ID A0A420I068_9PEZI Unreviewed; 552 AA.
AC A0A420I068;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE RecName: Full=GPI-anchored wall transfer protein {ECO:0000256|RuleBase:RU280819};
DE EC=2.3.-.- {ECO:0000256|RuleBase:RU280819};
GN ORFNames=OnM2_028032 {ECO:0000313|EMBL:RKF63068.1};
OS Erysiphe neolycopersici.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Erysiphales; Erysiphaceae; Erysiphe.
OX NCBI_TaxID=212602 {ECO:0000313|EMBL:RKF63068.1, ECO:0000313|Proteomes:UP000286134};
RN [1] {ECO:0000313|EMBL:RKF63068.1, ECO:0000313|Proteomes:UP000286134}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UMSG2 {ECO:0000313|EMBL:RKF63068.1};
RX PubMed=30253736; DOI=10.1186/s12864-018-5069-z;
RA Wu Y., Ma X., Pan Z., Kale S.D., Song Y., King H., Zhang Q., Presley C.,
RA Deng X., Wei C.I., Xiao S.;
RT "Comparative genome analyses reveal sequence features reflecting distinct
RT modes of host-adaptation between dicot and monocot powdery mildew.";
RL BMC Genomics 19:705-705(2018).
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}.
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:RKF63068.1}.
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DR EMBL; MCFK01002821; RKF63068.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A420I068; -.
DR STRING; 212602.A0A420I068; -.
DR UniPathway; UPA00196; -.
DR Proteomes; UP000286134; Unassembled WGS sequence.
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 Reference proteome {ECO:0000313|Proteomes:UP000286134};
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 81..102
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU280819"
FT TRANSMEM 108..127
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU280819"
FT TRANSMEM 190..209
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU280819"
FT TRANSMEM 221..243
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU280819"
FT TRANSMEM 263..281
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU280819"
FT TRANSMEM 293..313
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU280819"
FT TRANSMEM 325..343
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU280819"
FT TRANSMEM 363..382
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU280819"
FT TRANSMEM 402..420
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU280819"
FT TRANSMEM 440..463
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU280819"
FT TRANSMEM 498..519
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU280819"
FT TRANSMEM 525..546
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU280819"
SQ SEQUENCE 552 AA; 61559 MW; 124CB2AA68779EB7 CRC64;
MSRAAVEQIK AASYKVLKED FVSNLTGGSI SEINYVTAVA PVSVLIWSVL QSRYGFFTPT
QRKIKKNAIA TTDDSTTTST VWICTIVEFL INVLSILLAT TLYASKPVLL NLLLLAPLLI
VVYLLPLPKR VAGTLFSKKR NRKKFLLKPT PDRHRSASGL SSSVNDDKNV DFKALNNPLP
KRPFLTTYRG CMLVITCISI LAVDFHVFPR RFAKVETWGT SLMDVGVGSF VFSTGIVAAR
PLLLDQGEAG SSKTMLRGRL LQAGRNSLPL LLLGLIRLWS VKELDYAEHV SEYGVHWNFF
FTLGFLPPFV TLFQSAFKYL PSYSILALIL GAAYQASLDF TNLKTFILSG PRNNLLSMNR
EGIFSFVGYL AIFLMGQETG LYVLPRRLLP KCFSAWQQRR RLLLCLGGMS LTWALLFMAT
TNRIYGLKIT VSRRLANLPY IIWIAAFNTS QLTVFCLIET IFFPSVWKLS ENATLLEEEE
IYQNATSGVL EAYNRNGLAV FLLANLLTGV VNLSISTLYC SDLKSMVILV LYAASISGTA
VALNWWDISI KF
//
