ID   CARP1_RHINI             Reviewed;         389 AA.
AC   P10602;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1989, sequence version 1.
DT   03-AUG-2022, entry version 99.
DE   RecName: Full=Rhizopuspepsin-1;
DE            EC=3.4.23.21;
DE   AltName: Full=Aspartate protease;
DE   Flags: Precursor;
GN   Name=RNAP;
OS   Rhizopus niveus.
OC   Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC   Mucoromycetes; Mucorales; Mucorineae; Rhizopodaceae; Rhizopus.
OX   NCBI_TaxID=4844;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RC   STRAIN=NBRC 4810 / AS 3.4817;
RX   PubMed=3275615; DOI=10.1128/jb.170.1.272-278.1988;
RA   Horiuchi H., Yanai K., Okazaki T., Takagi M., Yano K.;
RT   "Isolation and sequencing of a genomic clone encoding aspartic proteinase
RT   of Rhizopus niveus.";
RL   J. Bacteriol. 170:272-278(1988).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of proteins with broad specificity similar to that
CC         of pepsin A, preferring hydrophobic residues at P1 and P1'. Clots
CC         milk and activates trypsinogen. Does not cleave 4-Gln-|-His-5, but
CC         does cleave 10-His-|-Leu-11 and 12-Val-|-Glu-13 in B chain of
CC         insulin.; EC=3.4.23.21;
CC   -!- SIMILARITY: Belongs to the peptidase A1 family. {ECO:0000305}.
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DR   EMBL; M19100; AAA33882.1; -; Genomic_DNA.
DR   PIR; A28672; A28672.
DR   AlphaFoldDB; P10602; -.
DR   SMR; P10602; -.
DR   MEROPS; A01.012; -.
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..21
FT                   /evidence="ECO:0000255"
FT   PROPEP          22..66
FT                   /note="Activation peptide"
FT                   /id="PRO_0000025883"
FT   CHAIN           67..389
FT                   /note="Rhizopuspepsin-1"
FT                   /id="PRO_0000025884"
FT   DOMAIN          82..385
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
FT   ACT_SITE        100
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10094"
FT   ACT_SITE        283
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10094"
FT   DISULFID        113..116
FT                   /evidence="ECO:0000250"
FT   DISULFID        317..350
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   389 AA;  40802 MW;  AFEC0AA3903DBFB2 CRC64;
     MKFTLISSCV ALAAMTLAVE AAPNGKKINI PLAKNNSYKP SAKNALNKAL AKYNRRKVGS
     GGITTEASGS VPMVDYENDV EYYGEVTVGT PGIKLKLDFD TGSSDMWFAS TLCSSCSNSH
     TKYDPKKSST YAADGRTWSI SYGDGSSASG ILATDNVNLG GLLIKKQTIE LAKRESSAFA
     TDVIDGLLGL GFNTITTVRG VKTPVDNLIS QGLISRPIFG VYLGKQSNGG GGEYIFGGYD
     SSKFKGSLTT VPIDNSEGFW GVTVKSTKIG GTTVSASFDA ILDTGTTLLL LPDDVAAKVA
     RSYGASDNGD GTYSITCDTS KLQPLVFTLG SSTFEVPSDS LIFEKDGNKC IAGFAAGGDL
     AILGDVFLKN NYVVFNQEVP EVQIAPVAN