ID A0A2I2FUR9_9EURO Unreviewed; 324 AA.
AC A0A2I2FUR9;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 02-APR-2025, entry version 26.
DE RecName: Full=N-acetylglucosaminylphosphatidylinositol deacetylase {ECO:0000256|ARBA:ARBA00012176};
DE EC=3.5.1.89 {ECO:0000256|ARBA:ARBA00012176};
GN ORFNames=P170DRAFT_285108 {ECO:0000313|EMBL:PLB44372.1};
OS Aspergillus steynii IBT 23096.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=1392250 {ECO:0000313|EMBL:PLB44372.1, ECO:0000313|Proteomes:UP000234275};
RN [1] {ECO:0000313|EMBL:PLB44372.1, ECO:0000313|Proteomes:UP000234275}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBT 23096 {ECO:0000313|EMBL:PLB44372.1,
RC ECO:0000313|Proteomes:UP000234275};
RG DOE Joint Genome Institute;
RA Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA Salamov A., Henrissat B., Wiebenga A., De Vries R.P., Grigoriev I.V.,
RA Mortensen U.H., Andersen M.R., Baker S.E.;
RT "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT speciation.";
RL Submitted (DEC-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the PIGL family.
CC {ECO:0000256|ARBA:ARBA00006066}.
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:PLB44372.1}.
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DR EMBL; MSFO01000009; PLB44372.1; -; Genomic_DNA.
DR RefSeq; XP_024699674.1; XM_024843202.1.
DR AlphaFoldDB; A0A2I2FUR9; -.
DR STRING; 1392250.A0A2I2FUR9; -.
DR GeneID; 36550901; -.
DR VEuPathDB; FungiDB:P170DRAFT_285108; -.
DR OrthoDB; 440160at2759; -.
DR UniPathway; UPA00196; -.
DR Proteomes; UP000234275; Unassembled WGS sequence.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:TreeGrafter.
DR GO; GO:0016020; C:membrane; IEA:GOC.
DR GO; GO:0000225; F:N-acetylglucosaminylphosphatidylinositol deacetylase activity; IEA:UniProtKB-EC.
DR GO; GO:0006506; P:GPI anchor biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.40.50.10320; LmbE-like; 1.
DR InterPro; IPR003737; GlcNAc_PI_deacetylase-related.
DR InterPro; IPR024078; LmbE-like_dom_sf.
DR PANTHER; PTHR12993:SF11; N-ACETYLGLUCOSAMINYL-PHOSPHATIDYLINOSITOL DE-N-ACETYLASE; 1.
DR PANTHER; PTHR12993; N-ACETYLGLUCOSAMINYL-PHOSPHATIDYLINOSITOL DE-N-ACETYLASE-RELATED; 1.
DR Pfam; PF02585; PIG-L; 1.
DR SUPFAM; SSF102588; LmbE-like; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000234275};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..324
FT /note="N-acetylglucosaminylphosphatidylinositol
FT deacetylase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5014115663"
FT REGION 143..174
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 148..159
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 324 AA; 35175 MW; E94F41708C1861A6 CRC64;
MSSSLISLGV AIAAVFLFWT MSSTSSSPFA RNFPRLYNQR ICLLIAHPDD EAMFFAPTVL
ALTKPELGNH LKILCLSTDA DGLGHIRKKE LQQSALQLGL RNESDVYVVD DPSRFPDSMS
TTWSEADVSD LLASAFAPDL LAGGGGSSST SSATAASSSA RKRDSNSSSN AKNASPTATI
DMILTFDQHG ISNHPNHRSL YHGALYFLRS LMKDKPGYSC PVSLYTLHTT TLLRKYIGVL
DAPVTMARGA LSSLVSSLAR NWGSAGSREG GNPSQLLFVS SVGEWMTAQS AMVKAHKSQM
VWFRWGWITL GRYMAVNDLQ REKI
//
