ID A0A0D2GTL2_9EURO Unreviewed; 1635 AA.
AC A0A0D2GTL2;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 08-NOV-2023, entry version 29.
DE RecName: Full=GPI inositol-deacylase {ECO:0000256|ARBA:ARBA00015856, ECO:0000256|RuleBase:RU365011};
DE EC=3.1.-.- {ECO:0000256|RuleBase:RU365011};
GN ORFNames=Z517_04916 {ECO:0000313|EMBL:KIW81890.1};
OS Fonsecaea pedrosoi CBS 271.37.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Fonsecaea.
OX NCBI_TaxID=1442368 {ECO:0000313|EMBL:KIW81890.1, ECO:0000313|Proteomes:UP000053029};
RN [1] {ECO:0000313|EMBL:KIW81890.1, ECO:0000313|Proteomes:UP000053029}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 271.37 {ECO:0000313|EMBL:KIW81890.1,
RC ECO:0000313|Proteomes:UP000053029};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Fonsecaea pedrosoi CBS 271.37.";
RL Submitted (JAN-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|RuleBase:RU365011}.
CC -!- SIMILARITY: Belongs to the GPI inositol-deacylase family.
CC {ECO:0000256|RuleBase:RU365011}.
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DR EMBL; KN846971; KIW81890.1; -; Genomic_DNA.
DR RefSeq; XP_013285698.1; XM_013430244.1.
DR AlphaFoldDB; A0A0D2GTL2; -.
DR GeneID; 25304406; -.
DR VEuPathDB; FungiDB:Z517_04916; -.
DR HOGENOM; CLU_001384_1_0_1; -.
DR OrthoDB; 2331935at2759; -.
DR Proteomes; UP000053029; 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 Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 2.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR012908; PGAP1-like.
DR InterPro; IPR011047; Quinoprotein_ADH-like_supfam.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_rpt.
DR PANTHER; PTHR10039; AMELOGENIN; 1.
DR PANTHER; PTHR10039:SF14; NACHT AND TPR DOMAIN PROTEIN (AFU_ORTHOLOGUE AFUA_7G06670); 1.
DR Pfam; PF07819; PGAP1; 1.
DR SMART; SM00320; WD40; 3.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF50998; Quinoprotein alcohol dehydrogenase-like; 1.
DR SUPFAM; SSF50960; TolB, C-terminal domain; 1.
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:UP000053029};
KW Transport {ECO:0000256|RuleBase:RU365011}.
SQ SEQUENCE 1635 AA; 183859 MW; C4FD3B924B405B90 CRC64;
MCGRRAEDVP STLVLTDLTI FLKSSRTSHR KINEFAASLI LPQGKQPSES PSVPSTIDYD
EAVDEKGPLG LNLLYTPSEP LVDLIFVHGL GGGSRKTWSL GPSIAQNYWP KEWLSKDPAF
KNVRIHSFGY NSDYVKHRDD CWTIHSFGQS LLADLRTSPY ISSTDTQLIM MGHSMGGLVI
KRAYMLAKHD KSLDSLTSRF RAIYFLATPH QGSDWAKILD RMLHALSLSP TFVEELKKAS
GTLQSINEEF RHYFDGFQLF SFYEMQPMKY LRSRVVEPES AVLNLPGEIQ TPMAADHRSI
CKFKSKTDGN YTKLRNSLAM TVASILGELA KRNKAQQKHE LDDLSQHLRI PHQPEDDLEL
AQGSQLPGTC EWIARKESYL AWRDLSANTP PILWISGKPA TGKSVLAGYI ITQLQQQKSN
SSYYFFRHGE NSKTRLINCL KSLAFQMACN NEHTRRILSD LYKENTYIDG DNERTLWRKI
FVSTIFRSHN EPHYWIIDGL DECEAPEVFI EALLSQLDSA TKLRVLLTAR DMPKIKAAFL
SLGSHRFCEL PISTPDTLQD IQLVIEAKSH SLMVKNDEFR AALLGRVLEK SQGSFLWTLL
VLEELANTYG EAELNKVLDD VPRDMNSLYR RVLDSMELTT VGSGKRVAKA ILTWVACAMR
PLSTKELTDA LNLDLGDKYD ALEEIIPKLC GQLVAIDKFN NVQIIHETVR EYLTKDGLQS
DFAVTKPQAH KRIAVTCLSY LTSDRMRPSR TRRRASRRRS GTTIEDSNIQ FSTYACAAFA
YHLANADCES LDVLVLVSRF LEANVISWID SIAQTGVLTP IIRAAKDLRM YAKQCNAPPI
SKEIQMIKAA SMDLVRVVAK FSDVLVNNPG AIYTHIPPFC PRNSTLYKAC QRCRTTTLSI
SGMSYDQWDD RLTSIELQGD DFTSIAYGDE LFAVGTASGL VNLYHATSCE EQRALDHGEA
VRLLHFKPKS DILVSCGLKN VTVWNSRTGD ALHRLSAPFR PIALEFDKDV LLVASRRNFL
TSWDLNNNAL PQADRPWSHS DEETEQPSPL QPCAISFSIG HQKMAVAYIG QPVTIWDLQY
DEYYGSCGRI LANGEVSKHL VTSLSFNPNP DIRLLAVSYL DGQLALLDPF EEQEVECFRA
NCRALTSSPN GRLLGGVAAC ETINLYEFDT LRLLYRIRSS EQGIKQIIFS RDNFHFADVR
RSQCNIWEPT MLLRDTVAEN LSESTSTSVI EATTSDDKVR ISTMVLHSQD QVVICGKDDG
SVCLYDARTG AFLQQIHEHK SPIRTLTWQT RDNITTSVDA SNGVLASTLM RDHKGGWISN
ELPLQLRLDC GHAIVQVLRS ETTSNLILST RESDYLWDSN GKQIAARSYL EKPGIRLWIQ
HPQSQRHVIC IEGEDARIFC WCHLSEVSRL QLGVDTTNVQ LKSVRGYDSG QRRWMLLELS
ELNGSARTRS IYVFDATPFN LEDGTCLGDR LEREKAGIHG LVDMEVPAAL TSECESSLSE
PSIGEPMLQT YQQHVLKPLI GRQILALTPH VFHVIHLTDT GKLIFLDTNS WVSSIDLDNL
DRSVATAAAV STPWPPSPPI QYSRHFFVPH DWFSGTRDIV CATTARDVLF ARNGEVAVIK
NGLDYEEEVT VRVSS
//
