ID A0A0L0SG82_ALLM3 Unreviewed; 499 AA.
AC A0A0L0SG82;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=GPI-anchored wall transfer protein {ECO:0000256|RuleBase:RU280819};
DE EC=2.3.-.- {ECO:0000256|RuleBase:RU280819};
GN ORFNames=AMAG_06326 {ECO:0000313|EMBL:KNE61508.1};
OS Allomyces macrogynus (strain ATCC 38327) (Allomyces javanicus var.
OS macrogynus).
OC Eukaryota; Fungi; Fungi incertae sedis; Blastocladiomycota;
OC Blastocladiomycetes; Blastocladiales; Blastocladiaceae; Allomyces.
OX NCBI_TaxID=578462 {ECO:0000313|EMBL:KNE61508.1, ECO:0000313|Proteomes:UP000054350};
RN [1] {ECO:0000313|EMBL:KNE61508.1, ECO:0000313|Proteomes:UP000054350}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 38327 {ECO:0000313|EMBL:KNE61508.1,
RC ECO:0000313|Proteomes:UP000054350};
RG The Broad Institute Genome Sequencing Platform;
RA Russ C., Cuomo C., Burger G., Gray M.W., Holland P.W.H., King N.,
RA Lang F.B.F., Roger A.J., Ruiz-Trillo I., Young S.K., Zeng Q., Gargeya S.,
RA Fitzgerald M., Haas B., Abouelleil A., Alvarado L., Arachchi H.M.,
RA Berlin A., Chapman S.B., Gearin G., Goldberg J., Griggs A., Gujja S.,
RA Hansen M., Heiman D., Howarth C., Larimer J., Lui A., MacDonald P.J.P.,
RA McCowen C., Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Stolte C., Sykes S., Wortman J.,
RA Nusbaum C., Birren B.;
RT "Annotation of Allomyces macrogynus ATCC 38327.";
RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KNE61508.1, ECO:0000313|Proteomes:UP000054350}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 38327 {ECO:0000313|EMBL:KNE61508.1,
RC ECO:0000313|Proteomes:UP000054350};
RG The Broad Institute Genome Sequencing Platform;
RA Russ C., Cuomo C., Shea T., Young S.K., Zeng Q., Koehrsen M., Haas B.,
RA Borodovsky M., Guigo R., Alvarado L., Berlin A., Borenstein D., Chen Z.,
RA Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A., Gujja S.,
RA Heiman D., Hepburn T., Howarth C., Jen D., Larson L., Lewis B., Mehta T.,
RA Park D., Pearson M., Roberts A., Saif S., Shenoy N., Sisk P., Stolte C.,
RA Sykes S., Walk T., White J., Yandava C., Burger G., Gray M.W.,
RA Holland P.W.H., King N., Lang F.B.F., Roger A.J., Ruiz-Trillo I.,
RA Lander E., Nusbaum C.;
RT "The Genome Sequence of Allomyces macrogynus strain ATCC 38327.";
RL Submitted (NOV-2009) 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|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|RuleBase:RU280819}; Multi-pass membrane protein
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: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|RuleBase:RU280819}.
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DR EMBL; GG745338; KNE61508.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0L0SG82; -.
DR STRING; 578462.A0A0L0SG82; -.
DR EnsemblFungi; KNE61508; KNE61508; AMAG_06326.
DR VEuPathDB; FungiDB:AMAG_06326; -.
DR eggNOG; KOG0411; Eukaryota.
DR OMA; GLYVMQP; -.
DR OrthoDB; 228697at2759; -.
DR UniPathway; UPA00196; -.
DR Proteomes; UP000054350; 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:UP000054350};
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 63..82
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU280819"
FT TRANSMEM 94..112
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU280819"
FT TRANSMEM 169..190
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU280819"
FT TRANSMEM 269..287
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU280819"
FT TRANSMEM 367..391
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU280819"
FT TRANSMEM 403..427
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU280819"
FT TRANSMEM 439..458
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU280819"
FT TRANSMEM 470..491
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU280819"
FT REGION 16..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 499 AA; 54666 MW; 22C1C2378DF845F0 CRC64;
MEEQLAAVLR DADQFQPASH APGSPPFAAT GPGTMSEQEI RRREKEQFVS GLTGTSMEEV
HRVMLVAVFS YLALKLIIHQ FGHGSSYLAR VPRPIRWLLE FAFLVAVPNA AVLWPDLLAH
RATICAMFGL LVAVAYPRPG SLARMPPSHA HMKEWTRQLN DRVKPAVTVY RALMMSLTCF
AILAVDFHVF PRRFAKTEVF GTSLMDIGVG CFVFSQGLTV GLKQGSTSAS TPSVWASIRR
GWPLWLLGLG RVISVKGLDY QEHVSEYGVH WNFFFTLAAL GPIVVFLDRW VRWSDAPMAA
MLLIDYEVLL AKGLQHYVLT APRTNLISAN REGLTSLFGY VAIFLAARHV GRTLASPLPT
VTAWRRLLFR TLAPQIALTA AALWVARTAF LTDVSRRLCN APFVLWTVAV NAGMVALLVL
VDAVVFTDSA TAAIEVADAV NANGLVVFLG ANLATGAVNM VVDTLRVPDA AAVAVLSAYM
SSVVLVALGM YRMRWIVKF
//
