ID A0A0A2KMP2_PENIT Unreviewed; 1584 AA.
AC A0A0A2KMP2;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 08-NOV-2023, entry version 31.
DE RecName: Full=GPI inositol-deacylase {ECO:0000256|ARBA:ARBA00015856, ECO:0000256|RuleBase:RU365011};
DE EC=3.1.-.- {ECO:0000256|RuleBase:RU365011};
GN ORFNames=PITC_038700 {ECO:0000313|EMBL:KGO68203.1};
OS Penicillium italicum (Blue mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=40296 {ECO:0000313|EMBL:KGO68203.1, ECO:0000313|Proteomes:UP000030104};
RN [1] {ECO:0000313|EMBL:KGO68203.1, ECO:0000313|Proteomes:UP000030104}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PHI-1 {ECO:0000313|EMBL:KGO68203.1,
RC ECO:0000313|Proteomes:UP000030104};
RX PubMed=25338147; DOI=10.1094/MPMI-09-14-0261-FI;
RA Ballester A.R., Marcet-Houben M., Levin E., Sela N., Selma-Lazaro C.,
RA Carmona L., Wisniewski M., Droby S., Gonzalez-Candelas L., Gabaldon T.;
RT "Genome, transcriptome, and functional analyses of Penicillium expansum
RT provide new insights into secondary metabolism and pathogenicity.";
RL Mol. Plant Microbe Interact. 28:232-248(2015).
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}.
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:KGO68203.1}.
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DR EMBL; JQGA01001228; KGO68203.1; -; Genomic_DNA.
DR HOGENOM; CLU_001384_1_0_1; -.
DR OMA; QCNVWEP; -.
DR OrthoDB; 2331935at2759; -.
DR PhylomeDB; A0A0A2KMP2; -.
DR Proteomes; UP000030104; 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:0017000; P:antibiotic biosynthetic process; IEA:UniProt.
DR GO; GO:0072330; P:monocarboxylic acid biosynthetic process; IEA:UniProt.
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; IPR036322; WD40_repeat_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; 7.
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|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:UP000030104};
KW Transport {ECO:0000256|RuleBase:RU365011}.
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1015..1034
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 13..30
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1584 AA; 176832 MW; FAAB46BE66EB4FB0 CRC64;
MFLRKQRRAK PNLHPDSSSS SRDSTKSSRS LFSLSKSLSQ PSTISSDQVE GVKGPLGLSL
LYSPTAPGID VIFIHGLGGS SRKTWSKSSL ESHFWPKEWL SKDPAFKNVR IHSYGYDSYY
LKGKEDCLNV HHIGKSFLGA ISTSPYIVNS GTYLIVIGHS MGGLVMKKAY ILAKQDEVHK
ALAERFTAFY FLATPHRGAD SAKTLRNLLK VAYDRAYVGD LEPNSGAIQV INDEFRHFSV
GLELWSFYET QNMKLFSSLI VDPESAVLGY REEKQIPMTA DHRSICKFDT PEDPNYALLR
NALASTVSKI ATTIAELDMK QRHERIKSLK KYLEVSDVLD DDFANVCEAR LHGSCRWILT
KASYVKWREG ESGNERTLWV KGKPATGKSV LAGYVIDQLK KSGQACSYFF FKHGDKSKSN
LDRCLRSLAF QMASSNAEAS DAILGMQADG VCLDRVEGRT LWRILFLSGI FQATLSRHYW
VIDALDECSN PAVLLHAALS KMDESIPLRI LITSRNTVDL DQGFSDIPSN LVQSLPISIK
DTEPDLRLLV ERRTQDFGIV GPDDRGTLAE KILDKSKGSF LWTLLVLEEL VRCHSRKEIH
RILENVPRGM ESLYKRTLDY MSQAARGKEL AKTILIWVAC AIRPMTIREL GGALSLDIHD
SFPKLEESIA ALCGQLVVVD KYGRVNMVHE TAREFLVAGT FESEFTIERS KAHTRMAQVC
LNYLIGEEMK PPRNSRRRFS ANFPAARLDF AAYAYTAYSY HLARADPLVA GTFQLVMQFL
SSNVLTWIET IAESRNLNHL IGASKHLKTY VNACAVERSP LDPRIKALRQ WTTDLARIPA
MFANALAVSP SSIYSLIPPF CPIDSMLYNT RIPGRRLAVL GVSNKQWNDR LLCIDFRQGQ
PRVLCYGDEF LAVGLSSGDV VLYNATSYQE YKVLEHGEAV KFVAFKAKTD LLATCGMKLA
KVWDFRSGQL VHSLASPPRP LGIEFYGDMF LIASSNNYIA TWDLGHNARP ESVRRPWCDT
DTPETNRTPP RGTPCAFTLS TNQRLLAVAY SGRPITLWDM EEDDYAGSCG KKNSSGETST
HVVVVALAFN PNPGISLLAV AYLDGDLALL DPFADQQLEC FRANCQTLAP SPNGRLLAAG
GANGIIQVYE FDTLKLLYQV KSFNSYIKQL AFTRDSMILA DIRGAQCTVW EPEALLRESI
SDESSGATIT TEVETVSMEA KAKITAMAVH HMSDVIFCGK DDGSVVLYER KTATSLGTLY
SHRSPVRLLV WIEQRDALLS VDASNRIFAH RIHKSADNGW LSDLTVLFKS HLDSDKAIIN
LLVGEIAGKF LVSTRESDHL FNLDSGKFER ERTYPQMPEI RKWLSHPESS LHLVCVDNVK
VCAYCWSDWS EVSSIALSLC NNTAEIKSAI FYSLGQKQRI ALDLLYPNSS VNINGVAIID
ADCLSVGKND NSLLLGKPLD QHAADEDDEN MVTTSGPVTP FYSWLTAFEL SVAHVIGIDE
SKKLVFLNRS FWVCSVRLSE LEIAQRKDPP AIEIFEHFFV PYDWFAGRRD IVCALAKRDI
MLTRGGDLAV IRGGLDYSER VSIR
//
