ID   B8YJG0_SYNRA            Unreviewed;       394 AA.
AC   B8YJG0;
DT   03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   03-MAR-2009, sequence version 1.
DT   22-FEB-2023, entry version 54.
DE   SubName: Full=Syncephapepsin {ECO:0000313|EMBL:ACL68086.1};
DE            EC=3.4.23.- {ECO:0000313|EMBL:ACL68086.1};
OS   Syncephalastrum racemosum (Filamentous fungus).
OC   Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC   Mucoromycetes; Mucorales; Syncephalastraceae; Syncephalastrum.
OX   NCBI_TaxID=13706 {ECO:0000313|EMBL:ACL68086.1};
RN   [1] {ECO:0000313|EMBL:ACL68086.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=BCRC 31638 {ECO:0000313|EMBL:ACL68086.1};
RX   PubMed=19722576; DOI=10.1021/jf8040337;
RA   Chen C.-C., Cho Y.-C., Lai C.-C., Hsu W.-H.;
RT   "Purification and characterization of a new Rhizopuspepsin from Rhizopus
RT   oryzae NBRC 4749.";
RL   J. Agric. Food Chem. 57:6742-6747(2009).
CC   -!- SIMILARITY: Belongs to the peptidase A1 family.
CC       {ECO:0000256|ARBA:ARBA00007447, ECO:0000256|RuleBase:RU000454}.
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DR   EMBL; FJ539001; ACL68086.1; -; Genomic_DNA.
DR   AlphaFoldDB; B8YJG0; -.
DR   MEROPS; A01.042; -.
DR   GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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   PANTHER; PTHR47966:SF1; ASPARTYL PROTEINASE; 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|PIRSR:PIRSR601461-2};
KW   Hydrolase {ECO:0000256|RuleBase:RU000454, ECO:0000313|EMBL:ACL68086.1};
KW   Protease {ECO:0000256|RuleBase:RU000454}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..394
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002880962"
FT   DOMAIN          88..390
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000259|PROSITE:PS51767"
FT   ACT_SITE        106
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT   ACT_SITE        287
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT   DISULFID        321..354
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
SQ   SEQUENCE   394 AA;  41470 MW;  F1E00D90BAE3D6C9 CRC64;
     MKFSLALLAT LALATISQAA PVEKQVAGKP FQLVKNPHYQ ANATRAILRA ERKYARHSTK
     IPEQGKTVVK AAGSGSVPMT DVDYDVEYYA TVSVGTPAQS IKLDFDTGSS DLWFSSTLCS
     SCGSKSFDPT KSSTYKKVGK SWQISYGDGS SASGITATDN VELGGLTITG QTIELATRES
     SSFSTGAIDG ILGLGFDTIA TVAGTKTPVD NLISQNLISK PIFGVWLGKQ SEGGGGEYVF
     GGYNTDHIDG SLTTVKVDNS QGWYGVTVSG LKVGSKSVAS SFDGILDTGT TLLIFDRSTA
     SQVARAYGAS DNGDGTYTIS CDQSKLQPLA LTMGGKDFFV PADSLIYVKQ GSQCIAGFGY
     SSMDFAIIGD TFLKNNYVVF NQEVPEVQIA PSKA
//