ID   C5DY50_ZYGRC            Unreviewed;       572 AA.
AC   C5DY50;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   24-JAN-2024, entry version 78.
DE   SubName: Full=ZYRO0F10274p {ECO:0000313|EMBL:CAR28711.1};
GN   OrderedLocusNames=ZYRO0F10274g {ECO:0000313|EMBL:CAR28711.1};
OS   Zygosaccharomyces rouxii (strain ATCC 2623 / CBS 732 / NBRC 1130 / NCYC 568
OS   / NRRL Y-229) (Candida mogii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Zygosaccharomyces.
OX   NCBI_TaxID=559307 {ECO:0000313|EMBL:CAR28711.1, ECO:0000313|Proteomes:UP000008536};
RN   [1] {ECO:0000313|Proteomes:UP000008536}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 2623 / CBS 732 / BCRC 21506 / NBRC 1130 / NCYC 568 / NRRL
RC   Y-229 {ECO:0000313|Proteomes:UP000008536};
RX   PubMed=19525356; DOI=10.1101/gr.091546.109;
RG   The Genolevures Consortium;
RA   Souciet J.-L., Dujon B., Gaillardin C., Johnston M., Baret P.V.,
RA   Cliften P., Sherman D.J., Weissenbach J., Westhof E., Wincker P., Jubin C.,
RA   Poulain J., Barbe V., Segurens B., Artiguenave F., Anthouard V.,
RA   Vacherie B., Val M.-E., Fulton R.S., Minx P., Wilson R., Durrens P.,
RA   Jean G., Marck C., Martin T., Nikolski M., Rolland T., Seret M.-L.,
RA   Casaregola S., Despons L., Fairhead C., Fischer G., Lafontaine I., Leh V.,
RA   Lemaire M., de Montigny J., Neuveglise C., Thierry A., Blanc-Lenfle I.,
RA   Bleykasten C., Diffels J., Fritsch E., Frangeul L., Goeffon A.,
RA   Jauniaux N., Kachouri-Lafond R., Payen C., Potier S., Pribylova L.,
RA   Ozanne C., Richard G.-F., Sacerdot C., Straub M.-L., Talla E.;
RT   "Comparative genomics of protoploid Saccharomycetaceae.";
RL   Genome Res. 19:1696-1709(2009).
CC   -!- SIMILARITY: Belongs to the peptidase A1 family.
CC       {ECO:0000256|ARBA:ARBA00007447, ECO:0000256|RuleBase:RU000454}.
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DR   EMBL; CU928178; CAR28711.1; -; Genomic_DNA.
DR   RefSeq; XP_002497644.1; XM_002497599.1.
DR   AlphaFoldDB; C5DY50; -.
DR   MEROPS; A01.030; -.
DR   GeneID; 8205409; -.
DR   KEGG; zro:ZYRO0F10274g; -.
DR   HOGENOM; CLU_013253_9_1_1; -.
DR   InParanoid; C5DY50; -.
DR   Proteomes; UP000008536; Chromosome F.
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:SF65; ASPARTIC-TYPE ENDOPEPTIDASE; 1.
DR   PANTHER; PTHR47966; BETA-SITE APP-CLEAVING ENZYME, ISOFORM A-RELATED; 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}; Hydrolase {ECO:0000256|RuleBase:RU000454};
KW   Protease {ECO:0000256|RuleBase:RU000454};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008536};
KW   Signal {ECO:0000256|ARBA:ARBA00022729}.
FT   DOMAIN          71..471
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000259|PROSITE:PS51767"
FT   REGION          513..543
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        528..543
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        89
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT   ACT_SITE        363
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
SQ   SEQUENCE   572 AA;  61086 MW;  4B59B88FA9CECC23 CRC64;
     MRFTDAVVSL LSVASTCKSA LIEQTSSPMV KLSFNKWHGP TYEESSLERR SLETRNNKEF
     NFIVENQQNF YSVDLLVGTP GQNITVLLDT GSSDLWLTAK NNPYCKSNAG SNDKKEDYRL
     EDGDNQSIVS MLTASGTGTN PIGGSGIPTA ISGSAQLTGT YTSGTGTGPS GSSPEPTMDC
     SQYGTFDVNK SKSFRSNKTE FYISYGDGSF ASGYWGTDSV NFANMNLEGV SFAVANETNS
     TVGVFGIGLP ENEATYTPDP SLNDFHPYEY QNFPQVLKSK GAINKAAYSL FLNSLDASSG
     DILFGAVDRS KYKGDLYTLP LLNSDPTKYK NPMEFDVTLQ GVGFTNGSSK TTFTTTKIPA
     LLDSGTSLIY LPDALAKGIA HKLGGSYNED IGYYVIGCPS ENDDSQLVFD FGGFTIKNNL
     SNYLLGSPDD GDDSQCVLGI LPSDVQAILG DVFLADAYVV YDLDDYEVSL AQASFDNSKE
     DIQIISDSIP GAKRAPGYSK TWSTPASIKS GGNIFTSSNK KTERDHTAAT ATPVSGSASS
     TSGAQISSQD VANGFSPSML ALLNAFILSF VI
//