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Conserved domains on  [gi|767914136|ref|XP_011530987|]
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methylcytosine dioxygenase TET3 isoform X3 [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 ...
 809-1149 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: 719.85  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914136  809 CDCVEQIVEKDEGPYYTHLGSGPTVASIRELMEERYGEKGKAIRIEKVIYTGKEGKSSRGCPIAKWVIRRHTLEEKLLCL 888
Cdd:cd18897     1 CDCVEQILEKDEGPYYTHLGSGPTVASIRELMEERYGEKGKAIRIEKVIYTGKEGKSSRGCPIAKWVIRRSSEEEKLLCL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914136  889 VRHRAGHHCQNAVIVILILAWEGIPRSLGDTLYQELTDTLRKYGNPTSRRCGLNDDRTCACQGKDPNTCGASFSFGCSWS 968
Cdd:cd18897    81 VRHRAGHHCQNAVIVILILAWEGIPRALGDKLYQELTETLTKYGNPTSRRCGLNDDRTCACQGKDPNTCGASFSFGCSWS 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914136  969 MYFNGCKYARSKTPRKFRLAGDNPKEEEVLRKSFQDLATEVAPLYKRLAPQAYQNQlgplsqktsllqskgkVTNEEIAI 1048
Cdd:cd18897   161 MYFNGCKYARSKTPRKFRLIGDNPKEEENLRDNFQDLATEVAPLYKRLAPQAYQNQ----------------VTNEDIAI 224

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914136 1049 DCRLGLKEGRPFAGVTACMDFCAHAHKDQHNLYNGCTVVCTLTKEDNRCVGKIPEDEQLHVLPLYKMANTDEFGSEENQN 1128
Cdd:cd18897   225 DCRLGLKEGRPFSGVTACMDFCAHAHKDQHNLYNGCTVVCTLTKEDNRTVGKIPEDEQLHVLPLYKMSTTDEFGSEENQN 304

                         330       340
                  ....*....|....*....|.
gi 767914136 1129 AKVGSGAIQVLTAFPREVRRL 1149
Cdd:cd18897   305 EKIGSGAIQVLTSFPREVREV 325
Tet_JBP super family cl40427
oxygenase domain of ten-eleven translocation (TET) enzymes, J-binding proteins (JBPs), and ...
 1635-1763 3.63e-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: 3.63e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914136 1635 LWSDSEHNFLDENIGGVAVAPAHGSILIECARRELHATTPLKKPNRCHPTRISLVFYQHKNLNQPNHGLALWEAKMKQLA 1714
Cdd:cd18897   325 VWSDSEHNFLDENIGGVAVAPAHGSILIECARRELHATTPLKKPNRCHPTRISLVFYQHKNLNQPNHGLALWEAKMKLLA 404

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 767914136 1715 ERARARQEEAARLGLgQQEAKLYGKKRKWGGTVVAEPQQKEKKGVVPTR 1763
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 2.26e-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: 2.26e-13
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 767914136    50 GRKKRKRCGTCEPCRRLENCGACTSCTNR-------RTHQICKLRKC 89
Cdd:pfam02008    2 NRRKRRRCGVCEGCQRPEDCGQCSFCLDMpkfggpgKKKQKCRLRRC 48
PHA03247 super family cl33720
large tegument protein UL36; Provisional
 364-733 6.46e-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: 6.46e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914136  364 PLPEALSPPAPFRS--PQSYLRAPSWPVVPPEEHSSFAPDSSAFP--PATPRTEFP-EAWGTDTPPATPRSSWPMPRPSP 438
Cdd:PHA03247 2554 PLPPAAPPAAPDRSvpPPRPAPRPSEPAVTSRARRPDAPPQSARPraPVDDRGDPRgPAPPSPLPPDTHAPDPPPPSPSP 2633

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914136  439 DPMAeleqlLGSASDYIQSVFKRPEALPTKPKVKVEAPSSSPAPAPSPVLQREAPTPSSEPDTHQKAQTALQQHLHHKRS 518
Cdd:PHA03247 2634 AANE-----PDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSPPQRPRRRAARPTVGSLTSLADPPPPPPTP 2708

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914136  519 LFLEQVHDTSFPAPSEPSAPGWWPPPSS---------PVPRLPDRPPKEKKKKLPTPAGGPVGTEKAAPGIKPSVRKPIQ 589
Cdd:PHA03247 2709 EPAPHALVSATPLPPGPAAARQASPALPaapappavpAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAV 2788

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914136  590 IKKSRPREAQPLfPPVRQIVLEGLRSPASQEVQAHPPAPLPASQGSAVPLPPEPSLALFAPSPSRDSLLPPTQEMRSPSP 669
Cdd:PHA03247 2789 ASLSESRESLPS-PWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSVAPGGDVRRRPP 2867

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767914136  670 MtalQPGSTGPLPPADDKLEELIRQFEAEFGDSFGLPGPPSVPIQDPENQQTCLPAPESPFATR 733
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 ...
 809-1149 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: 719.85  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914136  809 CDCVEQIVEKDEGPYYTHLGSGPTVASIRELMEERYGEKGKAIRIEKVIYTGKEGKSSRGCPIAKWVIRRHTLEEKLLCL 888
Cdd:cd18897     1 CDCVEQILEKDEGPYYTHLGSGPTVASIRELMEERYGEKGKAIRIEKVIYTGKEGKSSRGCPIAKWVIRRSSEEEKLLCL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914136  889 VRHRAGHHCQNAVIVILILAWEGIPRSLGDTLYQELTDTLRKYGNPTSRRCGLNDDRTCACQGKDPNTCGASFSFGCSWS 968
Cdd:cd18897    81 VRHRAGHHCQNAVIVILILAWEGIPRALGDKLYQELTETLTKYGNPTSRRCGLNDDRTCACQGKDPNTCGASFSFGCSWS 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914136  969 MYFNGCKYARSKTPRKFRLAGDNPKEEEVLRKSFQDLATEVAPLYKRLAPQAYQNQlgplsqktsllqskgkVTNEEIAI 1048
Cdd:cd18897   161 MYFNGCKYARSKTPRKFRLIGDNPKEEENLRDNFQDLATEVAPLYKRLAPQAYQNQ----------------VTNEDIAI 224

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914136 1049 DCRLGLKEGRPFAGVTACMDFCAHAHKDQHNLYNGCTVVCTLTKEDNRCVGKIPEDEQLHVLPLYKMANTDEFGSEENQN 1128
Cdd:cd18897   225 DCRLGLKEGRPFSGVTACMDFCAHAHKDQHNLYNGCTVVCTLTKEDNRTVGKIPEDEQLHVLPLYKMSTTDEFGSEENQN 304

                         330       340
                  ....*....|....*....|.
gi 767914136 1129 AKVGSGAIQVLTAFPREVRRL 1149
Cdd:cd18897   305 EKIGSGAIQVLTSFPREVREV 325
TET3 cd18897
oxygenase domain of ten-eleven translocation (TET)3 methylcytosine dioxygenase and similar ...
 1635-1763 3.63e-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: 3.63e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914136 1635 LWSDSEHNFLDENIGGVAVAPAHGSILIECARRELHATTPLKKPNRCHPTRISLVFYQHKNLNQPNHGLALWEAKMKQLA 1714
Cdd:cd18897   325 VWSDSEHNFLDENIGGVAVAPAHGSILIECARRELHATTPLKKPNRCHPTRISLVFYQHKNLNQPNHGLALWEAKMKLLA 404

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 767914136 1715 ERARARQEEAARLGLgQQEAKLYGKKRKWGGTVVAEPQQKEKKGVVPTR 1763
Cdd:cd18897   405 ERARARQEEAARLGL-QQEIKPYGKKRKWGGAPAAEPQPKEKKDKIPTR 452
Tet_JBP pfam12851
Oxygenase domain of the 2OGFeDO superfamily; A double-stranded beta helix (DSBH) fold domain ...
 966-1109 1.47e-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: 1.47e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914136   966 SWSMYFNGCKYARSKTPRKFRLAGDNPKEEEVLRKSFQDLATEVAPLYKRLAPQAYQNQlgplsqktsllqskgkVTNEE 1045
Cdd:pfam12851    1 SWSMYYDGCKFPGPRKPRKFSFTPRNPKEEIKLEDELQELAALLGAIYKQIAPDLYENQ----------------IEYEQ 64

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767914136  1046 IAIDCRLGLKEGRPFAGVTACMDFCAHAHKDQHNLYNGCTVVCTLTkedNRCVGKIPEDEQLHV 1109
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 2.26e-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: 2.26e-13
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 767914136    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 ...
 1650-1694 3.37e-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: 3.37e-11
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 767914136  1650 GVAVAPAHGSILIECARRELHATTPLKKPNRchPTRISLVFYQHK 1694
Cdd:pfam12851  124 GVAFAPTPGTVLIFCGKSLEHGVTPVKNPNR--WERVSLVFYWHK 166
PHA03247 PHA03247
large tegument protein UL36; Provisional
 364-733 6.46e-11

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 68.04  E-value: 6.46e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914136  364 PLPEALSPPAPFRS--PQSYLRAPSWPVVPPEEHSSFAPDSSAFP--PATPRTEFP-EAWGTDTPPATPRSSWPMPRPSP 438
Cdd:PHA03247 2554 PLPPAAPPAAPDRSvpPPRPAPRPSEPAVTSRARRPDAPPQSARPraPVDDRGDPRgPAPPSPLPPDTHAPDPPPPSPSP 2633

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914136  439 DPMAeleqlLGSASDYIQSVFKRPEALPTKPKVKVEAPSSSPAPAPSPVLQREAPTPSSEPDTHQKAQTALQQHLHHKRS 518
Cdd:PHA03247 2634 AANE-----PDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSPPQRPRRRAARPTVGSLTSLADPPPPPPTP 2708

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914136  519 LFLEQVHDTSFPAPSEPSAPGWWPPPSS---------PVPRLPDRPPKEKKKKLPTPAGGPVGTEKAAPGIKPSVRKPIQ 589
Cdd:PHA03247 2709 EPAPHALVSATPLPPGPAAARQASPALPaapappavpAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAV 2788

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914136  590 IKKSRPREAQPLfPPVRQIVLEGLRSPASQEVQAHPPAPLPASQGSAVPLPPEPSLALFAPSPSRDSLLPPTQEMRSPSP 669
Cdd:PHA03247 2789 ASLSESRESLPS-PWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSVAPGGDVRRRPP 2867

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767914136  670 MtalQPGSTGPLPPADDKLEELIRQFEAEFGDSFGLPGPPSVPIQDPENQQTCLPAPESPFATR 733
Cdd:PHA03247 2868 S---RSPAAKPAAPARPPVRRLARPAVSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQ 2928
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 307-726 2.42e-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: 2.42e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914136   307 SEVPQI-SPQEGLPLSQSAlsiaKEKNISLQTAIAIEALTQLSSALPQPSHSTPQASCPLPEALSPPAPFRSPQSYLRAP 385
Cdd:pfam03154  143 STSPSIpSPQDNESDSDSS----AQQQILQTQPPVLQAQSGAASPPSPPPPGTTQAATAGPTPSAPSVPPQGSPATSQPP 218

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914136   386 SWPVVPPEEHSSFAPDSSAFPPATPRTEFPEAWGTDTPPATPRSSWPMPRPS-PDPMAELEQLLGSASDYIqsvfkrPEA 464
Cdd:pfam03154  219 NQTQSTAAPHTLIQQTPTLHPQRLPSPHPPLQPMTQPPPPSQVSPQPLPQPSlHGQMPPMPHSLQTGPSHM------QHP 292

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914136   465 LPTKPkvkveapssspAPAPSPVLQREAPTPSSEPDTHQKAQTalqQHLHHKRSLFLEQVHDTSFPAPSEPSAPGWWPPP 544
Cdd:pfam03154  293 VPPQP-----------FPLTPQSSQSQVPPGPSPAAPGQSQQR---IHTPPSQSQLQSQQPPREQPLPPAPLSMPHIKPP 358

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914136   545 SSPVPRLPDRPPKEKKKKLPTpagGPVGTEKAAPGIKPSVRKPI-QIKKSRPREAQP----LFPPVRQIVLEGLRSPASQ 619
Cdd:pfam03154  359 PTTPIPQLPNPQSHKHPPHLS---GPSPFQMNSNLPPPPALKPLsSLSTHHPPSAHPpplqLMPQSQQLPPPPAQPPVLT 435

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914136   620 EVQAHPP----APLPASQGSAVPLPPEPSLAlFAPSPSRDSLLPPTQEMRSPSPMTALQP------GSTGPLPPADDKLE 689
Cdd:pfam03154  436 QSQSLPPpaasHPPTSGLHQVPSQSPFPQHP-FVPGGPPPITPPSGPPTSTSSAMPGIQPpssasvSSSGPVPAAVSCPL 514

                          410       420       430
                   ....*....|....*....|....*....|....*..
gi 767914136   690 ELIrQFEAEFGDSFGLPGPPSVPIQDPENQQTCLPAP 726
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 ...
 809-1149 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: 719.85  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914136  809 CDCVEQIVEKDEGPYYTHLGSGPTVASIRELMEERYGEKGKAIRIEKVIYTGKEGKSSRGCPIAKWVIRRHTLEEKLLCL 888
Cdd:cd18897     1 CDCVEQILEKDEGPYYTHLGSGPTVASIRELMEERYGEKGKAIRIEKVIYTGKEGKSSRGCPIAKWVIRRSSEEEKLLCL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914136  889 VRHRAGHHCQNAVIVILILAWEGIPRSLGDTLYQELTDTLRKYGNPTSRRCGLNDDRTCACQGKDPNTCGASFSFGCSWS 968
Cdd:cd18897    81 VRHRAGHHCQNAVIVILILAWEGIPRALGDKLYQELTETLTKYGNPTSRRCGLNDDRTCACQGKDPNTCGASFSFGCSWS 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914136  969 MYFNGCKYARSKTPRKFRLAGDNPKEEEVLRKSFQDLATEVAPLYKRLAPQAYQNQlgplsqktsllqskgkVTNEEIAI 1048
Cdd:cd18897   161 MYFNGCKYARSKTPRKFRLIGDNPKEEENLRDNFQDLATEVAPLYKRLAPQAYQNQ----------------VTNEDIAI 224

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914136 1049 DCRLGLKEGRPFAGVTACMDFCAHAHKDQHNLYNGCTVVCTLTKEDNRCVGKIPEDEQLHVLPLYKMANTDEFGSEENQN 1128
Cdd:cd18897   225 DCRLGLKEGRPFSGVTACMDFCAHAHKDQHNLYNGCTVVCTLTKEDNRTVGKIPEDEQLHVLPLYKMSTTDEFGSEENQN 304

                         330       340
                  ....*....|....*....|.
gi 767914136 1129 AKVGSGAIQVLTAFPREVRRL 1149
Cdd:cd18897   305 EKIGSGAIQVLTSFPREVREV 325
TET cd18892
oxygenase domain of ten-eleven translocation (TET)1, TET2, and TET3 methylcytosine ...
 809-1159 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: 653.21  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914136  809 CDCVEQIV-EKDEGPYYTHLGSGPTVASIRELMEERYGEKGKAIRIEKVIYTGKEGKSSRGCPIAKWVIRRHTLEEKLLC 887
Cdd:cd18892     1 CGCFPPDEsPPEPGPYYTHLGAGPSLAALRELLEKRTGVTGKAIRIEKVIYTGKEGKTSQGCPIAKWIIRRSSLEEKYLV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914136  888 LVRHRAGHHCQNAVIVILILAWEGIPRSLGDTLYQELTDTLRKYGNPTSRRCGLNDDRTCACQGKDPNTCGASFSFGCSW 967
Cdd:cd18892    81 LVKHRPGHFCHSAFIVICIVAWEGVPQSNADELYSLLTDKLNKFGLPTKRRCGTNEERTCACQGLDPETCGASFSFGCSW 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914136  968 SMYFNGCKYARSKTPRKFRLAGdnPKEEEVLRKSFQDLATEVAPLYKRLAPQAYQNQlgplsqktsllqskgkVTNEEIA 1047
Cdd:cd18892   161 SMYYNGCKFARSKTVRKFRLSD--KSEEEELEDKLQNLATHLAPLYKSLAPDSYKNQ----------------VQFEEEA 222

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914136 1048 IDCRLGLKEGRPFAGVTACMDFCAHAHKDQHNLYNGCTVVCTLTKEDNRCvGKIPEDEQLHVLPLYKMANTDEFGSEENQ 1127
Cdd:cd18892   223 LDCRLGLKPGRPFSGVTACVDFCAHAHKDLHNMNNGCTVVVTLTKHRNLT-KPEPEQLHVLPLYLYDMTDEDEFGSVEGQ 301

                         330       340       350
                  ....*....|....*....|....*....|..
gi 767914136 1128 NAKVGSGAIQVLTAFPREVRRLPEPAKSCRQR 1159
Cdd:cd18892   302 EEKVRNGSIEVLTKYPCEVREYWSDSEECFLD 333
TET1 cd18895
oxygenase domain of ten-eleven translocation (TET)1 methylcytosine dioxygenase and similar ...
 809-1149 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: 606.91  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914136  809 CDCVEQIVEKDEGPYYTHLGSGPTVASIRELMEERYGEKGKAIRIEKVIYTGKEGKSSRGCPIAKWVIRRHTLEEKLLCL 888
Cdd:cd18895     1 CDCVEQIIEKDEGPYYTHLGAGPSVAAVREIMENRYGEKGNAIRIEVVVYTGKEGKSSQGCPIAKWVIRRSSDEEKLLCL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914136  889 VRHRAGHHCQNAVIVILILAWEGIPRSLGDTLYQELTDTLRKYGNPTSRRCGLNDDRTCACQGKDPNTCGASFSFGCSWS 968
Cdd:cd18895    81 VRQRAGHHCQTAVIVILILAWEGIPRLLADRLYQELTQTLKKYGSPTSRRCALNEDRTCACQGLDPETCGASFSFGCSWS 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914136  969 MYFNGCKYARSKTPRKFRLAGDNPKEEEVLRKSFQDLATEVAPLYKRLAPQAYQNQlgplsqktsllqskgkVTNEEIAI 1048
Cdd:cd18895   161 MYFNGCKFARSKYPRKFRLLTDDPKEEENLESNLQNLATDVAPVYKKLAPEAFQNQ----------------VENENVAP 224

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914136 1049 DCRLGLKEGRPFAGVTACMDFCAHAHKDQHNLYNGCTVVCTLTKEDNRCVGKIPEDEQLHVLPLYKMANTDEFGSEENQN 1128
Cdd:cd18895   225 DCRLGSKEGRPFSGVTACIDFCAHAHKDTHNMHNGSTVVCTLTKEDNRSVGVIPEDEQLHVLPLYKISDTDEFGSEEGQE 304

                         330       340
                  ....*....|....*....|.
gi 767914136 1129 AKVGSGAIQVLTAFPREVRRL 1149
Cdd:cd18895   305 AKIKNGAIQVLSAFPREVREV 325
TET2 cd18896
oxygenase domain of ten-eleven translocation (TET)2 methylcytosine dioxygenase and similar ...
 805-1161 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: 602.34  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914136  805 EFPTCDCVEQIVEKDEGPYYTHLGSGPTVASIRELMEERYGEKGKAIRIEKVIYTGKEGKSSRGCPIAKWVIRRHTLEEK 884
Cdd:cd18896     1 DFPSCSCVEQIIEKDEGPYYTHLGAGPNVAAIREIMEERFGQKGKAIRIERVIYTGKEGKSSQGCPIAKWVIRRSSEEEK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914136  885 LLCLVRHRAGHHCQNAVIVILILAWEGIPRSLGDTLYQELTDTLRKYGNPTSRRCGLNDDRTCACQGKDPNTCGASFSFG 964
Cdd:cd18896    81 LLCLVRERAGHSCETAVIVILILVWEGIPISLADKLYSELTDTLRKYGTLTNRRCALNEERTCACQGLDPETCGASFSFG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914136  965 CSWSMYFNGCKYARSKTPRKFRLAGDNPKEEEVLRKSFQDLATEVAPLYKRLAPQAYQNQlgplsqktsllqskgkVTNE 1044
Cdd:cd18896   161 CSWSMYYNGCKFARSKIPRKFKLLGDDPKEEEKLESNLQNLSTLMAPTYKKLAPDAYNNQ----------------IEYE 224

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914136 1045 EIAIDCRLGLKEGRPFAGVTACMDFCAHAHKDQHNLYNGCTVVCTLTKEDNRCVGKIPEDEQLHVLPLYKMANTDEFGSE 1124
Cdd:cd18896   225 HRAPDCRLGLKEGRPFSGVTACLDFCAHAHRDLHNMQNGSTLVCTLTREDNREIGKIPEDEQLHVLPLYKVSDVDEFGST 304

                         330       340       350
                  ....*....|....*....|....*....|....*..
gi 767914136 1125 ENQNAKVGSGAIQVLTAFPREVRRLPEPAKSCRQRQL 1161
Cdd:cd18896   305 EAQEEKKRNGAIQVLSSFRRKVRMLAEPVKTCRQRKL 341
TET3 cd18897
oxygenase domain of ten-eleven translocation (TET)3 methylcytosine dioxygenase and similar ...
 1635-1763 3.63e-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: 3.63e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914136 1635 LWSDSEHNFLDENIGGVAVAPAHGSILIECARRELHATTPLKKPNRCHPTRISLVFYQHKNLNQPNHGLALWEAKMKQLA 1714
Cdd:cd18897   325 VWSDSEHNFLDENIGGVAVAPAHGSILIECARRELHATTPLKKPNRCHPTRISLVFYQHKNLNQPNHGLALWEAKMKLLA 404

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 767914136 1715 ERARARQEEAARLGLgQQEAKLYGKKRKWGGTVVAEPQQKEKKGVVPTR 1763
Cdd:cd18897   405 ERARARQEEAARLGL-QQEIKPYGKKRKWGGAPAAEPQPKEKKDKIPTR 452
Tet_JBP cd14946
oxygenase domain of ten-eleven translocation (TET) enzymes, J-binding proteins (JBPs), and ...
 836-1114 5.17e-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: 190.28  E-value: 5.17e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914136  836 IRELMEERYG-EKGKAIRIEKVIYTGKEGKSsRGCPIAKWVIRRhtleEKLLCLVRHRAGhhcqnavIVILILAWEGIPR 914
Cdd:cd14946     1 LLENMLSKCGtQQSFANANITLKYEGKEGKS-QGCPKALKNVRT----SKLAYFVCDHDG-------SVILAYVPEVLPK 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914136  915 SLGDTLYQELTDTLRKYGNptsrrcglnddrtcacqgKDPNTCGASFSFGCSWSMYFNGCKyarsktprkfRLAGDNPKE 994
Cdd:cd14946    69 ELVEEFTEKLESIQTKRGT------------------LDPETKGDTGYSGILDNSMPFNYV----------TADLSQELG 120

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914136  995 EEVLRKSFQDLATEVAPLYKRLAPQAYQNQlgplsqktsllqskgkVTNEEIAIDCRLGLKEGRPFAGVTACMD-FCAHA 1073
Cdd:cd14946   121 QYLSEIVNPQISYYISKLLTCVSPRTINYL----------------VEYEHRSLNDSYYALNNCLYPSTAFNSLkRIRKP 184

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 767914136 1074 HKDQHNLYNGCTVVCTLTKEDNrcvgkipeDEQLHVLPLYK 1114
Cdd:cd14946   185 HKDNLDIQNGPSSLFYFGNFQN--------TEGYLELTLKK 217
TET2 cd18896
oxygenase domain of ten-eleven translocation (TET)2 methylcytosine dioxygenase and similar ...
 1635-1727 9.74e-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: 9.74e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914136 1635 LWSDSEHNFLDENIGGVAVAPAHGSILIECARRELHATTPLKKPNRCHPTRISLVFYQHKNLNQPNHGLALWEAKMkqlA 1714
Cdd:cd18896   345 VWSDSEQSFLDPDIGGVAVAPSHGSILIECAKRELHATTPLKNPNRNHPTRISLVFYQHKSMNEPKHGLALWEAKM---A 421

                          90
                  ....*....|...
gi 767914136 1715 ERARARQEEAARL 1727
Cdd:cd18896   422 EKAREKEEECEKY 434
TET1 cd18895
oxygenase domain of ten-eleven translocation (TET)1 methylcytosine dioxygenase and similar ...
 1635-1723 2.69e-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: 2.69e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914136 1635 LWSDSEHNFLDENIGGVAVAPAHGSILIECARRELHATTPLKKPNRCHPTRISLVFYQHKNLNQPNHGLALWEAKMkqlA 1714
Cdd:cd18895   325 VWSDSEHNFLDEDIGGVAVAPSHGSILIECARRELHATTPIKKPNRNHPTRISLVFYQHKNLNEPKHGLALWEAKM---A 401


                  ....*....
gi 767914136 1715 ERARARQEE 1723
Cdd:cd18895   402 EKAKEKEKE 410
TET cd18892
oxygenase domain of ten-eleven translocation (TET)1, TET2, and TET3 methylcytosine ...
 1636-1710 2.71e-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: 154.76  E-value: 2.71e-40
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767914136 1636 WSDSEHNFLDENIGGVAVAPAHGSILIECARRELHATTPLKKPNRCHPTRISLVFYQHKNLNQPNHGLALWEAKM 1710
Cdd:cd18892   324 WSDSEECFLDPDIGGVAIALSHGSVLFECAKRELHATTPLKNPNRQHPTRISLVFYQHKNLNYSRHGLAEYEAKM 398
Tet_JBP pfam12851
Oxygenase domain of the 2OGFeDO superfamily; A double-stranded beta helix (DSBH) fold domain ...
 966-1109 1.47e-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: 1.47e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914136   966 SWSMYFNGCKYARSKTPRKFRLAGDNPKEEEVLRKSFQDLATEVAPLYKRLAPQAYQNQlgplsqktsllqskgkVTNEE 1045
Cdd:pfam12851    1 SWSMYYDGCKFPGPRKPRKFSFTPRNPKEEIKLEDELQELAALLGAIYKQIAPDLYENQ----------------IEYEQ 64

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767914136  1046 IAIDCRLGLKEGRPFAGVTACMDFCAHAHKDQHNLYNGCTVVCTLTkedNRCVGKIPEDEQLHV 1109
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 2.26e-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: 2.26e-13
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 767914136    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 ...
 1648-1694 7.33e-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: 7.33e-13
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 767914136 1648 IGGVAVAPAHGSILIECARRELHATTPLKKPNRcHPTRISLVFYQHK 1694
Cdd:cd14946   219 IGNCAVFVQPGDVLFFKGNEYKHVVTNITNPNN-HGWRISLVYYAHK 264
Tet_JBP pfam12851
Oxygenase domain of the 2OGFeDO superfamily; A double-stranded beta helix (DSBH) fold domain ...
 1650-1694 3.37e-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: 3.37e-11
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 767914136  1650 GVAVAPAHGSILIECARRELHATTPLKKPNRchPTRISLVFYQHK 1694
Cdd:pfam12851  124 GVAFAPTPGTVLIFCGKSLEHGVTPVKNPNR--WERVSLVFYWHK 166
PHA03247 PHA03247
large tegument protein UL36; Provisional
 364-733 6.46e-11

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 68.04  E-value: 6.46e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914136  364 PLPEALSPPAPFRS--PQSYLRAPSWPVVPPEEHSSFAPDSSAFP--PATPRTEFP-EAWGTDTPPATPRSSWPMPRPSP 438
Cdd:PHA03247 2554 PLPPAAPPAAPDRSvpPPRPAPRPSEPAVTSRARRPDAPPQSARPraPVDDRGDPRgPAPPSPLPPDTHAPDPPPPSPSP 2633

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914136  439 DPMAeleqlLGSASDYIQSVFKRPEALPTKPKVKVEAPSSSPAPAPSPVLQREAPTPSSEPDTHQKAQTALQQHLHHKRS 518
Cdd:PHA03247 2634 AANE-----PDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSPPQRPRRRAARPTVGSLTSLADPPPPPPTP 2708

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914136  519 LFLEQVHDTSFPAPSEPSAPGWWPPPSS---------PVPRLPDRPPKEKKKKLPTPAGGPVGTEKAAPGIKPSVRKPIQ 589
Cdd:PHA03247 2709 EPAPHALVSATPLPPGPAAARQASPALPaapappavpAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAV 2788

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914136  590 IKKSRPREAQPLfPPVRQIVLEGLRSPASQEVQAHPPAPLPASQGSAVPLPPEPSLALFAPSPSRDSLLPPTQEMRSPSP 669
Cdd:PHA03247 2789 ASLSESRESLPS-PWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSVAPGGDVRRRPP 2867

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767914136  670 MtalQPGSTGPLPPADDKLEELIRQFEAEFGDSFGLPGPPSVPIQDPENQQTCLPAPESPFATR 733
Cdd:PHA03247 2868 S---RSPAAKPAAPARPPVRRLARPAVSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQ 2928
PHA03247 PHA03247
large tegument protein UL36; Provisional
 340-715 7.26e-08

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 58.03  E-value: 7.26e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914136  340 AIEALTQLSSALPQPSHSTPQASCPLPEALSPPAPFRSPQSYLRAPSWPVVPPEEHSSFAPDSSAFPPATPRTEFPEAwg 419
Cdd:PHA03247 2691 TVGSLTSLADPPPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPA-- 2768

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914136  420 tDTPPATPRSSWP--MPRPSPDPMAELEQLLGSASDYIQSVFKRPEALPTKPKVKVEAPSsspapapspvlqrEAPTPSS 497
Cdd:PHA03247 2769 -PAPPAAPAAGPPrrLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGP-------------LPPPTSA 2834

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914136  498 EPdthqkaqtalqqhlhhkrslfleqvhdTSFPAPSEPSAPGWWPPPSSPVprlpdrppkekkkklptpaGGPV---GTE 574
Cdd:PHA03247 2835 QP---------------------------TAPPPPPGPPPPSLPLGGSVAP-------------------GGDVrrrPPS 2868

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914136  575 KAAPGI-----KPSVRKPIQIKKSRPREAQPLFPPvrqivleglrspaSQEVQAHPPAPLPASQGSAVPLPPEPSLALFA 649
Cdd:PHA03247 2869 RSPAAKpaapaRPPVRRLARPAVSRSTESFALPPD-------------QPERPPQPQAPPPPQPQPQPPPPPQPQPPPPP 2935

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767914136  650 PSPSRDSLLPPTQEMRSPSPMTALQPGSTGPLPPADdklEELIRQFEAEFGDSFGLPGPPSVPIQD 715
Cdd:PHA03247 2936 PPRPQPPLAPTTDPAGAGEPSGAVPQPWLGALVPGR---VAVPRFRVPQPAPSREAPASSTPPLTG 2998
PHA03247 PHA03247
large tegument protein UL36; Provisional
 366-784 4.46e-07

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 55.33  E-value: 4.46e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914136  366 PEALSPPAPFRSPQSYLRAPSWPVVPPEEHS---SFAPDSSAFPPATPRT----------------EFPEAWGTDTPPAT 426
Cdd:PHA03247 2484 AEARFPFAAGAAPDPGGGGPPDPDAPPAPSRlapAILPDEPVGEPVHPRMltwirgleelasddagDPPPPLPPAAPPAA 2563

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914136  427 PRSSWPMPRPSPDPmaeleqllgsASDYIQSVFKRPEALP--TKPKVKVEAPSSSPapapspvlqREAPTPSSEPDTHQK 504
Cdd:PHA03247 2564 PDRSVPPPRPAPRP----------SEPAVTSRARRPDAPPqsARPRAPVDDRGDPR---------GPAPPSPLPPDTHAP 2624

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914136  505 AqtalqqhlhhkrslfleqvhdtsfPAPSEPSApgwwppPSSPVPRLPDRPPKEKKKKLPTPAGGPVGTEKAAPGIKPSV 584
Cdd:PHA03247 2625 D------------------------PPPPSPSP------AANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAA 2674

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914136  585 RKPIQIKKSRPREAQPLFPPvrqivLEGLRSPASQEvqaHPPAPLPASQGSAVPLPPEPSLALFAPSPSRDSLLPPtqem 664
Cdd:PHA03247 2675 QASSPPQRPRRRAARPTVGS-----LTSLADPPPPP---PTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPP---- 2742

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914136  665 rsPSPMTALQPGstGPLPPADDKLEElirqfeaefgdSFGLPGPPSVPIQDPENQQT------CLPAPESPFATRSPKQI 738
Cdd:PHA03247 2743 --AVPAGPATPG--GPARPARPPTTA-----------GPPAPAPPAAPAAGPPRRLTrpavasLSESRESLPSPWDPADP 2807

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*.
gi 767914136  739 KIESSGAVTVLSTTcfhSEEGGQEATPTKAENPLTPTLSGFLESPL 784
Cdd:PHA03247 2808 PAAVLAPAAALPPA---ASPAGPLPPPTSAQPTAPPPPPGPPPPSL 2850
PHA03247 PHA03247
large tegument protein UL36; Provisional
 294-682 1.47e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 50.32  E-value: 1.47e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914136  294 AGLPAPSTRP----LLSSEVPQISPQEGLPLSQSALSIAKEKNISLQTAIAIEALTQLSSALPQPSHSTPQASCPLPEAL 369
Cdd:PHA03247 2609 RGPAPPSPLPpdthAPDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSPPQRPRRRAA 2688

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914136  370 SPPApfrSPQSYLRAPSWPVVPPEehssfaPDSSAFPPATPRTEFPEAWGTDTPPATPRsswPMPRPSPDpmaeleqllG 449
Cdd:PHA03247 2689 RPTV---GSLTSLADPPPPPPTPE------PAPHALVSATPLPPGPAAARQASPALPAA---PAPPAVPA---------G 2747

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914136  450 SASDYIQSVFKRPEAL-----PTKPKVKVEAPSSSPAPAPSPVLQREAPTPSSEPDTHQKAQTALQQHlhhkrslflEQV 524
Cdd:PHA03247 2748 PATPGGPARPARPPTTagppaPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPA---------AAL 2818

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914136  525 HDTSFPAPSEPSAPGWWPPPSSPVPRLPDRPPKEkkkklptpaGGPVgtekaAPGIKPSVRKPIQIKKSRPreAQPLFPP 604
Cdd:PHA03247 2819 PPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPL---------GGSV-----APGGDVRRRPPSRSPAAKP--AAPARPP 2882

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914136  605 VRQIVLEGL-RSPASQEVQAHPPAPLPASQGSAVPLPPEPSLALFAPSPsrdsllPPTQEMRSPSPM-----TALQPGST 678
Cdd:PHA03247 2883 VRRLARPAVsRSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQP------PPPPPPRPQPPLapttdPAGAGEPS 2956


                  ....
gi 767914136  679 GPLP 682
Cdd:PHA03247 2957 GAVP 2960
PRK14950 PRK14950
DNA polymerase III subunits gamma and tau; Provisional
 325-465 2.14e-04

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237864 [Multi-domain]  Cd Length: 585  Bit Score: 45.96  E-value: 2.14e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914136  325 LSIAKEKNISLQTAIaIEALTqlsSALPQPSHSTPQASCPLPeALSPPAPFRSPQSYLRAPSwPVVPPEEHSSFAPDSSA 404
Cdd:PRK14950  341 LRTTSYGQLPLELAV-IEALL---VPVPAPQPAKPTAAAPSP-VRPTPAPSTRPKAAAAANI-PPKEPVRETATPPPVPP 414

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767914136  405 FPPATPRTEFPEAWGTDTP-----PATPRSSWPMPRPSPD-----PMAELEQLLGSASDYIQSVFKRPEAL 465
Cdd:PRK14950  415 RPVAPPVPHTPESAPKLTRaaipvDEKPKYTPPAPPKEEEkaliaDGDVLEQLEAIWKQILRDVPPRSPAV 485
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 307-726 2.42e-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: 2.42e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914136   307 SEVPQI-SPQEGLPLSQSAlsiaKEKNISLQTAIAIEALTQLSSALPQPSHSTPQASCPLPEALSPPAPFRSPQSYLRAP 385
Cdd:pfam03154  143 STSPSIpSPQDNESDSDSS----AQQQILQTQPPVLQAQSGAASPPSPPPPGTTQAATAGPTPSAPSVPPQGSPATSQPP 218

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914136   386 SWPVVPPEEHSSFAPDSSAFPPATPRTEFPEAWGTDTPPATPRSSWPMPRPS-PDPMAELEQLLGSASDYIqsvfkrPEA 464
Cdd:pfam03154  219 NQTQSTAAPHTLIQQTPTLHPQRLPSPHPPLQPMTQPPPPSQVSPQPLPQPSlHGQMPPMPHSLQTGPSHM------QHP 292

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914136   465 LPTKPkvkveapssspAPAPSPVLQREAPTPSSEPDTHQKAQTalqQHLHHKRSLFLEQVHDTSFPAPSEPSAPGWWPPP 544
Cdd:pfam03154  293 VPPQP-----------FPLTPQSSQSQVPPGPSPAAPGQSQQR---IHTPPSQSQLQSQQPPREQPLPPAPLSMPHIKPP 358

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914136   545 SSPVPRLPDRPPKEKKKKLPTpagGPVGTEKAAPGIKPSVRKPI-QIKKSRPREAQP----LFPPVRQIVLEGLRSPASQ 619
Cdd:pfam03154  359 PTTPIPQLPNPQSHKHPPHLS---GPSPFQMNSNLPPPPALKPLsSLSTHHPPSAHPpplqLMPQSQQLPPPPAQPPVLT 435

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914136   620 EVQAHPP----APLPASQGSAVPLPPEPSLAlFAPSPSRDSLLPPTQEMRSPSPMTALQP------GSTGPLPPADDKLE 689
Cdd:pfam03154  436 QSQSLPPpaasHPPTSGLHQVPSQSPFPQHP-FVPGGPPPITPPSGPPTSTSSAMPGIQPpssasvSSSGPVPAAVSCPL 514

                          410       420       430
                   ....*....|....*....|....*....|....*..
gi 767914136   690 ELIrQFEAEFGDSFGLPGPPSVPIQDPENQQTCLPAP 726
Cdd:pfam03154  515 PPV-QIKEEALDEAEEPESPPPPPRSPSPEPTVVNTP 550
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
570-734 3.95e-04

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 45.25  E-value: 3.95e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914136  570 PVGTEKAAPGIKPSVRKPIQIKKSRPREAQPLfPPVRQIVLEGlRSPASQEVQAHPPAPLPASQGSAVPLPPEPSLALFA 649
Cdd:PRK12323  402 PPAAPAAAPAAAAAARAVAAAPARRSPAPEAL-AAARQASARG-PGGAPAPAPAPAAAPAAAARPAAAGPRPVAAAAAAA 479

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914136  650 PSPSR--------DSLLPPTQEMRSPSPMTALQPGSTGPLP-PADDKLEELIRQFEAEFGDSfgLPGPPSVPIQDPENQQ 720
Cdd:PRK12323  480 PARAApaaapapaDDDPPPWEELPPEFASPAPAQPDAAPAGwVAESIPDPATADPDDAFETL--APAPAAAPAPRAAAAT 557

                         170
                  ....*....|....
gi 767914136  721 TCLPAPESPFATRS 734
Cdd:PRK12323  558 EPVVAPRPPRASAS 571
PTZ00449 PTZ00449
104 kDa microneme/rhoptry antigen; Provisional
 570-805 4.57e-04

104 kDa microneme/rhoptry antigen; Provisional


Pssm-ID: 185628 [Multi-domain]  Cd Length: 943  Bit Score: 45.07  E-value: 4.57e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914136  570 PVGTEKAAPGIKP-SVRKPIQIKKS-RPREAQ-PLFP--PVRQIVLEGLRSPASQEVQAHPPAPLPASQGSAvPLPPEPS 644
Cdd:PTZ00449  573 PTLSKKPEFPKDPkHPKDPEEPKKPkRPRSAQrPTRPksPKLPELLDIPKSPKRPESPKSPKRPPPPQRPSS-PERPEGP 651

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914136  645 LALFAPSPSRDSLLP--PT--QEMRSPSPMTALQPGSTGPLPPADDKLEELIRQFEAEF-GDSFGLPGP----------- 708
Cdd:PTZ00449  652 KIIKSPKPPKSPKPPfdPKfkEKFYDDYLDAAAKSKETKTTVVLDESFESILKETLPETpGTPFTTPRPlppklprdeef 731

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914136  709 PSVPIQDPENQQtclPAPESPFATRSPKQIKIESSGAVTVLSTTCfhSEEGGQEATPTKAENPLTPTLSGflESPLKYLD 788
Cdd:PTZ00449  732 PFEPIGDPDAEQ---PDDIEFFTPPEEERTFFHETPADTPLPDIL--AEEFKEEDIHAETGEPDEAMKRP--DSPSEHED 804

                         250
                  ....*....|....*..
gi 767914136  789 TPTKSLLDTPAKRAQAE 805
Cdd:PTZ00449  805 KPPGDHPSLPKKRHRLD 821
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 348-737 1.39e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 43.44  E-value: 1.39e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914136  348 SSALPQPSHSTPQAscPLPEALSPPAPFRSPQSYLRAPSWPVVP-PEEHSSFAPDSSAFPPATPRTEFPEAWGTDTPPAT 426
Cdd:PRK07764  419 AAAAPAPAAAPQPA--PAPAPAPAPPSPAGNAPAGGAPSPPPAAaPSAQPAPAPAAAPEPTAAPAPAPPAAPAPAAAPAA 496

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914136  427 PRSswPMPRPSPDPMAELE----QLLGSASDYIQSVFkrpEALPTKPKVkveapssspAPAPSPVLQREAPTPS-----S 497
Cdd:PRK07764  497 PAA--PAAPAGADDAATLRerwpEILAAVPKRSRKTW---AILLPEATV---------LGVRGDTLVLGFSTGGlarrfA 562

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914136  498 EPDTHQKAQTALQQHLHhkRSLFLEQVHDTSFPAPSEPSAPGWWPPPSSPVPRLPDRPPKEKKKKLPTPAGGPVGTEKAA 577
Cdd:PRK07764  563 SPGNAEVLVTALAEELG--GDWQVEAVVGPAPGAAGGEGPPAPASSGPPEEAARPAAPAAPAAPAAPAPAGAAAAPAEAS 640

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914136  578 PGIKPSVRKPIQIKKSRPREAQPLFPPVRQIVLEGLRSPASQEVQAHPPAPLPASQGSAVPLPPEPslalfAPSPSRDSL 657
Cdd:PRK07764  641 AAPAPGVAAPEHHPKHVAVPDASDGGDGWPAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPA-----ATPPAGQAD 715

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914136  658 LPPTQEMRSPSPMTALQPGSTGPLPPADdkleelirqfEAEFGDSFGLPGPPSVPIQDPENQQTclPAPESPFATRSPKQ 737
Cdd:PRK07764  716 DPAAQPPQAAQGASAPSPAADDPVPLPP----------EPDDPPDPAGAPAQPPPPPAPAPAAA--PAAAPPPSPPSEEE 783
GGN pfam15685
Gametogenetin; GGN is a family of proteins largely found in mammals. It reacts with POG in the ...
 569-747 1.48e-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: 43.60  E-value: 1.48e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914136   569 GPVGTEKAAPGIK---PSVRKPIQIKKSRPreaQPLFPPVRQIVLEGLRSPASQEVQAHPPAPLPASQGSAVPlPPEPSL 645
Cdd:pfam15685  388 GPWGSPPPPPGKAhpiPGPRRPAPALLAPP---MFIFPAPTNGEPVRPGPPAPQALLPRPPPPTPPATPPPVP-PPIPQL 463

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914136   646 ALFAPSPsRDSLLPPTQEMRSPSPMTALQPGSTGPLPPAddkleELIRQFEAEFGDSFGLPGPPSVPIQ-DPenqqtcLP 724
Cdd:pfam15685  464 PALQPMP-LAAARPPTPRPCPGHGESALAPAPTAPLPPA-----LAADQAPAPALAAAPAPSPAPAPATaDP------LP 531

                          170       180
                   ....*....|....*....|...
gi 767914136   725 APESPFATRSPKQIKIESSGAVT 747
Cdd:pfam15685  532 PAPAPIKARTRKNKGPRAARGAT 554
TALPID3 pfam15324
Hedgehog signalling target; TALPID3 is a family of eukaryotic proteins that are targets for ...
 345-440 1.56e-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: 1.56e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914136   345 TQLSSALPQPSHSTPQASCPLPEALSP-PAPFRSPQ-SYLRAPSWPVVPPEEHSSFAPDSSAF--PPATPRTEFPEAwGT 420
Cdd:pfam15324  982 TLLPTPVPTPQPTPPCSPPSPLKEPSPvKTPDSSPCvSEHDFFPVKEIPPEKGADTGPAVSLVitPTVTPIATPPPA-AT 1060

                           90       100
                   ....*....|....*....|
gi 767914136   421 DTPPATPRSSWPMPRPSPDP 440
Cdd:pfam15324 1061 PTPPLSENSIDKLKSPSPEL 1080
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
293-443 1.66e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 43.33  E-value: 1.66e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914136  293 EAGLPAPSTRPLLSSEVPQISPQEGLPLSQSALSIAKEKNISLQTAIAIEALTQLSSALPQPSHSTPQASCPLPEALSPP 372
Cdd:PRK12323  399 PAAPPAAPAAAPAAAAAARAVAAAPARRSPAPEALAAARQASARGPGGAPAPAPAPAAAPAAAARPAAAGPRPVAAAAAA 478

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767914136  373 APFRSPQSYLRAPSWPVVPPEEH-----SSFAPDSSAFPPATPRTEFPEAWGTDTPPATPRSSWPMPRPSPDPMAE 443
Cdd:PRK12323  479 APARAAPAAAPAPADDDPPPWEElppefASPAPAQPDAAPAGWVAESIPDPATADPDDAFETLAPAPAAAPAPRAA 554
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 570-735 2.11e-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: 2.11e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914136   570 PVGTEKAAPGIKPSVRKPIQIKKSRPREAQPlfpPVRQIVLEGLRSPASQEVQAHP---PAPLPASQGSAVPLPPEPSLA 646
Cdd:pfam03154  187 PPPGTTQAATAGPTPSAPSVPPQGSPATSQP---PNQTQSTAAPHTLIQQTPTLHPqrlPSPHPPLQPMTQPPPPSQVSP 263

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914136   647 LFAPSPSRDSLLPPTqemrsPSPMTALQPGSTGPLPPADDKLEELIRQFEaefgdsfgLPGPPSVPIQDPENQQTCLPAP 726
Cdd:pfam03154  264 QPLPQPSLHGQMPPM-----PHSLQTGPSHMQHPVPPQPFPLTPQSSQSQ--------VPPGPSPAAPGQSQQRIHTPPS 330


                   ....*....
gi 767914136   727 ESPFATRSP 735
Cdd:pfam03154  331 QSQLQSQQP 339
PRK14951 PRK14951
DNA polymerase III subunits gamma and tau; Provisional
 328-445 4.09e-03

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237865 [Multi-domain]  Cd Length: 618  Bit Score: 42.01  E-value: 4.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914136  328 AKEKNISLQTAIAIEALTQLSSALPQPSHSTPQASCPLPEALSP----PAPFRSPQSYLRAPSWPVVPPEEH--SSFAPD 401
Cdd:PRK14951  369 AAEAAAPAEKKTPARPEAAAPAAAPVAQAAAAPAPAAAPAAAASapaaPPAAAPPAPVAAPAAAAPAAAPAAapAAVALA 448

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 767914136  402 SSAFPPATPRTEFPEAWGTDTPPATPRSSWPMPRPSPDPMAELE 445
Cdd:PRK14951  449 PAPPAQAAPETVAIPVRVAPEPAVASAAPAPAAAPAAARLTPTE 492
PRK14951 PRK14951
DNA polymerase III subunits gamma and tau; Provisional
 567-684 5.02e-03

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237865 [Multi-domain]  Cd Length: 618  Bit Score: 41.62  E-value: 5.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914136  567 AGGPVGTEKAAPgIKPSVRKPiqikkSRPREAQPLFPPVRQIVLEGLRSPASQEVQAHPPAPLPASQGSAVPLPPEPSLA 646
Cdd:PRK14951  370 AEAAAPAEKKTP-ARPEAAAP-----AAAPVAQAAAAPAPAAAPAAAASAPAAPPAAAPPAPVAAPAAAAPAAAPAAAPA 443

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 767914136  647 LFAPSPSrdSLLPPTQEMRSPSPMTALQPGSTGPLPPA 684
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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