ID   CARP_SYNRA              Reviewed;         395 AA.
AC   P81214;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   15-JUL-1999, sequence version 1.
DT   03-AUG-2022, entry version 77.
DE   RecName: Full=Syncephapepsin;
DE            EC=3.4.23.-;
DE   Flags: Precursor;
GN   Name=SPSR;
OS   Syncephalastrum racemosum (Filamentous fungus).
OC   Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC   Mucoromycetes; Mucorales; Syncephalastraceae; Syncephalastrum.
OX   NCBI_TaxID=13706;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 72-395.
RA   Ho H.-C., Shiau P.-F., Liao J.-M., Chung J.-G.;
RT   "Amino-acid sequence and gene cloning of syncephapepsin from
RT   Syncephalastrum racemosum.";
RL   Submitted (JAN-1998) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   PARTIAL PROTEIN SEQUENCE.
RX   PubMed=8837744; DOI=10.1006/abbi.1996.0434;
RA   Ho H.-C., Chen L.-Y., Liao T.H.;
RT   "Identification of a fungal protein of Syncephalastrum racemosum as
RT   aspartic proteinase.";
RL   Arch. Biochem. Biophys. 334:97-103(1996).
RN   [3]
RP   CHARACTERIZATION.
RX   PubMed=9535708; DOI=10.1006/prep.1997.0842;
RA   Ho H.-C., Shiau P.F., Wu S.L.;
RT   "Single-column purification of syncephapepsin -- an aspartic proteinase
RT   from Syncephalastrum racemosum.";
RL   Protein Expr. Purif. 12:399-403(1998).
CC   -!- FUNCTION: Hydrolysis of proteins with a broad specificity. Residues
CC       recognized to be cleaved were primarily those of trypsin and
CC       chymotrypsin and Lys was the most susceptible.
CC   -!- SUBUNIT: Monomer.
CC   -!- SIMILARITY: Belongs to the peptidase A1 family. {ECO:0000305}.
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DR   EMBL; AF043552; AAC69517.1; -; mRNA.
DR   AlphaFoldDB; P81214; -.
DR   SMR; P81214; -.
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; -; 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; PTHR47966; 1.
DR   Pfam; PF00026; Asp; 1.
DR   PRINTS; PR00792; PEPSIN.
DR   SUPFAM; SSF50630; SSF50630; 1.
DR   PROSITE; PS00141; ASP_PROTEASE; 2.
DR   PROSITE; PS51767; PEPTIDASE_A1; 1.
PE   1: Evidence at protein level;
KW   Aspartyl protease; Direct protein sequencing; Disulfide bond; Hydrolase;
KW   Protease; Signal; Zymogen.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   PROPEP          20..71
FT                   /note="Activation peptide"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000025897"
FT   CHAIN           72..395
FT                   /note="Syncephapepsin"
FT                   /id="PRO_0000025898"
FT   DOMAIN          89..391
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
FT   ACT_SITE        107
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10094"
FT   ACT_SITE        288
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10094"
FT   DISULFID        120..123
FT   DISULFID        322..355
SQ   SEQUENCE   395 AA;  41388 MW;  C4B3AFFD79B03D16 CRC64;
     MKFSLALLAT VALATISQAA PVEKQVAGKP FQLVKNPHYQ ANATRAIFRA EKKYARHTAI
     PEQGKTIVKS AASGTGSVPM TDVDYDVEYY ATVSVGTPAQ SIKLDFDTGS SDLWFSSTLC
     TSCGSKSFDP TKSSTYKKVG KSWQISYGDG SSASGITATD NVELGGLKIT GQTIELATRE
     SSSFSSGAID GILGLGFDTI STVAGTKTPV DNLISQNLIS KPIFGVWLGK QSEGGGGEYV
     FGGYNTDHID GSLTTVKVDN SQGWYGVTVS GLKVGSKSVA SSFDGILDTG TTLLIFDQAT
     GSKVAAAYGA KDNGDGTYTI SCDQSKLQPL ALTMGGKDFF VPADSLIYVK QGSQCIAGFG
     YSSMDFAIIG DTFLKNNYVV FNQGVPEVQI APSKA