ID   A0A197JIP1_9FUNG        Unreviewed;       458 AA.
AC   A0A197JIP1;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   22-FEB-2023, entry version 22.
DE   RecName: Full=GPI inositol-deacylase {ECO:0000256|RuleBase:RU365011};
DE            EC=3.1.-.- {ECO:0000256|RuleBase:RU365011};
GN   ORFNames=K457DRAFT_141982 {ECO:0000313|EMBL:OAQ24381.1};
OS   Linnemannia elongata AG-77.
OC   Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mortierellomycotina;
OC   Mortierellomycetes; Mortierellales; Mortierellaceae; Linnemannia.
OX   NCBI_TaxID=1314771 {ECO:0000313|EMBL:OAQ24381.1, ECO:0000313|Proteomes:UP000078512};
RN   [1] {ECO:0000313|EMBL:OAQ24381.1, ECO:0000313|Proteomes:UP000078512}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AG-77 {ECO:0000313|EMBL:OAQ24381.1,
RC   ECO:0000313|Proteomes:UP000078512};
RG   DOE Joint Genome Institute;
RA   Uehling J., Gryganskyi A., Hameed K., Tschaplinski T., Misztal P., Wu S.,
RA   Desiro A., Vande Pol N., Du Z.-Y., Zienkiewicz A., Zienkiewicz K.,
RA   Morin E., Tisserant E., Splivallo R., Hainaut M., Henrissat B., Ohm R.,
RA   Kuo A., Yan J., Lipzen A., Nolan M., Labutti K., Barry K., Goldstein A.,
RA   Labbe J., Schadt C., Tuskan G., Grigoriev I., Martin F., Vilgalys R.,
RA   Bonito G.;
RT   "Genome sequencing reveals origins of a unique bacterial endosymbiosis in
RT   the earliest lineages of terrestrial Fungi.";
RL   Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Involved in inositol deacylation of GPI-anchored proteins
CC       which plays important roles in the quality control and ER-associated
CC       degradation of GPI-anchored proteins. {ECO:0000256|RuleBase:RU365011}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000256|RuleBase:RU365011}.
CC   -!- SIMILARITY: Belongs to the GPI inositol-deacylase family.
CC       {ECO:0000256|RuleBase:RU365011}.
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DR   EMBL; KV442095; OAQ24381.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A197JIP1; -.
DR   STRING; 1314771.A0A197JIP1; -.
DR   OrthoDB; 2718971at2759; -.
DR   Proteomes; UP000078512; Unassembled WGS sequence.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016788; F:hydrolase activity, acting on ester bonds; IEA:InterPro.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR012908; PGAP1-like.
DR   PANTHER; PTHR11440:SF97; BCDNA.GH02384; 1.
DR   PANTHER; PTHR11440; LECITHIN-CHOLESTEROL ACYLTRANSFERASE-RELATED; 1.
DR   Pfam; PF07819; PGAP1; 1.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE   3: Inferred from homology;
KW   Endoplasmic reticulum {ECO:0000256|RuleBase:RU365011};
KW   Hydrolase {ECO:0000256|RuleBase:RU365011, ECO:0000313|EMBL:OAQ24381.1};
KW   Membrane {ECO:0000256|RuleBase:RU365011};
KW   Protein transport {ECO:0000256|RuleBase:RU365011};
KW   Reference proteome {ECO:0000313|Proteomes:UP000078512};
KW   Transport {ECO:0000256|RuleBase:RU365011}.
FT   REGION          41..116
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        41..58
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        59..77
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        78..98
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   458 AA;  51203 MW;  87D04229D7470A13 CRC64;
     MLMNTTSFLA SHLRATISSA VNSTVSLTVA LRSKIGFLGQ QMTHQQDDSS SSSMRQQQHQ
     HEQEYHRQDR SESLSSNTRE YHQEQSTVSA STYNHQELEG SLPPPPSSRL THEQYPSLQP
     WKNLDRRIKN FGLSMPVSTT YIAPRHPIVL CHGLFGFDKM GPENMPSLQI HYWNGIHKAL
     TKLGAKVIVA GVPRTGAIRE RAEDLHRILS ATMEGSPVNF IAHSMGGLDS RYLISHIHDK
     NYHVESLTTF STPHRGSPMM DWFRDYIGVG LLQQSEEEAM RKLGEEASRL AAVAAAAAVG
     TASTPEAKAA AAQEAAQHSR NMQAQAPLWS RFLIPFLDTP AYANLTTEYC TQVFNPNTPD
     DPRVAYYSYG ASIPRLPIWA PLGFPWEVIR AKEGENDGLV SVASARWGKY IETVECDHWD
     LNNRWRLKIG YPSSKTGSPF DAVELYMSAA TRLFHEGH
//