ID S2KFC6_MUCC1 Unreviewed; 366 AA.
AC S2KFC6;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 24-JAN-2024, entry version 42.
DE RecName: Full=rhizopuspepsin {ECO:0000256|ARBA:ARBA00013205};
DE EC=3.4.23.21 {ECO:0000256|ARBA:ARBA00013205};
GN ORFNames=HMPREF1544_02124 {ECO:0000313|EMBL:EPB91055.1};
OS Mucor circinelloides f. circinelloides (strain 1006PhL) (Mucormycosis
OS agent) (Calyptromyces circinelloides).
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Mucorineae; Mucoraceae; Mucor.
OX NCBI_TaxID=1220926 {ECO:0000313|EMBL:EPB91055.1, ECO:0000313|Proteomes:UP000014254};
RN [1] {ECO:0000313|Proteomes:UP000014254}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1006PhL {ECO:0000313|Proteomes:UP000014254};
RG The Broad Institute Genomics Platform;
RA Cuomo C., Earl A., Findley K., Lee S.C., Walker B., Young S., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome sequence of Mucor circinelloides f. circinelloides 1006PhL.";
RL Submitted (MAY-2013) 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; KE123913; EPB91055.1; -; Genomic_DNA.
DR AlphaFoldDB; S2KFC6; -.
DR STRING; 1220926.S2KFC6; -.
DR MEROPS; A01.A66; -.
DR VEuPathDB; FungiDB:HMPREF1544_02124; -.
DR eggNOG; KOG1339; Eukaryota.
DR InParanoid; S2KFC6; -.
DR OrthoDB; 4946at2759; -.
DR Proteomes; UP000014254; 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; NAPSIN-A; 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|RuleBase:RU000454};
KW Protease {ECO:0000256|RuleBase:RU000454};
KW Reference proteome {ECO:0000313|Proteomes:UP000014254}.
FT DOMAIN 44..362
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT ACT_SITE 62
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 247
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT DISULFID 75..79
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
SQ SEQUENCE 366 AA; 39595 MW; 3B04D37EAA1E92A0 CRC64;
MNTPARVKRA LAKYGIVDEK INSRLNSASN AAIELFSAYV DIEYIGEIAI GTPPQKFNVD
FDTGSSDIWV PSSRCGSSCS THHRFDGSKS STYKEMGNKT WHLSYGDGSS VRGYTALDAV
HLGNVTQPQQ LIGLVTQQTP EFASDKFLDG IFGLAFPPLA YTGIKASIVE DLHMAGSIPS
PIVSFHLGHS RDGGKGEILF GDINQNHFEG ELKYVPVTVK KYWQVDMTGV EVGGTNVLAS
TMPAIVDTGT TLIIVPSAVS KAIHKAIPGA EYDPMYGWRI PCAFADDSST ESINIKLGDQ
DFPLYLRDLV RAKASQSLST GKSRLCYSGV AEANTPLVIL GDTFLRSYYS VYDFGNARVG
LARAKP
//