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Database: UniProt
Entry: A0A484FL94_COLOR
LinkDB: A0A484FL94_COLOR
Original site: A0A484FL94_COLOR 
ID   A0A484FL94_COLOR        Unreviewed;       921 AA.
AC   A0A484FL94;
DT   05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT   05-JUN-2019, sequence version 1.
DT   08-NOV-2023, entry version 16.
DE   RecName: Full=N-acetylglucosaminylphosphatidylinositol deacetylase {ECO:0000256|ARBA:ARBA00012176};
DE            EC=3.5.1.89 {ECO:0000256|ARBA:ARBA00012176};
GN   Name=VPS62 {ECO:0000313|EMBL:TDZ18812.1};
GN   ORFNames=Cob_v008178 {ECO:0000313|EMBL:TDZ18812.1};
OS   Colletotrichum orbiculare (strain 104-T / ATCC 96160 / CBS 514.97 / LARS
OS   414 / MAFF 240422) (Cucumber anthracnose fungus) (Colletotrichum
OS   lagenarium).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC   Colletotrichum orbiculare species complex.
OX   NCBI_TaxID=1213857 {ECO:0000313|EMBL:TDZ18812.1, ECO:0000313|Proteomes:UP000014480};
RN   [1] {ECO:0000313|Proteomes:UP000014480}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=104-T / ATCC 96160 / CBS 514.97 / LARS 414 / MAFF 240422
RC   {ECO:0000313|Proteomes:UP000014480};
RX   PubMed=23252678; DOI=10.1111/nph.12085;
RA   Gan P., Ikeda K., Irieda H., Narusaka M., O'Connell R.J., Narusaka Y.,
RA   Takano Y., Kubo Y., Shirasu K.;
RT   "Comparative genomic and transcriptomic analyses reveal the hemibiotrophic
RT   stage shift of Colletotrichum fungi.";
RL   New Phytol. 197:1236-1249(2013).
RN   [2] {ECO:0000313|Proteomes:UP000014480}
RP   GENOME REANNOTATION.
RC   STRAIN=104-T / ATCC 96160 / CBS 514.97 / LARS 414 / MAFF 240422
RC   {ECO:0000313|Proteomes:UP000014480};
RX   PubMed=30893003; DOI=10.1094/MPMI-12-18-0352-A;
RA   Gan P., Tsushima A., Narusaka M., Narusaka Y., Takano Y., Kubo Y.,
RA   Shirasu K.;
RT   "Genome sequence resources for four phytopathogenic fungi from the
RT   Colletotrichum orbiculare species complex.";
RL   Mol. Plant Microbe Interact. 32:1088-1090(2019).
CC   -!- FUNCTION: Involved in the second step of GPI biosynthesis. De-N-
CC       acetylation of N-acetylglucosaminyl-phosphatidylinositol.
CC       {ECO:0000256|ARBA:ARBA00024639}.
CC   -!- SIMILARITY: Belongs to the PIGL family.
CC       {ECO:0000256|ARBA:ARBA00006066}.
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:TDZ18812.1}.
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DR   EMBL; AMCV02000022; TDZ18812.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A484FL94; -.
DR   STRING; 1213857.A0A484FL94; -.
DR   UniPathway; UPA00196; -.
DR   Proteomes; UP000014480; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0000225; F:N-acetylglucosaminylphosphatidylinositol deacetylase activity; IEA:UniProtKB-EC.
DR   Gene3D; 3.40.50.10320; LmbE-like; 1.
DR   InterPro; IPR003737; GlcNAc_PI_deacetylase-related.
DR   InterPro; IPR024078; LmbE-like_dom_sf.
DR   InterPro; IPR009291; Vps62.
DR   PANTHER; PTHR48172; -; 1.
DR   PANTHER; PTHR48172:SF2; BNAC05G02270D PROTEIN; 1.
DR   Pfam; PF02585; PIG-L; 1.
DR   Pfam; PF06101; Vps62; 1.
DR   SUPFAM; SSF102588; LmbE-like; 1.
PE   3: Inferred from homology;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000014480};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        214..237
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        402..421
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   REGION          320..347
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          601..641
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          825..850
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        322..339
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   921 AA;  104255 MW;  CC75C8C22B02AC54 CRC64;
     MSPKPARNVF RNLYPWCRAL RIRRRLLVRF AVVAVLVLAV LQWALAYPLG GDARLLPQEL
     QDAKNVLIVT AHPDDECLFF APSILGVLDR DHHVKGGLLV MSRGNNKGIG DLRQQELKGS
     CDALRIDPSR CEALDHPDLQ DNPKVWWDTA KIQPILKKYV QKWKIDAIIT FDEYGVSGHI
     NHRAVSAAVS EYVNSDSDAP MAYKLVTTAL IRKYTFLFDL PFTAAAFGWR IVAAIFYPAS
     KMDPSYSTKA LVVNTWGRYL KTRDAFASHD SQYSWDRHLY MILSRYTWFT VAADPGATVP
     PPAIPERGGW MACERKRAGL TGPLTSSRTP RTDTHSPRPE QAPQPFLDSL KVSGAPEMNL
     RGYRDAAHRH MLSASDYCAS LRRFLPNVSK PTASRTLRSI RWFLRVVFLP IFLVLCSLWF
     LTSLLPRILN PTPPDEAKQR WNEEWISSSP YWLDRQACRW VSLCGVHHVK WDSPTLGQKP
     VTGAARDGPL RLELRSLGGI DGMPDGWKDT FAESISQGCK SEGRNATKAI PDYVWEYAPL
     VYLHSEENFW PADIAEHVRH MNPHLDGEPL NQSVSLSDLH SLDERRGSVF LTSKDDVESR
     PEWLHSHVGI PEPWEQEEGN DATGSPPKKE SSQADDSEQR PLYRISDPRR FRWLPSSART
     PADKVIRRQL DELITSRSES QTGRGGRSAA PATLVIVEKE DGIVDAFWFF FYAYNLGQTV
     LGMRFGNHVG DWEHSVVRFQ HGKPRAVFLS EHAAGQVYTY EALEKRGVRP VLYSAVGSHA
     MYPNPGNHPY VLPFNMLKDV TDRGYLWDPA KNTYSYWYDA KKETDVPSTT GNRTCSGSPD
     GFTPSAENPD APTSWLSFTG AWGDNIYPLA DARQWRLFNQ YHYDEGPYGP KLKNLERGAL
     CLRGDRCKIL EAITPGQKWY D
//
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