ID   B3LT85_YEAS1            Unreviewed;       508 AA.
AC   B3LT85;
DT   02-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   02-SEP-2008, sequence version 1.
DT   27-MAR-2024, entry version 64.
DE   SubName: Full=Aspartic proteinase yapsin-3 {ECO:0000313|EMBL:EDV09420.1};
GN   ORFNames=SCRG_05103 {ECO:0000313|EMBL:EDV09420.1};
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:EDV09420.1, 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}.
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; CH408054; EDV09420.1; -; Genomic_DNA.
DR   AlphaFoldDB; B3LT85; -.
DR   MEROPS; A01.035; -.
DR   HOGENOM; CLU_013253_9_1_1; -.
DR   Proteomes; UP000008335; Unassembled WGS sequence.
DR   GO; GO:0071944; C:cell periphery; IEA:UniProt.
DR   GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd05474; SAP_like; 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; IPR033876; SAP-like.
DR   PANTHER; PTHR47966; BETA-SITE APP-CLEAVING ENZYME, ISOFORM A-RELATED; 1.
DR   PANTHER; PTHR47966:SF81; PEPTIDASE A1 DOMAIN-CONTAINING PROTEIN; 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..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..508
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002789468"
FT   DOMAIN          63..394
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000259|PROSITE:PS51767"
FT   REGION          448..480
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        81
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT   ACT_SITE        288
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT   DISULFID        323..357
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
SQ   SEQUENCE   508 AA;  54551 MW;  195C3B242AAD3135 CRC64;
     MKLQLAAVAT LAVLTSPAFG RVLPDGKYVK IPFTKKKNGD NGELSKRSNG HEKFVLANEQ
     SFYSVELAIG TPSQNLTVLL DTGSADLWVP GKGNPYCGSV MDCDQYGVFD KTKSSTFKAN
     KSSPFYAAYG DGTYAEGAFG QDKLKYNELD LSGLSFAVAN ESNSTFGVLG IGLSTLEVTY
     SGKVAIMDKR SYEYDNFPLF LKHSGAIDAT AYSLFLNDES QSSGSILFGA VDHSKYEGQL
     YTIPLVNLYK SQGYQHPVAF DVTLQGLGLQ TDKRNITLTT TKLPALLDSG TTLTYLPSQA
     VALLAKSLNA SYSKTLGYYE YTCPSSDNKT SVAFDFGGFR INAPLSDFTM QTSVGTCVLA
     IIPQAGNATA ILGDSFLRNA YVVYHLDNYE ISLAQAKYGT GKENVEVIKS TVPSAIRAPS
     YNNTWSNYAS ATSGGNIFTT VRTFNGTSTA TTTRSSTTKK TSSTTTAKST HKSKRALQRA
     ATNSASSIRS TLGLLLVPSL LILSVFFS
//