612339 1654 LWSDSEHNFLDENIGGVAVAPAHGSILIECARRELHATTPLKKPNRCHPTRISLVFYQHKNLNQPNHGLALWEAKMkqlA 1733
Cdd:cd18895    325 VWSDSEHNFLDEDIGGVAVAPSHGSILIECARRELHATTPIKKPNRNHPTRISLVFYQHKNLNEPKHGLALWEAKM---A 401


                   ....*....
gi 1034612339 1734 ERARARQEE 1742
Cdd:cd18895    402 EKAKEKEKE 410
TET cd18892
oxygenase domain of ten-eleven translocation (TET)1, TET2, and TET3 methylcytosine ...
 1655-1729 2.47e-40

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: 155.14  E-value: 2.47e-40
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034612339 1655 WSDSEHNFLDENIGGVAVAPAHGSILIECARRELHATTPLKKPNRCHPTRISLVFYQHKNLNQPNHGLALWEAKM 1729
Cdd:cd18892    324 WSDSEECFLDPDIGGVAIALSHGSVLFECAKRELHATTPLKNPNRQHPTRISLVFYQHKNLNYSRHGLAEYEAKM 398
Tet_JBP pfam12851
Oxygenase domain of the 2OGFeDO superfamily; A double-stranded beta helix (DSBH) fold domain ...
 985-1128 1.43e-39

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: 144.83  E-value: 1.43e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034612339  985 SWSMYFNGCKYARSKTPRKFRLAGDNPKEEEVLRKSFQDLATEVAPLYKRLAPQAYQNQlgplsqktsllqskgkVTNEE 1064
Cdd:pfam12851    1 SWSMYYDGCKFPGPRKPRKFSFTPRNPKEEIKLEDELQELAALLGAIYKQIAPDLYENQ----------------IEYEQ 64

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034612339 1065 IAIDCRLGLKEGRPFAGVTACMDFCAHAHKDQHNLYNGCTVVCTLTkedNRCVGKIPEDEQLHV 1128
Cdd:pfam12851   65 DAAICRLGRKWGRPFSGVTVNLNFETISHRDLGNFRNGSTLLCTLT---GRYEGGRLALPQLGV 125
zf-CXXC pfam02008
CXXC zinc finger domain; This domain contains eight conserved cysteine residues that bind to ...
 50-89 2.22e-13

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: 65.84  E-value: 2.22e-13
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1034612339   50 GRKKRKRCGTCEPCRRLENCGACTSCTNR-------RTHQICKLRKC 89
Cdd:pfam02008    2 NRRKRRRCGVCEGCQRPEDCGQCSFCLDMpkfggpgKKKQKCRLRRC 48
Tet_JBP cd14946
oxygenase domain of ten-eleven translocation (TET) enzymes, J-binding proteins (JBPs), and ...
 1667-1713 7.15e-13

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: 70.87  E-value: 7.15e-13
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1034612339 1667 IGGVAVAPAHGSILIECARRELHATTPLKKPNRcHPTRISLVFYQHK 1713
Cdd:cd14946    219 IGNCAVFVQPGDVLFFKGNEYKHVVTNITNPNN-HGWRISLVYYAHK 264
Tet_JBP pfam12851
Oxygenase domain of the 2OGFeDO superfamily; A double-stranded beta helix (DSBH) fold domain ...
 1669-1713 3.31e-11

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: 63.55  E-value: 3.31e-11
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 1034612339 1669 GVAVAPAHGSILIECARRELHATTPLKKPNRchPTRISLVFYQHK 1713
Cdd:pfam12851  124 GVAFAPTPGTVLIFCGKSLEHGVTPVKNPNR--WERVSLVFYWHK 166
PHA03247 PHA03247
large tegument protein UL36; Provisional
 383-752 6.54e-11

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 68.04  E-value: 6.54e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034612339  383 PLPEALSPPAPFRS--PQSYLRAPSWPVVPPEEHSSFAPDSSAFP--PATPRTEFP-EAWGTDTPPATPRSSWPMPRPSP 457
Cdd:PHA03247  2554 PLPPAAPPAAPDRSvpPPRPAPRPSEPAVTSRARRPDAPPQSARPraPVDDRGDPRgPAPPSPLPPDTHAPDPPPPSPSP 2633

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034612339  458 DPMAeleqlLGSASDYIQSVFKRPEALPTKPKVKVEAPSSSPAPAPSPVLQREAPTPSSEPDTHQKAQTALQQHLHHKRS 537
Cdd:PHA03247  2634 AANE-----PDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSPPQRPRRRAARPTVGSLTSLADPPPPPPTP 2708

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034612339  538 LFLEQVHDTSFPAPSEPSAPGWWPPPSS---------PVPRLPDRPPKEKKKKLPTPAGGPVGTEKAAPGIKPSVRKPIQ 608
Cdd:PHA03247  2709 EPAPHALVSATPLPPGPAAARQASPALPaapappavpAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAV 2788

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034612339  609 IKKSRPREAQPLfPPVRQIVLEGLRSPASQEVQAHPPAPLPASQGSAVPLPPEPSLALFAPSPSRDSLLPPTQEMRSPSP 688
Cdd:PHA03247  2789 ASLSESRESLPS-PWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSVAPGGDVRRRPP 2867

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034612339  689 MtalQPGSTGPLPPADDKLEELIRQFEAEFGDSFGLPGPPSVPIQDPENQQTCLPAPESPFATR 752
Cdd:PHA03247  2868 S---RSPAAKPAAPARPPVRRLARPAVSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQ 2928
PHA03247 PHA03247
large tegument protein UL36; Provisional
 359-734 7.60e-08

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 58.03  E-value: 7.60e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034612339  359 AIEALTQLSSALPQPSHSTPQASCPLPEALSPPAPFRSPQSYLRAPSWPVVPPEEHSSFAPDSSAFPPATPRTEFPEAwg 438
Cdd:PHA03247  2691 TVGSLTSLADPPPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPA-- 2768

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034612339  439 tDTPPATPRSSWP--MPRPSPDPMAELEQLLGSASDYIQSVFKRPEALPTKPKVKVEAPSsspapapspvlqrEAPTPSS 516
Cdd:PHA03247  2769 -PAPPAAPAAGPPrrLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGP-------------LPPPTSA 2834

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034612339  517 EPdthqkaqtalqqhlhhkrslfleqvhdTSFPAPSEPSAPGWWPPPSSPVprlpdrppkekkkklptpaGGPV---GTE 593
Cdd:PHA03247  2835 QP---------------------------TAPPPPPGPPPPSLPLGGSVAP-------------------GGDVrrrPPS 2868

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034612339  594 KAAPGI-----KPSVRKPIQIKKSRPREAQPLFPPvrqivleglrspaSQEVQAHPPAPLPASQGSAVPLPPEPSLALFA 668
Cdd:PHA03247  2869 RSPAAKpaapaRPPVRRLARPAVSRSTESFALPPD-------------QPERPPQPQAPPPPQPQPQPPPPPQPQPPPPP 2935

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034612339  669 PSPSRDSLLPPTQEMRSPSPMTALQPGSTGPLPPADdklEELIRQFEAEFGDSFGLPGPPSVPIQD 734
Cdd:PHA03247  2936 PPRPQPPLAPTTDPAGAGEPSGAVPQPWLGALVPGR---VAVPRFRVPQPAPSREAPASSTPPLTG 2998
PHA03247 PHA03247
large tegument protein UL36; Provisional
 385-803 4.70e-07

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 55.33  E-value: 4.70e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034612339  385 PEALSPPAPFRSPQSYLRAPSWPVVPPEEHS---SFAPDSSAFPPATPRT----------------EFPEAWGTDTPPAT 445
Cdd:PHA03247  2484 AEARFPFAAGAAPDPGGGGPPDPDAPPAPSRlapAILPDEPVGEPVHPRMltwirgleelasddagDPPPPLPPAAPPAA 2563

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034612339  446 PRSSWPMPRPSPDPmaeleqllgsASDYIQSVFKRPEALP--TKPKVKVEAPSSSPapapspvlqREAPTPSSEPDTHQK 523
Cdd:PHA03247  2564 PDRSVPPPRPAPRP----------SEPAVTSRARRPDAPPqsARPRAPVDDRGDPR---------GPAPPSPLPPDTHAP 2624

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034612339  524 AqtalqqhlhhkrslfleqvhdtsfPAPSEPSApgwwppPSSPVPRLPDRPPKEKKKKLPTPAGGPVGTEKAAPGIKPSV 603
Cdd:PHA03247  2625 D------------------------PPPPSPSP------AANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAA 2674

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034612339  604 RKPIQIKKSRPREAQPLFPPvrqivLEGLRSPASQEvqaHPPAPLPASQGSAVPLPPEPSLALFAPSPSRDSLLPPtqem 683
Cdd:PHA03247  2675 QASSPPQRPRRRAARPTVGS-----LTSLADPPPPP---PTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPP---- 2742

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034612339  684 rsPSPMTALQPGstGPLPPADDKLEElirqfeaefgdSFGLPGPPSVPIQDPENQQT------CLPAPESPFATRSPKQI 757
Cdd:PHA03247  2743 --AVPAGPATPG--GPARPARPPTTA-----------GPPAPAPPAAPAAGPPRRLTrpavasLSESRESLPSPWDPADP 2807

                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*.
gi 1034612339  758 KIESSGAVTVLSTTcfhSEEGGQEATPTKAENPLTPTLSGFLESPL 803
Cdd:PHA03247  2808 PAAVLAPAAALPPA---ASPAGPLPPPTSAQPTAPPPPPGPPPPSL 2850
PHA03247 PHA03247
large tegument protein UL36; Provisional
 313-701 1.49e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 50.32  E-value: 1.49e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034612339  313 AGLPAPSTRP----LLSSEVPQISPQEGLPLSQSALSIAKEKNISLQTAIAIEALTQLSSALPQPSHSTPQASCPLPEAL 388
Cdd:PHA03247  2609 RGPAPPSPLPpdthAPDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSPPQRPRRRAA 2688

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034612339  389 SPPApfrSPQSYLRAPSWPVVPPEehssfaPDSSAFPPATPRTEFPEAWGTDTPPATPRsswPMPRPSPDpmaeleqllG 468
Cdd:PHA03247  2689 RPTV---GSLTSLADPPPPPPTPE------PAPHALVSATPLPPGPAAARQASPALPAA---PAPPAVPA---------G 2747

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034612339  469 SASDYIQSVFKRPEAL-----PTKPKVKVEAPSSSPAPAPSPVLQREAPTPSSEPDTHQKAQTALQQHlhhkrslflEQV 543
Cdd:PHA03247  2748 PATPGGPARPARPPTTagppaPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPA---------AAL 2818

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034612339  544 HDTSFPAPSEPSAPGWWPPPSSPVPRLPDRPPKEkkkklptpaGGPVgtekaAPGIKPSVRKPIQIKKSRPreAQPLFPP 623
Cdd:PHA03247  2819 PPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPL---------GGSV-----APGGDVRRRPPSRSPAAKP--AAPARPP 2882

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034612339  624 VRQIVLEGL-RSPASQEVQAHPPAPLPASQGSAVPLPPEPSLALFAPSPsrdsllPPTQEMRSPSPM-----TALQPGST 697
Cdd:PHA03247  2883 VRRLARPAVsRSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQP------PPPPPPRPQPPLapttdPAGAGEPS 2956


                   ....
gi 1034612339  698 GPLP 701
Cdd:PHA03247  2957 GAVP 2960
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 326-745 2.12e-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: 46.30  E-value: 2.12e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034612339  326 SEVPQI-SPQEGLPLSQSAlsiaKEKNISLQTAIAIEALTQLSSALPQPSHSTPQASCPLPEALSPPAPFRSPQSYLRAP 404
Cdd:pfam03154  143 STSPSIpSPQDNESDSDSS----AQQQILQTQPPVLQAQSGAASPPSPPPPGTTQAATAGPTPSAPSVPPQGSPATSQPP 218

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034612339  405 SWPVVPPEEHSSFAPDSSAFPPATPRTEFPEAWGTDTPPATPRSSWPMPRPS-PDPMAELEQLLGSASDYIqsvfkrPEA 483
Cdd:pfam03154  219 NQTQSTAAPHTLIQQTPTLHPQRLPSPHPPLQPMTQPPPPSQVSPQPLPQPSlHGQMPPMPHSLQTGPSHM------QHP 292

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034612339  484 LPTKPkvkveapssspAPAPSPVLQREAPTPSSEPDTHQKAQTalqQHLHHKRSLFLEQVHDTSFPAPSEPSAPGWWPPP 563
Cdd:pfam03154  293 VPPQP-----------FPLTPQSSQSQVPPGPSPAAPGQSQQR---IHTPPSQSQLQSQQPPREQPLPPAPLSMPHIKPP 358

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034612339  564 SSPVPRLPDRPPKEKKKKLPTpagGPVGTEKAAPGIKPSVRKPI-QIKKSRPREAQP----LFPPVRQIVLEGLRSPASQ 638
Cdd:pfam03154  359 PTTPIPQLPNPQSHKHPPHLS---GPSPFQMNSNLPPPPALKPLsSLSTHHPPSAHPpplqLMPQSQQLPPPPAQPPVLT 435

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034612339  639 EVQAHPP----APLPASQGSAVPLPPEPSLAlFAPSPSRDSLLPPTQEMRSPSPMTALQP------GSTGPLPPADDKLE 708
Cdd:pfam03154  436 QSQSLPPpaasHPPTSGLHQVPSQSPFPQHP-FVPGGPPPITPPSGPPTSTSSAMPGIQPpssasvSSSGPVPAAVSCPL 514

                          410       420       430
                   ....*....|....*....|....*....|....*..
gi 1034612339  709 ELIrQFEAEFGDSFGLPGPPSVPIQDPENQQTCLPAP 745
Cdd:pfam03154  515 PPV-QIKEEALDEAEEPESPPPPPRSPSPEPTVVNTP 550
PRK14950 PRK14950
DNA polymerase III subunits gamma and tau; Provisional
 344-484 2.17e-04

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237864 [Multi-domain]  Cd Length: 585  Bit Score: 45.96  E-value: 2.17e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034612339  344 LSIAKEKNISLQTAIaIEALTqlsSALPQPSHSTPQASCPLPeALSPPAPFRSPQSYLRAPSwPVVPPEEHSSFAPDSSA 423
Cdd:PRK14950   341 LRTTSYGQLPLELAV-IEALL---VPVPAPQPAKPTAAAPSP-VRPTPAPSTRPKAAAAANI-PPKEPVRETATPPPVPP 414

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034612339  424 FPPATPRTEFPEAWGTDTP-----PATPRSSWPMPRPSPD-----PMAELEQLLGSASDYIQSVFKRPEAL 484
Cdd:PRK14950   415 RPVAPPVPHTPESAPKLTRaaipvDEKPKYTPPAPPKEEEkaliaDGDVLEQLEAIWKQILRDVPPRSPAV 485
PTZ00449 PTZ00449
104 kDa microneme/rhoptry antigen; Provisional
 589-824 4.11e-04

104 kDa microneme/rhoptry antigen; Provisional


Pssm-ID: 185628 [Multi-domain]  Cd Length: 943  Bit Score: 45.45  E-value: 4.11e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034612339  589 PVGTEKAAPGIKP-SVRKPIQIKKS-RPREAQ-PLFP--PVRQIVLEGLRSPASQEVQAHPPAPLPASQGSAvPLPPEPS 663
Cdd:PTZ00449   573 PTLSKKPEFPKDPkHPKDPEEPKKPkRPRSAQrPTRPksPKLPELLDIPKSPKRPESPKSPKRPPPPQRPSS-PERPEGP 651

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034612339  664 LALFAPSPSRDSLLP--PT--QEMRSPSPMTALQPGSTGPLPPADDKLEELIRQFEAEF-GDSFGLPGP----------- 727
Cdd:PTZ00449   652 KIIKSPKPPKSPKPPfdPKfkEKFYDDYLDAAAKSKETKTTVVLDESFESILKETLPETpGTPFTTPRPlppklprdeef 731

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034612339  728 PSVPIQDPENQQtclPAPESPFATRSPKQIKIESSGAVTVLSTTCfhSEEGGQEATPTKAENPLTPTLSGflESPLKYLD 807
Cdd:PTZ00449   732 PFEPIGDPDAEQ---PDDIEFFTPPEEERTFFHETPADTPLPDIL--AEEFKEEDIHAETGEPDEAMKRP--DSPSEHED 804

                          250
                   ....*....|....*..
gi 1034612339  808 TPTKSLLDTPAKRAQAE 824
Cdd:PTZ00449   805 KPPGDHPSLPKKRHRLD 821
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
589-753 4.24e-04

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 45.25  E-value: 4.24e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034612339  589 PVGTEKAAPGIKPSVRKPIQIKKSRPREAQPLfPPVRQIVLEGlRSPASQEVQAHPPAPLPASQGSAVPLPPEPSLALFA 668
Cdd:PRK12323   402 PPAAPAAAPAAAAAARAVAAAPARRSPAPEAL-AAARQASARG-PGGAPAPAPAPAAAPAAAARPAAAGPRPVAAAAAAA 479

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034612339  669 PSPSR--------DSLLPPTQEMRSPSPMTALQPGSTGPLP-PADDKLEELIRQFEAEFGDSfgLPGPPSVPIQDPENQQ 739
Cdd:PRK12323   480 PARAApaaapapaDDDPPPWEELPPEFASPAPAQPDAAPAGwVAESIPDPATADPDDAFETL--APAPAAAPAPRAAAAT 557

                          170
                   ....*....|....
gi 1034612339  740 TCLPAPESPFATRS 753
Cdd:PRK12323   558 EPVVAPRPPRASAS 571
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 367-756 1.49e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 43.44  E-value: 1.49e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034612339  367 SSALPQPSHSTPQAscPLPEALSPPAPFRSPQSYLRAPSWPVVP-PEEHSSFAPDSSAFPPATPRTEFPEAWGTDTPPAT 445
Cdd:PRK07764   419 AAAAPAPAAAPQPA--PAPAPAPAPPSPAGNAPAGGAPSPPPAAaPSAQPAPAPAAAPEPTAAPAPAPPAAPAPAAAPAA 496

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034612339  446 PRSswPMPRPSPDPMAELE----QLLGSASDYIQSVFkrpEALPTKPKVkveapssspAPAPSPVLQREAPTPS-----S 516
Cdd:PRK07764   497 PAA--PAAPAGADDAATLRerwpEILAAVPKRSRKTW---AILLPEATV---------LGVRGDTLVLGFSTGGlarrfA 562

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034612339  517 EPDTHQKAQTALQQHLHhkRSLFLEQVHDTSFPAPSEPSAPGWWPPPSSPVPRLPDRPPKEKKKKLPTPAGGPVGTEKAA 596
Cdd:PRK07764   563 SPGNAEVLVTALAEELG--GDWQVEAVVGPAPGAAGGEGPPAPASSGPPEEAARPAAPAAPAAPAAPAPAGAAAAPAEAS 640

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034612339  597 PGIKPSVRKPIQIKKSRPREAQPLFPPVRQIVLEGLRSPASQEVQAHPPAPLPASQGSAVPLPPEPslalfAPSPSRDSL 676
Cdd:PRK07764   641 AAPAPGVAAPEHHPKHVAVPDASDGGDGWPAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPA-----ATPPAGQAD 715

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034612339  677 LPPTQEMRSPSPMTALQPGSTGPLPPADdkleelirqfEAEFGDSFGLPGPPSVPIQDPENQQTclPAPESPFATRSPKQ 756
Cdd:PRK07764   716 DPAAQPPQAAQGASAPSPAADDPVPLPP----------EPDDPPDPAGAPAQPPPPPAPAPAAA--PAAAPPPSPPSEEE 783
TALPID3 pfam15324
Hedgehog signalling target; TALPID3 is a family of eukaryotic proteins that are targets for ...
 364-459 1.50e-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: 43.72  E-value: 1.50e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034612339  364 TQLSSALPQPSHSTPQASCPLPEALSP-PAPFRSPQ-SYLRAPSWPVVPPEEHSSFAPDSSAF--PPATPRTEFPEAwGT 439
Cdd:pfam15324  982 TLLPTPVPTPQPTPPCSPPSPLKEPSPvKTPDSSPCvSEHDFFPVKEIPPEKGADTGPAVSLVitPTVTPIATPPPA-AT 1060

                           90       100
                   ....*....|....*....|
gi 1034612339  440 DTPPATPRSSWPMPRPSPDP 459
Cdd:pfam15324 1061 PTPPLSENSIDKLKSPSPEL 1080
GGN pfam15685
Gametogenetin; GGN is a family of proteins largely found in mammals. It reacts with POG in the ...
 588-766 1.54e-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: 43.22  E-value: 1.54e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034612339  588 GPVGTEKAAPGIK---PSVRKPIQIKKSRPreaQPLFPPVRQIVLEGLRSPASQEVQAHPPAPLPASQGSAVPlPPEPSL 664
Cdd:pfam15685  388 GPWGSPPPPPGKAhpiPGPRRPAPALLAPP---MFIFPAPTNGEPVRPGPPAPQALLPRPPPPTPPATPPPVP-PPIPQL 463

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034612339  665 ALFAPSPsRDSLLPPTQEMRSPSPMTALQPGSTGPLPPAddkleELIRQFEAEFGDSFGLPGPPSVPIQ-DPenqqtcLP 743
Cdd:pfam15685  464 PALQPMP-LAAARPPTPRPCPGHGESALAPAPTAPLPPA-----LAADQAPAPALAAAPAPSPAPAPATaDP------LP 531

                          170       180
                   ....*....|....*....|...
gi 1034612339  744 APESPFATRSPKQIKIESSGAVT 766
Cdd:pfam15685  532 PAPAPIKARTRKNKGPRAARGAT 554
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
312-462 1.65e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 43.33  E-value: 1.65e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034612339  312 EAGLPAPSTRPLLSSEVPQISPQEGLPLSQSALSIAKEKNISLQTAIAIEALTQLSSALPQPSHSTPQASCPLPEALSPP 391
Cdd:PRK12323   399 PAAPPAAPAAAPAAAAAARAVAAAPARRSPAPEALAAARQASARGPGGAPAPAPAPAAAPAAAARPAAAGPRPVAAAAAA 478

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034612339  392 APFRSPQSYLRAPSWPVVPPEEH-----SSFAPDSSAFPPATPRTEFPEAWGTDTPPATPRSSWPMPRPSPDPMAE 462
Cdd:PRK12323   479 APARAAPAAAPAPADDDPPPWEElppefASPAPAQPDAAPAGWVAESIPDPATADPDDAFETLAPAPAAAPAPRAA 554
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 589-754 1.86e-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: 43.22  E-value: 1.86e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034612339  589 PVGTEKAAPGIKPSVRKPIQIKKSRPREAQPlfpPVRQIVLEGLRSPASQEVQAHP---PAPLPASQGSAVPLPPEPSLA 665
Cdd:pfam03154  187 PPPGTTQAATAGPTPSAPSVPPQGSPATSQP---PNQTQSTAAPHTLIQQTPTLHPqrlPSPHPPLQPMTQPPPPSQVSP 263

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034612339  666 LFAPSPSRDSLLPPTqemrsPSPMTALQPGSTGPLPPADDKLEELIRQFEaefgdsfgLPGPPSVPIQDPENQQTCLPAP 745
Cdd:pfam03154  264 QPLPQPSLHGQMPPM-----PHSLQTGPSHMQHPVPPQPFPLTPQSSQSQ--------VPPGPSPAAPGQSQQRIHTPPS 330


                   ....*....
gi 1034612339  746 ESPFATRSP 754
Cdd:pfam03154  331 QSQLQSQQP 339
PRK14951 PRK14951
DNA polymerase III subunits gamma and tau; Provisional
 347-464 4.21e-03

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237865 [Multi-domain]  Cd Length: 618  Bit Score: 42.01  E-value: 4.21e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034612339  347 AKEKNISLQTAIAIEALTQLSSALPQPSHSTPQASCPLPEALSP----PAPFRSPQSYLRAPSWPVVPPEEH--SSFAPD 420
Cdd:PRK14951   369 AAEAAAPAEKKTPARPEAAAPAAAPVAQAAAAPAPAAAPAAAASapaaPPAAAPPAPVAAPAAAAPAAAPAAapAAVALA 448

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1034612339  421 SSAFPPATPRTEFPEAWGTDTPPATPRSSWPMPRPSPDPMAELE 464
Cdd:PRK14951   449 PAPPAQAAPETVAIPVRVAPEPAVASAAPAPAAAPAAARLTPTE 492
PRK14951 PRK14951
DNA polymerase III subunits gamma and tau; Provisional
 586-703 5.12e-03

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237865 [Multi-domain]  Cd Length: 618  Bit Score: 41.62  E-value: 5.12e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034612339  586 AGGPVGTEKAAPgIKPSVRKPiqikkSRPREAQPLFPPVRQIVLEGLRSPASQEVQAHPPAPLPASQGSAVPLPPEPSLA 665
Cdd:PRK14951   370 AEAAAPAEKKTP-ARPEAAAP-----AAAPVAQAAAAPAPAAAPAAAASAPAAPPAAAPPAPVAAPAAAAPAAAPAAAPA 443

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1034612339  666 LFAPSPSrdSLLPPTQEMRSPSPMTALQPGSTGPLPPA 703
Cdd:PRK14951   444 AVALAPA--PPAQAAPETVAIPVRVAPEPAVASAAPAP 479
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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