ID   A0A238FF90_9BASI        Unreviewed;      1188 AA.
AC   A0A238FF90;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   22-FEB-2023, entry version 19.
DE   RecName: Full=GPI inositol-deacylase {ECO:0000256|RuleBase:RU365011};
DE            EC=3.1.-.- {ECO:0000256|RuleBase:RU365011};
GN   ORFNames=BQ2448_3543 {ECO:0000313|EMBL:SCV70781.1};
OS   Microbotryum intermedium.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC   Microbotryomycetes; Microbotryales; Microbotryaceae; Microbotryum.
OX   NCBI_TaxID=269621 {ECO:0000313|EMBL:SCV70781.1, ECO:0000313|Proteomes:UP000198372};
RN   [1] {ECO:0000313|Proteomes:UP000198372}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Jeantristanb JTB J.-T., Ricardo R.;
RL   Submitted (SEP-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|ARBA:ARBA00004477}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004477}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the GPI inositol-deacylase family.
CC       {ECO:0000256|ARBA:ARBA00006931, ECO:0000256|RuleBase:RU365011}.
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DR   EMBL; FMSP01000006; SCV70781.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A238FF90; -.
DR   STRING; 269621.A0A238FF90; -.
DR   OrthoDB; 5477082at2759; -.
DR   Proteomes; UP000198372; 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   InterPro; IPR039529; PGAP1/BST1.
DR   PANTHER; PTHR15495:SF7; GPI INOSITOL-DEACYLASE; 1.
DR   PANTHER; PTHR15495; NEGATIVE REGULATOR OF VESICLE FORMATION-RELATED; 1.
DR   Pfam; PF07819; PGAP1; 1.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE   3: Inferred from homology;
KW   Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824,
KW   ECO:0000256|RuleBase:RU365011};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU365011};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU365011};
KW   Protein transport {ECO:0000256|ARBA:ARBA00022927,
KW   ECO:0000256|RuleBase:RU365011};
KW   Reference proteome {ECO:0000313|Proteomes:UP000198372};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW   ECO:0000256|RuleBase:RU365011};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|RuleBase:RU365011};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU365011}.
FT   TRANSMEM        73..94
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU365011"
FT   TRANSMEM        804..825
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU365011"
FT   TRANSMEM        846..865
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU365011"
FT   TRANSMEM        902..929
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU365011"
FT   TRANSMEM        1024..1047
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU365011"
FT   TRANSMEM        1090..1111
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU365011"
FT   REGION          1..52
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1152..1188
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        19..52
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1155..1188
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1188 AA;  129070 MW;  B53F1B40D3F6971E CRC64;
     MPPSAGVASQ ERRAGEAGAV SSSRSTNPSE ALDAATTTTT TTTTTTTTTR KTTTSHVRYA
     VTNRSSFGRS PSAGFVAVVL VSLAALVTVF LAHVDSPPRY PLGSLPLDAR GGGAGSCRQS
     WMSPSYLHIA GTSLPLFRLW SSRVPEAHAR FFVPRSPSPA PDPTGFGREY SRLGAGPWGM
     YLYREEGWDE DPLEQHAGHG AASTDRTSRA FALAGTPVVF VPGNAGSFRQ VRSLASAASR
     AYYELPGVRR KGMGSKEGGR PLDFFTLDFN DDFSAFHGQT LLDQAEYLAD SIRYILSLYH
     QDSNARQGRP DPTSVIVVGH SMGGIVARAA LLHPHYQSGS ISTLVTIATP HAVPPVTVDI
     GVDRVYDEIN SFWRRAHHLE AMSSPPSRRE LRGEVELSDL VLVSISGGIS DTTVASESAS
     LTSIMPLNDS HGFTVFTTAI PGVQTPIDHL AMLWCRQLME TVATALLTIV DVRSPLGVLP
     REARVEKLAE RLLGAIESYP SKLDGRKSTL ESLERGRRGQ ELAIGERLSL PSHGDERSTF
     LLPIPPRRTY GSARVFSLLT SATIGRSLDS LVEVYACGRN ESMPESTRGS SCRSLFPSFV
     TTVPISPHSA QSPLLPAPVE DGTMAFLNVD VSQLEAQEVI AVVVKPGNAW LLAEFGDKDR
     RVHTVEKSAF QLMLGGFKIE NFPATPSLIS ELWLPALDSS LLTFKRTLAD SSAVLFAPLL
     RQYSSLLHES KYFPNVREVS LYTHASGPYL PAPASPFVSS GARLQFIVDP TCARETSGAS
     ADMAIEIKLD LWASLGNLAM RYRMAVVAFP FALILLVFAC QLRDYNSGHS FPPFATALGA
     FLRHQFLPLL GVIVALSFLQ SILLGTRLSF VEAKLASADA HVVSSLPPRW ISEMLLGNQN
     PFFAFLGAFI LFIMLSVVVL EYAALYLLVV VLARLIQVLH QCGPPPLRSF ISVFEPRETL
     PLQRIVTMGA LVLLVLFFAP YQFAFLVIFL VHFLSTVKSL LLAQDISAPS TPASTRRLWD
     RYHYSFVILL AMFGLLPINA MILAVWVRNL AVGWLAPFST DHNVLNVLGF LLNVEALHSG
     KMLQRTPGSV ASTVSVALPL IGAGFALLYG IRWTYNIYPL ANAFFLWLAS NHSHHLVGAL
     NEAVKAKRRL SISTTAGRHP EQSSAKQLSS SALSPSPTPR TPTKRQCL
//