SPAZ_ARTOA
ID SPAZ_ARTOA Reviewed; 409 AA.
AC G1X8P8; P83290; Q00226; Q6SZH4; Q8NJT9;
DT 25-JAN-2012, integrated into UniProtKB/Swiss-Prot.
DT 16-NOV-2011, sequence version 1.
DT 03-AUG-2022, entry version 44.
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 Arthrobotrys oligospora (strain ATCC 24927 / CBS 115.81 / DSM 1491)
OS (Nematode-trapping fungus) (Didymozoophaga oligospora).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Orbiliomycetes;
OC Orbiliales; Orbiliaceae; Orbilia; Orbilia oligospora.
OX NCBI_TaxID=756982;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 124-133; 140-146;
RP 193-209; 212-216 AND 392-403, ACTIVITY REGULATION, AND INDUCTION.
RC STRAIN=ATCC 24927 / CBS 115.81 / DSM 1491;
RX PubMed=8757725; DOI=10.1099/13500872-142-7-1605;
RA Ahman J., Ek B., Rask L., Tunlid A.;
RT "Sequence analysis and regulation of a gene encoding a cuticle-degrading
RT serine protease from the nematophagous fungus Arthrobotrys oligospora.";
RL Microbiology 142:1605-1616(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24927 / CBS 115.81 / DSM 1491;
RX PubMed=21909256; DOI=10.1371/journal.ppat.1002179;
RA Yang J., Wang L., Ji X., Feng Y., Li X., Zou C., Xu J., Ren Y., Mi Q.,
RA Wu J., Liu S., Liu Y., Huang X., Wang H., Niu X., Li J., Liang L., Luo Y.,
RA Ji K., Zhou W., Yu Z., Li G., Liu Y., Li L., Qiao M., Feng L., Zhang K.-Q.;
RT "Genomic and proteomic analyses of the fungus Arthrobotrys oligospora
RT provide insights into nematode-trap formation.";
RL PLoS Pathog. 7:E1002179-E1002179(2011).
CC -!- FUNCTION: Hydrolyzes gelatin, casein, the chromogenic substrate azocoll
CC and the cuticle of the nematode P.redivivus. Immobilizes P.redivivus.
CC -!- ACTIVITY REGULATION: Inhibited by PMSF, SSI, the peptide Phe-Val and by
CC Phe, but not by EDTA. {ECO:0000269|PubMed:8757725}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- INDUCTION: By easily metabolized forms of nitrogen, including ammonia,
CC nitrate and amino acids, and by glucose. {ECO:0000269|PubMed:8757725}.
CC -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000305}.
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DR EMBL; X94121; CAA63841.1; -; Genomic_DNA.
DR EMBL; ADOT01000122; EGX50454.1; -; Genomic_DNA.
DR RefSeq; XP_011120860.1; XM_011122558.1.
DR AlphaFoldDB; G1X8P8; -.
DR SMR; G1X8P8; -.
DR STRING; 13349.G1X8P8; -.
DR MEROPS; S08.120; -.
DR EnsemblFungi; EGX50454; EGX50454; AOL_s00076g4.
DR GeneID; 22892173; -.
DR eggNOG; KOG1153; Eukaryota.
DR HOGENOM; CLU_011263_1_4_1; -.
DR OMA; ATSWSNY; -.
DR OrthoDB; 308083at2759; -.
DR Proteomes; UP000008784; 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: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; Reference proteome; Secreted; Serine protease; Signal; Zymogen.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT PROPEP 22..123
FT /evidence="ECO:0000269|PubMed:8757725"
FT /id="PRO_0000390696"
FT CHAIN 124..409
FT /note="Cuticle-degrading serine protease"
FT /id="PRO_0000076415"
FT DOMAIN 39..122
FT /note="Inhibitor I9"
FT /evidence="ECO:0000255"
FT DOMAIN 130..409
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 CONFLICT 54..58
FT /note="SKHTN -> QTYH (in Ref. 1; CAA63841)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 409 AA; 41914 MW; ECF7054B88FF2A7B 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 GGSKSAALNT AVDAIFNAGI TIVVAAGNEN QDAKNVSPAS
APNAITVGAI DSSNKIASFS NWGTLIDVFA PGVGVLSSWA TSDKETKTIS GTSMACPHVA
GLAAYYISAS EGGADPATIT DKITSSAVSG QVTGNIRGSP NKIAYNGYA
