ID K2S0E3_MACPH Unreviewed; 641 AA. AC K2S0E3; DT 28-NOV-2012, integrated into UniProtKB/TrEMBL. DT 28-NOV-2012, sequence version 1. DT 06-JUL-2016, entry version 18. DE SubName: Full=Peptidase S8/S53 subtilisin/kexin/sedolisin {ECO:0000313|EMBL:EKG10175.1}; GN ORFNames=MPH_12775 {ECO:0000313|EMBL:EKG10175.1}; OS Macrophomina phaseolina (strain MS6) (Charcoal rot fungus). OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; OC Dothideomycetes; Dothideomycetes incertae sedis; Botryosphaeriales; OC Botryosphaeriaceae; Macrophomina. OX NCBI_TaxID=1126212 {ECO:0000313|EMBL:EKG10175.1, ECO:0000313|Proteomes:UP000007129}; RN [1] {ECO:0000313|EMBL:EKG10175.1, ECO:0000313|Proteomes:UP000007129} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MS6 {ECO:0000313|EMBL:EKG10175.1, RC ECO:0000313|Proteomes:UP000007129}; RX PubMed=22992219; DOI=10.1186/1471-2164-13-493; RA Islam M.S., Haque M.S., Islam M.M., Emdad E.M., Halim A., RA Hossen Q.M.M., Hossain M.Z., Ahmed B., Rahim S., Rahman M.S., RA Alam M.M., Hou S., Wan X., Saito J.A., Alam M.; RT "Tools to kill: Genome of one of the most destructive plant pathogenic RT fungi Macrophomina phaseolina."; RL BMC Genomics 13:493-493(2012). 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:EKG10175.1}. 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; AHHD01000526; EKG10175.1; -; Genomic_DNA. DR ProteinModelPortal; K2S0E3; -. DR MEROPS; S53.007; -. DR EnsemblFungi; EKG10175; EKG10175; MPH_12775. DR InParanoid; K2S0E3; -. DR OrthoDB; EOG783N4W; -. DR Proteomes; UP000007129; Unassembled WGS sequence. DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro. DR Gene3D; 3.40.50.200; -; 1. DR InterPro; IPR000209; Peptidase_S8/S53_dom. DR InterPro; IPR009020; Propept_inh. DR InterPro; IPR015366; S53_propep. DR InterPro; IPR030400; Sedolisin_dom. DR Pfam; PF09286; Pro-kuma_activ; 1. DR SMART; SM00944; Pro-kuma_activ; 1. DR SUPFAM; SSF52743; SSF52743; 2. DR SUPFAM; SSF54897; SSF54897; 1. DR PROSITE; PS51695; SEDOLISIN; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000007129}; KW Hydrolase {ECO:0000256|SAAS:SAAS00449563}; KW Protease {ECO:0000256|SAAS:SAAS00449536}; KW Reference proteome {ECO:0000313|Proteomes:UP000007129}; KW Serine protease {ECO:0000256|SAAS:SAAS00449573}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 18 {ECO:0000256|SAM:SignalP}. FT CHAIN 19 641 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5003867203. FT DOMAIN 214 640 Peptidase S53. {ECO:0000259|PROSITE: FT PS51695}. SQ SEQUENCE 641 AA; 70247 MW; 2082D4A511680189 CRC64; MRASFFLGIA ACCRLIAAAP SSPGHFVVHE KRNSHPHEWT KRDRAHGDQI LPIRIGLQQR NLHLADEYLQ DVSDPASPNF GKHWSAEKVA KTFAPSREAT NSVTKWLQES GIDTSRITYS AGRNWVQFNG TVDEAERLFN TQYHFFEHKE TGGYRIACDE YHLPQHIQQH VDFAMPTIQL DGLRPVANLN IAHAAALTPL NLTGLTGTQN CDRLITIDCL RALYKFSFLN SSIAGNEMGI GEWADYLYNP DLVPFFEHWT SPKIPSDTVP EFISIDGGKP SNITQAEAGT VIESALDFQT AYSIIWPQKL RLYQVGDGVN VDSVGTFNIF LDALDASYCT YEGGDAPYVD PAYPDPNLGG YTGPLQCGGA PISNVYSFSY NQIEAALPEF YQRRQCNEWM KLGLQGVSVL FASGDSGVAN RYNAGYENSC LNADELYVDV NGTRFSPAFP CNCPYVTVVG ATQLLDGTIE GGERAVSDPD KTNPKEDYYS GGGFSNIFSL PSYQKDAVNG YLQNYPPPYD SKTYNNSGTS RAYPDVAALG LNITTVYLNR TYGVGGTSAS TPIVASLVNL LNEERYQAGK GPVGFLNPIF YAHPEAFNDV TVGANPGCGT DGFAAQPGWD PVTGLGTPDY QKLKKIFLDL P //