ID C5DXS3_ZYGRC Unreviewed; 418 AA.
AC C5DXS3;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 80.
DE SubName: Full=ZYRO0F07392p {ECO:0000313|EMBL:CAR28584.1};
GN OrderedLocusNames=ZYRO0F07392g {ECO:0000313|EMBL:CAR28584.1};
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:CAR28584.1, 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; CAR28584.1; -; Genomic_DNA.
DR RefSeq; XP_002497517.1; XM_002497472.1.
DR AlphaFoldDB; C5DXS3; -.
DR SMR; C5DXS3; -.
DR STRING; 559307.C5DXS3; -.
DR MEROPS; A01.018; -.
DR GeneID; 8205279; -.
DR KEGG; zro:ZYRO0F07392g; -.
DR HOGENOM; CLU_013253_3_4_1; -.
DR InParanoid; C5DXS3; -.
DR Proteomes; UP000008536; Chromosome F.
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 Reference proteome {ECO:0000313|Proteomes:UP000008536};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..418
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002948991"
FT DOMAIN 105..415
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT ACT_SITE 123
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 307
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT DISULFID 136..141
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
FT DISULFID 341..374
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
SQ SEQUENCE 418 AA; 46013 MW; 495F82921D280A5D CRC64;
MLTKNLLPLA LSLLGYVEVG ESKVHHAKIQ KNEPLNVEEF AMAPMFQNFD HADILKEKYL
TQFQKAYPEA VFKNDHDDES SSYYPFGFYQ SGHSVPLTNY LNAQYYTEVS LGTPPQNFKV
ILDTGSSNLW VPSTECSSLA CFLHSKYDHD SSSSYKPNGT EFAIRYGSGS LEGYISQDTL
NLGDLSITKQ DFAEATSEPG LQFAFGKFDG ILGLGYDTIS VDGVVPPFYN AWKQGLLDEP
KFAFYLGRDG ESQDGGVATF GGVDDSKYEG EITWLPIRRK AYWEVKFDGI GLGEEYAELE
NHGAAIDTGT SLIALPSGLA EIINAEIGAK KSWTGQYTVE CEARSSLPNM TFTLGGHNFE
LTAYDYILEV SGQCISAIFP MDFPEPVGPL AIIGDSFLRK YYSIYDLGNN AVGLADAV
//
