ID A0A165F248_9APHY Unreviewed; 552 AA.
AC A0A165F248;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-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=LAESUDRAFT_757895 {ECO:0000313|EMBL:KZT08215.1};
OS Laetiporus sulphureus 93-53.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Laetiporus.
OX NCBI_TaxID=1314785 {ECO:0000313|EMBL:KZT08215.1, ECO:0000313|Proteomes:UP000076871};
RN [1] {ECO:0000313|EMBL:KZT08215.1, ECO:0000313|Proteomes:UP000076871}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=93-53 {ECO:0000313|EMBL:KZT08215.1,
RC ECO:0000313|Proteomes:UP000076871};
RX PubMed=26659563; DOI=10.1093/molbev/msv337;
RA Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT Insights into the Origins of Lignocellulose Decay Capabilities.";
RL Mol. Biol. Evol. 33:959-970(2016).
CC -!- FUNCTION: Probable acetyltransferase, which acetylates the inositol
CC ring of phosphatidylinositol during biosynthesis of GPI-anchor.
CC {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; KV427616; KZT08215.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A165F248; -.
DR STRING; 1314785.A0A165F248; -.
DR InParanoid; A0A165F248; -.
DR OrthoDB; 228697at2759; -.
DR UniPathway; UPA00196; -.
DR Proteomes; UP000076871; 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:UP000076871};
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 20..41
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU280819"
FT TRANSMEM 53..72
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU280819"
FT TRANSMEM 146..164
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU280819"
FT TRANSMEM 176..199
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU280819"
FT TRANSMEM 249..266
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU280819"
FT TRANSMEM 278..299
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU280819"
FT TRANSMEM 319..337
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU280819"
FT TRANSMEM 395..415
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU280819"
FT TRANSMEM 427..450
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU280819"
FT TRANSMEM 499..519
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU280819"
FT TRANSMEM 525..543
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU280819"
FT REGION 109..131
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 345..385
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 348..372
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 552 AA; 60203 MW; CF7E1F7C662943AE CRC64;
MDSSYKNSKE AFISGMAGSS IGHINMVSLA ALSSIALYSA MKTRLFMNKS MGFLVEFVIL
VVPLLLSVTL FARSPGQLTL ILLSPTGLLL LMSRGGSGVV LPSSSNSIRV TKGSGESGAA
SQGREKADSP PVRSFNRLPA LTTYRAHMLL LTFLCILAVD FPVFPRMLAK CETFGVSLMD
LGVGSFVFSQ GIISAMPVVK NPAHLTEPLV AKVLKVIRKC YPLFVLGLFR TLSVKGVEYP
EHQTEYGTHW NFFFTLGFIP ILQVLLHPLM VGIPISLLAV LVALLQQVAL SNGLMSYVFK
APRVNLVSSN KEGIVSLSGY LAIHLLGLYT GTIVLPPSPS YFRRCQKGLS QPKDKSGKRP
THEHDESKRK VDNMSSGLSS AQQTNRENDK TAIELCAYSV LWWTLLGCTM LLDIGGGVSR
RLVNLQYILW VAAYNTSFLL GYLVLDLLFF ASPSSRSRYS PYSKLKVKPD PAVLSTSERT
LRAAARAPPL LEAINHNGLV LFLLANLATG LVNLTMPTMY MSDPAAMAVL SLYSLTICGV
AWTSRNTKLW TF
//
