ID M3J0J0_CANMX Unreviewed; 551 AA.
AC M3J0J0;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE RecName: Full=candidapepsin {ECO:0000256|ARBA:ARBA00013207};
DE EC=3.4.23.24 {ECO:0000256|ARBA:ARBA00013207};
GN ORFNames=G210_4447 {ECO:0000313|EMBL:EMG45373.1};
OS Candida maltosa (strain Xu316) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=1245528 {ECO:0000313|EMBL:EMG45373.1, ECO:0000313|Proteomes:UP000011777};
RN [1] {ECO:0000313|EMBL:EMG45373.1, ECO:0000313|Proteomes:UP000011777}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Xu316 {ECO:0000313|Proteomes:UP000011777};
RA Yu J., Wang Q., Geng X., Bao W., He P., Cai J.;
RT "Genome sequence of Candida maltosa Xu316, a potential industrial strain
RT for xylitol and ethanol production.";
RL Submitted (FEB-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Preferential cleavage at the carboxyl of hydrophobic amino
CC acids, but fails to cleave 15-Leu-|-Tyr-16, 16-Tyr-|-Leu-17 and 24-
CC Phe-|-Phe-25 of insulin B chain. Activates trypsinogen, and degrades
CC keratin.; EC=3.4.23.24; Evidence={ECO:0000256|ARBA:ARBA00001675};
CC -!- SIMILARITY: Belongs to the peptidase A1 family.
CC {ECO:0000256|ARBA:ARBA00007447, ECO:0000256|RuleBase:RU000454}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EMG45373.1}.
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DR EMBL; AOGT01002512; EMG45373.1; -; Genomic_DNA.
DR AlphaFoldDB; M3J0J0; -.
DR STRING; 1245528.M3J0J0; -.
DR MEROPS; A01.067; -.
DR eggNOG; KOG1339; Eukaryota.
DR HOGENOM; CLU_013253_9_1_1; -.
DR OMA; IWGYDDV; -.
DR OrthoDB; 615305at2759; -.
DR Proteomes; UP000011777; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Hydrolase {ECO:0000256|RuleBase:RU000454};
KW Protease {ECO:0000256|RuleBase:RU000454};
KW Reference proteome {ECO:0000313|Proteomes:UP000011777};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
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 /note="candidapepsin"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004035011"
FT DOMAIN 67..470
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT REGION 496..525
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 85
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 362
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
SQ SEQUENCE 551 AA; 58929 MW; F9F88606C29F5A7A CRC64;
MKLSTLSLLS TIASTALATA TVPFRIDFNV RRGSSKDQLS PEDDSTPKFV KRDGSFEMIL
SNQQTFYMAD LKIGSNQDEN RVLVDTGSSD LWVMSHDLNC VPTPNQRRSM QSFEEGTGVR
YCQRRNDAVV PNPTKTIREV KREGEEKAGA SVYSTVFITE GAFGTNSPFV GSAGGSGSGS
NTCTSYGSFN TENSDTFTEN NTYPFVIQYA DDTHAIGIWG YDNVIINNVT VNNLSFAVAN
ETSSDVGVLG IGLPGLEVTS QYGYMYENLP IKLRNQGVIN KAIYSLYLDT ADARTGSILF
GAIDHAKYQG DLVTVNMMRT YRAISYPVRI QVPMTNIDFV QRGSTTNILS ASASSPTGVV
LDTGSTLSYV FPSTLQALGN AVGGRYSNTV GAYIVDCNLA NSDATVNIEF GGNKTIEVPL
SDLVLQASRT QCILGVLAQS ADSSYMLFGD NILRSAYIVY DIDDYQVSLA QVAYTNDTSI
EIVSANGISN TTGLGTASSS SSSSGSSSSS SSTTSSRSSS TSTGQRNAAA GLVSTPIQIM
ISLCVFYSIF I
//
