ID G1XUP4_ARTOA Unreviewed; 407 AA. AC G1XUP4; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 16-SEP-2015, entry version 24. 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. 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., RA Luo Y., Ji K., Zhou W., Yu Z., Li G., Liu Y., Li L., Qiao M., Feng L., RA 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|RuleBase:RU003355}. CC -!- SIMILARITY: Contains peptidase S8 domain. CC {ECO:0000256|SAAS:SAAS00151873}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {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 ProteinModelPortal; G1XUP4; -. DR MEROPS; S08.120; -. DR EnsemblFungi; EGX43093; EGX43093; AOL_s00215g702. DR GeneID; 22899160; -. DR InParanoid; G1XUP4; -. DR OrthoDB; EOG7WT4B5; -. DR Proteomes; UP000008784; Unassembled WGS sequence. DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro. DR Gene3D; 3.30.70.80; -; 1. DR Gene3D; 3.40.50.200; -; 1. DR InterPro; IPR000209; Peptidase_S8/S53_dom. 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; IPR009020; Prot_inh_propept. DR InterPro; IPR010259; S8pro/Inhibitor_I9. DR PANTHER; PTHR10795; PTHR10795; 1. DR Pfam; PF05922; Inhibitor_I9; 1. DR Pfam; PF00082; Peptidase_S8; 1. DR PRINTS; PR00723; SUBTILISIN. DR SUPFAM; SSF52743; SSF52743; 1. DR SUPFAM; SSF54897; SSF54897; 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 Complete proteome {ECO:0000313|Proteomes:UP000008784}; KW Hydrolase {ECO:0000256|RuleBase:RU004261, KW ECO:0000256|SAAS:SAAS00066207}; KW Protease {ECO:0000256|RuleBase:RU004261, KW ECO:0000256|SAAS:SAAS00066236}; KW Reference proteome {ECO:0000313|Proteomes:UP000008784}; KW Serine protease {ECO:0000256|RuleBase:RU004261, KW ECO:0000256|SAAS:SAAS00066164}. 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 //