ID A0A183SFM8_SCHSO Unreviewed; 1032 AA.
AC A0A183SFM8;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=protein O-GlcNAc transferase {ECO:0000256|ARBA:ARBA00011970};
DE EC=2.4.1.255 {ECO:0000256|ARBA:ARBA00011970};
GN ORFNames=SSLN_LOCUS3026 {ECO:0000313|EMBL:VDL89411.1};
OS Schistocephalus solidus (Tapeworm).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Cestoda;
OC Eucestoda; Diphyllobothriidea; Diphyllobothriidae; Schistocephalus.
OX NCBI_TaxID=70667 {ECO:0000313|Proteomes:UP000050788, ECO:0000313|WBParaSite:SSLN_0000312601-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:SSLN_0000312601-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (JUN-2016) to UniProtKB.
RN [2] {ECO:0000313|EMBL:VDL89411.1, ECO:0000313|Proteomes:UP000275846}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NST_G2 {ECO:0000313|EMBL:VDL89411.1,
RC ECO:0000313|Proteomes:UP000275846};
RG Pathogen Informatics;
RL Submitted (NOV-2018) 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; UYSU01032404; VDL89411.1; -; Genomic_DNA.
DR STRING; 70667.A0A183SFM8; -.
DR WBParaSite; SSLN_0000312601-mRNA-1; SSLN_0000312601-mRNA-1; SSLN_0000312601.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000050788; Unplaced.
DR Proteomes; UP000275846; 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; 2.
DR Pfam; PF00515; TPR_1; 2.
DR Pfam; PF13414; TPR_11; 3.
DR Pfam; PF13424; TPR_12; 1.
DR Pfam; PF13181; TPR_8; 2.
DR SMART; SM00028; TPR; 11.
DR SUPFAM; SSF48452; TPR-like; 3.
DR PROSITE; PS50005; TPR; 10.
DR PROSITE; PS50293; TPR_REGION; 5.
PE 3: Inferred from homology;
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676};
KW Reference proteome {ECO:0000313|Proteomes:UP000275846};
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 98..131
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REPEAT 132..165
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REPEAT 200..233
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REPEAT 234..267
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REPEAT 268..301
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REPEAT 302..335
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REPEAT 336..369
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REPEAT 370..403
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REPEAT 404..437
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REPEAT 438..471
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT DOMAIN 485..734
FT /note="O-GlcNAc transferase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13844"
FT DOMAIN 736..1003
FT /note="O-GlcNAc transferase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13844"
SQ SEQUENCE 1032 AA; 115271 MW; 4BE02EF4DE09F562 CRC64;
MLERQSVLHL SDSASGRTML SHDRAALSAL AELADVAHRE YQAGDYERAE HHCMQLWHQD
PENTSTLLLL SSIHFQCRRL EKSAYFSQLA IKQNPLMAEA YSNLGNVLKE RGQLKEAIDN
YRHALNIKPD FIDGYINLAA ALVAAGDTES AVSAYATALQ CNPDLYCVRS DLGNLLKALG
RLDEAKSCYL KAIETCPTFA VAWSNLGCVF NAQNEIWLAI HHFEKAVTLD PTFLDAYINL
GNVLKEARIF DRAVAAYLRA LALAPNHAVV HGNLACVYYE QNLIDLAIET YKRAIELQPN
FPDAYCNLAN ALKEKGKVGE AEEYYNTALR LCPTHADSLN NLANIKREQG RAEEAIRLYV
RALEIYPEFA VAHSNLASML QLQGKLQEAL RHYREAIRIS PTFADAYSNM GNTLKELQDV
QGAMQCYQRA IQINPAFADA HSNLASILKD GGNLAEAINS YKTALKLKPN FPDAFCNLAH
CMQIVCDWTD YKERMKKLVG IVQEQLDSNR LPSVHPHHSM LYPLSHSQRK RIAGKHASLC
LEKIALLHHP PFRFPKRQPG QRLRIGYVSS DFCNHPTSHL MQSLPGMHDR AKVEVFCYSL
SADDGTTFRA KVNREAEHFI DLSGVQCHGK AAERIAADGV HILLNMNGYT KGARNEIFAL
KPAPIQAMWL GYPGTSGSTF MDFIITDAVT SPLALAAQYS EKLAYMPKTF FIGDHAQMFP
HLRNRVIIES AEEVAKMICG GRISEQCGSQ VKEFSYYIKV QVITVPSLQP IREMIRNSAP
SCSIAGVILQ NGLTTQQTQS RASAGEEIPS HIIITSRQHY GLPDDAIVFC NFNQLYKIDP
STMRMWVEIL KNVTNSVLWI LRFPAAGEAN ILAAASDFGL QNPHRRIIFS NVAPKEEHVR
RGQVADVCLD TPLCNGHTTG MDVLWAGCPV VTLPLETLAS RVAASQLHCL GCPELVAKSS
EDYVRIATKL GTNREYLQAM RAKVWKLRET SALFNCRSYA ADLEALYARM WSQYESGLPF
EHITDWANRP KE
//
