ID A0A194W2H0_9PEZI Unreviewed; 498 AA.
AC A0A194W2H0;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=GPI-anchored wall transfer protein {ECO:0000256|RuleBase:RU280819};
DE EC=2.3.-.- {ECO:0000256|RuleBase:RU280819};
GN ORFNames=VM1G_06147 {ECO:0000313|EMBL:KUI70472.1};
OS Valsa mali.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Diaporthales; Valsaceae; Valsa.
OX NCBI_TaxID=105487 {ECO:0000313|EMBL:KUI70472.1};
RN [1] {ECO:0000313|EMBL:KUI70472.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=03-8 {ECO:0000313|EMBL:KUI70472.1};
RA Yin Z., Liu H., Gao X., Li Z., Song N., Ke X., Dai Q., Wu Y., Sun Y.,
RA Xu J.-R., Kang Z.K., Wang L., Huang L.;
RT "Genome Sequence of Valsa Canker Pathogens Uncovers a Specific Adaption of
RT Colonization on Woody Bark.";
RL Submitted (DEC-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Probable acetyltransferase, which acetylates the inositol
CC ring of phosphatidylinositol during biosynthesis of GPI-anchor.
CC {ECO:0000256|ARBA:ARBA00002531, ECO:0000256|RuleBase:RU280819}.
CC -!- PATHWAY: Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor
CC biosynthesis. {ECO:0000256|ARBA:ARBA00004687,
CC ECO:0000256|RuleBase:RU280819}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000256|ARBA:ARBA00004477, ECO:0000256|RuleBase:RU280819}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004477,
CC ECO:0000256|RuleBase:RU280819}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the PIGW family. {ECO:0000256|ARBA:ARBA00007559,
CC ECO:0000256|RuleBase:RU280819}.
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DR EMBL; CM003103; KUI70472.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A194W2H0; -.
DR OrthoDB; 228697at2759; -.
DR UniPathway; UPA00196; -.
DR Proteomes; UP000078559; Chromosome 6.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IEA:UniProt.
DR GO; GO:0006506; P:GPI anchor biosynthetic process; IEA:UniProtKB-UniPathway.
DR InterPro; IPR009447; PIGW/GWT1.
DR PANTHER; PTHR20661; PHOSPHATIDYLINOSITOL-GLYCAN BIOSYNTHESIS CLASS W PROTEIN; 1.
DR PANTHER; PTHR20661:SF0; PHOSPHATIDYLINOSITOL-GLYCAN BIOSYNTHESIS CLASS W PROTEIN; 1.
DR Pfam; PF06423; GWT1; 1.
DR PIRSF; PIRSF017321; GWT1; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|RuleBase:RU280819};
KW Endoplasmic reticulum {ECO:0000256|RuleBase:RU280819};
KW GPI-anchor biosynthesis {ECO:0000256|ARBA:ARBA00022502,
KW ECO:0000256|RuleBase:RU280819};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU280819};
KW Transferase {ECO:0000256|RuleBase:RU280819};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU280819};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU280819}.
FT TRANSMEM 27..44
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU280819"
FT TRANSMEM 56..76
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU280819"
FT TRANSMEM 82..99
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU280819"
FT TRANSMEM 136..155
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU280819"
FT TRANSMEM 175..193
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU280819"
FT TRANSMEM 214..232
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU280819"
FT TRANSMEM 244..261
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU280819"
FT TRANSMEM 268..286
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU280819"
FT TRANSMEM 311..331
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU280819"
FT TRANSMEM 351..369
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU280819"
FT TRANSMEM 389..416
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU280819"
FT TRANSMEM 444..463
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU280819"
FT TRANSMEM 469..492
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU280819"
FT REGION 104..124
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 498 AA; 54015 MW; C46DE970FBFCE451 CRC64;
MSNSTATYKQ LKEDFVSNLT GGPVSEIAAV TAVLPVGALV WSVLQARQLF FKPYTGIAFV
VDYFLNVGAI LLAITLYSDS PILLIVLLLA PALLVYALPP NLGTRRKKPK PPPTAQSKSK
GPAADLNVLP TKPFLTVFRG SMLVITCLAI LAVDFRIFPR RFAKVETWGT SLMDIGVGAF
VFSAGVVAAR PVLKERAEGR TTPLLRRLVY SMRHSLPLLV LGVVRLLSVK GLDYAEHVSE
YGVHWNFFFT LGFLPPFVAA FQSALKFVPS YAALALILGV VYQVVLESTD LKAYILTAPR
VDLLSKNREG VFSFIGYLAI FLAGQDTGMY VLPRNIGSKG GSSATKQRTT LLVTMAVWSC
IWCLLFFLVT DYNYGSGLSV SRRLANLPYI LGVISFNSVQ LLACCLVETF CFPAAYNATD
SKSEKEAYET ATSRVLRAYN RNGLAIFLLA NLLTGLVNMT VPTLNAGPIA SMGILVAYSA
VLTAVAVALD AYNISIKL
//
