ID W6R8V7_PENRF Unreviewed; 398 AA.
AC W6R8V7;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE SubName: Full=GPI-anchor transamidase {ECO:0000313|EMBL:CDM38247.1};
GN Name=PIGK {ECO:0000313|EMBL:CDM38247.1};
GN ORFNames=PROQFM164_S10g000061 {ECO:0000313|EMBL:CDM38247.1};
OS Penicillium roqueforti (strain FM164).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=1365484 {ECO:0000313|EMBL:CDM38247.1};
RN [1] {ECO:0000313|EMBL:CDM38247.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FM164 {ECO:0000313|EMBL:CDM38247.1};
RX PubMed=24407037; DOI=10.1038/ncomms3876;
RA Cheeseman K., Ropars J., Renault P., Dupont J., Gouzy J., Branca A.,
RA Abraham A.L., Ceppi M., Conseiller E., Debuchy R., Malagnac F., Goarin A.,
RA Silar P., Lacoste S., Sallet E., Bensimon A., Giraud T., Brygoo Y.;
RT "Multiple recent horizontal transfers of a large genomic region in cheese
RT making fungi.";
RL Nat. Commun. 5:2876-2876(2014).
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; HG792024; CDM38247.1; -; Genomic_DNA.
DR AlphaFoldDB; W6R8V7; -.
DR STRING; 1365484.W6R8V7; -.
DR OMA; PGHTNNW; -.
DR OrthoDB; 1122658at2759; -.
DR UniPathway; UPA00196; -.
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}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..398
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5027918476"
FT ACT_SITE 146
FT /evidence="ECO:0000256|PIRSR:PIRSR019663-1"
FT ACT_SITE 188
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR019663-1"
SQ SEQUENCE 398 AA; 44592 MW; 24B0AA91CCCA58FA CRC64;
MALLFRFLQA FALLLLASAV VAEHTSNWAV LVSTSRFWFN YRHLANVLSL YRTVKRLGIP
DSQIILMLPD DMACNPRNAF PGTVYSNADR AVDLYGDNIE VDYRGYEVTV ENFIRLLTDR
LDEDVPRSKR LGSDAGSNVL VYMTGHGGDQ FLKFQDAEEI GAWDLADAFG QMWEKKRYHE
LLFMIDTCQA NTMYTHFYSP NIVATGSSEI DQSSYSHHAD NDVGVAVIDR WTYYVLEFLE
TQVTSVTSKL NLGDLFDSYD ESKIHSQPGV RWDLFPGGEQ EGRLRTVVDF FGNVQNVEVE
NANATEPGSL KEDLAEIARL VEKWQNRDEE YSAMLADSAT NVTEDLHSSS LHLKLKSTVG
PTKMAEDSSW GKRLVGISVV GACTAIWVAG SFLGRSSV
//
