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Database: UniProt
Entry: C5DY49_ZYGRC
LinkDB: C5DY49_ZYGRC
Original site: C5DY49_ZYGRC 
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
//
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