ORYZ_ASPCL
ID ORYZ_ASPCL Reviewed; 403 AA.
AC A1CIA7;
DT 05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 89.
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 Flags: Precursor;
GN Name=alp1; Synonyms=alk1, alp; ORFNames=ACLA_050840;
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 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 -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000305}.
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DR EMBL; DS027054; EAW10612.1; -; Genomic_DNA.
DR RefSeq; XP_001272038.1; XM_001272037.1.
DR AlphaFoldDB; A1CIA7; -.
DR SMR; A1CIA7; -.
DR STRING; 5057.CADACLAP00004700; -.
DR MEROPS; S08.053; -.
DR EnsemblFungi; EAW10612; EAW10612; ACLA_050840.
DR GeneID; 4703741; -.
DR KEGG; act:ACLA_050840; -.
DR VEuPathDB; FungiDB:ACLA_050840; -.
DR eggNOG; KOG1153; Eukaryota.
DR HOGENOM; CLU_011263_1_4_1; -.
DR OMA; NWAIASY; -.
DR OrthoDB; 921536at2759; -.
DR BRENDA; 3.4.21.63; 502.
DR Proteomes; UP000006701; 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 3: Inferred from homology;
KW Glycoprotein; Hydrolase; Protease; Reference proteome; Secreted;
KW Serine protease; Signal; Zymogen.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT PROPEP 22..125
FT /evidence="ECO:0000250"
FT /id="PRO_0000406992"
FT CHAIN 126..403
FT /note="Alkaline protease 1"
FT /id="PRO_0000406993"
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"
FT CARBOHYD 307
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 403 AA; 41840 MW; 2DCEDE1D77BDDDFC CRC64;
MQSIKRTLLL LGALLPAALA APAREPHPSS NIIPGKYIIT FKSGIDTAAI ESHTAWASNI
HKRNLERRGL VGGEFPAGIE RKFKIKDFAA YAGSFDPATI EEIRNSEDVA HVEEDQIWYL
DALTTQSGAP WGLGSISHKG QASTNYVYDT SAGAGTYAYV VDSGINVDHI EFQGRATKAY
NAVGGDHVDT LGHGTHVAGT IGGKTYGVAK QTNLLSVKVF EGRTGSTSVI LDGFNWAAND
IVSKGRKGKA AINMSLGGGY SYAFNNAVES AYEQGVLSVV AAGNEGVDAS NSSPASAPNA
LTVGATNKSN ARASFSNYGK VLDIFAPGQD ILSAWIGSTT ATNTISGTSM ATPHVVGLAV
YLMGLEGVSG PAAVTQRILQ LATSGVISDV KGSPNKLAYN GAA
