PEPA_ASPCL
ID PEPA_ASPCL Reviewed; 394 AA.
AC A1CBR4;
DT 05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=Aspergillopepsin-1 {ECO:0000305};
DE EC=3.4.23.18 {ECO:0000250|UniProtKB:Q12567};
DE AltName: Full=Aspartic protease pepA;
DE AltName: Full=Aspergillopepsin I;
DE AltName: Full=Aspergillopeptidase A;
DE Flags: Precursor;
GN Name=pepA; ORFNames=ACLA_016280;
OS Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 /
OS NRRL 1 / QM 1276 / 107).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=344612;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1;
RX PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT fumigatus.";
RL PLoS Genet. 4:E1000046-E1000046(2008).
CC -!- FUNCTION: Secreted aspartic endopeptidase that allows assimilation of
CC proteinaceous substrates. The scissile peptide bond is attacked by a
CC nucleophilic water molecule activated by two aspartic residues in the
CC active site. Shows a broad primary substrate specificity. Favors
CC hydrophobic residues at the P1 and P1' positions, but also accepts a
CC lysine residue in the P1 position, leading to the activation of
CC trypsinogen and chymotrypsinogen A. {ECO:0000250|UniProtKB:Q12567}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of proteins with broad specificity. Generally
CC favors hydrophobic residues in P1 and P1', but also accepts Lys in
CC P1, which leads to activation of trypsinogen. Does not clot milk.;
CC EC=3.4.23.18; Evidence={ECO:0000250|UniProtKB:Q12567};
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:Q12567}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q12567}.
CC -!- SIMILARITY: Belongs to the peptidase A1 family. {ECO:0000255|PROSITE-
CC ProRule:PRU01103}.
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DR EMBL; DS027049; EAW13182.1; -; Genomic_DNA.
DR RefSeq; XP_001274608.1; XM_001274607.1.
DR AlphaFoldDB; A1CBR4; -.
DR SMR; A1CBR4; -.
DR STRING; 344612.A1CBR4; -.
DR MEROPS; A01.026; -.
DR EnsemblFungi; EAW13182; EAW13182; ACLA_016280.
DR GeneID; 4706595; -.
DR KEGG; act:ACLA_016280; -.
DR VEuPathDB; FungiDB:ACLA_016280; -.
DR eggNOG; KOG1339; Eukaryota.
DR HOGENOM; CLU_013253_0_1_1; -.
DR OMA; GFWEFTA; -.
DR OrthoDB; 1619495at2759; -.
DR Proteomes; UP000006701; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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; -; 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; PTHR47966; 1.
DR Pfam; PF00026; Asp; 1.
DR PRINTS; PR00792; PEPSIN.
DR SUPFAM; SSF50630; SSF50630; 1.
DR PROSITE; PS00141; ASP_PROTEASE; 2.
DR PROSITE; PS51767; PEPTIDASE_A1; 1.
PE 3: Inferred from homology;
KW Aspartyl protease; Disulfide bond; Hydrolase; Protease; Reference proteome;
KW Secreted; Signal; Zymogen.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT PROPEP 21..69
FT /note="Activation peptide"
FT /evidence="ECO:0000250|UniProtKB:Q12567"
FT /id="PRO_0000407039"
FT CHAIN 70..394
FT /note="Aspergillopepsin-1"
FT /id="PRO_0000407040"
FT DOMAIN 85..391
FT /note="Peptidase A1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
FT ACT_SITE 101
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
FT ACT_SITE 283
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
FT DISULFID 319..354
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
SQ SEQUENCE 394 AA; 40934 MW; C5E9F9851AAEFBA3 CRC64;
MVVFSKVTAA VFGLATIASA APAPPTRKGF TVQQQARPAQ KKQVNLPAMY AHALTKFGGS
VPESVKVAAS KGSAVTTPEA GDVEYLTPVN VGGTVMNLDF DTGSADLWVF SGELPASETS
GHSVYKPGRT ASKLPGGSWQ ISYGDGSSAS GDVYKDTVVV GGVTAHGQAV EAAAQISSQF
LQDKNNDGLL GLAFSSLNTV QPQPQTTFFD TVKSSLDRPL FAVTLKHNAP GSFDFGYIDH
SKYTGEIAYT DVDNSQGFWS FTADGYSIGG GQSSGSSISG IADTGTTLLL LDDNVVSDFY
QHVEGAQNSD EYGGYVFPCS AKVPSFTTII GGYKAVTPGK LINYGPVTDG SSTCYGGIQS
SGGVGQNIFG DIFLKSQFVV FDSEGPRLGF AAQA
