ID A0A139HW35_9PEZI Unreviewed; 1139 AA.
AC A0A139HW35;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 22-FEB-2023, entry version 20.
DE RecName: Full=GPI inositol-deacylase {ECO:0000256|ARBA:ARBA00015856, ECO:0000256|RuleBase:RU365011};
DE EC=3.1.-.- {ECO:0000256|RuleBase:RU365011};
GN ORFNames=AC578_8538 {ECO:0000313|EMBL:KXT06695.1};
OS Pseudocercospora eumusae.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Pseudocercospora.
OX NCBI_TaxID=321146 {ECO:0000313|EMBL:KXT06695.1, ECO:0000313|Proteomes:UP000070133};
RN [1] {ECO:0000313|EMBL:KXT06695.1, ECO:0000313|Proteomes:UP000070133}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 114824 {ECO:0000313|EMBL:KXT06695.1,
RC ECO:0000313|Proteomes:UP000070133};
RA Chang T.-C., Salvucci A., Crous P.W., Stergiopoulos I.;
RT "Comparative genomics of the Sigatoka disease complex on banana suggests a
RT link between parallel evolutionary changes in Pseudocercospora fijiensis
RT and Pseudocercospora eumusae and increased virulence on the banana host.";
RL Submitted (JUL-2015) 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:KXT06695.1}.
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DR EMBL; LFZN01000005; KXT06695.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A139HW35; -.
DR STRING; 321146.A0A139HW35; -.
DR OrthoDB; 5477082at2759; -.
DR Proteomes; UP000070133; 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:UP000070133};
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 123..146
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365011"
FT TRANSMEM 786..804
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365011"
FT TRANSMEM 827..846
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365011"
FT TRANSMEM 885..918
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365011"
FT TRANSMEM 1000..1020
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365011"
FT TRANSMEM 1032..1050
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365011"
FT TRANSMEM 1062..1082
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365011"
FT TRANSMEM 1088..1106
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365011"
FT REGION 1..104
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 25..48
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 49..65
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 72..101
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1139 AA; 126670 MW; 815D56275AD8E74D CRC64;
MRRRPSCSGE DEDSSKSAPT SATSDKGDKT RDREREMTTR EHGRATRQSA RQQKQQQQQA
GGDLKVTPLS RSEQKAAWSR TTPISSPALE ADPQSDATLV TSRPDPMADQ LHRLARLRSP
WRCSLLTLAT SISAIVILLT VIHSFLNRQQ DPKGCAMSYM RPRFDPFPDF DTEHTRFASK
YSLYLYREGG IDNDSRVRGI PVLFIPGNAG SYKQVRPIAA EAATYFHDAL REDMASIRDG
KRSLDFFTVD FNEELIAFHG QTLLDQAEYL NEAVAYILAL YHNPHRSARD PGLPDPKSVI
ILGHSMGGVV ARTMLRMPNY QEHTINTILT LSAPHARPPI SFDAAMLSTY NDINTYWRES
FSGSAAGRNP LDDVTLVSVA GGGLDTMIPS EYTSLTSLVP DTHGFTVFTS SIPNVWTGMD
HLAIMWCDQF RKALVKAIYD VIDVRRPSQT RSQPERIRAL RKRLLTGMEP VVEKGVLEQE
PTTYLTLEHS STGIMSHGQR LVLRSLGDTG ATKAHVMPIP AQPFTEGSKF TLLTDQSLDS
EEDDGTLSVL LCSVFPPPSA FSVLSYAINL DASNSNAGST RLACKNAVND VSLLPASTNT
SANAFDKVKP FSYLQYELPS IADYQFVAVV EKAKDLTPGW VVAEFSNSAE SAIQVSKGHH
QILISGMKVK LPANRPMMTE IKIPEIHSTM FAYSLQVKRK ECRKYEESFA PLVRQYIAEP
YESKYFVNTR GGNINVHGLS PFMPPPLAGG PTDGLSLQLW ADPTCNSTVE VSLQVDMLGS
AGKLVMRYRT VFAAFPLLVV ALVLRKQFKV YDTTGVFMSF TQSMDQCIRS SIPAIWVALT
FFAIAVSKSS HSVWTRNLLS TSTGTSEQTI DFTVNDLMLG TSDPFFWFLV PLFAIISVGI
CIVMNYVVLM LTHVFALITA YTRPWTQRLP DGTTSYGGAM SQRLFTTGML LLLVVTVIPY
QFAYLVLCTR QVFTCVGSLR GAQETQSAAS YNFYNYTHSM LILMLWILPI NMPVLVVWIH
NLTVHWWTPF STHHNLLSVL GYILLVEVMS TNSMIPRVTS RIRFLTNTLM FALALYAAVY
GVTYAYRMHY LVNALCFWLF IIHLSNGPYS LANMAKFLSG SGQTSPPPEG PSSHGKKRP
//
