ID K1VA77_TRIAC Unreviewed; 793 AA.
AC K1VA77;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, 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=A1Q2_08079 {ECO:0000313|EMBL:EKC97620.1};
OS Trichosporon asahii var. asahii (strain CBS 8904) (Yeast).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Trichosporonales; Trichosporonaceae; Trichosporon.
OX NCBI_TaxID=1220162 {ECO:0000313|EMBL:EKC97620.1, ECO:0000313|Proteomes:UP000006757};
RN [1] {ECO:0000313|EMBL:EKC97620.1, ECO:0000313|Proteomes:UP000006757}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 8904 {ECO:0000313|EMBL:EKC97620.1,
RC ECO:0000313|Proteomes:UP000006757};
RX PubMed=23193141; DOI=10.1128/EC.00264-12;
RA Yang R.Y., Li H.T., Zhu H., Zhou G.P., Wang M., Wang L.;
RT "Genome sequence of the Trichosporon asahii environmental strain CBS
RT 8904.";
RL Eukaryot. Cell 11:1586-1587(2012).
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:EKC97620.1}.
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DR EMBL; AMBO01000406; EKC97620.1; -; Genomic_DNA.
DR AlphaFoldDB; K1VA77; -.
DR STRING; 1220162.K1VA77; -.
DR eggNOG; KOG1111; Eukaryota.
DR eggNOG; KOG2848; Eukaryota.
DR HOGENOM; CLU_019267_1_0_1; -.
DR InParanoid; K1VA77; -.
DR OMA; MSEDMAV; -.
DR OrthoDB; 24420at2759; -.
DR UniPathway; UPA00196; -.
DR Proteomes; UP000006757; Unassembled WGS sequence.
DR GO; GO:0000506; C:glycosylphosphatidylinositol-N-acetylglucosaminyltransferase (GPI-GnT) complex; IEA:InterPro.
DR GO; GO:0016746; F:acyltransferase activity; 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 CDD; cd07989; LPLAT_AGPAT-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 InterPro; IPR002123; Plipid/glycerol_acylTrfase.
DR PANTHER; PTHR45871; N-ACETYLGLUCOSAMINYL-PHOSPHATIDYLINOSITOL BIOSYNTHETIC PROTEIN; 1.
DR PANTHER; PTHR45871:SF1; PHOSPHATIDYLINOSITOL N-ACETYLGLUCOSAMINYLTRANSFERASE SUBUNIT A; 1.
DR Pfam; PF01553; Acyltransferase; 1.
DR Pfam; PF00534; Glycos_transf_1; 1.
DR Pfam; PF08288; PIGA; 1.
DR SMART; SM00563; PlsC; 1.
DR SUPFAM; SSF69593; Glycerol-3-phosphate (1)-acyltransferase; 1.
DR SUPFAM; SSF53756; UDP-Glycosyltransferase/glycogen phosphorylase; 1.
PE 4: Predicted;
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676};
KW GPI-anchor biosynthesis {ECO:0000256|ARBA:ARBA00022502};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000006757};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EKC97620.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 14..34
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 81..175
FT /note="Phospholipid/glycerol acyltransferase"
FT /evidence="ECO:0000259|SMART:SM00563"
FT REGION 223..265
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 772..793
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 793 AA; 87634 MW; 5B7CB4929E795D4E CRC64;
MSVLSKAGYY LRSIQYYTLL LSVGFLATFI ALVATACGRR FDTDYYVART FYYIAGPLMG
WSFDVEGEEH LTNLEKEGKS AVLLGNHQNV VDILYLGRIF PKHAAIMAKK ELKWVPGLGW
FMSLSGSVFI DRGNNKSAIQ SMKLAGDEMK RKKKGAFYLA IQSGTPIVPV VCENYSRLLK
KGSYFKTGTL KIKVLPPIET KGLKVPDDVP ALIEKVRGQM SATLKEISQP APKTSKKETP
KRSSSPTPLL KESKHKSYQS TDKTDVAVDA VPKDAEEKDS KLAVALIEKR MISDFFHPNV
GGVEGHIYSL SVELLRRGHK VIVITHHAGK RVGVRYLAPG LKVYHVPFVT LASSASLPNY
LMFLPWFRTI ILREKINLVH GHGSLSSLAH EAIHHGGLLG VRSVFSDHSL FSFDDSVGIL
TNKLLASALR NVYACICVSH TGRENTSLRG EVEPERISVI PNALVASQFQ PTAPYIPSAG
DNSITIVVIS RLVYRKGIDL LVSAAPRICA AYPNVRFLIG GDGPKMLDLL QMRENNQLQD
RVELLGSVRP RDVNDTLRRG QIYLNTSLTE AFGISIIEAA CSGLFVVSTR VGGVPEILPG
DMVEFARADE DGESASERSE LRPPVEKCGL TLDIIRALTR AIETIQSGSH DPALAHQRME
DMYSWASVAE RTEQVYRRVM AQPVWTPYER LSRLFSLGPV FGPILCAITA VQWWWYLFVC
AVVPESEIEV VEDDWDAGRF AQAKNQGEPK EVVMSEDMAV SKPEWTGVIQ QRPADAQPCS
QDAAEPATAA YPV
//
