ID A0A0B7MXZ6_9FUNG Unreviewed; 454 AA.
AC A0A0B7MXZ6;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=rhizopuspepsin {ECO:0000256|ARBA:ARBA00013205};
DE EC=3.4.23.21 {ECO:0000256|ARBA:ARBA00013205};
GN Name=PARPA_01107.1 scaffold 1359 {ECO:0000313|EMBL:CEP07799.1};
OS Parasitella parasitica.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Mucorineae; Mucoraceae; Parasitella.
OX NCBI_TaxID=35722 {ECO:0000313|EMBL:CEP07799.1, ECO:0000313|Proteomes:UP000054107};
RN [1] {ECO:0000313|EMBL:CEP07799.1, ECO:0000313|Proteomes:UP000054107}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 412.66 {ECO:0000313|EMBL:CEP07799.1,
RC ECO:0000313|Proteomes:UP000054107};
RA Ellenberger Sabrina;
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
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; Evidence={ECO:0000256|ARBA:ARBA00001130};
CC -!- SIMILARITY: Belongs to the peptidase A1 family.
CC {ECO:0000256|ARBA:ARBA00007447, ECO:0000256|RuleBase:RU000454}.
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DR EMBL; LN719426; CEP07799.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0B7MXZ6; -.
DR STRING; 35722.A0A0B7MXZ6; -.
DR MEROPS; A01.013; -.
DR OrthoDB; 1359512at2759; -.
DR Proteomes; UP000054107; Unassembled WGS sequence.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd05471; pepsin_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; IPR034164; Pepsin-like_dom.
DR InterPro; IPR033121; PEPTIDASE_A1.
DR InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR PANTHER; PTHR47966; BETA-SITE APP-CLEAVING ENZYME, ISOFORM A-RELATED; 1.
DR PANTHER; PTHR47966:SF51; 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; 1.
DR PROSITE; PS51767; PEPTIDASE_A1; 1.
PE 3: Inferred from homology;
KW Aspartyl protease {ECO:0000256|ARBA:ARBA00022750,
KW ECO:0000256|RuleBase:RU000454};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU000454};
KW Protease {ECO:0000256|RuleBase:RU000454};
KW Reference proteome {ECO:0000313|Proteomes:UP000054107}.
FT DOMAIN 39..412
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT ACT_SITE 57
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 281
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
SQ SEQUENCE 454 AA; 49887 MW; B9A4F527681D4775 CRC64;
MDALANKVLR FPIIEQPTSQ IEKRDIGIAS LFNFNSKEYI IKVGLGTPVQ NFNVTLDTGS
SGLWVPSSEC PSSNCLYSKF NEAASSTLKH TGKTFDAQYG SGSAKGLLAY ESVTFTHLAT
NDSFVNWTSP NHLIGLASAT TGMSTSPSST RVSGILGLGL RGLQSDPTKR TFIEQLHANG
VINRPVFSIF LNRQANHGYS GEMVLGGLDE RRLQNEQVYA INLLQYNKQG QPNIGASYKM
NATDMTFKYW AVAAQGVSSS KSNHSQIFKN EYREVVPVIL DTGTTLSYLP EQDVISILET
ITKDYVPLKL NGGASQGYQV HCSDFTKEGM WFDFELTDAL GFTNAPAIIR VPLVEMALPQ
DTEDINTATS CLFGLAPISN NSPHGYGWIL GQTVLRSAYV VYNMEDYTVW IGQAVNNYTI
PYAEASLSVT NLACHQHYYI LILSFLVITM SNFL
//
