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Database: UniProt
Entry: A0A1G3EC93_9GAMM
LinkDB: A0A1G3EC93_9GAMM
Original site: A0A1G3EC93_9GAMM 
ID   A0A1G3EC93_9GAMM        Unreviewed;       813 AA.
AC   A0A1G3EC93;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   RecName: Full=protein O-GlcNAc transferase {ECO:0000256|ARBA:ARBA00011970};
DE            EC=2.4.1.255 {ECO:0000256|ARBA:ARBA00011970};
GN   ORFNames=A2Y50_12475 {ECO:0000313|EMBL:OHC29581.1};
OS   Pseudomonadales bacterium RIFCSPLOWO2_12_59_9.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales.
OX   NCBI_TaxID=1802009 {ECO:0000313|EMBL:OHC29581.1, ECO:0000313|Proteomes:UP000179365};
RN   [1] {ECO:0000313|EMBL:OHC29581.1, ECO:0000313|Proteomes:UP000179365}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=27774985; DOI=10.1038/ncomms13219;
RA   Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA   Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA   Williams K.H., Hubbard S.S., Banfield J.F.;
RT   "Thousands of microbial genomes shed light on interconnected biogeochemical
RT   processes in an aquifer system.";
RL   Nat. Commun. 7:13219-13219(2016).
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:OHC29581.1}.
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DR   EMBL; MHZN01000103; OHC29581.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G3EC93; -.
DR   STRING; 1802009.A2Y50_12475; -.
DR   UniPathway; UPA00378; -.
DR   Proteomes; UP000179365; 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; 3.10.450.50; -; 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; IPR004027; SEC_C_motif.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   InterPro; IPR001440; TPR_1.
DR   InterPro; IPR019734; TPR_repeat.
DR   PANTHER; PTHR44835:SF1; PROTEIN O-GLCNAC TRANSFERASE; 1.
DR   PANTHER; PTHR44835; UDP-N-ACETYLGLUCOSAMINE--PEPTIDE N-ACETYLGLUCOSAMINYLTRANSFERASE SPINDLY-RELATED; 1.
DR   Pfam; PF13844; Glyco_transf_41; 2.
DR   Pfam; PF02810; SEC-C; 1.
DR   Pfam; PF00515; TPR_1; 1.
DR   Pfam; PF13432; TPR_16; 2.
DR   Pfam; PF13181; TPR_8; 1.
DR   SMART; SM00028; TPR; 6.
DR   SUPFAM; SSF103642; Sec-C motif; 1.
DR   SUPFAM; SSF48452; TPR-like; 2.
DR   PROSITE; PS50005; TPR; 2.
PE   3: Inferred from homology;
KW   Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676};
KW   TPR repeat {ECO:0000256|ARBA:ARBA00022803, ECO:0000256|PROSITE-
KW   ProRule:PRU00339}; Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   REPEAT          269..302
FT                   /note="TPR"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT   REPEAT          337..370
FT                   /note="TPR"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT   DOMAIN          438..597
FT                   /note="O-GlcNAc transferase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF13844"
FT   DOMAIN          621..794
FT                   /note="O-GlcNAc transferase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF13844"
SQ   SEQUENCE   813 AA;  92169 MW;  12B1970B3F8E5E80 CRC64;
     MLGQVAVYQP GRNDPCPCGS GLKYKKCCLQ TNTQQILKQC LEQAFLSQEW ERVISLVGEI
     QTPSAQDLRA EALARYRAGQ RADAYPLVKS ARRNFPKDSE LLAALADLEL DHNLIEAEAL
     ARLALALDPS QWLASLALSA CYARTNRLGE AESTLRELIK ASPECDLAWQ RLSTLLRKNH
     RLDDDLAAMH EWTQRCPSNP DAWCHLGMSA VTAELNLEEA RGYLEKALSL KPEHHEALCW
     LGLSYQHQQN PQAALGYLLQ GLQLKPDYQL GWNMLGAVYH SVGRQHEAEG CFMRAIAIAP
     KQSLSWNNLA NTYLDASLLS DAEKVMRVAL DINQNEAVLW NNLGNILGAR KRLREAYKAY
     LKALEISPSF KQVFVNLAGI ESQFGDFDTA IEQLRQVLDN PLARTNILFT VNYHPDWSGE
     EIFAVYREVV EGYFPKRKYF EYMNERLPRR RLRIGYVSPD FCHHVCSYFI EPLLRNHNHE
     QFEIFAYSLV KREDHVTERF VQYADHWRLC TGLTSEAIAE QVYADQIDIL VDLAGHTGNN
     RLEAFAIKPA PVQVSWWVGF AFGSGLKQMD YFLADEQMLP PGCESSFSES LWRMPAPAIV
     YEPSVAMPEL SDLPALRNGY ITFGSLTRPI RVNYRVIKVW AELLKRVPGS RLVLDSHSFQ
     DLSLCEHYRN EFAKQGVSPE RLIIGFTSPV SAVLKKIDIA LDCFPHNSGT TLFESLWMGL
     PFVSLRHRPS MGRVGATILH GVGRDEWIAD SEAEYLDKLV ALASDVDALA GIRAGLREEM
     KASPLCNGPD FTRRMEQTYQ QMWQRYCEQG ESQ
//
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