ID A0A0L6UZ00_9BASI Unreviewed; 392 AA.
AC A0A0L6UZ00;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=N-acetylglucosaminylphosphatidylinositol deacetylase {ECO:0000256|ARBA:ARBA00012176};
DE EC=3.5.1.89 {ECO:0000256|ARBA:ARBA00012176};
GN ORFNames=VP01_3136g2 {ECO:0000313|EMBL:KNZ53781.1};
OS Puccinia sorghi.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Pucciniomycetes; Pucciniales; Pucciniaceae; Puccinia.
OX NCBI_TaxID=27349 {ECO:0000313|EMBL:KNZ53781.1, ECO:0000313|Proteomes:UP000037035};
RN [1] {ECO:0000313|EMBL:KNZ53781.1, ECO:0000313|Proteomes:UP000037035}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RO10H11247 {ECO:0000313|EMBL:KNZ53781.1,
RC ECO:0000313|Proteomes:UP000037035};
RA Rochi L., Burguener G., Darino M., Turjanski A., Kreff E., Dieguez M.J.,
RA Sacco F.;
RT "Next Generation Sequencing and Analysis of the Genome of Puccinia sorghi L
RT Schw, the Causal Agent of Maize Common Rust.";
RL Submitted (AUG-2015) to the EMBL/GenBank/DDBJ databases.
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:KNZ53781.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LAVV01008098; KNZ53781.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0L6UZ00; -.
DR STRING; 27349.A0A0L6UZ00; -.
DR VEuPathDB; FungiDB:VP01_3136g2; -.
DR OrthoDB; 276931at2759; -.
DR UniPathway; UPA00196; -.
DR Proteomes; UP000037035; 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 GO; GO:0006506; P:GPI anchor biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.40.50.10320; LmbE-like; 1.
DR InterPro; IPR003737; GlcNAc_PI_deacetylase-related.
DR InterPro; IPR024078; LmbE-like_dom_sf.
DR PANTHER; PTHR12993:SF11; N-ACETYLGLUCOSAMINYL-PHOSPHATIDYLINOSITOL DE-N-ACETYLASE; 1.
DR PANTHER; PTHR12993; N-ACETYLGLUCOSAMINYL-PHOSPHATIDYLINOSITOL DE-N-ACETYLASE-RELATED; 1.
DR Pfam; PF02585; PIG-L; 1.
DR SUPFAM; SSF102588; LmbE-like; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000037035};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 99..119
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 1..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 392 AA; 44805 MW; CDA7BFEDA83CF9E7 CRC64;
MASSSRSNDR TSEDSILPIS PLLEPSYHNH PSSDNQIREY DYGDREDVLA DAEELDSTNL
HYPPSSKRSN NKYQNRKPTR TILNAISLGL RKHRTKIRLL IIFLITWPLL CWTGIFLLFS
DHPALFPDSL KSSKSTLFVV AHPDDECLFF APSIVATVKR AKSHGALLVM SSGNHYGQGA
LRRKELLRSC KELGIREERC DVLDISQIQD DPKSWWPVDR VGKVVNERIE KWMIDSIVTF
DDYGVSGHIN HRAVSASVTE LAISIYQKSL SPESSKAPPK LFIVRSVFVL RKYLGLFDLP
LSFIRFVPSI ILGPSRQVNS PLKSLKYEAK TEQSTRTSEF ERTAVSKHFE KGLLVSGWSG
YRTARRAFWS HQSQMVWDRH LYMILSQFIT KH
//
