ID A0A1S3HMU6_LINUN Unreviewed; 1023 AA.
AC A0A1S3HMU6;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=protein O-GlcNAc transferase {ECO:0000256|ARBA:ARBA00011970};
DE EC=2.4.1.255 {ECO:0000256|ARBA:ARBA00011970};
GN Name=LOC106156607 {ECO:0000313|RefSeq:XP_013387388.1};
OS Lingula unguis.
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Brachiopoda; Linguliformea;
OC Lingulata; Lingulida; Linguloidea; Lingulidae; Lingula.
OX NCBI_TaxID=7574 {ECO:0000313|Proteomes:UP000085678, ECO:0000313|RefSeq:XP_013387388.1};
RN [1] {ECO:0000313|RefSeq:XP_013387388.1}
RP IDENTIFICATION.
RC TISSUE=Gonads {ECO:0000313|RefSeq:XP_013387388.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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}.
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DR RefSeq; XP_013387388.1; XM_013531934.1.
DR RefSeq; XP_013387389.1; XM_013531935.1.
DR AlphaFoldDB; A0A1S3HMU6; -.
DR STRING; 7574.A0A1S3HMU6; -.
DR EnsemblMetazoa; XM_013531934.1; XP_013387388.1; LOC106156607.
DR GeneID; 106156607; -.
DR KEGG; lak:106156607; -.
DR InParanoid; A0A1S3HMU6; -.
DR OrthoDB; 34780at2759; -.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000085678; Unplaced.
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; 4.
DR Pfam; PF13431; TPR_17; 1.
DR Pfam; PF13181; TPR_8; 2.
DR SMART; SM00028; TPR; 12.
DR SUPFAM; SSF48452; TPR-like; 2.
DR PROSITE; PS50005; TPR; 11.
DR PROSITE; PS50293; TPR_REGION; 6.
PE 3: Inferred from homology;
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676,
KW ECO:0000313|RefSeq:XP_013387388.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000085678};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW TPR repeat {ECO:0000256|ARBA:ARBA00022803, ECO:0000256|PROSITE-
KW ProRule:PRU00339};
KW Transferase {ECO:0000256|ARBA:ARBA00022676,
KW ECO:0000313|RefSeq:XP_013387388.1}.
FT REPEAT 76..109
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REPEAT 110..143
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REPEAT 144..177
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 464..998
FT /note="O-GlcNAc transferase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13844"
SQ SEQUENCE 1023 AA; 114685 MW; 9FAC44085EDB87CC CRC64;
MGTQFIDTTG LAELAHREYQ AGDYERAEQH CMQLWRQEPD NTGVLLLLSS IHFQCRRLDK
SAYFSQLAIK QNPLLAEAYS NLGNVYKERG QLQEALENYR HAVRLKPDFI DGYINLAAAL
VAAGDMEQAV QAYVTALQYN PDLYCVRSDL GNLLKALGRL DEAKACYLKA IETQPNFAVA
WSNLGCVFNA QGEIWLAIHH FEKAVALDPS FLDAYINLGN VLKEARIFDR AVAAYLRALS
LSPNHAIVHG NLACVYYEQG LIDLAIDTYR RAIELQPNFP DAYCNLANAL KEKVQVAEAE
KCYNTALKLC PTHADSLNNL ANIKREQGHT EEAVRLYLKA LEVFPEFAAA HSNLASILQQ
QGKLTDALMH YKEAIRISPT FADAYSNMGN TLKEMQDIQG ALQCYTRAIQ INPAFADAHS
NLASIHKDSG NIPEAISSYR TALKLKPDFP DAYCNLAHCL QITCDWTDYD ARMKRLVQIV
EDQLQKNRLP SVHPHHSMLY PLTHQQRKAI AAKHANLCLE KINVLHKPPY QHPTHKLEGE
RLRIGYLSSD FGNHPTSHLM QSIPGEHKRE NVEIFCYALS PDDGTTFRSK VMREAEHFID
LSQVPCNGKA ADRIHADGIH ILVNMNGYTK GARNEIFALR PAPIQVMWLG YPGTSGASFM
DYIITDKITS PYELRDQYSE KLAYMPETFF IGDHMNMFPH MIERAILDTK DGKVADTISI
VNATDLTPVL ETASEVKEIV QVAASCKDDK TPAEVVTPVV ELTTSHPVVS MVQTGQPHTC
INGLVLQNGL TTQQTNNKAA TGEEVPQNPM LTTRKQYHLP DEAIVYCNFN QLYKIDPSTL
EMWVEILKQV PNGVLWLLRF PAVGEPNLVQ TAQNMGIAPG RIIFSPVAPK EEHVRRGQLA
DVCLDTPLCN GHTTGMDVLW AGTPMVTLTG ETLASRVAAS QLHCLGCPEL VATAPEDYIR
IAVKLGTDRD YLKATRAKVW NNRTARSLFN TNIYASNMEK LFHRMWMKYE TDQTVDHLVQ
PWD
//
