ID A0A1G4BPK6_9PEZI Unreviewed; 1285 AA.
AC A0A1G4BPK6;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 22-FEB-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};
DE Flags: Fragment;
GN ORFNames=CORC01_01442 {ECO:0000313|EMBL:OHF03389.1};
OS Colletotrichum orchidophilum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum.
OX NCBI_TaxID=1209926 {ECO:0000313|EMBL:OHF03389.1, ECO:0000313|Proteomes:UP000176998};
RN [1] {ECO:0000313|EMBL:OHF03389.1, ECO:0000313|Proteomes:UP000176998}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IMI 309357 {ECO:0000313|EMBL:OHF03389.1,
RC ECO:0000313|Proteomes:UP000176998};
RA Capua I., De Benedictis P., Joannis T., Lombin L.H., Cattoli G.;
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|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}.
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:OHF03389.1}.
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DR EMBL; MJBS01000007; OHF03389.1; -; Genomic_DNA.
DR STRING; 1209926.A0A1G4BPK6; -.
DR OrthoDB; 5477082at2759; -.
DR Proteomes; UP000176998; 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:UP000176998};
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 265..288
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365011"
FT TRANSMEM 935..953
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365011"
FT TRANSMEM 1032..1054
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365011"
FT TRANSMEM 1061..1078
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365011"
FT TRANSMEM 1098..1129
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365011"
FT TRANSMEM 1150..1173
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365011"
FT TRANSMEM 1222..1241
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365011"
FT REGION 44..151
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 173..241
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 44..67
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:OHF03389.1"
SQ SEQUENCE 1285 AA; 143417 MW; EE1D512F043A7078 CRC64;
EGTYLYSRLR TFFSRCFVPV VSSCCHHLHV FLWTSLPSTL SFSSSTLPPS HPARKTTNPS
TARLNDTLPF LEDSIEPSPP MKRRPSGSTD VSDEPLADPP VIQQPARTRD CAHLSKQPAA
VTVAAAATSR PSSARSRRSN DPNWRLEHGP DANPILDNHL LTALSSSPLS APSLAVPSPA
YQNHTHQLPN HHHHHSQAVG NDPQPSQSEI HYLDGDNEDG QGGGDGLNDG IVDTGREDET
TMTAEKMPDV RLAGRRSRFR SPWSVTILTL TVAVLGITLL CAILNSSWTR QLDAKGCRMS
YMRPSYIRLR DFDTEHTRFA TKYSLYLYRE QGVDDERKLR GVPVLFIPGN AGSYKQVRPI
AAEAANYYHE SLQHDEAAVA AGARNLDFFT VDFNEDITAF HGQTMLDQAE YLNEAIRYIL
SLYMDPRMSA RDQDLPDPTS VLVLGHSMGG IVARTMLIMP NYQSNSINTI ITMSAPHSRP
PVTFDGQIVK IYDEINDYWR HAYSQKWANN NPLWHVTLVS IAGGGLDTVV PSDYASVEPI
IPETHGFTVF TTGIPGVWTS MDHQAILWCD QFRKVVARAM YDVVDVHRSS QTKPRAERMR
VFKKYFLTGM ESIAEQTVAT EGPSTLLTLE DNSNAIMAQG ERLVLRRLGR DTKVAAHLLP
VPPQGSPEGK RFTLLTDSAL DRPGEHGKLE VLLCSVFPLQ PGQSTTLFST NMDLSGDSTG
STRLACKNAA SDAILLPPST RMLHQPFALE NEPVTRPFSY LQFDIEDIAD HQFVAVIDKS
IKPSQNFVVA EFSDHSQSHR RRNISLRRIL AFGMTLRLPS NRPLVAEINI PTLQSSLLAY
NLEIGNQACG STSGLFSPLI RQHLAQPYES KFFVNARHAS ISMHGVAPFV PPPLRHKVQE
EQGLSLQFWT DPTCESTIQV TLTVDVLGSL GKLYMRYRTV FAAFPLLVVT LVLRKQFRIY
DTTGAFISFS ESLDLCLRQS LPLMFLSLTF LSLSMTGSWS SGPSVFWHWR NTTSAAADFH
SNDLLTGTQD PFFWFLIPLI GVVCIGVCAC LHFITLALTQ LLGFLYAWIA LRSFAVGRDE
RRRPHLPIFV ASSPRRRMIT TAVLLFLVST FIPYQFAYLV ACLVQLFTVV RAHRIASELK
SGPTQDFYHY AHSILVLMLW VLPINLPILA VWIRNLAVHW LTPFSSHHNV LSIMPFILLV
ENLTTGRMVP RVTGRMRHLT SVLLFGTAIY AAIYGVSYAY MLHYLVNLIA GWLVVIHSTS
DNWPLAGFSS IFDSHHEGPK RGKTP
//
