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Conserved domains on  [gi|1622858794|ref|XP_014968151|]
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methylcytosine dioxygenase TET3 isoform X2 [Macaca mulatta]

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 ...
735-1059 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: 730.63  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622858794  735 CDCVEQIVEKDEGPYYTHLGSGPTVASIRELMEERYGEKGKAIRIEKVIYTGKEGKSSRGCPIAKWVIRRHTLEEKLLCL 814
Cdd:cd18897      1 CDCVEQILEKDEGPYYTHLGSGPTVASIRELMEERYGEKGKAIRIEKVIYTGKEGKSSRGCPIAKWVIRRSSEEEKLLCL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622858794  815 VRHRAGHHCQNAVIVILILAWEGIPRSLGDTLYQELTDTLRKYGNPTSRRCGLNDDRTCACQGKDPNTCGASFSFGCSWS 894
Cdd:cd18897     81 VRHRAGHHCQNAVIVILILAWEGIPRALGDKLYQELTETLTKYGNPTSRRCGLNDDRTCACQGKDPNTCGASFSFGCSWS 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622858794  895 MYFNGCKYARSKTPRKFRLAGDNPKEEEVLRKSFQDLATEVAPLYKRLAPQAYQNQVTNEEIAIDCRLGLKEGRPFAGVT 974
Cdd:cd18897    161 MYFNGCKYARSKTPRKFRLIGDNPKEEENLRDNFQDLATEVAPLYKRLAPQAYQNQVTNEDIAIDCRLGLKEGRPFSGVT 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622858794  975 ACMDFCAHAHKDQHNLYNGCTVVCTLTKEDNRCVGKIPEDEQLHVLPLYKMASTDEFGSEENQNAKVGSGAIQVLTAFPR 1054
Cdd:cd18897    241 ACMDFCAHAHKDQHNLYNGCTVVCTLTKEDNRTVGKIPEDEQLHVLPLYKMSTTDEFGSEENQNEKIGSGAIQVLTSFPR 320

                   ....*
gi 1622858794 1055 EVRRL 1059
Cdd:cd18897    321 EVREV 325
Tet_JBP super family cl40427
oxygenase domain of ten-eleven translocation (TET) enzymes, J-binding proteins (JBPs), and ...
1545-1673 3.98e-81

oxygenase domain of ten-eleven translocation (TET) enzymes, J-binding proteins (JBPs), and similar proteins; TET proteins are involved in DNA demethylation through iteratively oxidizing 5-methylcytosine (5mC) into 5-hydroxymethylcytosine (5hmC), 5-formylcytosine (5fC) and 5-carboxylcytosine (5caC). TET proteins contain a C-terminal catalytic domain which consists of a cysteine-rich region and a double-stranded beta-helix (DSBH) fold. Alterations in TET protein function have been linked to cancer, and TETs influence many cell differentiation processes. J binding protein (JBP) 1 and JBP2 are thymidine hydroxylases that catalyze the first step of base J biosynthesis: the hydroxylation of thymine in DNA to form 5-hydroxymethyluracil (hmU). Base J (beta-d-glucopyranosyloxymethyluracil) is a hyper-modified DNA base found in the DNA of kinetoplastids (Trypanosoma brucei, Trypanosoma cruzi, and Leishmania). JBP1 and JBP2 each contain a J-DNA binding domain and a thymidine hydroxylase domain. Members of this TET/JBP family of dioxygenases require Fe2+ and alpha-ketoglutarate (also known as 2-oxoglutarate) for activity.


The actual alignment was detected with superfamily member cd18897:

Pssm-ID: 394797  Cd Length: 452  Bit Score: 275.33  E-value: 3.98e-81
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622858794 1545 LWSDSEHNFLDENIGGVAVAPAHGSILIECARRELHATTPLKKPNRCHPTRISLVFYQHKNLNQPNHGLALWEAKMKQLA 1624
Cdd:cd18897    325 VWSDSEHNFLDENIGGVAVAPAHGSILIECARRELHATTPLKKPNRCHPTRISLVFYQHKNLNQPNHGLALWEAKMKLLA 404
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 1622858794 1625 ERARARQEEAARLGLgQQEAKLYGKKRKWGGAMVAEPQQKEKKGVVPTR 1673
Cdd:cd18897    405 ERARARQEEAARLGL-QQEIKPYGKKRKWGGAPAAEPQPKEKKDKIPTR 452
PHA03247 super family cl33720
large tegument protein UL36; Provisional
290-659 7.18e-12

large tegument protein UL36; Provisional


The actual alignment was detected with superfamily member PHA03247:

Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 71.12  E-value: 7.18e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622858794  290 PLPEALSPPAPFRS--PQSYLRAPSWPVVPPEEHSSFAPDSSAFP--PATPRTEFP-EVWGTDTPPATPRSSWPMPRPSH 364
Cdd:PHA03247  2554 PLPPAAPPAAPDRSvpPPRPAPRPSEPAVTSRARRPDAPPQSARPraPVDDRGDPRgPAPPSPLPPDTHAPDPPPPSPSP 2633
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622858794  365 DPMAeleqlLGSASDYIQSVFKRPEALPTKPKVKVEAPSSSPALAPSPVLQREAPTPSSEPDTHQKAQTALQQHLHHKRS 444
Cdd:PHA03247  2634 AANE-----PDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSPPQRPRRRAARPTVGSLTSLADPPPPPPTP 2708
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622858794  445 LFLEQAHDTSFPAPSEPSAPGWWPPPSS---------PAPRLPDRPPKEKKKKLPTPAGGPVGTEKAAPGIKPSVRKPIQ 515
Cdd:PHA03247  2709 EPAPHALVSATPLPPGPAAARQASPALPaapappavpAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAV 2788
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622858794  516 IKKSRPREAQPLfPPVRQIVLEGLRSPASQEVQAHPPAPLPASQGSAVPLPPEPSLALFAPSPSRDSLLPPTQEMRSPSP 595
Cdd:PHA03247  2789 ASLSESRESLPS-PWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSVAPGGDVRRRPP 2867
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622858794  596 MttlQPGSTGPLPPADDKLEELIRQFEAEFGDSFGLPGPPSVPIQDPENQQTCLPAPESPFATR 659
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 ...
735-1059 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: 730.63  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622858794  735 CDCVEQIVEKDEGPYYTHLGSGPTVASIRELMEERYGEKGKAIRIEKVIYTGKEGKSSRGCPIAKWVIRRHTLEEKLLCL 814
Cdd:cd18897      1 CDCVEQILEKDEGPYYTHLGSGPTVASIRELMEERYGEKGKAIRIEKVIYTGKEGKSSRGCPIAKWVIRRSSEEEKLLCL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622858794  815 VRHRAGHHCQNAVIVILILAWEGIPRSLGDTLYQELTDTLRKYGNPTSRRCGLNDDRTCACQGKDPNTCGASFSFGCSWS 894
Cdd:cd18897     81 VRHRAGHHCQNAVIVILILAWEGIPRALGDKLYQELTETLTKYGNPTSRRCGLNDDRTCACQGKDPNTCGASFSFGCSWS 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622858794  895 MYFNGCKYARSKTPRKFRLAGDNPKEEEVLRKSFQDLATEVAPLYKRLAPQAYQNQVTNEEIAIDCRLGLKEGRPFAGVT 974
Cdd:cd18897    161 MYFNGCKYARSKTPRKFRLIGDNPKEEENLRDNFQDLATEVAPLYKRLAPQAYQNQVTNEDIAIDCRLGLKEGRPFSGVT 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622858794  975 ACMDFCAHAHKDQHNLYNGCTVVCTLTKEDNRCVGKIPEDEQLHVLPLYKMASTDEFGSEENQNAKVGSGAIQVLTAFPR 1054
Cdd:cd18897    241 ACMDFCAHAHKDQHNLYNGCTVVCTLTKEDNRTVGKIPEDEQLHVLPLYKMSTTDEFGSEENQNEKIGSGAIQVLTSFPR 320

                   ....*
gi 1622858794 1055 EVRRL 1059
Cdd:cd18897    321 EVREV 325
TET3 cd18897
oxygenase domain of ten-eleven translocation (TET)3 methylcytosine dioxygenase and similar ...
1545-1673 3.98e-81

oxygenase domain of ten-eleven translocation (TET)3 methylcytosine dioxygenase and similar proteins; TET3 is involved in DNA demethylation through iteratively oxidizing 5-methylcytosine (5mC) into 5-hydroxymethylcytosine (5hmC), 5-formylcytosine (5fC) and 5-carboxylcytosine (5caC). TET proteins contain a C-terminal catalytic domain which consists of a cysteine-rich region and a double-stranded beta-helix (DSBH) fold. TET3 serves as a tumor suppressor; it acts as a suppressor of ovarian cancer by demethylating the miR-30d precursor gene promoter to block TGF-beta1 induced epithelial-mesenchymal transition (EMT). TET3 (and TET2) promoters are silenced in melanoma cells by mechanisms triggered by TGF-beta and mediated by DNA methyltransferase 3 alpha (DNMT3A), which play a functional role in the EMT process and metastasis. In addition, TET3 (and TET2) may be guardians of regulatory T cell stability and immune homeostasis. TET3 has been shown to prevent terminal differentiation of adult neural stem cells by a mechanism involving direct binding and repression of TET3 to the imprinted gene Snrpn. TET3 has also been shown to mediate the activation of hepatic stellate cells via modulation of the long non-coding RNA HIF1A-AS1 expression. TET1 belongs to the TET/JBP family of dioxygenases that require Fe2+ and alpha-ketoglutarate (also known as 2-oxoglutarate) for activity.


Pssm-ID: 380676  Cd Length: 452  Bit Score: 275.33  E-value: 3.98e-81
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622858794 1545 LWSDSEHNFLDENIGGVAVAPAHGSILIECARRELHATTPLKKPNRCHPTRISLVFYQHKNLNQPNHGLALWEAKMKQLA 1624
Cdd:cd18897    325 VWSDSEHNFLDENIGGVAVAPAHGSILIECARRELHATTPLKKPNRCHPTRISLVFYQHKNLNQPNHGLALWEAKMKLLA 404
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 1622858794 1625 ERARARQEEAARLGLgQQEAKLYGKKRKWGGAMVAEPQQKEKKGVVPTR 1673
Cdd:cd18897    405 ERARARQEEAARLGL-QQEIKPYGKKRKWGGAPAAEPQPKEKKDKIPTR 452
Tet_JBP pfam12851
Oxygenase domain of the 2OGFeDO superfamily; A double-stranded beta helix (DSBH) fold domain ...
892-1019 3.66e-43

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: 155.23  E-value: 3.66e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622858794  892 SWSMYFNGCKYARSKTPRKFRLAGDNPKEEEVLRKSFQDLATEVAPLYKRLAPQAYQNQVTNEEIAIDCRLGLKEGRPFA 971
Cdd:pfam12851    1 SWSMYYDGCKFPGPRKPRKFSFTPRNPKEEIKLEDELQELAALLGAIYKQIAPDLYENQIEYEQDAAICRLGRKWGRPFS 80
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 1622858794  972 GVTACMDFCAHAHKDQHNLYNGCTVVCTLTkedNRCVGKIPEDEQLHV 1019
Cdd:pfam12851   81 GVTVNLNFETISHRDLGNFRNGSTLLCTLT---GRYEGGRLALPQLGV 125
PHA03247 PHA03247
large tegument protein UL36; Provisional
290-659 7.18e-12

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 71.12  E-value: 7.18e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622858794  290 PLPEALSPPAPFRS--PQSYLRAPSWPVVPPEEHSSFAPDSSAFP--PATPRTEFP-EVWGTDTPPATPRSSWPMPRPSH 364
Cdd:PHA03247  2554 PLPPAAPPAAPDRSvpPPRPAPRPSEPAVTSRARRPDAPPQSARPraPVDDRGDPRgPAPPSPLPPDTHAPDPPPPSPSP 2633
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622858794  365 DPMAeleqlLGSASDYIQSVFKRPEALPTKPKVKVEAPSSSPALAPSPVLQREAPTPSSEPDTHQKAQTALQQHLHHKRS 444
Cdd:PHA03247  2634 AANE-----PDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSPPQRPRRRAARPTVGSLTSLADPPPPPPTP 2708
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622858794  445 LFLEQAHDTSFPAPSEPSAPGWWPPPSS---------PAPRLPDRPPKEKKKKLPTPAGGPVGTEKAAPGIKPSVRKPIQ 515
Cdd:PHA03247  2709 EPAPHALVSATPLPPGPAAARQASPALPaapappavpAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAV 2788
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622858794  516 IKKSRPREAQPLfPPVRQIVLEGLRSPASQEVQAHPPAPLPASQGSAVPLPPEPSLALFAPSPSRDSLLPPTQEMRSPSP 595
Cdd:PHA03247  2789 ASLSESRESLPS-PWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSVAPGGDVRRRPP 2867
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622858794  596 MttlQPGSTGPLPPADDKLEELIRQFEAEFGDSFGLPGPPSVPIQDPENQQTCLPAPESPFATR 659
Cdd:PHA03247  2868 S---RSPAAKPAAPARPPVRRLARPAVSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQ 2928
Tet_JBP pfam12851
Oxygenase domain of the 2OGFeDO superfamily; A double-stranded beta helix (DSBH) fold domain ...
1560-1604 3.41e-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: 3.41e-11
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 1622858794 1560 GVAVAPAHGSILIECARRELHATTPLKKPNRchPTRISLVFYQHK 1604
Cdd:pfam12851  124 GVAFAPTPGTVLIFCGKSLEHGVTPVKNPNR--WERVSLVFYWHK 166
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
233-652 2.17e-06

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: 52.85  E-value: 2.17e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622858794  233 SEVPQI-SPQEGLPLSQSAlsiaKEKNISLQTAIAIEALTQLSSALPQPSHSTPQASCPLPEALSPPAPFRSPQSYLRAP 311
Cdd:pfam03154  143 STSPSIpSPQDNESDSDSS----AQQQILQTQPPVLQAQSGAASPPSPPPPGTTQAATAGPTPSAPSVPPQGSPATSQPP 218
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622858794  312 SWPVVPPEEHSSFAPDSSAFPPATPRTEFPEVWGTDTPPATPRSSWPMPRPS-HDPMAELEQLLGSASDYIqsvfkrPEA 390
Cdd:pfam03154  219 NQTQSTAAPHTLIQQTPTLHPQRLPSPHPPLQPMTQPPPPSQVSPQPLPQPSlHGQMPPMPHSLQTGPSHM------QHP 292
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622858794  391 LPTKPkVKVEAPSSSPALAPSPvlQREAPTPSSEPDTHQKAQTALQQhlhhkrslfleQAHDTSFPAPSEPSAPGWWPPP 470
Cdd:pfam03154  293 VPPQP-FPLTPQSSQSQVPPGP--SPAAPGQSQQRIHTPPSQSQLQS-----------QQPPREQPLPPAPLSMPHIKPP 358
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622858794  471 SSPAPRLPDRPPKEKKKKLPTpagGPVGTEKAAPGIKPSVRKPI-QIKKSRPREAQP----LFPPVRQIVLEGLRSPASQ 545
Cdd:pfam03154  359 PTTPIPQLPNPQSHKHPPHLS---GPSPFQMNSNLPPPPALKPLsSLSTHHPPSAHPpplqLMPQSQQLPPPPAQPPVLT 435
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622858794  546 EVQAHPP----APLPASQGSAVPLPPEPSLAlFAPSPSRDSLLPPTQEMRSPSPMTTLQP------GSTGPLPPADDKLE 615
Cdd:pfam03154  436 QSQSLPPpaasHPPTSGLHQVPSQSPFPQHP-FVPGGPPPITPPSGPPTSTSSAMPGIQPpssasvSSSGPVPAAVSCPL 514
                          410       420       430
                   ....*....|....*....|....*....|....*..
gi 1622858794  616 ELIrQFEAEFGDSFGLPGPPSVPIQDPENQQTCLPAP 652
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 ...
735-1059 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: 730.63  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622858794  735 CDCVEQIVEKDEGPYYTHLGSGPTVASIRELMEERYGEKGKAIRIEKVIYTGKEGKSSRGCPIAKWVIRRHTLEEKLLCL 814
Cdd:cd18897      1 CDCVEQILEKDEGPYYTHLGSGPTVASIRELMEERYGEKGKAIRIEKVIYTGKEGKSSRGCPIAKWVIRRSSEEEKLLCL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622858794  815 VRHRAGHHCQNAVIVILILAWEGIPRSLGDTLYQELTDTLRKYGNPTSRRCGLNDDRTCACQGKDPNTCGASFSFGCSWS 894
Cdd:cd18897     81 VRHRAGHHCQNAVIVILILAWEGIPRALGDKLYQELTETLTKYGNPTSRRCGLNDDRTCACQGKDPNTCGASFSFGCSWS 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622858794  895 MYFNGCKYARSKTPRKFRLAGDNPKEEEVLRKSFQDLATEVAPLYKRLAPQAYQNQVTNEEIAIDCRLGLKEGRPFAGVT 974
Cdd:cd18897    161 MYFNGCKYARSKTPRKFRLIGDNPKEEENLRDNFQDLATEVAPLYKRLAPQAYQNQVTNEDIAIDCRLGLKEGRPFSGVT 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622858794  975 ACMDFCAHAHKDQHNLYNGCTVVCTLTKEDNRCVGKIPEDEQLHVLPLYKMASTDEFGSEENQNAKVGSGAIQVLTAFPR 1054
Cdd:cd18897    241 ACMDFCAHAHKDQHNLYNGCTVVCTLTKEDNRTVGKIPEDEQLHVLPLYKMSTTDEFGSEENQNEKIGSGAIQVLTSFPR 320

                   ....*
gi 1622858794 1055 EVRRL 1059
Cdd:cd18897    321 EVREV 325
TET cd18892
oxygenase domain of ten-eleven translocation (TET)1, TET2, and TET3 methylcytosine ...
735-1069 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: 664.76  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622858794  735 CDCVEQIV-EKDEGPYYTHLGSGPTVASIRELMEERYGEKGKAIRIEKVIYTGKEGKSSRGCPIAKWVIRRHTLEEKLLC 813
Cdd:cd18892      1 CGCFPPDEsPPEPGPYYTHLGAGPSLAALRELLEKRTGVTGKAIRIEKVIYTGKEGKTSQGCPIAKWIIRRSSLEEKYLV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622858794  814 LVRHRAGHHCQNAVIVILILAWEGIPRSLGDTLYQELTDTLRKYGNPTSRRCGLNDDRTCACQGKDPNTCGASFSFGCSW 893
Cdd:cd18892     81 LVKHRPGHFCHSAFIVICIVAWEGVPQSNADELYSLLTDKLNKFGLPTKRRCGTNEERTCACQGLDPETCGASFSFGCSW 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622858794  894 SMYFNGCKYARSKTPRKFRLAGdnPKEEEVLRKSFQDLATEVAPLYKRLAPQAYQNQVTNEEIAIDCRLGLKEGRPFAGV 973
Cdd:cd18892    161 SMYYNGCKFARSKTVRKFRLSD--KSEEEELEDKLQNLATHLAPLYKSLAPDSYKNQVQFEEEALDCRLGLKPGRPFSGV 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622858794  974 TACMDFCAHAHKDQHNLYNGCTVVCTLTKEDNRCvGKIPEDEQLHVLPLYKMASTDEFGSEENQNAKVGSGAIQVLTAFP 1053
Cdd:cd18892    239 TACVDFCAHAHKDLHNMNNGCTVVVTLTKHRNLT-KPEPEQLHVLPLYLYDMTDEDEFGSVEGQEEKVRNGSIEVLTKYP 317
                          330
                   ....*....|....*.
gi 1622858794 1054 REVRRLPEPAKSCRQR 1069
Cdd:cd18892    318 CEVREYWSDSEECFLD 333
TET1 cd18895
oxygenase domain of ten-eleven translocation (TET)1 methylcytosine dioxygenase and similar ...
735-1059 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: 617.31  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622858794  735 CDCVEQIVEKDEGPYYTHLGSGPTVASIRELMEERYGEKGKAIRIEKVIYTGKEGKSSRGCPIAKWVIRRHTLEEKLLCL 814
Cdd:cd18895      1 CDCVEQIIEKDEGPYYTHLGAGPSVAAVREIMENRYGEKGNAIRIEVVVYTGKEGKSSQGCPIAKWVIRRSSDEEKLLCL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622858794  815 VRHRAGHHCQNAVIVILILAWEGIPRSLGDTLYQELTDTLRKYGNPTSRRCGLNDDRTCACQGKDPNTCGASFSFGCSWS 894
Cdd:cd18895     81 VRQRAGHHCQTAVIVILILAWEGIPRLLADRLYQELTQTLKKYGSPTSRRCALNEDRTCACQGLDPETCGASFSFGCSWS 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622858794  895 MYFNGCKYARSKTPRKFRLAGDNPKEEEVLRKSFQDLATEVAPLYKRLAPQAYQNQVTNEEIAIDCRLGLKEGRPFAGVT 974
Cdd:cd18895    161 MYFNGCKFARSKYPRKFRLLTDDPKEEENLESNLQNLATDVAPVYKKLAPEAFQNQVENENVAPDCRLGSKEGRPFSGVT 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622858794  975 ACMDFCAHAHKDQHNLYNGCTVVCTLTKEDNRCVGKIPEDEQLHVLPLYKMASTDEFGSEENQNAKVGSGAIQVLTAFPR 1054
Cdd:cd18895    241 ACIDFCAHAHKDTHNMHNGSTVVCTLTKEDNRSVGVIPEDEQLHVLPLYKISDTDEFGSEEGQEAKIKNGAIQVLSAFPR 320

                   ....*
gi 1622858794 1055 EVRRL 1059
Cdd:cd18895    321 EVREV 325
TET2 cd18896
oxygenase domain of ten-eleven translocation (TET)2 methylcytosine dioxygenase and similar ...
731-1071 0e+00

oxygenase domain of ten-eleven translocation (TET)2 methylcytosine dioxygenase and similar proteins; TET2 is involved in DNA demethylation through iteratively oxidizing 5-methylcytosine (5mC) into 5-hydroxymethylcytosine (5hmC), 5-formylcytosine (5fC) and 5-carboxylcytosine (5caC). Human TET2 (and TET1) have been shown to be more active on 5mC-DNA than 5hmC/5fC-DNA substrates. TET proteins contain a C-terminal catalytic domain which consists of a cysteine-rich region and a double-stranded beta-helix (DSBH) fold. TET2 acts as a tumor suppressor in hematopoiesis; mutations/deletions of the TET2 gene frequently occur in multiple spectra of myeloid malignancies. TET2 (and TET3) promoters are silenced in melanoma cells by mechanisms triggered by TGF-beta and mediated by DNA methyltransferase 3 alpha (DNMT3A), which play a functional role in the epithelial-mesenchymal transition process and metastasis. In addition, TET2 (and TET3) may be guardians of regulatory T cell stability and immune homeostasis. TET2 belongs to the TET/JBP family of dioxygenases that require Fe2+ and alpha-ketoglutarate (also known as 2-oxoglutarate) for activity.


Pssm-ID: 380675  Cd Length: 434  Bit Score: 613.13  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622858794  731 EFPTCDCVEQIVEKDEGPYYTHLGSGPTVASIRELMEERYGEKGKAIRIEKVIYTGKEGKSSRGCPIAKWVIRRHTLEEK 810
Cdd:cd18896      1 DFPSCSCVEQIIEKDEGPYYTHLGAGPNVAAIREIMEERFGQKGKAIRIERVIYTGKEGKSSQGCPIAKWVIRRSSEEEK 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622858794  811 LLCLVRHRAGHHCQNAVIVILILAWEGIPRSLGDTLYQELTDTLRKYGNPTSRRCGLNDDRTCACQGKDPNTCGASFSFG 890
Cdd:cd18896     81 LLCLVRERAGHSCETAVIVILILVWEGIPISLADKLYSELTDTLRKYGTLTNRRCALNEERTCACQGLDPETCGASFSFG 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622858794  891 CSWSMYFNGCKYARSKTPRKFRLAGDNPKEEEVLRKSFQDLATEVAPLYKRLAPQAYQNQVTNEEIAIDCRLGLKEGRPF 970
Cdd:cd18896    161 CSWSMYYNGCKFARSKIPRKFKLLGDDPKEEEKLESNLQNLSTLMAPTYKKLAPDAYNNQIEYEHRAPDCRLGLKEGRPF 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622858794  971 AGVTACMDFCAHAHKDQHNLYNGCTVVCTLTKEDNRCVGKIPEDEQLHVLPLYKMASTDEFGSEENQNAKVGSGAIQVLT 1050
Cdd:cd18896    241 SGVTACLDFCAHAHRDLHNMQNGSTLVCTLTREDNREIGKIPEDEQLHVLPLYKVSDVDEFGSTEAQEEKKRNGAIQVLS 320
                          330       340
                   ....*....|....*....|.
gi 1622858794 1051 AFPREVRRLPEPAKSCRQRQL 1071
Cdd:cd18896    321 SFRRKVRMLAEPVKTCRQRKL 341
TET3 cd18897
oxygenase domain of ten-eleven translocation (TET)3 methylcytosine dioxygenase and similar ...
1545-1673 3.98e-81

oxygenase domain of ten-eleven translocation (TET)3 methylcytosine dioxygenase and similar proteins; TET3 is involved in DNA demethylation through iteratively oxidizing 5-methylcytosine (5mC) into 5-hydroxymethylcytosine (5hmC), 5-formylcytosine (5fC) and 5-carboxylcytosine (5caC). TET proteins contain a C-terminal catalytic domain which consists of a cysteine-rich region and a double-stranded beta-helix (DSBH) fold. TET3 serves as a tumor suppressor; it acts as a suppressor of ovarian cancer by demethylating the miR-30d precursor gene promoter to block TGF-beta1 induced epithelial-mesenchymal transition (EMT). TET3 (and TET2) promoters are silenced in melanoma cells by mechanisms triggered by TGF-beta and mediated by DNA methyltransferase 3 alpha (DNMT3A), which play a functional role in the EMT process and metastasis. In addition, TET3 (and TET2) may be guardians of regulatory T cell stability and immune homeostasis. TET3 has been shown to prevent terminal differentiation of adult neural stem cells by a mechanism involving direct binding and repression of TET3 to the imprinted gene Snrpn. TET3 has also been shown to mediate the activation of hepatic stellate cells via modulation of the long non-coding RNA HIF1A-AS1 expression. TET1 belongs to the TET/JBP family of dioxygenases that require Fe2+ and alpha-ketoglutarate (also known as 2-oxoglutarate) for activity.


Pssm-ID: 380676  Cd Length: 452  Bit Score: 275.33  E-value: 3.98e-81
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622858794 1545 LWSDSEHNFLDENIGGVAVAPAHGSILIECARRELHATTPLKKPNRCHPTRISLVFYQHKNLNQPNHGLALWEAKMKQLA 1624
Cdd:cd18897    325 VWSDSEHNFLDENIGGVAVAPAHGSILIECARRELHATTPLKKPNRCHPTRISLVFYQHKNLNQPNHGLALWEAKMKLLA 404
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 1622858794 1625 ERARARQEEAARLGLgQQEAKLYGKKRKWGGAMVAEPQQKEKKGVVPTR 1673
Cdd:cd18897    405 ERARARQEEAARLGL-QQEIKPYGKKRKWGGAPAAEPQPKEKKDKIPTR 452
Tet_JBP cd14946
oxygenase domain of ten-eleven translocation (TET) enzymes, J-binding proteins (JBPs), and ...
762-1024 8.19e-58

oxygenase domain of ten-eleven translocation (TET) enzymes, J-binding proteins (JBPs), and similar proteins; TET proteins are involved in DNA demethylation through iteratively oxidizing 5-methylcytosine (5mC) into 5-hydroxymethylcytosine (5hmC), 5-formylcytosine (5fC) and 5-carboxylcytosine (5caC). TET proteins contain a C-terminal catalytic domain which consists of a cysteine-rich region and a double-stranded beta-helix (DSBH) fold. Alterations in TET protein function have been linked to cancer, and TETs influence many cell differentiation processes. J binding protein (JBP) 1 and JBP2 are thymidine hydroxylases that catalyze the first step of base J biosynthesis: the hydroxylation of thymine in DNA to form 5-hydroxymethyluracil (hmU). Base J (beta-d-glucopyranosyloxymethyluracil) is a hyper-modified DNA base found in the DNA of kinetoplastids (Trypanosoma brucei, Trypanosoma cruzi, and Leishmania). JBP1 and JBP2 each contain a J-DNA binding domain and a thymidine hydroxylase domain. Members of this TET/JBP family of dioxygenases require Fe2+ and alpha-ketoglutarate (also known as 2-oxoglutarate) for activity.


Pssm-ID: 380670  Cd Length: 264  Bit Score: 201.07  E-value: 8.19e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622858794  762 IRELMEERYG-EKGKAIRIEKVIYTGKEGKSsRGCPIAKWVIRRhtleEKLLCLVRHRAGhhcqnavIVILILAWEGIPR 840
Cdd:cd14946      1 LLENMLSKCGtQQSFANANITLKYEGKEGKS-QGCPKALKNVRT----SKLAYFVCDHDG-------SVILAYVPEVLPK 68
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622858794  841 SLGDTLYQELTDTLRKYGNptsrrcglnddrtcacqgKDPNTCGASFSFGCSWSMYFNGCKyarsktprkfRLAGDNPKE 920
Cdd:cd14946     69 ELVEEFTEKLESIQTKRGT------------------LDPETKGDTGYSGILDNSMPFNYV----------TADLSQELG 120
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622858794  921 EEVLRKSFQDLATEVAPLYKRLAPQAYQNQVTNEEIAIDCRLGLKEGRPFAGVTACMD-FCAHAHKDQHNLYNGCTVVCT 999
Cdd:cd14946    121 QYLSEIVNPQISYYISKLLTCVSPRTINYLVEYEHRSLNDSYYALNNCLYPSTAFNSLkRIRKPHKDNLDIQNGPSSLFY 200
                          250       260
                   ....*....|....*....|....*
gi 1622858794 1000 LTKEDNrcvgkipeDEQLHVLPLYK 1024
Cdd:cd14946    201 FGNFQN--------TEGYLELTLKK 217
TET2 cd18896
oxygenase domain of ten-eleven translocation (TET)2 methylcytosine dioxygenase and similar ...
1545-1637 8.38e-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: 8.38e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622858794 1545 LWSDSEHNFLDENIGGVAVAPAHGSILIECARRELHATTPLKKPNRCHPTRISLVFYQHKNLNQPNHGLALWEAKMkqlA 1624
Cdd:cd18896    345 VWSDSEQSFLDPDIGGVAVAPSHGSILIECAKRELHATTPLKNPNRNHPTRISLVFYQHKSMNEPKHGLALWEAKM---A 421
                           90
                   ....*....|...
gi 1622858794 1625 ERARARQEEAARL 1637
Cdd:cd18896    422 EKAREKEEECEKY 434
TET1 cd18895
oxygenase domain of ten-eleven translocation (TET)1 methylcytosine dioxygenase and similar ...
1545-1633 2.27e-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: 2.27e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622858794 1545 LWSDSEHNFLDENIGGVAVAPAHGSILIECARRELHATTPLKKPNRCHPTRISLVFYQHKNLNQPNHGLALWEAKMkqlA 1624
Cdd:cd18895    325 VWSDSEHNFLDEDIGGVAVAPSHGSILIECARRELHATTPIKKPNRNHPTRISLVFYQHKNLNEPKHGLALWEAKM---A 401

                   ....*....
gi 1622858794 1625 ERARARQEE 1633
Cdd:cd18895    402 EKAKEKEKE 410
Tet_JBP pfam12851
Oxygenase domain of the 2OGFeDO superfamily; A double-stranded beta helix (DSBH) fold domain ...
892-1019 3.66e-43

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: 155.23  E-value: 3.66e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622858794  892 SWSMYFNGCKYARSKTPRKFRLAGDNPKEEEVLRKSFQDLATEVAPLYKRLAPQAYQNQVTNEEIAIDCRLGLKEGRPFA 971
Cdd:pfam12851    1 SWSMYYDGCKFPGPRKPRKFSFTPRNPKEEIKLEDELQELAALLGAIYKQIAPDLYENQIEYEQDAAICRLGRKWGRPFS 80
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 1622858794  972 GVTACMDFCAHAHKDQHNLYNGCTVVCTLTkedNRCVGKIPEDEQLHV 1019
Cdd:pfam12851   81 GVTVNLNFETISHRDLGNFRNGSTLLCTLT---GRYEGGRLALPQLGV 125
TET cd18892
oxygenase domain of ten-eleven translocation (TET)1, TET2, and TET3 methylcytosine ...
1546-1620 1.69e-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: 155.53  E-value: 1.69e-40
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622858794 1546 WSDSEHNFLDENIGGVAVAPAHGSILIECARRELHATTPLKKPNRCHPTRISLVFYQHKNLNQPNHGLALWEAKM 1620
Cdd:cd18892    324 WSDSEECFLDPDIGGVAIALSHGSVLFECAKRELHATTPLKNPNRQHPTRISLVFYQHKNLNYSRHGLAEYEAKM 398
Tet_JBP cd14946
oxygenase domain of ten-eleven translocation (TET) enzymes, J-binding proteins (JBPs), and ...
1558-1604 6.08e-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: 6.08e-13
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1622858794 1558 IGGVAVAPAHGSILIECARRELHATTPLKKPNRcHPTRISLVFYQHK 1604
Cdd:cd14946    219 IGNCAVFVQPGDVLFFKGNEYKHVVTNITNPNN-HGWRISLVYYAHK 264
PHA03247 PHA03247
large tegument protein UL36; Provisional
290-659 7.18e-12

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 71.12  E-value: 7.18e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622858794  290 PLPEALSPPAPFRS--PQSYLRAPSWPVVPPEEHSSFAPDSSAFP--PATPRTEFP-EVWGTDTPPATPRSSWPMPRPSH 364
Cdd:PHA03247  2554 PLPPAAPPAAPDRSvpPPRPAPRPSEPAVTSRARRPDAPPQSARPraPVDDRGDPRgPAPPSPLPPDTHAPDPPPPSPSP 2633
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622858794  365 DPMAeleqlLGSASDYIQSVFKRPEALPTKPKVKVEAPSSSPALAPSPVLQREAPTPSSEPDTHQKAQTALQQHLHHKRS 444
Cdd:PHA03247  2634 AANE-----PDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSPPQRPRRRAARPTVGSLTSLADPPPPPPTP 2708
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622858794  445 LFLEQAHDTSFPAPSEPSAPGWWPPPSS---------PAPRLPDRPPKEKKKKLPTPAGGPVGTEKAAPGIKPSVRKPIQ 515
Cdd:PHA03247  2709 EPAPHALVSATPLPPGPAAARQASPALPaapappavpAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAV 2788
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622858794  516 IKKSRPREAQPLfPPVRQIVLEGLRSPASQEVQAHPPAPLPASQGSAVPLPPEPSLALFAPSPSRDSLLPPTQEMRSPSP 595
Cdd:PHA03247  2789 ASLSESRESLPS-PWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSVAPGGDVRRRPP 2867
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622858794  596 MttlQPGSTGPLPPADDKLEELIRQFEAEFGDSFGLPGPPSVPIQDPENQQTCLPAPESPFATR 659
Cdd:PHA03247  2868 S---RSPAAKPAAPARPPVRRLARPAVSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQ 2928
Tet_JBP pfam12851
Oxygenase domain of the 2OGFeDO superfamily; A double-stranded beta helix (DSBH) fold domain ...
1560-1604 3.41e-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: 3.41e-11
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 1622858794 1560 GVAVAPAHGSILIECARRELHATTPLKKPNRchPTRISLVFYQHK 1604
Cdd:pfam12851  124 GVAFAPTPGTVLIFCGKSLEHGVTPVKNPNR--WERVSLVFYWHK 166
PHA03247 PHA03247
large tegument protein UL36; Provisional
266-641 3.02e-09

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 62.26  E-value: 3.02e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622858794  266 AIEALTQLSSALPQPSHSTPQASCPLPEALSPPAPFRSPQSYLRAPSWPVVPPEEHSSFAPDSSAFPPATPRTEFPEvwg 345
Cdd:PHA03247  2691 TVGSLTSLADPPPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAGPP--- 2767
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622858794  346 TDTPPATPRSSWP--MPRPSHDPMAELEQLLGSASDyiqsvfKRPEALPTKPKVKVEAPSSSPAlAPSPVLQREAPTPSS 423
Cdd:PHA03247  2768 APAPPAAPAAGPPrrLTRPAVASLSESRESLPSPWD------PADPPAAVLAPAAALPPAASPA-GPLPPPTSAQPTAPP 2840
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622858794  424 EPdthqkaqtalqqhlhhkrslfleqahdtsfPAPSEPSapgwwpppsspaprlpdrppkeKKKKLPTPAGGPV---GTE 500
Cdd:PHA03247  2841 PP------------------------------PGPPPPS----------------------LPLGGSVAPGGDVrrrPPS 2868
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622858794  501 KAAPGI-----KPSVRKPIQIKKSRPREAQPLFPPvrqivleglrspaSQEVQAHPPAPLPASQGSAVPLPPEPSLALFA 575
Cdd:PHA03247  2869 RSPAAKpaapaRPPVRRLARPAVSRSTESFALPPD-------------QPERPPQPQAPPPPQPQPQPPPPPQPQPPPPP 2935
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622858794  576 PSPSRDSLLPPTQEMRSPSPMTTLQPGSTGPLPPADdklEELIRQFEAEFGDSFGLPGPPSVPIQD 641
Cdd:PHA03247  2936 PPRPQPPLAPTTDPAGAGEPSGAVPQPWLGALVPGR---VAVPRFRVPQPAPSREAPASSTPPLTG 2998
PHA03247 PHA03247
large tegument protein UL36; Provisional
187-655 6.67e-09

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 61.11  E-value: 6.67e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622858794  187 PDYLEWLEGKIKSVVMEGGEERPRLPGPlppgeaglpAPSTRPLLSSEVPQISPQeglPLSQSALSIAKEKNISLQTAia 266
Cdd:PHA03247  2531 PRMLTWIRGLEELASDDAGDPPPPLPPA---------APPAAPDRSVPPPRPAPR---PSEPAVTSRARRPDAPPQSA-- 2596
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622858794  267 iEALTQLSSALPQPSHSTPQASCPLPEALSPPAPFRSPQSYLRAPSWPVVPPEehssfaPDSSAFPPATPRTEFPEVWGT 346
Cdd:PHA03247  2597 -RPRAPVDDRGDPRGPAPPSPLPPDTHAPDPPPPSPSPAANEPDPHPPPTVPP------PERPRDDPAPGRVSRPRRARR 2669
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622858794  347 DTPPATPRSSWPMPRPSHDPMAeleqlLGSASDyiqsvFKRPEALPTKPKVKVEAPSSSPALAPSPVLQREA-PTPSSEP 425
Cdd:PHA03247  2670 LGRAAQASSPPQRPRRRAARPT-----VGSLTS-----LADPPPPPPTPEPAPHALVSATPLPPGPAAARQAsPALPAAP 2739
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622858794  426 DTHQKAQTALQQHLHHKRSLFLEQAHDTSFPAPSEPSAPGWWPPPSSPAPRLPDRPPKEKKKKLPTPAGGPVGTEKAA-- 503
Cdd:PHA03247  2740 APPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAAlp 2819
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622858794  504 PGIKPSVRKPIQIKKSRPREAQPLFPPVRQIVLEGLRSPASqEVQAHPPAPLPASQGSAVPLPPEPSLALFAPSPSRDSL 583
Cdd:PHA03247  2820 PAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSVAPGG-DVRRRPPSRSPAAKPAAPARPPVRRLARPAVSRSTESF 2898
                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622858794  584 -LPPTQEMRSPSPMTTLQPGSTGPLPPADDKLEELIRQfeaefgdsfGLPGPPSVPIQDPENQQTCLPAPESP 655
Cdd:PHA03247  2899 aLPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPP---------PRPQPPLAPTTDPAGAGEPSGAVPQP 2962
PHA03247 PHA03247
large tegument protein UL36; Provisional
292-710 2.67e-07

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 56.10  E-value: 2.67e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622858794  292 PEALSPPAPFRSPQSYLRAPSWPVVPPEEHS---SFAPDSSAFPPATPRT----------------EFPEVWGTDTPPAT 352
Cdd:PHA03247  2484 AEARFPFAAGAAPDPGGGGPPDPDAPPAPSRlapAILPDEPVGEPVHPRMltwirgleelasddagDPPPPLPPAAPPAA 2563
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622858794  353 PRSSWPMPRPSHDPmaeleqllgsASDYIQSVFKRPEALP--TKPKVKVEAPSSSPALAPSpvlqreAPTPssePDTHQK 430
Cdd:PHA03247  2564 PDRSVPPPRPAPRP----------SEPAVTSRARRPDAPPqsARPRAPVDDRGDPRGPAPP------SPLP---PDTHAP 2624
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622858794  431 AqtalqqhlhhkrslfleqahdtsfPAPSEPSApgwwppPSSPAPRLPDRPPKEKKKKLPTPAGGPVGTEKAAPGIKPSV 510
Cdd:PHA03247  2625 D------------------------PPPPSPSP------AANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAA 2674
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622858794  511 RKPIQIKKSRPREAQPLFPPvrqivLEGLRSPASQEvqaHPPAPLPASQGSAVPLPPEPSLALFAPSPSRDSLLPPtqem 590
Cdd:PHA03247  2675 QASSPPQRPRRRAARPTVGS-----LTSLADPPPPP---PTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPP---- 2742
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622858794  591 rsPSPMTTLQPGstGPLPPADDKLEElirqfeaefgdSFGLPGPPSVPIQDPENQQT------CLPAPESPFATRSPKQI 664
Cdd:PHA03247  2743 --AVPAGPATPG--GPARPARPPTTA-----------GPPAPAPPAAPAAGPPRRLTrpavasLSESRESLPSPWDPADP 2807
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*.
gi 1622858794  665 KIESSGAVTVLSTTcfhSEEGGQEATPTKAENPLTPTLSGFLESPL 710
Cdd:PHA03247  2808 PAAVLAPAAALPPA---ASPAGPLPPPTSAQPTAPPPPPGPPPPSL 2850
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
233-652 2.17e-06

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: 52.85  E-value: 2.17e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622858794  233 SEVPQI-SPQEGLPLSQSAlsiaKEKNISLQTAIAIEALTQLSSALPQPSHSTPQASCPLPEALSPPAPFRSPQSYLRAP 311
Cdd:pfam03154  143 STSPSIpSPQDNESDSDSS----AQQQILQTQPPVLQAQSGAASPPSPPPPGTTQAATAGPTPSAPSVPPQGSPATSQPP 218
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622858794  312 SWPVVPPEEHSSFAPDSSAFPPATPRTEFPEVWGTDTPPATPRSSWPMPRPS-HDPMAELEQLLGSASDYIqsvfkrPEA 390
Cdd:pfam03154  219 NQTQSTAAPHTLIQQTPTLHPQRLPSPHPPLQPMTQPPPPSQVSPQPLPQPSlHGQMPPMPHSLQTGPSHM------QHP 292
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622858794  391 LPTKPkVKVEAPSSSPALAPSPvlQREAPTPSSEPDTHQKAQTALQQhlhhkrslfleQAHDTSFPAPSEPSAPGWWPPP 470
Cdd:pfam03154  293 VPPQP-FPLTPQSSQSQVPPGP--SPAAPGQSQQRIHTPPSQSQLQS-----------QQPPREQPLPPAPLSMPHIKPP 358
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622858794  471 SSPAPRLPDRPPKEKKKKLPTpagGPVGTEKAAPGIKPSVRKPI-QIKKSRPREAQP----LFPPVRQIVLEGLRSPASQ 545
Cdd:pfam03154  359 PTTPIPQLPNPQSHKHPPHLS---GPSPFQMNSNLPPPPALKPLsSLSTHHPPSAHPpplqLMPQSQQLPPPPAQPPVLT 435
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622858794  546 EVQAHPP----APLPASQGSAVPLPPEPSLAlFAPSPSRDSLLPPTQEMRSPSPMTTLQP------GSTGPLPPADDKLE 615
Cdd:pfam03154  436 QSQSLPPpaasHPPTSGLHQVPSQSPFPQHP-FVPGGPPPITPPSGPPTSTSSAMPGIQPpssasvSSSGPVPAAVSCPL 514
                          410       420       430
                   ....*....|....*....|....*....|....*..
gi 1622858794  616 ELIrQFEAEFGDSFGLPGPPSVPIQDPENQQTCLPAP 652
Cdd:pfam03154  515 PPV-QIKEEALDEAEEPESPPPPPRSPSPEPTVVNTP 550
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
278-643 7.90e-05

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 47.86  E-value: 7.90e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622858794  278 PQPSHSTPQASCPLPEALSPPAPFRSPQSYLRAPSWPVVPPEEHSSFAPDSSAFPPATPRTEFPEVWGTDTPPATPRSsw 357
Cdd:PHA03307    75 PGTEAPANESRSTPTWSLSTLAPASPAREGSPTPPGPSSPDPPPPTPPPASPPPSPAPDLSEMLRPVGSPGPPPAASP-- 152
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622858794  358 PMPRPSHDPMAELEQLLGSASDYIQSVfkrPEALPTKPKVKVEAPSSSPALAPSPvlqREAPTPSSEPDTHQKAQTALQQ 437
Cdd:PHA03307   153 PAAGASPAAVASDAASSRQAALPLSSP---EETARAPSSPPAEPPPSTPPAAASP---RPPRRSSPISASASSPAPAPGR 226
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622858794  438 HLHHKRSlfleQAHDTSFPAPSEPSAPGWWPPPSSPAPRLPDRPPKEKKKKLPTPAGGPVGTEKAAPGIKPSVRKPiqik 517
Cdd:PHA03307   227 SAADDAG----ASSSDSSSSESSGCGWGPENECPLPRPAPITLPTRIWEASGWNGPSSRPGPASSSSSPRERSPSP---- 298
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622858794  518 kSRPREAQPLFPPVRQIVLEGLRSPASQEVQAHPPAPLPASQGSAVPLPPEPSLALFAPSPSRDSLLPPTQEMRSPSPMT 597
Cdd:PHA03307   299 -SPSSPGSGPAPSSPRASSSSSSSRESSSSSTSSSSESSRGAAVSPGPSPSRSPSPSRPPPPADPSSPRKRPRPSRAPSS 377
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*.
gi 1622858794  598 TLQPGSTGPLPPADDKLEELIRQFEAEFgdSFGLPGPPSVPIQDPE 643
Cdd:PHA03307   378 PAASAGRPTRRRARAAVAGRARRRDATG--RFPAGRPRPSPLDAGA 421
PHA03132 PHA03132
thymidine kinase; Provisional
314-446 1.51e-04

thymidine kinase; Provisional


Pssm-ID: 222997 [Multi-domain]  Cd Length: 580  Bit Score: 46.29  E-value: 1.51e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622858794  314 PVVPPEEHSSFAPDSSAFPPATPRTEFPEVWGTDTPPATPRSSWPMPRPSHDPMAELEQLLGS--ASDYIQSVFKRPEAL 391
Cdd:PHA03132    53 DLYPPRETGSGGGVATSTIYTVPRPPRGPEQTLDKPDSLPASRELPPGPTPVPPGGFRGASSPrlGADSTSPRFLYQVNF 132
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1622858794  392 PTKPKVKVEAPSSSPALAPSPVLQREAPTPSSE-PDTHQKAQTALQQHLHHKRSLF 446
Cdd:PHA03132   133 PVILAPIGESNSSSEELSEEEEHSRPPPSESLKvKNGGKVYPKGFSKHKTHKRSEF 188
PTZ00449 PTZ00449
104 kDa microneme/rhoptry antigen; Provisional
278-582 2.21e-04

104 kDa microneme/rhoptry antigen; Provisional


Pssm-ID: 185628 [Multi-domain]  Cd Length: 943  Bit Score: 46.22  E-value: 2.21e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622858794  278 PQPSHSTPQASCPLpealSPPAPFRsPQSyLRAPSWPVVPPEEHSSFAPDSSAFPPATPRTEFPEVWGTDTPPATprssw 357
Cdd:PTZ00449   594 PKKPKRPRSAQRPT----RPKSPKL-PEL-LDIPKSPKRPESPKSPKRPPPPQRPSSPERPEGPKIIKSPKPPKS----- 662
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622858794  358 pmPRPSHDPMAElEQLLGSASD----------------YIQSVFKrpEALPTKPKVKVEAPSSSPALAPSpvlQREAP-T 420
Cdd:PTZ00449   663 --PKPPFDPKFK-EKFYDDYLDaaaksketkttvvldeSFESILK--ETLPETPGTPFTTPRPLPPKLPR---DEEFPfE 734
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622858794  421 PSSEPDTHQKAQTALQQHLHHKRSLFLEQAHDTSFP-----------------APSEPSAPGWWPPPSSPAPRLPDRPPK 483
Cdd:PTZ00449   735 PIGDPDAEQPDDIEFFTPPEEERTFFHETPADTPLPdilaeefkeedihaetgEPDEAMKRPDSPSEHEDKPPGDHPSLP 814
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622858794  484 EKKKKLPTPAGGPVGTEKAAPGI-KPSVRKPIQIKKSRP-------REAQPLFPPVRQIVLEGLRSPASQEvQAHPPApl 555
Cdd:PTZ00449   815 KKRHRLDGLALSTTDLESDAGRIaKDASGKIVKLKRSKSfddlttvEEAEEMGAEARKIVVDDDGTEADDE-DTHPPE-- 891
                          330       340
                   ....*....|....*....|....*..
gi 1622858794  556 pASQGSAVPLPPEPSLALFAPSPSRDS 582
Cdd:PTZ00449   892 -EKHKSEVRRRRPPKKPSKPKKPSKPK 917
PRK14950 PRK14950
DNA polymerase III subunits gamma and tau; Provisional
251-391 3.35e-04

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237864 [Multi-domain]  Cd Length: 585  Bit Score: 45.19  E-value: 3.35e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622858794  251 LSIAKEKNISLQTAIaIEALTqlsSALPQPSHSTPQASCPLPeALSPPAPFRSPQSYLRAPSwPVVPPEEHSSFAPDSSA 330
Cdd:PRK14950   341 LRTTSYGQLPLELAV-IEALL---VPVPAPQPAKPTAAAPSP-VRPTPAPSTRPKAAAAANI-PPKEPVRETATPPPVPP 414
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622858794  331 FPPATPRTEFPEVWGTDTP-----PATPRSSWPMPRPSHD-----PMAELEQLLGSASDYIQSVFKRPEAL 391
Cdd:PRK14950   415 RPVAPPVPHTPESAPKLTRaaipvDEKPKYTPPAPPKEEEkaliaDGDVLEQLEAIWKQILRDVPPRSPAV 485
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
496-660 1.18e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 43.71  E-value: 1.18e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622858794  496 PVGTEKAAPGIKPSVRKPIQIKKSRPREAQPLfPPVRQIVLEGlRSPASQEVQAHPPAPLPASQGSAVPLPPEPSLALFA 575
Cdd:PRK12323   402 PPAAPAAAPAAAAAARAVAAAPARRSPAPEAL-AAARQASARG-PGGAPAPAPAPAAAPAAAARPAAAGPRPVAAAAAAA 479
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622858794  576 PSPSR--------DSLLPPTQEMRSPSPMTTLQPGSTGPLP-PADDKLEELIRQFEAEFGDSfgLPGPPSVPIQDPENQQ 646
Cdd:PRK12323   480 PARAApaaapapaDDDPPPWEELPPEFASPAPAQPDAAPAGwVAESIPDPATADPDDAFETL--APAPAAAPAPRAAAAT 557
                          170
                   ....*....|....
gi 1622858794  647 TCLPAPESPFATRS 660
Cdd:PRK12323   558 EPVVAPRPPRASAS 571
PTZ00449 PTZ00449
104 kDa microneme/rhoptry antigen; Provisional
496-731 1.83e-03

104 kDa microneme/rhoptry antigen; Provisional


Pssm-ID: 185628 [Multi-domain]  Cd Length: 943  Bit Score: 43.14  E-value: 1.83e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622858794  496 PVGTEKAAPGIKP-SVRKPIQIKKS-RPREAQ-PLFP--PVRQIVLEGLRSPASQEVQAHPPAPLPASQGSAvPLPPEPS 570
Cdd:PTZ00449   573 PTLSKKPEFPKDPkHPKDPEEPKKPkRPRSAQrPTRPksPKLPELLDIPKSPKRPESPKSPKRPPPPQRPSS-PERPEGP 651
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622858794  571 LALFAPSPSRDSLLPPTQEMRSPSPMTTLQPGS----TGPLPPADDKLEELIRQFEAEF-GDSFGLPGP----------- 634
Cdd:PTZ00449   652 KIIKSPKPPKSPKPPFDPKFKEKFYDDYLDAAAkskeTKTTVVLDESFESILKETLPETpGTPFTTPRPlppklprdeef 731
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622858794  635 PSVPIQDPENQQtclPAPESPFATRSPKQIKIESSGAVTVLSTTCfhSEEGGQEATPTKAENPLTPTLSGflESPLKYLD 714
Cdd:PTZ00449   732 PFEPIGDPDAEQ---PDDIEFFTPPEEERTFFHETPADTPLPDIL--AEEFKEEDIHAETGEPDEAMKRP--DSPSEHED 804
                          250
                   ....*....|....*..
gi 1622858794  715 TPTKSLLDTPAKRAQAE 731
Cdd:PTZ00449   805 KPPGDHPSLPKKRHRLD 821
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
496-661 3.66e-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: 42.06  E-value: 3.66e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622858794  496 PVGTEKAAPGIKPSVRKPIQIKKSRPREAQPlfpPVRQIVLEGLRSPASQEVQAHP---PAPLPASQGSAVPLPPEPSLA 572
Cdd:pfam03154  187 PPPGTTQAATAGPTPSAPSVPPQGSPATSQP---PNQTQSTAAPHTLIQQTPTLHPqrlPSPHPPLQPMTQPPPPSQVSP 263
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622858794  573 LFAPSPSRDSLLPPTqemrsPSPMTTLQPGSTGPLPPADDKLEELIRQFEaefgdsfgLPGPPSVPIQDPENQQTCLPAP 652
Cdd:pfam03154  264 QPLPQPSLHGQMPPM-----PHSLQTGPSHMQHPVPPQPFPLTPQSSQSQ--------VPPGPSPAAPGQSQQRIHTPPS 330

                   ....*....
gi 1622858794  653 ESPFATRSP 661
Cdd:pfam03154  331 QSQLQSQQP 339
PHA02682 PHA02682
ORF080 virion core protein; Provisional
270-431 6.09e-03

ORF080 virion core protein; Provisional


Pssm-ID: 177464 [Multi-domain]  Cd Length: 280  Bit Score: 40.61  E-value: 6.09e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622858794  270 LTQLSSAL----PQPSHSTPQASCPLPEALSPPAPF------RSPQSYLRAPSWPVVPPEEHSSFAPDSsafPPATPRTE 339
Cdd:PHA02682    18 LADTSSSLftkcPQATIPAPAAPCPPDADVDPLDKYsvkeagRYYQSRLKANSACMQRPSGQSPLAPSP---ACAAPAPA 94
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622858794  340 FPevwgTDTPPA-TPRSSWPMPRPSHDPMAeleqllgsasdyiQSVFKRPEALPTKPKVKVEAPSSSPALAPSPVLQREA 418
Cdd:PHA02682    95 CP----ACAPAApAPAVTCPAPAPACPPAT-------------APTCPPPAVCPAPARPAPACPPSTRQCPPAPPLPTPK 157
                          170
                   ....*....|...
gi 1622858794  419 PTPSSEPDTHQKA 431
Cdd:PHA02682   158 PAPAAKPIFLHNQ 170
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
274-663 6.88e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 41.12  E-value: 6.88e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622858794  274 SSALPQPSHSTPQAscPLPEALSPPAPFRSPQSYLRAPSWPVVP-PEEHSSFAPDSSAFPPATPRTEFPEVWGTDTPPAT 352
Cdd:PRK07764   419 AAAAPAPAAAPQPA--PAPAPAPAPPSPAGNAPAGGAPSPPPAAaPSAQPAPAPAAAPEPTAAPAPAPPAAPAPAAAPAA 496
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622858794  353 PRSSWPMPRPSHDPM-----AELEQLLGSASDYIQSVFKrPEALPTKpkvkVEAPS-----SSPALApspvlQREAptps 422
Cdd:PRK07764   497 PAAPAAPAGADDAATlrerwPEILAAVPKRSRKTWAILL-PEATVLG----VRGDTlvlgfSTGGLA-----RRFA---- 562
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622858794  423 sEPDTHQKAQTALQQHLHhkRSLFLEQAHDTSFPAPSEPSAPGWWPPPSSPAPRLPDRPPKEKKKKLPTPAGGPVGTEKA 502
Cdd:PRK07764   563 -SPGNAEVLVTALAEELG--GDWQVEAVVGPAPGAAGGEGPPAPASSGPPEEAARPAAPAAPAAPAAPAPAGAAAAPAEA 639
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622858794  503 APGIKPSVRKPIQIKKSRPREAQPLFPPVRQIVLEGLRSPASQEVQAHPPAPLPASQGSAVPLPPEPslalfAPSPSRDS 582
Cdd:PRK07764   640 SAAPAPGVAAPEHHPKHVAVPDASDGGDGWPAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPA-----ATPPAGQA 714
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622858794  583 LLPPTQEMRSPSPMTTLQPGSTGPLPPADdkleelirqfEAEFGDSFGLPGPPSVPIQDPENQQTclPAPESPFATRSPK 662
Cdd:PRK07764   715 DDPAAQPPQAAQGASAPSPAADDPVPLPP----------EPDDPPDPAGAPAQPPPPPAPAPAAA--PAAAPPPSPPSEE 782

                   .
gi 1622858794  663 Q 663
Cdd:PRK07764   783 E 783
PRK07003 PRK07003
DNA polymerase III subunit gamma/tau;
265-610 7.23e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 235906 [Multi-domain]  Cd Length: 830  Bit Score: 40.99  E-value: 7.23e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622858794  265 IAIEALTQLSSALPQPSHSTPQASCPLPEALSPPAPFRSPQSYLRAPSWPVVPPEEHSSFAPDSSAFPPATPRTEFPevw 344
Cdd:PRK07003   356 LAFEPAVTGGGAPGGGVPARVAGAVPAPGARAAAAVGASAVPAVTAVTGAAGAALAPKAAAAAAATRAEAPPAAPAP--- 432
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622858794  345 gtdtppatprsswpmprpshdpmaeleqllGSASDYIQSVFKRPEALPTKPKVKVEAPSSSPALAPSPVLQRE---APTP 421
Cdd:PRK07003   433 ------------------------------PATADRGDDAADGDAPVPAKANARASADSRCDERDAQPPADSGsasAPAS 482
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622858794  422 SSEPDTHQKAQTALQQHLHHKRSLFLEQAHDTSFPAPSEPSAPGWWPPPSSPAPRLPDRPPKEKKKKLPT-----PAGGP 496
Cdd:PRK07003   483 DAPPDAAFEPAPRAAAPSAATPAAVPDARAPAAASREDAPAAAAPPAPEARPPTPAAAAPAARAGGAAAAldvlrNAGMR 562
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622858794  497 VGTEK---AAPGIKPSVRKPIQIKKSRPREAQPLFPPvrqivlEGLRSPASQEVQAHPPAPLPASQGSAVP----LPPEP 569
Cdd:PRK07003   563 VSSDRgarAAAAAKPAAAPAAAPKPAAPRVAVQVPTP------RARAATGDAPPNGAARAEQAAESRGAPPpwedIPPDD 636
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|
gi 1622858794  570 SLALFAPS---PSRDSLLP-----PTQEMRSPSPMTT-LQPGSTGPLPPA 610
Cdd:PRK07003   637 YVPLSADEgfgGPDDGFVPvfdsgPDDVRVAPKPADApAPPVDTRPLPPA 686
GGN pfam15685
Gametogenetin; GGN is a family of proteins largely found in mammals. It reacts with POG in the ...
495-660 7.39e-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: 40.91  E-value: 7.39e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622858794  495 GPVGTEKAAPGIKPSVRKPIQIKKSRPREAQPLFPPVRQIVLEGLRSPASQEVQAHPPAPLPASQGSAVPlPPEPSLALF 574
Cdd:pfam15685  388 GPWGSPPPPPGKAHPIPGPRRPAPALLAPPMFIFPAPTNGEPVRPGPPAPQALLPRPPPPTPPATPPPVP-PPIPQLPAL 466
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622858794  575 APSPsRDSLLPPTQEMRSPSPMTTLQPGSTGPLPPAddkleELIRQFEAEFGDSFGLPGPPSVPIqdpenqqTCLPAPES 654
Cdd:pfam15685  467 QPMP-LAAARPPTPRPCPGHGESALAPAPTAPLPPA-----LAADQAPAPALAAAPAPSPAPAPA-------TADPLPPA 533

                   ....*.
gi 1622858794  655 PFATRS 660
Cdd:pfam15685  534 PAPIKA 539
PRK14951 PRK14951
DNA polymerase III subunits gamma and tau; Provisional
493-610 9.29e-03

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237865 [Multi-domain]  Cd Length: 618  Bit Score: 40.85  E-value: 9.29e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622858794  493 AGGPVGTEKAAPgIKPSVRKPiqikkSRPREAQPLFPPVRQIVLEGLRSPASQEVQAHPPAPLPASQGSAVPLPPEPSLA 572
Cdd:PRK14951   370 AEAAAPAEKKTP-ARPEAAAP-----AAAPVAQAAAAPAPAAAPAAAASAPAAPPAAAPPAPVAAPAAAAPAAAPAAAPA 443
                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1622858794  573 LFAPSPSrdSLLPPTQEMRSPSPMTTLQPGSTGPLPPA 610
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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