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Database: UniProt
Entry: M1VVU0_CLAP2
LinkDB: M1VVU0_CLAP2
Original site: M1VVU0_CLAP2 
ID   M1VVU0_CLAP2            Unreviewed;       493 AA.
AC   M1VVU0;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   RecName: Full=phosphatidylinositol N-acetylglucosaminyltransferase {ECO:0000256|ARBA:ARBA00012420};
DE            EC=2.4.1.198 {ECO:0000256|ARBA:ARBA00012420};
DE   AltName: Full=GlcNAc-PI synthesis protein {ECO:0000256|ARBA:ARBA00032160};
GN   ORFNames=CPUR_03955 {ECO:0000313|EMBL:CCE30107.1};
OS   Claviceps purpurea (strain 20.1) (Ergot fungus) (Sphacelia segetum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Clavicipitaceae; Claviceps.
OX   NCBI_TaxID=1111077 {ECO:0000313|EMBL:CCE30107.1, ECO:0000313|Proteomes:UP000016801};
RN   [1] {ECO:0000313|EMBL:CCE30107.1, ECO:0000313|Proteomes:UP000016801}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=20.1 {ECO:0000313|EMBL:CCE30107.1,
RC   ECO:0000313|Proteomes:UP000016801};
RX   PubMed=23468653; DOI=10.1371/journal.pgen.1003323;
RA   Schardl C.L., Young C.A., Hesse U., Amyotte S.G., Andreeva K., Calie P.J.,
RA   Fleetwood D.J., Haws D.C., Moore N., Oeser B., Panaccione D.G.,
RA   Schweri K.K., Voisey C.R., Farman M.L., Jaromczyk J.W., Roe B.A.,
RA   O'Sullivan D.M., Scott B., Tudzynski P., An Z., Arnaoudova E.G.,
RA   Bullock C.T., Charlton N.D., Chen L., Cox M., Dinkins R.D., Florea S.,
RA   Glenn A.E., Gordon A., Gueldener U., Harris D.R., Hollin W., Jaromczyk J.,
RA   Johnson R.D., Khan A.K., Leistner E., Leuchtmann A., Li C., Liu J., Liu J.,
RA   Liu M., Mace W., Machado C., Nagabhyru P., Pan J., Schmid J., Sugawara K.,
RA   Steiner U., Takach J.E., Tanaka E., Webb J.S., Wilson E.V., Wiseman J.L.,
RA   Yoshida R., Zeng Z.;
RT   "Plant-symbiotic fungi as chemical engineers: Multi-genome analysis of the
RT   Clavicipitaceae reveals dynamics of alkaloid loci.";
RL   PLoS Genet. 9:E1003323-E1003323(2013).
CC   -!- FUNCTION: Catalytic subunit in the complex catalyzing the transfer of
CC       N-acetylglucosamine from UDP-N-acetylglucosamine to
CC       phosphatidylinositol, the first step of GPI biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00003265}.
CC   -!- PATHWAY: Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor
CC       biosynthesis. {ECO:0000256|ARBA:ARBA00004687}.
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:CCE30107.1}.
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DR   EMBL; CAGA01000019; CCE30107.1; -; Genomic_DNA.
DR   AlphaFoldDB; M1VVU0; -.
DR   STRING; 1111077.M1VVU0; -.
DR   VEuPathDB; FungiDB:CPUR_03955; -.
DR   eggNOG; KOG1111; Eukaryota.
DR   HOGENOM; CLU_009583_19_2_1; -.
DR   OrthoDB; 24420at2759; -.
DR   PhylomeDB; M1VVU0; -.
DR   UniPathway; UPA00196; -.
DR   Proteomes; UP000016801; Unassembled WGS sequence.
DR   GO; GO:0000506; C:glycosylphosphatidylinositol-N-acetylglucosaminyltransferase (GPI-GnT) complex; IEA:InterPro.
DR   GO; GO:0017176; F:phosphatidylinositol N-acetylglucosaminyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006506; P:GPI anchor biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd03796; GT4_PIG-A-like; 1.
DR   Gene3D; 3.40.50.2000; Glycogen Phosphorylase B; 2.
DR   InterPro; IPR001296; Glyco_trans_1.
DR   InterPro; IPR039507; PIG-A/GPI3.
DR   InterPro; IPR013234; PIGA_GPI_anchor_biosynthesis.
DR   PANTHER; PTHR45871; N-ACETYLGLUCOSAMINYL-PHOSPHATIDYLINOSITOL BIOSYNTHETIC PROTEIN; 1.
DR   PANTHER; PTHR45871:SF1; PHOSPHATIDYLINOSITOL N-ACETYLGLUCOSAMINYLTRANSFERASE SUBUNIT A; 1.
DR   Pfam; PF00534; Glycos_transf_1; 1.
DR   Pfam; PF08288; PIGA; 1.
DR   SUPFAM; SSF53756; UDP-Glycosyltransferase/glycogen phosphorylase; 1.
PE   4: Predicted;
KW   Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676,
KW   ECO:0000313|EMBL:CCE30107.1};
KW   GPI-anchor biosynthesis {ECO:0000256|ARBA:ARBA00022502};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000016801};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:CCE30107.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        430..453
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          45..134
FT                   /note="PIGA GPI anchor biosynthesis"
FT                   /evidence="ECO:0000259|Pfam:PF08288"
FT   DOMAIN          213..342
FT                   /note="Glycosyl transferase family 1"
FT                   /evidence="ECO:0000259|Pfam:PF00534"
FT   REGION          472..493
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   493 AA;  55775 MW;  16348F39F45B8DB3 CRC64;
     MTRRRYNIAM VSDFFFPQPG GIESHIYQLS SKLIDRGHKV IIITHSHDDR KGVRYLTNGL
     KVYHVPFLVI YRQATFPTVF SFFPILRYIF IRERIEIVHG HGSLSCLCHE GILHARTMGL
     RTVFTDHSLF GFADAASILT NKLLKFILSD VDHSICVSHT CKENTVLRAS LDPLMVSVIP
     NAVVAENFRP RDYPSSPTAS FAPDPSPQRL GPNDMITIVV ISRLFYNKGT DLLIAAIPRI
     LETHPNTRFI IAGSGPKAID LEQMIEQNVL QDRVEMLGPV RHEDVRDVMI RGHIYLHPSL
     TEAFGTVIVE AASCGLYVVC TQVGGIPEVL PSHMTTFAKP EEDDLVLATC KAITAVRAGK
     VRTEKFHEQV KKMYSWSNVA MRTERVYDGI TGTISEDEFY GFDTGGYNGS RTRNFALIDR
     LKRYYGCGIW AGKLFCLCVV IDYLFFLFLE WWFPRDNIDI CPDWPRKALL DDTKKRSGES
     KSNRSSTSPR TVG
//
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