ID A0A2H3T949_FUSOX Unreviewed; 1122 AA.
AC A0A2H3T949;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 22-FEB-2023, entry version 17.
DE RecName: Full=GPI inositol-deacylase {ECO:0000256|ARBA:ARBA00015856, ECO:0000256|RuleBase:RU365011};
DE EC=3.1.-.- {ECO:0000256|RuleBase:RU365011};
GN ORFNames=FRV6_05457 {ECO:0000313|EMBL:SCO81244.1};
OS Fusarium oxysporum (Fusarium vascular wilt).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium oxysporum species complex.
OX NCBI_TaxID=5507 {ECO:0000313|EMBL:SCO81244.1, ECO:0000313|Proteomes:UP000219369};
RN [1] {ECO:0000313|Proteomes:UP000219369}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=V64-1 {ECO:0000313|Proteomes:UP000219369};
RA Guldener U.;
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}.
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DR EMBL; FMJY01000003; SCO81244.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2H3T949; -.
DR VEuPathDB; FungiDB:FOC1_g10006684; -.
DR VEuPathDB; FungiDB:FOC4_g10006807; -.
DR VEuPathDB; FungiDB:FOIG_06698; -.
DR VEuPathDB; FungiDB:FOMG_02980; -.
DR VEuPathDB; FungiDB:FOXG_04203; -.
DR VEuPathDB; FungiDB:FOZG_02905; -.
DR VEuPathDB; FungiDB:HZS61_014318; -.
DR OrthoDB; 5477082at2759; -.
DR Proteomes; UP000219369; 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:0016829; F:lyase activity; IEA:UniProtKB-KW.
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 Lyase {ECO:0000313|EMBL:SCO81244.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU365011};
KW Protein transport {ECO:0000256|ARBA:ARBA00022927,
KW ECO:0000256|RuleBase:RU365011};
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 102..125
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365011"
FT TRANSMEM 770..789
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365011"
FT TRANSMEM 810..830
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365011"
FT TRANSMEM 867..886
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365011"
FT TRANSMEM 893..913
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365011"
FT TRANSMEM 933..964
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365011"
FT TRANSMEM 985..1008
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365011"
FT TRANSMEM 1020..1038
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365011"
FT TRANSMEM 1050..1068
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365011"
FT TRANSMEM 1074..1091
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365011"
FT REGION 1..97
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 21..52
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 59..73
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 82..96
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1122 AA; 125087 MW; 1E0A8E3452BE00B8 CRC64;
MKRRSSGSAD DGDESSLDSD IPDPDPNSKT RTSPARARRP SSLNWKPSND RNGRNGQPRE
EPRQTTALKP TSLAAPSTPD MALARTPTQS PSPNRRIPRP RFSIVVLLTS ALGIVILISI
LRSLVTSQLD PKGCRMSYMR PSYVRFTEFD TEHTRFATKY SLYLYREQGI EPPDKLLGIP
VLFIPGNAGS YKQVRPIAAE AANYFHNNLQ HDHGALDAGI RSLDFFTVDF NEDITAFHGQ
TLLDQAEYLN EAVRYILSLY SDPQRATREG HLPDPTSVIV LGHSMGGVVA RAMLVQPNYQ
TNSINTIITM SAPHARPPVT FDGQIVQIYD EINDYWRQAY SQKWANNNPL WHVTLVSIAG
GGLDTVVPSD YASLESLVPP THGFTVFTTG IPTVWTSMDH QAILWCDQFR KVITKTLYDI
VNVHRGSQTK PRADRMKTFK KRFLTGMEPT MEKDLPLKEA TTLLTLSDDS NSILPAGQRL
VLSQIGQQPK PRAHLLPIPP QGSPEVKRFT VLTDASLDEA GENGKVEVLF CSVFPFQSGQ
ATSLYPFQID LSTDDSGSTR LACKNAASDR ILLPASTSSS RYPFYLDRER EIVPFSFLQY
DLDQLPDHQF VAIIEKSVSS TRSFLIAEFS DQSAFSKKED ASLAKLLLSG ITVDLPANRP
LTTEVNIASL QSALLAYKLE ITSPHCQAEK VLFSPLVRQY LDQPYESKYF VNAQSVDVSL
HGVAPYLPPS LGSGAEKGVT FQVWTDPSCG SSIHLQIKPD FWGSLGKLYM RYRTVFAAFP
MLTVALVLRK QFRVYDSSGV FISFSQSLDL CLRQSIPLLL VSLTLLSMSM EGVPATWLGR
WWYQAPAAPL SIDFHRHDIL IGTDDPFFWF LVPLIGVVCI GVCAMVHYMT KAFTHVLGFL
YWALTLLPLS SGAEDDGVAR TPAFVPSTPK RRMITTAILL FLVWTFIPYQ FAYLVACLVQ
LFTVIRALRI NETAPSDANS NYYHYAHSVL LLMLWILPIN LPILAVWIRN LAVHWLTPFS
SHHNVLSIMP FILLVENLTT GKMVPQVGRL FGYVTSLLLF ATALYAAMYG ISHAYMLHYL
VNIIAAWLVV LHSTKDPFSL SGLGAIFESS PTEEHKKSKA SL
//
