ID G1XUP4_ARTOA Unreviewed; 407 AA. AC G1XUP4; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 24-JUL-2024, entry version 64. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EGX43093.1}; GN ORFNames=AOL_s00215g702 {ECO:0000313|EMBL:EGX43093.1}; 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 {ECO:0000313|EMBL:EGX43093.1, ECO:0000313|Proteomes:UP000008784}; RN [1] {ECO:0000313|EMBL:EGX43093.1, ECO:0000313|Proteomes:UP000008784} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 24927 / CBS 115.81 / DSM 1491 RC {ECO:0000313|Proteomes:UP000008784}; 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 -!- SIMILARITY: Belongs to the peptidase S8 family. CC {ECO:0000256|ARBA:ARBA00011073, ECO:0000256|PROSITE-ProRule:PRU01240, CC ECO:0000256|RuleBase:RU003355}. CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:EGX43093.1}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; ADOT01000321; EGX43093.1; -; Genomic_DNA. DR RefSeq; XP_011128206.1; XM_011129904.1. DR AlphaFoldDB; G1XUP4; -. DR SMR; G1XUP4; -. DR STRING; 756982.G1XUP4; -. DR GeneID; 22899160; -. DR eggNOG; KOG1153; Eukaryota. DR HOGENOM; CLU_011263_1_4_1; -. DR InParanoid; G1XUP4; -. DR OMA; FASHSAW; -. DR OrthoDB; 380531at2759; -. DR Proteomes; UP000008784; Unassembled WGS sequence. DR GO; GO:0005615; C:extracellular space; IEA:TreeGrafter. DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule. DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW. DR CDD; cd04077; Peptidases_S8_PCSK9_ProteinaseK_like; 1. DR Gene3D; 3.30.70.80; Peptidase S8 propeptide/proteinase inhibitor I9; 1. DR Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 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; IPR050131; Peptidase_S8_subtilisin-like. DR InterPro; IPR015500; Peptidase_S8_subtilisin-rel. DR InterPro; IPR010259; S8pro/Inhibitor_I9. DR InterPro; IPR037045; S8pro/Inhibitor_I9_sf. DR PANTHER; PTHR43806:SF59; CEREVISIN-RELATED; 1. DR PANTHER; PTHR43806; PEPTIDASE S8; 1. DR Pfam; PF05922; Inhibitor_I9; 1. DR Pfam; PF00082; Peptidase_S8; 1. DR PRINTS; PR00723; SUBTILISIN. DR SUPFAM; SSF54897; Protease propeptides/inhibitors; 1. DR SUPFAM; SSF52743; Subtilisin-like; 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 Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE- KW ProRule:PRU01240}; KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE- KW ProRule:PRU01240}; Reference proteome {ECO:0000313|Proteomes:UP000008784}; KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE- KW ProRule:PRU01240}; KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}. FT SIGNAL 1..21 FT /evidence="ECO:0000256|SAM:SignalP" FT CHAIN 22..407 FT /evidence="ECO:0000256|SAM:SignalP" FT /id="PRO_5003426758" FT DOMAIN 37..116 FT /note="Inhibitor I9" FT /evidence="ECO:0000259|Pfam:PF05922" FT DOMAIN 151..379 FT /note="Peptidase S8/S53" FT /evidence="ECO:0000259|Pfam:PF00082" FT ACT_SITE 160 FT /note="Charge relay system" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240" FT ACT_SITE 192 FT /note="Charge relay system" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240" FT ACT_SITE 345 FT /note="Charge relay system" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240" SQ SEQUENCE 407 AA; 43644 MW; CF1CED117B4175CA CRC64; MHFIPLASLL PLAGLILQVA ADLTVLGAGS KDKIPNSYIV VLKPSTNQAQ VQEHTQRISN YHTRRSLQER GVTTGIREQF DIQSVKGYTV ECDHGTLSQI LTSPEVQYVE QEGKTKVQVT QKPSTWGLSR ISWKTLPKAP YSYRYQNTWG GRGTTIYIVD SGVRISHKEF EARATWGYNA VPDSPNTDNH GHGTHVAGTA AGKTYGVAKY ARIVAVKVIG DDGTGQDSYT LAGLNYISKV AKPGKSVVNM SIGGPKSEAV NAAVEALYKK GIVVVAAAGN ENENAGLSSP ASARSAITVG ATDETDTRAR FSNFGSIVDI FAPGVNILSA DITSDTASRL DNGTSMASPH VAGLAAYFIS SRTTSQSPLN IHSLFITYSQ KGLVKSPGPS PNRLAYNGWD EYQPYPY //