ID B8M382_TALSN Unreviewed; 424 AA.
AC B8M382;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE SubName: Full=GPI anchor transamidase, putative {ECO:0000313|EMBL:EED22254.1};
GN ORFNames=TSTA_095000 {ECO:0000313|EMBL:EED22254.1};
OS Talaromyces stipitatus (strain ATCC 10500 / CBS 375.48 / QM 6759 / NRRL
OS 1006) (Penicillium stipitatum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC Talaromyces sect. Talaromyces.
OX NCBI_TaxID=441959 {ECO:0000313|EMBL:EED22254.1, ECO:0000313|Proteomes:UP000001745};
RN [1] {ECO:0000313|Proteomes:UP000001745}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10500 / CBS 375.48 / QM 6759 / NRRL 1006
RC {ECO:0000313|Proteomes:UP000001745};
RX PubMed=25676766; DOI=10.1128/genomea.01559-14;
RA Nierman W.C., Fedorova-Abrams N.D., Andrianopoulos A.;
RT "Genome sequence of the AIDS-associated pathogen Penicillium marneffei
RT (ATCC18224) and its near taxonomic relative Talaromyces stipitatus
RT (ATCC10500).";
RL Genome Announc. 3:E0155914-E0155914(2015).
CC -!- PATHWAY: Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor
CC biosynthesis. {ECO:0000256|ARBA:ARBA00004687}.
CC -!- SIMILARITY: Belongs to the peptidase C13 family.
CC {ECO:0000256|ARBA:ARBA00009941}.
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DR EMBL; EQ962653; EED22254.1; -; Genomic_DNA.
DR RefSeq; XP_002479217.1; XM_002479172.1.
DR AlphaFoldDB; B8M382; -.
DR STRING; 441959.B8M382; -.
DR MEROPS; C13.005; -.
DR GeneID; 8103830; -.
DR VEuPathDB; FungiDB:TSTA_095000; -.
DR eggNOG; KOG1349; Eukaryota.
DR HOGENOM; CLU_044656_2_2_1; -.
DR InParanoid; B8M382; -.
DR OrthoDB; 1122658at2759; -.
DR PhylomeDB; B8M382; -.
DR UniPathway; UPA00196; -.
DR Proteomes; UP000001745; Unassembled WGS sequence.
DR GO; GO:0042765; C:GPI-anchor transamidase complex; IEA:InterPro.
DR GO; GO:0003923; F:GPI-anchor transamidase activity; IEA:InterPro.
DR GO; GO:0016255; P:attachment of GPI anchor to protein; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.1460; -; 1.
DR InterPro; IPR028361; GPI_transamidase.
DR InterPro; IPR001096; Peptidase_C13.
DR PANTHER; PTHR48067; GPI-ANCHOR TRANSAMIDASE; 1.
DR PANTHER; PTHR48067:SF1; GPI-ANCHOR TRANSAMIDASE; 1.
DR Pfam; PF01650; Peptidase_C13; 1.
DR PIRSF; PIRSF500138; GPI8; 1.
DR PIRSF; PIRSF019663; Legumain; 1.
DR PRINTS; PR00776; HEMOGLOBNASE.
PE 3: Inferred from homology;
KW GPI-anchor biosynthesis {ECO:0000256|ARBA:ARBA00022502};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000001745}.
FT REGION 360..380
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 360..377
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 165
FT /evidence="ECO:0000256|PIRSR:PIRSR019663-1"
FT ACT_SITE 207
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR019663-1"
SQ SEQUENCE 424 AA; 47288 MW; 3B77EE5174C37E32 CRC64;
MSSEIGIVDS PSDPPGRFST SVRAGLATLL LSCTIPVSVF GEHTSNWAVL VSTSRFWFNY
RHLANVLSLY RTVKRLGIPD SQIILMLPDD MACNPRNAFP GTVYSNADRA VDLYGENIEV
DYRGYEVTVE NFIRLLTDRL DEDVPRSKRL GSDAGSNVLV YMTGHGGDRF LKFQDSEEIG
AWDLADAFGQ MWEKKRYHEL LFMIDTCQAN TMYTHFYSPN IIATGSSALD ESSYSHHADN
DVGVAVIDRW TYYVLEFLET QVTSPNSKLT LGDLFDSYDE SKIHSQPGLR WDLFPGGEQE
GRLRTVVDFF GNTQAVQVES NATRGPGSLK EDLDEIAKLV EKWQRREQGY PFLQNRTIAS
DEKQKQSEPS STAAAAATDR HRQVVVGASK MTDEDSWTKR LVGLAVIGAG TGLWLAGSVF
GRET
//
