ID I1BLH8_RHIO9 Unreviewed; 391 AA.
AC I1BLH8;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 24-JAN-2024, entry version 54.
DE RecName: Full=rhizopuspepsin {ECO:0000256|ARBA:ARBA00013205};
DE EC=3.4.23.21 {ECO:0000256|ARBA:ARBA00013205};
DE AltName: Full=Aspartate protease {ECO:0000256|ARBA:ARBA00042718};
GN ORFNames=RO3G_01759 {ECO:0000313|EMBL:EIE77055.1}, RO3G_01762
GN {ECO:0000313|EMBL:EIE77058.1};
OS Rhizopus delemar (strain RA 99-880 / ATCC MYA-4621 / FGSC 9543 / NRRL
OS 43880) (Mucormycosis agent) (Rhizopus arrhizus var. delemar).
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Mucorineae; Rhizopodaceae; Rhizopus.
OX NCBI_TaxID=246409 {ECO:0000313|EMBL:EIE77058.1, ECO:0000313|Proteomes:UP000009138};
RN [1] {ECO:0000313|EMBL:EIE77058.1, ECO:0000313|Proteomes:UP000009138}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RA 99-880 {ECO:0000313|EMBL:EIE77058.1}, and RA 99-880 / ATCC
RC MYA-4621 / FGSC 9543 / NRRL 43880 {ECO:0000313|Proteomes:UP000009138};
RX PubMed=19578406; DOI=10.1371/journal.pgen.1000549;
RA Ma L.-J., Ibrahim A.S., Skory C., Grabherr M.G., Burger G., Butler M.,
RA Elias M., Idnurm A., Lang B.F., Sone T., Abe A., Calvo S.E.,
RA Corrochano L.M., Engels R., Fu J., Hansberg W., Kim J.-M., Kodira C.D.,
RA Koehrsen M.J., Liu B., Miranda-Saavedra D., O'Leary S.,
RA Ortiz-Castellanos L., Poulter R., Rodriguez-Romero J., Ruiz-Herrera J.,
RA Shen Y.-Q., Zeng Q., Galagan J., Birren B.W., Cuomo C.A., Wickes B.L.;
RT "Genomic analysis of the basal lineage fungus Rhizopus oryzae reveals a
RT whole-genome duplication.";
RL PLoS Genet. 5:E1000549-E1000549(2009).
RN [2] {ECO:0000313|EMBL:EIE77058.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=RA 99-880 {ECO:0000313|EMBL:EIE77058.1};
RG The Broad Institute Genome Sequencing Platform;
RA Birren B., Lander E., Galagan J., Nusbaum C., Devon K., Ma L.-J., Jaffe D.,
RA Butler J., Alvarez P., Gnerre S., Grabherr M., Kleber M., Mauceli E.,
RA Brockman W., Rounsley S., Young S., LaButti K., Pushparaj V., DeCaprio D.,
RA Crawford M., Koehrsen M., Engels R., Montgomery P., Pearson M., Howarth C.,
RA Larson L., Luoma S., White J., O'Leary S., Kodira C., Zeng Q., Yandava C.,
RA Alvarado L., Skory C.D., Ibrahim A., Lang F., Wickes B.L., Liu B.;
RT "Annotation of the Rhizopus oryzae genome.";
RL Submitted (APR-2012) 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; CH476732; EIE77055.1; -; Genomic_DNA.
DR EMBL; CH476732; EIE77058.1; -; Genomic_DNA.
DR AlphaFoldDB; I1BLH8; -.
DR STRING; 246409.I1BLH8; -.
DR MEROPS; A01.012; -.
DR VEuPathDB; FungiDB:RO3G_01759; -.
DR VEuPathDB; FungiDB:RO3G_01762; -.
DR eggNOG; KOG1339; Eukaryota.
DR InParanoid; I1BLH8; -.
DR OMA; SQGFWQV; -.
DR OrthoDB; 1379710at2759; -.
DR Proteomes; UP000009138; 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; cd06097; Aspergillopepsin_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; IPR034163; Aspergillopepsin-like_cat_dom.
DR InterPro; IPR033121; PEPTIDASE_A1.
DR InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR PANTHER; PTHR47966:SF1; ASPARTYL PROTEINASE; 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; 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:UP000009138};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..391
FT /note="rhizopuspepsin"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5010119421"
FT DOMAIN 84..388
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT ACT_SITE 102
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 285
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT DISULFID 319..352
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
SQ SEQUENCE 391 AA; 41186 MW; BAE704238C07BF86 CRC64;
MKLTLISSCV ALAFMALATE AAPSGKKLSI PLTKNTNYKP SAKNAIQKAL AKYHRFRTTS
SSNSTSTEGT GSVPVTDYYN DIEYYGKVTV GTPGVTLKLD FDTGSSDLWF ASTLCTNCGS
SQTKYNPNQS STYAKDGRTW SISYGDGSSA SGILGTDTVT LGGLKITKQT IELAKREATS
FQSGPSDGLL GLGFDTITTV RGVKTPVDNL ISQGLISKPI FGVYLGKESN GGGGEYIFGG
YDSSKYSGSL TTIPVDNSNG WYGITIKGTT IGSSKVSSSF SAILDTGTTL LILPNNVASA
VARSYGASDN GDGTYTIDCD TSSFKPLVFS IGSSTFEVPA DSLVFEQDGS TCYAGFGYGD
YDFAIFGDVF LKNNYVVFNQ EVPEVQIAPI A
//