ID   A0A178DXI8_9PLEO        Unreviewed;      1020 AA.
AC   A0A178DXI8;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   28-JUN-2023, entry version 19.
DE   RecName: Full=GPI inositol-deacylase {ECO:0000256|ARBA:ARBA00015856, ECO:0000256|RuleBase:RU365011};
DE            EC=3.1.-.- {ECO:0000256|RuleBase:RU365011};
GN   ORFNames=IQ07DRAFT_119854 {ECO:0000313|EMBL:OAL47533.1};
OS   Pyrenochaeta sp. DS3sAY3a.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Cucurbitariaceae;
OC   Pyrenochaeta.
OX   NCBI_TaxID=765867 {ECO:0000313|EMBL:OAL47533.1, ECO:0000313|Proteomes:UP000077535};
RN   [1] {ECO:0000313|EMBL:OAL47533.1, ECO:0000313|Proteomes:UP000077535}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DS3sAY3a {ECO:0000313|EMBL:OAL47533.1,
RC   ECO:0000313|Proteomes:UP000077535};
RG   DOE Joint Genome Institute;
RA   Zeiner C.A., Purvine S.O., Zink E.M., Wu S., Pasa-Tolic L., Chaput D.L.,
RA   Haridas S., Grigoriev I.V., Santelli C.M., Hansel C.M.;
RT   "Comparative analysis of secretome profiles of manganese(II)-oxidizing
RT   ascomycete 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|ARBA:ARBA00003496,
CC       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; KV441651; OAL47533.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A178DXI8; -.
DR   STRING; 765867.A0A178DXI8; -.
DR   InParanoid; A0A178DXI8; -.
DR   OrthoDB; 5477082at2759; -.
DR   Proteomes; UP000077535; 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:UP000077535};
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        21..42
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU365011"
FT   TRANSMEM        676..695
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU365011"
FT   TRANSMEM        715..738
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU365011"
FT   TRANSMEM        776..807
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU365011"
FT   TRANSMEM        841..865
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU365011"
FT   TRANSMEM        885..911
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU365011"
FT   TRANSMEM        953..970
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU365011"
SQ   SEQUENCE   1020 AA;  113513 MW;  406649CF06BB6C2C CRC64;
     MAEHEDRKWR QQRRNPWACS LSTVATTLVG LGVILLMAHS FLTRQLDVKG CEMSWMRPIY
     SKQDAFSTEH TRFANKYSLY IYREGGIDED VRVKGVPVLF IPGNAGSYKQ VRSLASEAAY
     HYHNTVRYEA NAGKEKRPLD FFAVDFNEDF TAFHGQTLLD QAEYLNDAVT YILSLYHTPG
     HVLRDSSLPD PTSVIIVGHS MGGVVARTMF TMPNYQPNSI NTIVTLAAPH ARPPLSFDGD
     IVRTYKGVNE YWRRSYSQKP LLENPLRHVT LISIAGGGLD TMISSEYASI ESLIPETHGF
     TVFTSSIPNV WTGADHLAIT WCDQVRKSVV RALYDVIDVS HAAQTTSEAH RMSRFKKWFL
     PSLDSITEKS LHYGDAKVLL TLDLDILGVS QNERVALRNL GRSAQKPGVR LLPVSGGKRF
     TLLSNEKLDS TSEHGALEVL ACRKHAQHTE QSVIRFSVEL DLSGNSSNLV KLACKNTVAD
     VVTLPASTFQ STLPFKTDQP PFSYLQYDPE DLADYDFVAV LDKAGEHSAG WAIAEFSNTS
     DSLLKVDIGL QGLLTKGVSL HLPAKHPLVT EIRISAVQSS LLAYNIHVSK QSCKQGLLFA
     PLLRQYILDV YESKFFVKVQ EASINFYGVS PYMPPALPNK KDSRGLGLQI WSDPTYESSV
     EVTLKVDILG SLGKLWMRYR VVFAAFPLLI VALVLRHQFR VYDATGVFMS FAQGLNECVC
     SSLPLAFAAL TFLSIGLAGT SQQPRESSTL ETVARTTTAP ESHELLLGSA DIFFCFLVPL
     LGLMCVALCV IINYVALLLE FFFAYLVSFV KKPRLRIDGE KKTTSAAGIA WNRKRILTTC
     VLLSLVSAVV PYHLAYAVLC LVHLASCVRG FGLAKETRLD QDYHFYNYAH SIFILMLWIL
     PINIPVLVVW VRNLTIPWLT PFSPQHNIIS IMPFVFLVET LNTGRMIPRA RPGLSLVTGA
     LLFGFGAYAA VYGVSYAYML HHLANMFCAW LVALQFDTSS SSLYVSEGGS PSDREVKKRP
//