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Database: UniProt
Entry: S3CSF9_OPHP1
LinkDB: S3CSF9_OPHP1
Original site: S3CSF9_OPHP1 
ID   S3CSF9_OPHP1            Unreviewed;       517 AA.
AC   S3CSF9;
DT   18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT   18-SEP-2013, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   RecName: Full=GPI-anchored wall transfer protein {ECO:0000256|RuleBase:RU280819};
DE            EC=2.3.-.- {ECO:0000256|RuleBase:RU280819};
GN   ORFNames=F503_07359 {ECO:0000313|EMBL:EPE09583.1};
OS   Ophiostoma piceae (strain UAMH 11346) (Sap stain fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Ophiostomatales; Ophiostomataceae; Ophiostoma.
OX   NCBI_TaxID=1262450 {ECO:0000313|EMBL:EPE09583.1, ECO:0000313|Proteomes:UP000016923};
RN   [1] {ECO:0000313|EMBL:EPE09583.1, ECO:0000313|Proteomes:UP000016923}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UAMH 11346 {ECO:0000313|EMBL:EPE09583.1,
RC   ECO:0000313|Proteomes:UP000016923};
RX   PubMed=23725015; DOI=10.1186/1471-2164-14-373;
RA   Haridas S., Wang Y., Lim L., Massoumi Alamouti S., Jackman S., Docking R.,
RA   Robertson G., Birol I., Bohlmann J., Breuil C.;
RT   "The genome and transcriptome of the pine saprophyte Ophiostoma piceae, and
RT   a comparison with the bark beetle-associated pine pathogen Grosmannia
RT   clavigera.";
RL   BMC Genomics 14:373-373(2013).
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; KE148147; EPE09583.1; -; Genomic_DNA.
DR   AlphaFoldDB; S3CSF9; -.
DR   STRING; 1262450.S3CSF9; -.
DR   VEuPathDB; FungiDB:F503_07359; -.
DR   eggNOG; KOG0411; Eukaryota.
DR   HOGENOM; CLU_020802_2_2_1; -.
DR   OMA; GLYVMQP; -.
DR   OrthoDB; 228697at2759; -.
DR   UniPathway; UPA00196; -.
DR   Proteomes; UP000016923; 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:UP000016923};
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        36..53
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU280819"
FT   TRANSMEM        65..85
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU280819"
FT   TRANSMEM        91..108
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU280819"
FT   TRANSMEM        146..168
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU280819"
FT   TRANSMEM        188..206
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU280819"
FT   TRANSMEM        227..244
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU280819"
FT   TRANSMEM        256..273
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU280819"
FT   TRANSMEM        285..304
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU280819"
FT   TRANSMEM        324..345
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU280819"
FT   TRANSMEM        463..483
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU280819"
FT   TRANSMEM        489..511
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU280819"
FT   REGION          117..137
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   517 AA;  55868 MW;  9B0D72452A69C8BE CRC64;
     MAEPGSAAAA AAAASNYKKL KEDFVSNLSG GSASEVSLVT AVAPATILLW SVLQRRRSFF
     RPYTPFGFLI DFLLNAGGIL VTITAYADTP LLLNGLLIGM ALFVFALPRD VDEPRSRKVA
     KKPRAAKGKD SKASGKQVSS ALPKKAFLTT YRGAMMVVTC LAILAVDFRI FPRRFAKVET
     WGTSLMDMGV GSFVFSAGVV AARSVLKERI DGRVTPLGRR LLTSLRHSLP LLVLGIVRLI
     SVKGLDYAEH VTEYGVHWNF FFTLGLLPPF VAVSQSALQV IPSSAALALL LSGVYQVALE
     TTSLKAYVLT APRVDLISKN REGLASFIGY LAIFLAGQDT GMYLLPRSAP STSKSLKSKS
     TSAWLWQTIK ANPLPAWAVT WWVLHQLTIG VPYGLGLTES RRIANLPYVL WVLSFNTQQL
     SMFYLVDKYV FGEGPATADA EEEAAAHDEA TSLVLRAYNR NGLVVFLLAN LLTGLVNLTV
     PTLDVTRPVA SSILFAYAGV ITVVAVALEV YGITIKL
//
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