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}.
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; 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
//