ID A0A0C9LQG4_9FUNG Unreviewed; 381 AA.
AC A0A0C9LQG4;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=rhizopuspepsin {ECO:0000256|ARBA:ARBA00013205};
DE EC=3.4.23.21 {ECO:0000256|ARBA:ARBA00013205};
GN ORFNames=MAM1_0008c00903 {ECO:0000313|EMBL:GAN01470.1};
OS Mucor ambiguus.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Mucorineae; Mucoraceae; Mucor.
OX NCBI_TaxID=91626 {ECO:0000313|EMBL:GAN01470.1};
RN [1] {ECO:0000313|EMBL:GAN01470.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=NBRC 6742 {ECO:0000313|EMBL:GAN01470.1};
RA Takeda I., Yamane N., Morita T., Tamano K., Machida M., Baker S., Koike H.;
RT "Draft genome sequence of an oleaginous Mucoromycotina fungus Mucor
RT ambiguus NBRC6742.";
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; DF836297; GAN01470.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0C9LQG4; -.
DR STRING; 91626.A0A0C9LQG4; -.
DR OrthoDB; 3087283at2759; -.
DR Proteomes; UP000053815; 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:UP000053815}.
FT DOMAIN 21..369
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT ACT_SITE 39
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 245
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
SQ SEQUENCE 381 AA; 41459 MW; 382C8726A45FA948 CRC64;
MLQERSYYGL TSIYNDNQVQ YLVNIQVGTP SQTFVVIVDT GSPEFWVPSI DCPASQCPLV
NFNASKSSTL TDCHSNFSIT YTGGYARGSL VTDHVTLAGI SVENQAFGLV TSTEETVTVD
EIYSSIRADG ILGLSFPDSN TLQKGYISSI PFHMAANQLL TEPIFSICTN SIYQDGWAGD
IIFGGSNTSD YVGNLSYVPV APDPITQQYT LWQIDTKSVS LTSAVDNTLI TTSSAFDPRI
ISTIDTGTTF SYMSNDYIKS MMRAITGRDP LELDSGSGCY PIDCDYAYAD ENGANVVFEF
SVSDADKTTL ITIPVNELVE PVDSTSIQYA HQCVFSLCPT SAPTMLLGDS VIRALYLVFD
MEHKQMGFAP SLNTNSTVSQ Y
//
