ID C5DY49_ZYGRC Unreviewed; 551 AA.
AC C5DY49;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 24-JAN-2024, entry version 77.
DE SubName: Full=ZYRO0F10252p {ECO:0000313|EMBL:CAR28710.1};
GN OrderedLocusNames=ZYRO0F10252g {ECO:0000313|EMBL:CAR28710.1};
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:CAR28710.1, 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; CAR28710.1; -; Genomic_DNA.
DR RefSeq; XP_002497643.1; XM_002497598.1.
DR AlphaFoldDB; C5DY49; -.
DR MEROPS; A01.030; -.
DR GeneID; 8205408; -.
DR KEGG; zro:ZYRO0F10252g; -.
DR HOGENOM; CLU_013253_9_1_1; -.
DR InParanoid; C5DY49; -.
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, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..551
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002948124"
FT DOMAIN 60..418
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT REGION 97..124
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 434..523
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 440..523
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 78
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 311
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
SQ SEQUENCE 551 AA; 57351 MW; 0F4E6E864C00FA1D CRC64;
MKFLTSLVTS VLLSTASAGL VSPPVYKLSF NKLRGETFEK AVGNSNGHAN FDIKNQQNFY
SVELKVGTPA QNVLVLLDTG SSDLWITGSG NPYCSPSTRN SHLGSAGSNS STNNGPSSTA
NFPSSSATID CSQYGTFNLD GSETFKSNDS TFYLTYGDGS FAKGLWGMDH VYLDGLNVSD
VSFAVANESN STVGVFGVGL PGEEATVTPG VNGNHYQYKN FPQVLKDNGV VQKNAYSLYL
NSPDSNSGNI LFGAVDHSKY SGNLYTLPIV NTYADQGVAP REFDVTVQGI TVGNSSSNST
VSSDKTLALL DSGTTLMYLP TALADELAKS LGGKFSPSTG YYLIPKPSEN DDTKITFDFG
GFHIETKLSN YILQGSGPQD VAILGILRTE GDRAIFGDVF LVDAYVVYDL EDYEISLAQA
NFNSGSSDIE AISGSVPGAS RAPGYSQTYT GNQPSSSGSA SPGGSTGQEA SSSSSSSSSA
SNGDSESSSS SSSSSSSNSG SSGNNSESSS SSFSNSDKRG LTVSENGVGS LRAANPMILA
FVTTFITSML T
//