ID A0A0V0UR92_9BILA Unreviewed; 1026 AA.
AC A0A0V0UR92;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=protein O-GlcNAc transferase {ECO:0000256|ARBA:ARBA00011970};
DE EC=2.4.1.255 {ECO:0000256|ARBA:ARBA00011970};
GN ORFNames=T09_1126 {ECO:0000313|EMBL:KRX53828.1};
OS Trichinella sp. T9.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=181606 {ECO:0000313|EMBL:KRX53828.1, ECO:0000313|Proteomes:UP000054681};
RN [1] {ECO:0000313|EMBL:KRX53828.1, ECO:0000313|Proteomes:UP000054681}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS409 {ECO:0000313|EMBL:KRX53828.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-2015) 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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KRX53828.1}.
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DR EMBL; JYDN01000189; KRX53828.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V0UR92; -.
DR STRING; 181606.A0A0V0UR92; -.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000054681; Unassembled WGS sequence.
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; PF13414; TPR_11; 3.
DR Pfam; PF13424; TPR_12; 1.
DR Pfam; PF13181; TPR_8; 2.
DR SMART; SM00028; TPR; 13.
DR SUPFAM; SSF48452; TPR-like; 2.
DR PROSITE; PS50005; TPR; 9.
DR PROSITE; PS50293; TPR_REGION; 5.
PE 3: Inferred from homology;
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676,
KW ECO:0000313|EMBL:KRX53828.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000054681};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW TPR repeat {ECO:0000256|ARBA:ARBA00022803, ECO:0000256|PROSITE-
KW ProRule:PRU00339}; Transferase {ECO:0000313|EMBL:KRX53828.1}.
FT REPEAT 76..109
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REPEAT 178..211
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REPEAT 212..245
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REPEAT 246..279
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REPEAT 280..313
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REPEAT 314..347
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REPEAT 348..381
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REPEAT 382..415
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REPEAT 416..449
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT DOMAIN 463..1004
FT /note="O-GlcNAc transferase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13844"
SQ SEQUENCE 1026 AA; 115278 MW; 206378E9C332DFCB CRC64;
MNSISQDFAS LSELAHREYQ AANYEDAERH CMHLLRQEPS NISVLLLLSS IHFQCKRLEK
SAQFCSMAIK ANPVCAEAYS NLGNVFKERN QLPEALENYR HAIRLKPDFI DGYINLAAAL
VTAGHLEQAV QAYATALHYN ADLYCIRSDL GNLLKAMGRL EEAKACYLKA IDTQPTFAVA
WSNLGCVFSA QGEIWLAIHH FEKAVQLDPN FLDAYINLGN VLKEARIFDR AVSAYLRALS
LSPNHAAVHG NLACVYYEQG LIDLAIDTYK RAIELQPHFP DAYCNLANAL KEKGFVAEAE
ECYNTALNLC PQHADSLNNL ANIKREQGFI EEATRLYIKA LEIFPEFAAA HSNLASILQQ
QGRLTEAILH YKEAIRIAPT FADAYSNMGN TLKEMNDITG AMQCYSRAIQ INPAFADAHS
NLASIHKDSG NVPDAIQAYR TALKLKPDFP DAFCNLAHCL QVICDWTDYE ARTKKIVAIV
DEQLRRNRLP SVHPHHSMLY PLTHEQRKGI ATRHAQLCME KISVLHKSSY VHPTALASGE
RLRIGYVSSD FGNHPTSHLM QSIPGMHNRK KVEIFCYALS PDDNTNFRQK VSSQAEHFVD
LSQISDTGKA ADRIAMDKIH ILVNMNGYTK GARNEIFALR CAPIQVMWLG YPGTSGASFM
DYIITDRVTS PLHLAHAYTE KLAYMPHTFF IGDHMQMFPH LSERAILKGK DKPLDPRKDN
VTVVNATNLE PIMSKADVKA FVREAEVIHG PEKEVKVTEV VVPVLEISTT APVETMFYTG
QVQTSVEGVP VQNGVTALTQ THIKAATGEE VPQSILITSR HQYGLPEDAI VYCNFNQMYK
IDPMTLKMWC EILQRVPNSV LWLLRFPSHA EPNVLKFCES QGVNTKRIKF NNVAAKEEHV
RRGQLADLCL DTPLCNGHTT GMDMLWAGTP MVTLPLETFA SRVASSQLTA LGCPELIAKT
REDYVNIAVR LGTDVDYLRK IRAKVWKARK TTTLFDVKQY CSDMEDLFMK MWRRYESKLP
PDHITS
//
