ID A0A077Z8Y4_TRITR Unreviewed; 1079 AA.
AC A0A077Z8Y4;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=protein O-GlcNAc transferase {ECO:0000256|ARBA:ARBA00011970};
DE EC=2.4.1.255 {ECO:0000256|ARBA:ARBA00011970};
GN ORFNames=TTRE_0000492801 {ECO:0000313|EMBL:CDW56646.1};
OS Trichuris trichiura (Whipworm) (Trichocephalus trichiurus).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichuridae; Trichuris.
OX NCBI_TaxID=36087 {ECO:0000313|EMBL:CDW56646.1};
RN [1] {ECO:0000313|EMBL:CDW56646.1}
RP NUCLEOTIDE SEQUENCE.
RA Aslett M.;
RL Submitted (JAN-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CDW56646.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Foth B.J., Tsai I.J., Reid A.J., Bancroft A.J., Nichol S., Tracey A.,
RA Holroyd N., Cotton J.A., Stanley E.J., Zarowiecki M., Liu J.Z.,
RA Huckvale T., Cooper P.J., Grencis R.K., Berriman M.;
RT "The whipworm genome and dual-species transcriptomics of an intimate host-
RT pathogen interaction.";
RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000256|ARBA:ARBA00004922}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 41 family. O-GlcNAc
CC transferase subfamily. {ECO:0000256|ARBA:ARBA00005386}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; HG806064; CDW56646.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A077Z8Y4; -.
DR STRING; 36087.A0A077Z8Y4; -.
DR UniPathway; UPA00378; -.
DR GO; GO:0097363; F:protein O-acetylglucosaminyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.30.720.150; -; 1.
DR Gene3D; 3.40.50.11380; -; 1.
DR Gene3D; 3.40.50.2000; Glycogen Phosphorylase B; 1.
DR Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 2.
DR InterPro; IPR029489; OGT/SEC/SPY_C.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR001440; TPR_1.
DR InterPro; IPR019734; TPR_repeat.
DR PANTHER; PTHR44366; UDP-N-ACETYLGLUCOSAMINE--PEPTIDE N-ACETYLGLUCOSAMINYLTRANSFERASE 110 KDA SUBUNIT; 1.
DR PANTHER; PTHR44366:SF1; UDP-N-ACETYLGLUCOSAMINE--PEPTIDE N-ACETYLGLUCOSAMINYLTRANSFERASE 110 KDA SUBUNIT; 1.
DR Pfam; PF13844; Glyco_transf_41; 1.
DR Pfam; PF00515; TPR_1; 1.
DR Pfam; PF13374; TPR_10; 1.
DR Pfam; PF13414; TPR_11; 4.
DR Pfam; PF13181; TPR_8; 2.
DR SMART; SM00028; TPR; 13.
DR SUPFAM; SSF48452; TPR-like; 2.
DR PROSITE; PS50005; TPR; 11.
DR PROSITE; PS50293; TPR_REGION; 4.
PE 3: Inferred from homology;
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW TPR repeat {ECO:0000256|ARBA:ARBA00022803, ECO:0000256|PROSITE-
KW ProRule:PRU00339}; Transferase {ECO:0000256|ARBA:ARBA00022676}.
FT REPEAT 129..162
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REPEAT 163..196
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REPEAT 197..230
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REPEAT 231..264
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REPEAT 265..298
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REPEAT 299..332
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REPEAT 333..366
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REPEAT 367..400
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REPEAT 401..434
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REPEAT 435..468
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REPEAT 469..502
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT DOMAIN 516..1057
FT /note="O-GlcNAc transferase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13844"
SQ SEQUENCE 1079 AA; 120653 MW; 8209051ABB5FCC10 CRC64;
MFVCHVPSSE GGSKTLAVRM DVKRRIVRPV GDHFGLTNGD NAALSRWTLS PRRADDSFPS
STSLSELAHR EYLAADYDAA ERHCMQLWRQ DPTNISVLLL LSSVHFQCRR LDRSAQFCAM
AIKANPLCAE AYSNLGNVYK ERNQLVEAVE NYRHAVRLKP DFIDGYINLA AALVSSGQLE
QAVQAYVTAL HYGPDLYCVR SDLGNLLKVM GRYDEAKACY LKAIDTQPNF AVAWSNLGCV
FNAQGEIWLA IHHFEKAVQL DPNFLDAYIN LGNVLKEARI FERASAAYLR ALALNPSHAI
VHGNLACVYY EQGLIDLAID TYKRAIELQP HFPDAYCNLA NALKEKSLVS EAEECYNTAL
TLCPQHADSL NNLANIKREQ GLIEEATRLY VSALEIYPEF AAAHSNLASI LQQQGRLTEA
LVHYKEAIRI APTFADAYSN MGNTLKEMND IQGALQCYTR AIQINPAFAD AHSNLASIHK
DSGNIPEAIQ SYKTALKLKP DFPDAFCNLS HCLLVICDWT DYDSRTQKIL SIVEDQLHRN
RLPSVHPHHS MLYPLTHEQR KGIAARHAQL CLEKVSVLHK APYQHPKALS PNGRLRVGYV
SSDFGNHPTS HLMQSVPGMH DRSRVEIFCY ALSADDNTNF RQKVSSTSEH FVDLSQTLDN
GKAADRIAAD RIHILVNMNG YTKGARNEIF ALRPAPIQVM WLGYPGTSGA SFMDYIITDE
STSPLSLAHA YSEKLAYMPH TFFIGDHMQM FPHLSERAIL RGKDKPLDLR KDNVTVVNGT
NLQPIMSKVD VKALVREAEV VHGPEKEIKV TEVVVPVLEI STTAAVETMV STGQVQTSVE
GVPVQNGVTA LTQTHIKAAT GEEVPQTILI TSRHQYGLPE EAVVYCNFNQ MYKVDPPTLK
MWCEILNRVP NSVLWLLRFP AHAEHNVLKF CEKEGVDPKR VKFSNVAAKE EHVRRGQLAD
IGLDSPLCNG HTTGMDMLWA GTPMVTLPLE TFASRVASSQ LNALGCPELV AKSREDYVDI
AVRLGTDVDY LRRIRAKVWK ARTTTTLFDV KQYCVDMEKL YFKMWHRYES GLPPDHISS
//
