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Database: UniProt
Entry: A0A498J1D5_MALDO
LinkDB: A0A498J1D5_MALDO
Original site: A0A498J1D5_MALDO 
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
//
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