ID A0A0B7NJ82_9FUNG Unreviewed; 404 AA.
AC A0A0B7NJ82;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=rhizopuspepsin {ECO:0000256|ARBA:ARBA00013205};
DE EC=3.4.23.21 {ECO:0000256|ARBA:ARBA00013205};
GN Name=PARPA_09809.1 scaffold 39042 {ECO:0000313|EMBL:CEP15574.1};
OS Parasitella parasitica.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Mucorineae; Mucoraceae; Parasitella.
OX NCBI_TaxID=35722 {ECO:0000313|EMBL:CEP15574.1, ECO:0000313|Proteomes:UP000054107};
RN [1] {ECO:0000313|EMBL:CEP15574.1, ECO:0000313|Proteomes:UP000054107}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 412.66 {ECO:0000313|EMBL:CEP15574.1,
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; LN732581; CEP15574.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0B7NJ82; -.
DR STRING; 35722.A0A0B7NJ82; -.
DR OrthoDB; 4946at2759; -.
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; 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|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU000454};
KW Protease {ECO:0000256|RuleBase:RU000454};
KW Reference proteome {ECO:0000313|Proteomes:UP000054107};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..404
FT /note="rhizopuspepsin"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002135435"
FT DOMAIN 83..400
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT ACT_SITE 101
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 286
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT DISULFID 114..118
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
SQ SEQUENCE 404 AA; 43668 MW; B80B075FC8E049CA CRC64;
MVQQIGLLAS ATTLLMLLMA VEAQLSHLNV DLDFIEGNRM NTPARVKRSL AKYGIVDEKL
NSRLNSASSA AIELFSAYVD IEYVGEIAIG TPPQKFSVDF DTGSSDIWVP SSRCGSSCST
HNRFDGLKSS TYTDMGGKTW QLSYGDGSSV RGYTARDAVH LGNVTQPQQL IGLVSDETPE
FASDKFLDGI FGLAFPPLAY TGIKASIVED MHMAGSIPSP IVSFHLGHNR DGGKGEILFG
DINQNHFEGE LKYVPVTLKK YWQVDMTGVE VDGVNVLDAA MPAIVDTGTT LIIVPSAVSN
AIHKAIPGAK YDPMYGWRIP CSFADSSSTE SINIKLGDQD FPLFLKDLVR AKMSQSSGDK
NGLCYSGVAE ANTPLAILGD TFLRSYYSVY DFGNARVGLA RTRP
//
