ORYZ_EMENI
ID ORYZ_EMENI Reviewed; 403 AA.
AC Q00208; C8VG51; Q5B1M2;
DT 05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 131.
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, prtA; ORFNames=AN5558;
OS Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS M139) (Aspergillus nidulans).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Nidulantes.
OX NCBI_TaxID=227321;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INDUCTION.
RC STRAIN=MH2; TISSUE=Mycelium;
RX PubMed=7821793; DOI=10.1016/0378-1119(94)90439-1;
RA Katz M.E., Rice R.N., Cheetham B.F.;
RT "Isolation and characterization of an Aspergillus nidulans gene encoding an
RT alkaline protease.";
RL Gene 150:287-292(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=16372000; DOI=10.1038/nature04341;
RA Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT fumigatus and A. oryzae.";
RL Nature 438:1105-1115(2005).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA Oliver S.G., Turner G.;
RT "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT effort.";
RL Fungal Genet. Biol. 46:S2-13(2009).
RN [4]
RP INDUCTION.
RX PubMed=4589332; DOI=10.1099/00221287-79-2-311;
RA Cohen B.L.;
RT "Regulation of intracellular and extracellular neutral and alkaline
RT proteases in Aspergillus nidulans.";
RL J. Gen. Microbiol. 79:311-320(1973).
RN [5]
RP FUNCTION.
RX PubMed=10882536; DOI=10.1006/fgbi.2000.1195;
RA vanKuyk P.A., Cheetham B.F., Katz M.E.;
RT "Analysis of two Aspergillus nidulans genes encoding extracellular
RT proteases.";
RL Fungal Genet. Biol. 29:201-210(2000).
RN [6]
RP SUBCELLULAR LOCATION.
RX PubMed=25043916; DOI=10.1186/1471-2164-15-613;
RA Martins I., Hartmann D.O., Alves P.C., Martins C., Garcia H.,
RA Leclercq C.C., Ferreira R., He J., Renaut J., Becker J.D.,
RA Silva Pereira C.;
RT "Elucidating how the saprophytic fungus Aspergillus nidulans uses the plant
RT polyester suberin as carbon source.";
RL BMC Genomics 15:613-613(2014).
CC -!- FUNCTION: Secreted alkaline protease that allows assimilation of
CC proteinaceous substrates. {ECO:0000269|PubMed:10882536}.
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:0000269|PubMed:25043916}.
CC -!- INDUCTION: Highly expressed on medium lacking a nitrogen, carbon or
CC sulfur source. {ECO:0000269|PubMed:4589332,
CC ECO:0000269|PubMed:7821793}.
CC -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000305}.
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DR EMBL; L31778; AAA67705.1; -; Genomic_DNA.
DR EMBL; AACD01000095; EAA62263.1; -; Genomic_DNA.
DR EMBL; BN001305; CBF81670.1; -; Genomic_DNA.
DR RefSeq; XP_663162.1; XM_658070.1.
DR AlphaFoldDB; Q00208; -.
DR SMR; Q00208; -.
DR STRING; 162425.CADANIAP00003523; -.
DR MEROPS; S08.053; -.
DR PRIDE; Q00208; -.
DR EnsemblFungi; CBF81670; CBF81670; ANIA_05558.
DR EnsemblFungi; EAA62263; EAA62263; AN5558.2.
DR GeneID; 2871850; -.
DR KEGG; ani:AN5558.2; -.
DR eggNOG; KOG1153; Eukaryota.
DR HOGENOM; CLU_011263_1_4_1; -.
DR InParanoid; Q00208; -.
DR OMA; NWAIASY; -.
DR OrthoDB; 921536at2759; -.
DR Proteomes; UP000000560; Chromosome V.
DR Proteomes; UP000005890; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IMP:UniProtKB.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0008233; F:peptidase activity; IMP:UniProtKB.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IBA:GO_Central.
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..124
FT /evidence="ECO:0000250"
FT /id="PRO_0000406998"
FT CHAIN 125..403
FT /note="Alkaline protease 1"
FT /id="PRO_0000406999"
FT DOMAIN 35..119
FT /note="Inhibitor I9"
FT /evidence="ECO:0000255"
FT DOMAIN 129..403
FT /note="Peptidase S8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 161
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 192
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 348
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT CARBOHYD 252
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 403 AA; 42209 MW; 6971CD5B0E65E8C3 CRC64;
MHSFKRSLLL LGALLPAVFG APVEPRRAAE KVPGKYIVTF KSGLNVDQID AHTSWASNVH
KRNLERRGLA ERDQYSGIEK NYKINKFAAY SGSFDDATIE EIRNSADVAH VEEDQIWYID
ALTSQSGAPW GLGAISHKGE ASTTYVYDTS AGEGTYAYVV DTGINADHEE FGGRASLAYN
AVGGQHVDSV GHGTHVAGTI GGETYGVSKK ANLLSVKVFQ GESSSTSIIL DGFNWAANDI
VSKGRTGKSA INMSLGGGYS YAFNQAVEDA YDEGVLSVVA AGNDNIDASD SSPASAPNAL
TVAASTKSNT RASFSNYGSV VDIFAPGQDI LSAWIGSTTA TNTISGTSMA TPHVVGLSLY
LIALEGLSSA SAVVSRIKEL ATQGVLSNVQ GSPNLLAYNG ADE
