ID B3LKS3_YEAS1 Unreviewed; 405 AA.
AC B3LKS3;
DT 02-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 02-SEP-2008, sequence version 1.
DT 27-MAR-2024, entry version 68.
DE SubName: Full=Vacuolar proteinase A {ECO:0000313|EMBL:EDV11071.1};
GN ORFNames=SCRG_02342 {ECO:0000313|EMBL:EDV11071.1};
OS Saccharomyces cerevisiae (strain RM11-1a) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=285006 {ECO:0000313|EMBL:EDV11071.1, ECO:0000313|Proteomes:UP000008335};
RN [1] {ECO:0000313|Proteomes:UP000008335}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RM11-1a {ECO:0000313|Proteomes:UP000008335};
RG The Broad Institute Genome Sequencing Platform;
RA Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Cuomo C.,
RA Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M., Kleber M.,
RA Mauceli E.W., Brockman W., MacCallum I.A., Rounsley S., Young S.K.,
RA LaButti K., Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA O'Leary S., Kodira C.D., Zeng Q., Yandava C., Alvarado L., Pratt S.,
RA Kruglyak L.;
RT "Annotation of the Saccharomyces cerevisiae RM11-1a genome.";
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase A1 family.
CC {ECO:0000256|ARBA:ARBA00007447, ECO:0000256|RuleBase:RU000454}.
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DR EMBL; CH408046; EDV11071.1; -; Genomic_DNA.
DR AlphaFoldDB; B3LKS3; -.
DR SMR; B3LKS3; -.
DR MEROPS; A01.018; -.
DR HOGENOM; CLU_013253_3_4_1; -.
DR Proteomes; UP000008335; Unassembled WGS sequence.
DR GO; GO:0000324; C:fungal-type vacuole; IEA:InterPro.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd05488; Proteinase_A_fungi; 1.
DR Gene3D; 2.40.70.10; Acid Proteases; 2.
DR InterPro; IPR001461; Aspartic_peptidase_A1.
DR InterPro; IPR001969; Aspartic_peptidase_AS.
DR InterPro; IPR033121; PEPTIDASE_A1.
DR InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR InterPro; IPR033819; Saccharopepsin.
DR PANTHER; PTHR47966; BETA-SITE APP-CLEAVING ENZYME, ISOFORM A-RELATED; 1.
DR PANTHER; PTHR47966:SF89; SACCHAROPEPSIN; 1.
DR Pfam; PF00026; Asp; 1.
DR PRINTS; PR00792; PEPSIN.
DR SUPFAM; SSF50630; Acid proteases; 1.
DR PROSITE; PS00141; ASP_PROTEASE; 2.
DR PROSITE; PS51767; PEPTIDASE_A1; 1.
PE 3: Inferred from homology;
KW Aspartyl protease {ECO:0000256|ARBA:ARBA00022750,
KW ECO:0000256|RuleBase:RU000454};
KW Disulfide bond {ECO:0000256|PIRSR:PIRSR601461-2};
KW Hydrolase {ECO:0000256|RuleBase:RU000454};
KW Protease {ECO:0000256|RuleBase:RU000454};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..405
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002791208"
FT DOMAIN 91..402
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT ACT_SITE 109
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 294
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT DISULFID 122..127
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
FT DISULFID 328..361
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
SQ SEQUENCE 405 AA; 44499 MW; B0AA36BA098D2BF7 CRC64;
MFSLKALLPL ALLLVSANQV AAKVHKAKIY KHELSDEMKE VTFEQHLAHL GQKYLTQFEK
ANPEVVFSRE HPFFTEGGHD VPLTNYLNAQ YYTDITLGTP PQNFKVILDT GSSNLWVPSN
ECGSLACFLH SKYDHEASSS YKANGTEFAI QYGTGSLEGY ISQDTLSIGD LTIPKQDFAE
ATSEPGLTFA FGKFDGILGL GYDTISVDKV VPPFYNAIQQ DLLDEKRFAF YLGDTSKDTE
NGGEATFGGI DESKFKGDIT WLPVRRKAYW EVKFEGIGLG DEYAELESHG AAIDTGTSLI
TLPSGLAEMI NAEIGAKKGW TGQYTLDCNT RDNLPDLIFN FNGYNFTIGP YDYTLEVSGS
CISAITPMDF PEPVGPLAIV GDAFLRKYYS IYDLGNNAVG LAKAI
//
