ID A0A016V2S6_9BILA Unreviewed; 1216 AA.
AC A0A016V2S6;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=protein O-GlcNAc transferase {ECO:0000256|ARBA:ARBA00011970};
DE EC=2.4.1.255 {ECO:0000256|ARBA:ARBA00011970};
GN Name=Acey_s0020.g185 {ECO:0000313|EMBL:EYC21018.1};
GN Synonyms=Acey-ogt-1 {ECO:0000313|EMBL:EYC21018.1};
GN ORFNames=Y032_0020g185 {ECO:0000313|EMBL:EYC21018.1};
OS Ancylostoma ceylanicum.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Strongyloidea; Ancylostomatidae;
OC Ancylostomatinae; Ancylostoma.
OX NCBI_TaxID=53326 {ECO:0000313|EMBL:EYC21018.1, ECO:0000313|Proteomes:UP000024635};
RN [1] {ECO:0000313|Proteomes:UP000024635}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=HY135 {ECO:0000313|Proteomes:UP000024635};
RX PubMed=25730766; DOI=10.1038/ng.3237;
RA Schwarz E.M., Hu Y., Antoshechkin I., Miller M.M., Sternberg P.W.,
RA Aroian R.V.;
RT "The genome and transcriptome of the zoonotic hookworm Ancylostoma
RT ceylanicum identify infection-specific gene families.";
RL Nat. Genet. 47:416-422(2015).
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:EYC21018.1}.
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DR EMBL; JARK01001356; EYC21018.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A016V2S6; -.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000024635; 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; 3.
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; 2.
DR Pfam; PF13374; TPR_10; 1.
DR Pfam; PF13414; TPR_11; 4.
DR Pfam; PF13181; TPR_8; 1.
DR SMART; SM00028; TPR; 15.
DR SUPFAM; SSF48452; TPR-like; 3.
DR PROSITE; PS50005; TPR; 12.
DR PROSITE; PS50293; TPR_REGION; 6.
PE 3: Inferred from homology;
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676};
KW Reference proteome {ECO:0000313|Proteomes:UP000024635};
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 168..201
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REPEAT 202..235
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REPEAT 270..303
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REPEAT 304..337
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REPEAT 360..393
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REPEAT 394..427
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REPEAT 428..461
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REPEAT 462..495
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REPEAT 496..529
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REPEAT 530..563
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REPEAT 564..597
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REPEAT 598..631
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT DOMAIN 645..1187
FT /note="O-GlcNAc transferase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13844"
SQ SEQUENCE 1216 AA; 134951 MW; 6F07E24CF464E6CE CRC64;
MTGLPVNASP MDPSKQAFLI QQSLNKFVGA TGEQLAPGAV PQQPVLAAGL APSAHALSTL
QGHHLNNMVA AIQKQAQNVS FMQNSPGNAQ GSTQLGPLDV AAITEKAHRL YQAGDYANAE
RHCLMIYQQD RTNVSVLLLL SSIHFQLKNL EKSKQFSTMA IQANNQCAEA YSNLGNVFKE
RGELAEALEN YKYAVRLKPD FIDGYINLAA ALVAGGDLDQ AVAAYLSALN YNPELYCVRS
DLGNLLKAMG RLEDAKICYL KAIETQPQFA VAWSNLGCVF NAQGEIWLAI HHFEKAVQLD
PNFLDAYINL GNVLKEARIF DRAVAAYLRA LNLASNHAVV HGNLACICYL KAIETQPQFA
VAWSNLGCVF NAQGEIWLAI HHFEKAVQLD PNFLDAYINL GNVLKEARIF DRAVAAYLRA
LNLASNHAVV HGNLACVYYE QGLIDLAIDT YRRAIELQPN FPDAYCNLAN ALKEKGLVQE
AENAYMTALG LCPTHADSQN NLANIKREQG KIEEATRLYL KALEIYPEFA AAHSNLASIL
QQQGKLQEAI LHYKEAIRIA PTFADAYSNM GNTLKEMGDA ANAMQCYTRA IQINPAFADA
HSNLASIHKD SGNIPDAIQS YSTALKLKPD FPDAFCNLAH CLQIICDWTD YDNRMKRLVA
IVDDQLSKKR LPSVHPHHSM LYPLTHQTRI AIAAKHAQLC TEKVAMLNHP PFNFPDRLSV
RNGVSRLRIG YVSSDFGNHP TSHLMQSIPG MHDRSRIEVF CYALSANDGT NFRQKLMNEA
EHFVDLSQIT CNGKAADRIN QDGIHILINM NGYTKGARNE IFALRPAPLQ VMWLGYPGTS
GAPFMDYIIT DAVTSPLRLA HAYSEKLAYM PHTFFIGDHA QMLKHLTERV ILKDKCAPAE
KDNVAVVNAT NLEPLLSKAD VKHTVRETEV VYGPAKEKIK TEVVVPVVEV PTTEPLKQMI
GGGLIASSVV DGVHVHNGLT QIQMHHKAAT GEEVPQSLLL TSRQQYNLPE DAIVFCNFNQ
LYKIDPPTLD MWIEILKRVP RSVLWLLRFP FHGEAHVQKY CSERDIDPKR VVFSHVAAKE
EHVRRGQLAD VCLDTPLCNG HTTGMDILWT GTPMVTMPLE TLASRVASSQ LYALGVPELV
AKSREDYVNI AVKLGTDKNY LSAIRAKVWK ARTTSTLFNV KQYCTDMESL LHLMWRRYEE
GRPVDHLTQG AAQVDF
//
