ID E3L9F1_PUCGT Unreviewed; 464 AA.
AC E3L9F1;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 2.
DT 24-JAN-2024, entry version 57.
DE RecName: Full=GPI inositol-deacylase {ECO:0000256|RuleBase:RU365011};
DE EC=3.1.-.- {ECO:0000256|RuleBase:RU365011};
GN ORFNames=PGTG_19136 {ECO:0000313|EMBL:EFP93176.2};
OS Puccinia graminis f. sp. tritici (strain CRL 75-36-700-3 / race SCCL)
OS (Black stem rust fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Pucciniomycetes; Pucciniales; Pucciniaceae; Puccinia.
OX NCBI_TaxID=418459 {ECO:0000313|EMBL:EFP93176.2, ECO:0000313|Proteomes:UP000008783};
RN [1]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CRL 75-36-700-3;
RG The Broad Institute Genome Sequencing Platform;
RA Birren B., Lander E., Galagan J., Nusbaum C., Devon K., Cuomo C., Jaffe D.,
RA Butler J., Alvarez P., Gnerre S., Grabherr M., Mauceli E., Brockman W.,
RA Young S., LaButti K., Sykes S., DeCaprio D., Crawford M., Koehrsen M.,
RA Engels R., Montgomery P., Pearson M., Howarth C., Larson L., White J.,
RA Zeng Q., Kodira C., Yandava C., Alvarado L., O'Leary S., Szabo L., Dean R.,
RA Schein J.;
RT "The Genome Sequence of Puccinia graminis f. sp. tritici Strain CRL 75-36-
RT 700-3.";
RL Submitted (JAN-2007) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000008783}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CRL 75-36-700-3 / race SCCL
RC {ECO:0000313|Proteomes:UP000008783};
RX PubMed=21536894; DOI=10.1073/pnas.1019315108;
RA Duplessis S., Cuomo C.A., Lin Y.-C., Aerts A., Tisserant E.,
RA Veneault-Fourrey C., Joly D.L., Hacquard S., Amselem J., Cantarel B.L.,
RA Chiu R., Coutinho P.M., Feau N., Field M., Frey P., Gelhaye E.,
RA Goldberg J., Grabherr M.G., Kodira C.D., Kohler A., Kuees U.,
RA Lindquist E.A., Lucas S.M., Mago R., Mauceli E., Morin E., Murat C.,
RA Pangilinan J.L., Park R., Pearson M., Quesneville H., Rouhier N.,
RA Sakthikumar S., Salamov A.A., Schmutz J., Selles B., Shapiro H.,
RA Tanguay P., Tuskan G.A., Henrissat B., Van de Peer Y., Rouze P.,
RA Ellis J.G., Dodds P.N., Schein J.E., Zhong S., Hamelin R.C.,
RA Grigoriev I.V., Szabo L.J., Martin F.;
RT "Obligate biotrophy features unraveled by the genomic analysis of rust
RT fungi.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:9166-9171(2011).
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|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; DS178384; EFP93176.2; -; Genomic_DNA.
DR RefSeq; XP_003337595.2; XM_003337547.2.
DR AlphaFoldDB; E3L9F1; -.
DR STRING; 418459.E3L9F1; -.
DR EnsemblFungi; EFP93176; EFP93176; PGTG_19136.
DR GeneID; 10543326; -.
DR KEGG; pgr:PGTG_19136; -.
DR VEuPathDB; FungiDB:PGTG_19136; -.
DR eggNOG; ENOG502QQNH; Eukaryota.
DR HOGENOM; CLU_015737_1_2_1; -.
DR InParanoid; E3L9F1; -.
DR OrthoDB; 2718971at2759; -.
DR Proteomes; UP000008783; Unassembled WGS sequence.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004806; F:triglyceride lipase activity; IBA:GO_Central.
DR GO; GO:0006629; P:lipid metabolic process; IBA:GO_Central.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR012908; PGAP1-like.
DR PANTHER; PTHR11440:SF97; BCDNA.GH02384; 1.
DR PANTHER; PTHR11440; LECITHIN-CHOLESTEROL ACYLTRANSFERASE-RELATED; 1.
DR Pfam; PF07819; PGAP1; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 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:UP000008783};
KW Transport {ECO:0000256|RuleBase:RU365011}.
FT REGION 77..109
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 412..440
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 84..109
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 420..434
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 464 AA; 51603 MW; 4E192966067417D0 CRC64;
MMEQAQQAHP ILSPPLSAVL RAGTLSPGTR YAPSPTVKSL KRILEQQQKK GVLLTPLERN
IRSINYQYSL LFKNHHLHHQ HQHSPASSRS TTTVQISDSQ PPSQQQEQWA INTTTASRIK
RWFTLNWSPK SLPESSRNIT TTTATADVGA DQQNLIAADP DSFSKPKFPL VLCHGLLGFD
VLGPAALGLT YFRGVREALE ERGVEVYVAK VPACASIEER AKTLAQFIET RLPGQTVNLI
GHSMGGLDSR FMITHLRPTS FKVASLTTIG TPHRGSAFAD YLLLDILGRQ HHSKFLQISK
SLGLPGGGKA FVELTSEQMA VFNQNTPDLH GISYFSYAAV CEPSFASPFR LSWGVVYERE
GPNDGLVSVA SAQWGSYLGT LHNVNHAELV GWVEPWKTSS SKKHLANLHL DDQDQQHQKQ
KQKQQQQQQQ DLSRLMDPDK PHTHEFQVVP FYLQVVDSLA KKGF
//
