ID A0A178DJ88_9PLEO Unreviewed; 1578 AA.
AC A0A178DJ88;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, 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=IQ07DRAFT_650359 {ECO:0000313|EMBL:OAL43081.1};
OS Pyrenochaeta sp. DS3sAY3a.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Cucurbitariaceae;
OC Pyrenochaeta.
OX NCBI_TaxID=765867 {ECO:0000313|EMBL:OAL43081.1, ECO:0000313|Proteomes:UP000077535};
RN [1] {ECO:0000313|EMBL:OAL43081.1, ECO:0000313|Proteomes:UP000077535}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DS3sAY3a {ECO:0000313|EMBL:OAL43081.1,
RC ECO:0000313|Proteomes:UP000077535};
RG DOE Joint Genome Institute;
RA Zeiner C.A., Purvine S.O., Zink E.M., Wu S., Pasa-Tolic L., Chaput D.L.,
RA Haridas S., Grigoriev I.V., Santelli C.M., Hansel C.M.;
RT "Comparative analysis of secretome profiles of manganese(II)-oxidizing
RT ascomycete fungi.";
RL Submitted (MAY-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|RuleBase:RU365011}. Mitochondrion
CC {ECO:0000256|ARBA:ARBA00004173}.
CC -!- SIMILARITY: Belongs to the GPI inositol-deacylase family.
CC {ECO:0000256|RuleBase:RU365011}.
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DR EMBL; KV441670; OAL43081.1; -; Genomic_DNA.
DR InParanoid; A0A178DJ88; -.
DR OrthoDB; 2331935at2759; -.
DR Proteomes; UP000077535; Unassembled WGS sequence.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0016788; F:hydrolase activity, acting on ester bonds; IEA:InterPro.
DR GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 2.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR024977; Apc4-like_WD40_dom.
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; IPR036322; WD40_repeat_dom_sf.
DR PANTHER; PTHR48182; PROTEIN SERAC1; 1.
DR PANTHER; PTHR48182:SF2; PROTEIN SERAC1; 1.
DR Pfam; PF12894; ANAPC4_WD40; 1.
DR Pfam; PF07819; PGAP1; 1.
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; SSF50978; WD40 repeat-like; 1.
PE 3: Inferred from homology;
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824,
KW ECO:0000256|RuleBase:RU365011}; Hydrolase {ECO:0000256|RuleBase:RU365011};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU365011};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW Protein transport {ECO:0000256|RuleBase:RU365011};
KW Reference proteome {ECO:0000313|Proteomes:UP000077535};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989};
KW Transport {ECO:0000256|RuleBase:RU365011}.
FT DOMAIN 1066..1148
FT /note="Anaphase-promoting complex subunit 4-like WD40"
FT /evidence="ECO:0000259|Pfam:PF12894"
SQ SEQUENCE 1578 AA; 176592 MW; B24FB4B4E1E66B35 CRC64;
MAYDLPNRQR LKSAYAETFT SSLSESPTLS PSENTATFEL PADVRKGTSF LNRTFRSARP
QANVKGETTG PLGLRSLFCA PESLVDIIFV HGLRGGSIKT WRFGEDEHLF WPRYWLPKEP
EFAHASIHSY GYDSDWGSTK PSILSVHDFG RSLYEELLSS PSLRHSSNNN PIILVGHSMG
GLVIKKAYIL SQDDHKHPDL ARRIRCVFFL ATPHRGSDYA AVLNNILKCF GVTGLTSSRE
YLQDITAGSV STEVINSEFA RIAKELTVYS FYETEPTITG SSGLIVDKAS AVLGLYPDNE
HIFYQHANHR EICKFRTRQD STYIKLKDAL ATAVEDLTKN VTMANDQVSK EQMRNIEDLL
RIQDIPEEYH EKLEGSCRWI EDREDFQSWI GVEHKAETAA VPRPSMYWVQ AQPGAGKTVL
ATHIMSLLNH FRLPYSSHLF HFGKKSAQSL TGLLQSLAFQ MARANEEIRN KLVEIYTTTS
SFDQDDPRAI WNKVFLGGLF QVSLSSPQFW VIDAVDECVK YPELISLLKG IQPQFPLRLF
FTSRKLPDMP RLLRLLDIEV AVVEIPIQDT LDDISLYVRT RITDLPVDEE NEREDIAQQI
LAKSGTSFLW VRLVMDELEG VYGYDSIKQV LQAIPEGMFH YYSRAIAEMS EKKREQHVVK
AILLWVMLAT RPLSISELSH ALQLDINVHL PSAKAAIEGL CGQLVSVDVH TGLVHPVHAT
AREFILSEEA GSFQVSRTRG HEQIALTCLR LLASTEFQPP RHRRLLLQKR GKPPISILAD
YAITQFSEHV VGASTESDEL LLALAKFLKT TVLTWIEKIM VAKEAYRLLR AAKNLKAYLS
RRAKYHSPLN SHVSTITAWT TDLTRVLFTF GRALEWNPAS VYFLIPPLCP TESAMFQQFG
KTVDGLMLSG YRRSEWSDCI ASISFEEETA AAVACDNKLI TVGMESGTLQ MYNSRSYQKE
GTIDIGSSVD LIHTDISGSF VAVSGHKFVG VWDNTGHMRW KVRFRHGLIL LELSQDSLIG
ISTQGRSYSW DLQSGELVHE QKYTYSNPPS DADAPHTMSK APSTASLSPG LDLIALAYRN
SPVCIFDRDS GELIAWAVDE NKRAAEQILF NPSPDVGLLL IAYNESHLAL YDSWSGQLVE
SLEAENHVIL DSVACAPDGR TFATVDVRGH LRIWDFETLT PLYHVLIPHV SFSLLHFTAA
GLGLLHVTDH ELKVWAPSAL VRKTMEEEAS LSDQSPVVPV TEGQFERFQA SKINTLVAHP
LWPMLLAGNQ NGEVLIYQSK NGYDPLTLYT HHGIVIRCLA SSRHNIIASA DLHANVQVRQ
FDASSPQSLE DKAALVEKNF NSPVTQLLFD LSGSYLLVST ISTDYVYRIE DGVCVGSQDF
STQNRTPGNW FVVTAQDYSD YFLLLADGKL TAYSIKDFSS TPKILSRFSA VFEDASIRSV
TEIPGTLCVI VETQNPKSHV VSSYWFSMPS STVSVSVTPA VLIPLELCAQ FLGISKATKR
VVFMHPASWV CSTTLKDIET GQYVEHFFVP EEYSTIIGDD TSAVHPVQTA EGDFAFCMYD
KVRVLKGGLK FQTNRVHT
//
