ID A0A0B7NLK7_9FUNG Unreviewed; 466 AA.
AC A0A0B7NLK7;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 24-JAN-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_10676.1 scaffold 41646 {ECO:0000313|EMBL:CEP16410.1};
OS Parasitella parasitica.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Mucorineae; Mucoraceae; Parasitella.
OX NCBI_TaxID=35722 {ECO:0000313|EMBL:CEP16410.1, ECO:0000313|Proteomes:UP000054107};
RN [1] {ECO:0000313|EMBL:CEP16410.1, ECO:0000313|Proteomes:UP000054107}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 412.66 {ECO:0000313|EMBL:CEP16410.1,
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; LN733157; CEP16410.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0B7NLK7; -.
DR STRING; 35722.A0A0B7NLK7; -.
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:SF65; ASPARTIC-TYPE ENDOPEPTIDASE; 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; 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 Disulfide bond {ECO:0000256|PIRSR:PIRSR601461-2};
KW Hydrolase {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..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..466
FT /note="rhizopuspepsin"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002120800"
FT DOMAIN 53..425
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT ACT_SITE 71
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 294
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT DISULFID 335..384
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
SQ SEQUENCE 466 AA; 51152 MW; 985EE09C62BEA381 CRC64;
MPRYLGLLLL ASLTTNALAD KVLRFPIIEQ PTSQIAKRDV GAASIFNFNS REYIIEIGLG
TPAQNFNVTL DTGSSGLWVP SSACPSSDCL YSRFNETASS TLNHTGKPFD AQYGSRSAKG
LLAYDSVTFT LLNANDSFMN WTSPNHLIGL ANTTTGMSPS PSSTRVSGVL GLGLSELQSD
PTGRTFVEQL YANGLINSPV FSIFLNRQAN HGYSGQLVFG GLDESRLQND IYLIDLLQYN
KQGQPNIGKS YKRNATDLTF KYWAVAGQGV SSSKTNHSQI FKNYYKEVVP VILDTGTTLS
YLPEQDVISI LETITKDYAP LKLNDGAAQG YQVNCSDFTK EDMWFDFELT AAMGYTDDPA
IVRVPLVEMA LPQDTQDINT ATSCLFGLAP ISNNSPHGYG WILGQTVLRS AYVVYNMEDY
TVLIGQATNN YTIPYAKSLA VTSQACHQHY YILVLSFLII TLSHFL
//