ORYZ_ASPFN
ID ORYZ_ASPFN Reviewed; 403 AA.
AC B8N106; Q71RZ0;
DT 05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 80.
DE RecName: Full=Alkaline protease 1;
DE Short=ALP;
DE EC=3.4.21.63;
DE AltName: Full=Aspergillopeptidase B;
DE AltName: Full=Aspergillus proteinase B;
DE AltName: Full=Elastase;
DE AltName: Full=Elastinolytic serine proteinase;
DE AltName: Full=Oryzin;
DE AltName: Allergen=Asp fl 1;
DE Flags: Precursor;
GN Name=alp1; Synonyms=alk1, alp; ORFNames=AFLA_027810;
OS Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357
OS / JCM 12722 / SRRC 167).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=332952;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Chen Z., Cary J.W., Brown R.L., Damann K.E., Cleveland T.E.;
RT "Characterization of an Aspergillus flavus alkaline protease and its
RT possible role in the infection of maize kernels.";
RL Submitted (NOV-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 / SRRC
RC 167;
RX PubMed=25883274; DOI=10.1128/genomea.00168-15;
RA Nierman W.C., Yu J., Fedorova-Abrams N.D., Losada L., Cleveland T.E.,
RA Bhatnagar D., Bennett J.W., Dean R., Payne G.A.;
RT "Genome sequence of Aspergillus flavus NRRL 3357, a strain that causes
RT aflatoxin contamination of food and feed.";
RL Genome Announc. 3:E0016815-E0016815(2015).
CC -!- FUNCTION: Secreted alkaline protease that allows assimilation of
CC proteinaceous substrates. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of proteins with broad specificity, and of Bz-Arg-
CC OEt > Ac-Tyr-OEt. Does not hydrolyze peptide amides.; EC=3.4.21.63;
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- ALLERGEN: Causes an allergic reaction in human.
CC -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000305}.
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DR EMBL; AF324246; AAK52852.1; -; Genomic_DNA.
DR EMBL; EQ963473; EED55509.1; -; Genomic_DNA.
DR RefSeq; XP_002374291.1; XM_002374250.1.
DR AlphaFoldDB; B8N106; -.
DR SMR; B8N106; -.
DR STRING; 5059.CADAFLAP00002156; -.
DR Allergome; 81; Asp fl 13.
DR MEROPS; S08.053; -.
DR EnsemblFungi; EED55509; EED55509; AFLA_027810.
DR VEuPathDB; FungiDB:AFLA_027810; -.
DR eggNOG; KOG1153; Eukaryota.
DR HOGENOM; CLU_011263_1_4_1; -.
DR OMA; GEGVWAY; -.
DR BRENDA; 3.4.21.63; 506.
DR Proteomes; UP000001875; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd04077; Peptidases_S8_PCSK9_ProteinaseK_like; 1.
DR Gene3D; 3.30.70.80; -; 1.
DR Gene3D; 3.40.50.200; -; 1.
DR InterPro; IPR034193; PCSK9_ProteinaseK-like.
DR InterPro; IPR000209; Peptidase_S8/S53_dom.
DR InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR InterPro; IPR023827; Peptidase_S8_Asp-AS.
DR InterPro; IPR022398; Peptidase_S8_His-AS.
DR InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR InterPro; IPR010259; S8pro/Inhibitor_I9.
DR InterPro; IPR037045; S8pro/Inhibitor_I9_sf.
DR Pfam; PF05922; Inhibitor_I9; 1.
DR Pfam; PF00082; Peptidase_S8; 1.
DR PRINTS; PR00723; SUBTILISIN.
DR SUPFAM; SSF52743; SSF52743; 1.
DR PROSITE; PS51892; SUBTILASE; 1.
DR PROSITE; PS00136; SUBTILASE_ASP; 1.
DR PROSITE; PS00137; SUBTILASE_HIS; 1.
DR PROSITE; PS00138; SUBTILASE_SER; 1.
PE 1: Evidence at protein level;
KW Allergen; Glycoprotein; Hydrolase; Protease; Secreted; Serine protease;
KW Signal; Zymogen.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT PROPEP 22..125
FT /evidence="ECO:0000250"
FT /id="PRO_0000406996"
FT CHAIN 126..403
FT /note="Alkaline protease 1"
FT /id="PRO_0000406997"
FT DOMAIN 36..120
FT /note="Inhibitor I9"
FT /evidence="ECO:0000255"
FT DOMAIN 130..403
FT /note="Peptidase S8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 162
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 193
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 349
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT CARBOHYD 253
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 403 AA; 42571 MW; 39A8AC8B8790E010 CRC64;
MQSIKRTLLL LGAILPAVLG APVQETRRAA EKLPGKYIVT FKPGIDEAKI QEHTTWATNI
HQRSLERRGA TGGDLPVGIE RNYKINKFAA YAGSFDDATI EEIRKNEDVA YVEEDQIYYL
DGLTTQKSAP WGLGSISHKG QQSTDYIYDT SAGEGTYAYV VDSGVNVDHE EFEGRASKAY
NAAGGQHVDS IGHGTHVSGT IAGKTYGIAK KASILSVKVF QGESSSTSVI LDGFNWAAND
IVSKKRTSKA AINMSLGGGY SKAFNDAVEN AFEQGVLSVV AAGNENSDAG QTSPASAPDA
ITVAAIQKSN NRASFSNFGK VVDVFAPGQD ILSAWIGSSS ATNTISGTSM ATPHIVGLSL
YLAALENLDG PAAVTKRIKE LATKDVVKDV KGSPNLLAYN GNA
