ORYZ_NEOFI
ID ORYZ_NEOFI Reviewed; 403 AA.
AC A1CWF3;
DT 05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 93.
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=NFIA_104430;
OS Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164
OS / JCM 1740 / NRRL 181 / WB 181) (Aspergillus fischerianus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=331117;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 / NRRL 181
RC / WB 181;
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 -!- INDUCTION: Highly expressied on medium lacking a nitrogen, carbon or
CC sulfur source.
CC -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000305}.
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DR EMBL; DS027685; EAW24955.1; -; Genomic_DNA.
DR RefSeq; XP_001266852.1; XM_001266851.1.
DR AlphaFoldDB; A1CWF3; -.
DR SMR; A1CWF3; -.
DR STRING; 36630.CADNFIAP00009358; -.
DR MEROPS; S08.053; -.
DR EnsemblFungi; EAW24955; EAW24955; NFIA_104430.
DR GeneID; 4594003; -.
DR KEGG; nfi:NFIA_104430; -.
DR VEuPathDB; FungiDB:NFIA_104430; -.
DR eggNOG; KOG1153; Eukaryota.
DR HOGENOM; CLU_011263_1_4_1; -.
DR OMA; NWAIASY; -.
DR OrthoDB; 921536at2759; -.
DR Proteomes; UP000006702; 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 2: Evidence at transcript level;
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_0000407000"
FT CHAIN 126..403
FT /note="Alkaline protease 1"
FT /id="PRO_0000407001"
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; 42186 MW; E97FB2C408081068 CRC64;
MLSIKRTLLL LGAVLPAVFG APVQETRRAA QKIPGKYIVT FKPGTDAATI ESHTLWATDL
HKRNLERRDA TSGEPPIGIE KNYKIKDFAA YAGSFDDTTI EEIRKSADVA HVEEDQIWYI
DALTTQKGAP WGLGSISHKG QASTDYIYDT SAGAGTYAYV VDTGINVNHV EFEGRASLAY
NAAGGSHVDS VGHGTHVAGT IGGKTYGVAK KTNLLSVKVF QGESSSTSII LDGFNWAAND
IVSKGRTRKA AINMSLGGGY SYAFNNAVEN AFDEGVLSVV AAGNENTDAS NTSPASAPNA
LTVAAINRSN ARASFSNYGS VVDIFAPGQD ILSAWIGSNT ATNTISGTSM ATPHIVGLSV
YLMGLESLSG PAAVTSRIKQ LATNGVVTNA QGSPNKLAYN GNA
