SPAZ_ORBOL
ID SPAZ_ORBOL Reviewed; 426 AA.
AC G3FNQ9; P83290; Q00226; Q6SZH4; Q8NJT9;
DT 25-JAN-2012, integrated into UniProtKB/Swiss-Prot.
DT 25-JAN-2012, sequence version 2.
DT 03-AUG-2022, entry version 38.
DE RecName: Full=Cuticle-degrading serine protease;
DE EC=3.4.21.-;
DE AltName: Full=Neutral serine protease Aoz1;
DE Short=Aoz;
DE AltName: Full=PII;
DE Flags: Precursor;
OS Orbilia oligospora (Nematode-trapping fungus) (Arthrobotrys oligospora).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Orbiliomycetes;
OC Orbiliales; Orbiliaceae; Orbilia.
OX NCBI_TaxID=2813651;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 124-143, FUNCTION, ACTIVITY
RP REGULATION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=807;
RX AGRICOLA=IND43623331;
RA Zhao M.L., Zhang K.Q.;
RT "Characterization of a neutral serine protease and its full-length cDNA
RT from the nematode-trapping fungus Arthrobothrys oligospora.";
RL Mycologia 96:16-22(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=XA;
RA Wang J., Wang W., Meng Q., Qiao J.;
RT "Characterization of a neutral serine protease and its full-length cDNA
RT from the nematode-trapping fungus Arthrobothrys oligospora strain XA.";
RL Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 115-215.
RC STRAIN=Mankau4;
RX PubMed=15535071; DOI=10.1017/s0953756204000942;
RA Ahren D., Faedo M., Rajashekar B., Tunlid A.;
RT "Low genetic diversity among isolates of the nematode-trapping fungus
RT Duddingtonia flagrans: evidence for recent worldwide dispersion from a
RT single common ancestor.";
RL Mycol. Res. 108:1205-1214(2004).
CC -!- FUNCTION: Hydrolyzes gelatin, casein, the chromogenic substrate azocoll
CC and the cuticle of the nematode P.redivivus. Immobilizes P.redivivus.
CC {ECO:0000269|Ref.1}.
CC -!- ACTIVITY REGULATION: Inhibited by PMSF, SSI, the peptide Phe-Val and by
CC Phe, but not by EDTA. {ECO:0000269|Ref.1}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 6-8. {ECO:0000269|Ref.1};
CC Temperature dependence:
CC Optimum temperature is 45 degrees Celsius. {ECO:0000269|Ref.1};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- INDUCTION: By easily metabolized forms of nitrogen, including ammonia,
CC nitrate and amino acids, and by glucose.
CC -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000305}.
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DR EMBL; AF516146; AAM93666.1; -; mRNA.
DR EMBL; JF747254; AEO44978.1; -; Genomic_DNA.
DR EMBL; AY444597; AAR19138.1; -; Genomic_DNA.
DR AlphaFoldDB; G3FNQ9; -.
DR SMR; G3FNQ9; -.
DR MEROPS; S08.120; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0030574; P:collagen catabolic process; IEA:UniProtKB-KW.
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 Collagen degradation; Direct protein sequencing; Glycoprotein; Hydrolase;
KW Protease; Secreted; Serine protease; Signal; Zymogen.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT PROPEP 22..123
FT /evidence="ECO:0000269|Ref.1"
FT /id="PRO_0000415374"
FT CHAIN 124..426
FT /note="Cuticle-degrading serine protease"
FT /id="PRO_0000415342"
FT DOMAIN 39..122
FT /note="Inhibitor I9"
FT /evidence="ECO:0000255"
FT DOMAIN 130..426
FT /note="Peptidase S8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 164
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 200
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 353
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT CARBOHYD 178
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 252
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VARIANT 51
FT /note="S -> N (in strain: XA)"
FT VARIANT 266
FT /note="T -> A (in strain: XA)"
FT VARIANT 270
FT /note="A -> S (in strain: XA)"
FT VARIANT 274
FT /note="C -> S (in strain: XA)"
FT VARIANT 319
FT /note="L -> F (in strain: XA)"
FT VARIANT 378
FT /note="T -> I (in strain: XA)"
FT VARIANT 400
FT /note="P -> S (in strain: XA)"
FT VARIANT 411
FT /note="S -> N (in strain: XA)"
FT VARIANT 422
FT /note="T -> A (in strain: XA)"
SQ SEQUENCE 426 AA; 44360 MW; 41BCB5FE5F484CBF CRC64;
MLTNGLISLL AIAGLATNAF AGPIRKVSNA GAAGAIADKY IVVLKKGLSD SAVSKHTNRI
SSFHSNVARD LTGARAHGVG RKFRFSSTGF NGYVGGFDKA TLQEILNSPE VDYVEQDTVV
TTYAEQTDST WGLDRISHED YSAPYTYEYD ETAAGAGTTV YVIDTGIRIS HDEFQTVNGS
SRATWGFNSV DKTDSDGNGH GTHCAGTIAG KTYGVSKKAK VVAVKVLSAG GSGSTAGVVS
GMNWVAENAT PNFSVASMSL GGSKSTALNA AVDCIFNAGI TIVVAAGNEN QDAKNVSPAS
APNAITVGAI DSSNKIASLS NWGTLIDVFA PGVGVLSSWA TSDKETKTIS GTSMACPHVA
GLAAYYISAS EGGADPATIT DKITSSRRQW SGHREHPWLP KQDRLQRICL STHSPKTNHQ
VTIVAS
