ID A0A498J1D5_MALDO Unreviewed; 1748 AA.
AC A0A498J1D5;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE RecName: Full=GPI inositol-deacylase {ECO:0000256|RuleBase:RU365011};
DE EC=3.1.-.- {ECO:0000256|RuleBase:RU365011};
GN ORFNames=DVH24_031657 {ECO:0000313|EMBL:RXH89300.1};
OS Malus domestica (Apple) (Pyrus malus).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Rosales; Rosaceae; Amygdaloideae; Maleae; Malus.
OX NCBI_TaxID=3750 {ECO:0000313|EMBL:RXH89300.1, ECO:0000313|Proteomes:UP000290289};
RN [1] {ECO:0000313|EMBL:RXH89300.1, ECO:0000313|Proteomes:UP000290289}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. HFTH1 {ECO:0000313|Proteomes:UP000290289};
RC TISSUE=Young leaf {ECO:0000313|EMBL:RXH89300.1};
RA Hu J.;
RT "A high-quality apple genome assembly.";
RL Submitted (OCT-2018) 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|RuleBase:RU365011}.
CC -!- SIMILARITY: Belongs to the 'GDXG' lipolytic enzyme family.
CC {ECO:0000256|ARBA:ARBA00010515}.
CC -!- SIMILARITY: Belongs to the GPI inositol-deacylase family.
CC {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:RXH89300.1}.
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DR EMBL; RDQH01000335; RXH89300.1; -; Genomic_DNA.
DR STRING; 3750.A0A498J1D5; -.
DR Proteomes; UP000290289; Chromosome 9.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0004523; F:RNA-DNA hybrid ribonuclease activity; IEA:InterPro.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 2.
DR Gene3D; 3.30.420.10; Ribonuclease H-like superfamily/Ribonuclease H; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR013094; AB_hydrolase_3.
DR InterPro; IPR012908; PGAP1-like.
DR InterPro; IPR002156; RNaseH_domain.
DR InterPro; IPR036397; RNaseH_sf.
DR PANTHER; PTHR47346:SF1; GPI INOSITOL-DEACYLASE; 1.
DR PANTHER; PTHR47346; HYDROLASES, ACTING ON ESTER BOND; 1.
DR Pfam; PF07859; Abhydrolase_3; 1.
DR Pfam; PF07819; PGAP1; 1.
DR Pfam; PF13456; RVT_3; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 2.
PE 3: Inferred from homology;
KW Endoplasmic reticulum {ECO:0000256|RuleBase:RU365011};
KW Hydrolase {ECO:0000256|RuleBase:RU365011};
KW Membrane {ECO:0000256|RuleBase:RU365011};
KW Protein transport {ECO:0000256|RuleBase:RU365011};
KW Reference proteome {ECO:0000313|Proteomes:UP000290289};
KW Transmembrane {ECO:0000256|RuleBase:RU365011};
KW Transmembrane helix {ECO:0000256|RuleBase:RU365011};
KW Transport {ECO:0000256|RuleBase:RU365011}.
FT TRANSMEM 1317..1338
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365011"
FT TRANSMEM 1359..1377
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365011"
FT TRANSMEM 1397..1423
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365011"
FT TRANSMEM 1485..1511
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365011"
FT TRANSMEM 1584..1603
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365011"
FT TRANSMEM 1652..1673
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365011"
FT DOMAIN 183..442
FT /note="Alpha/beta hydrolase fold-3"
FT /evidence="ECO:0000259|Pfam:PF07859"
FT DOMAIN 477..544
FT /note="RNase H type-1"
FT /evidence="ECO:0000259|Pfam:PF13456"
FT REGION 79..150
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 105..150
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1748 AA; 194099 MW; A85AE151D2A4F034 CRC64;
MPSVAVQLYS VFFKFLLKHR LQNRIQNQPD EYNPFGVTSR PEETIVAPNP VFDDGVATKD
IHIDPLTSLS IRIFLPESAL TPPEPASKPR VIAAPKRSDL NNGPNRADPV RQSLNNLPAT
PSRRNSYGNP AVSNLAKSEQ RRNSYGSSND MEGLNLMANA GAGVYRGYSP GNSTRTGRKL
PVMLQFHGGG WVSGSNDSVA NDIFCRRIAK LCDVVVLAVG YRLAPENRYP AAFEDGLKVL
NWLGKQANLA ECSKSMGSGR GALGGVTEFK KTDSHRHIVD SFGASMVEPW LAAHGDPTRC
VLLGASCGAN IADYVARKAV EAGKLLDPVK VVARVLTYPF FIGSVPTRSE IKLANSYFYD
KAMCILAWKL FLPEDEYSLD HPAANPLIPD RGPPLKLMPP TLTVVAEHDW MRDRAIAYSE
ELRKVNVDAP VLEYKDAVHE FATLDMLLKT PQAQACAEDI AIWVKKYISL RGHDTEKMGW
NGIIIEFDSL DSVSCLQDLN SMGSWDAFPL LAKCTCMGKA FQDCRWSWVP RSANKAADSL
ASRHCREVCD SVWVKRPPSS LVHVLSNLRS GDPSPSLFSS SSQIYRLTRF KAQSRVALLV
AFLLCVCFAG LYDLLKPVSN GCIMTYMYPT YVPIPTTTPV SPAKYSLYLY HEGWKKIDFE
EHLKKLSGVP VLFIPGNGGS YKQVRSLAAE SDRGYQAGPL ERTYYQEAYL TPEEGGEEID
VTSFKLPNRY DSRLDWFTVD LEGEHSAMDS AILEEHAEYV VNSIHRILDQ YKESYKARQR
EGAATSGSSP KSVILVGHSM GGFVARAAVI HHRLRKSAVE TILTLSSPHQ YPPVALQPSL
GHYFERVNDE WRKGYEVQTT RAGHHVSGPV LSHVVVISIS GGYNDYQVRS KSESLDGIVP
PTHGFVISST GMRNVWLSME HQAILWCNQL VIQVAHTLLS LVDSGTGQPF SDTRIRTAIF
SKMLRSGIPQ SFDWRMQSHL SQQSIHIPTR DVKDKTESLY TSAACPSNVH WSDDGLERDL
YIQTTTVTVL AMDGRRRWLD IQKLGSNGRS HFMFVTNLAP CSGVRLHLWP EKRNSTSELP
ICIRILDVTS RMVRIPSGPA PTQIEPGSQT EQASPSAIFR LGPEDMRGFR FLTISVAPRP
TISGRPPPAV SMAVGQFFNP EEGEREFSPW SMPLPSYSYK EMSLKEDHPL ALNLSFTTSL
GLLPVMFSLK AAGCGIMNSG LPDEQAGDED NSKLCKLRCF PPIAFAWDHT SGLHIFPNMY
SEKIVVDSSP ALWSSPQSSE KTSVMLLVDP HCSYRSSMTV PVTAAASRFL LLYNSQIAGF
SLVVIFFALM QQICTWDLDQ HIPSILTAVE FNLRIPLPFL YLAIAPILLS FSLSFLISQP
FPSFSSFTIV SVTCYLLANG FVIILILISQ LIFYAAAVVH VFIKTRFQLG EKSVHRFINL
SSGFFSLKVS LFPSFTMGKD WQIGSFTFTW VFHGQLVRVL RANPVFVTAL VAITVACLVH
AAFGLFIILF FDALSCHSAL CSHARRHELF DCKKEDNGLS CQLPSKSDGI SNQNIHSEDC
CSNSPNSSKS FGETQLELFH HRHGLFILHL AAALMFVPSL VAWFQRIGMG HSFPWLLDSF
LCTGVILHGI FTSKPESSSF LISFPGFRNC EVRLNFLYLL AGYYSYISSL ALAPYRAFYG
YEYIVSRVGC VVRMTPVSTV LKSESSHGSK RPCPLVAEGF SFHAPERKTV YWTGTRVSFG
MVCAVPFQ
//