ID K2S0E3_MACPH Unreviewed; 641 AA. AC K2S0E3; DT 28-NOV-2012, integrated into UniProtKB/TrEMBL. DT 28-NOV-2012, sequence version 1. DT 27-NOV-2024, entry version 42. DE RecName: Full=tripeptidyl-peptidase II {ECO:0000256|ARBA:ARBA00012462}; DE EC=3.4.14.10 {ECO:0000256|ARBA:ARBA00012462}; GN ORFNames=MPH_12775 {ECO:0000313|EMBL:EKG10175.1}; OS Macrophomina phaseolina (strain MS6) (Charcoal rot fungus). OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes; OC Dothideomycetes incertae sedis; Botryosphaeriales; Botryosphaeriaceae; OC 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., Hossen Q.M.M., RA Hossain M.Z., Ahmed B., Rahim S., Rahman M.S., Alam M.M., Hou S., Wan X., RA 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 -!- FUNCTION: Secreted tripeptidyl-peptidase which degrades proteins at CC acidic pHs and is involved in virulence. CC {ECO:0000256|ARBA:ARBA00002451}. CC -!- CATALYTIC ACTIVITY: CC Reaction=Release of an N-terminal tripeptide from a polypeptide.; CC EC=3.4.14.10; Evidence={ECO:0000256|ARBA:ARBA00001910}; CC -!- COFACTOR: CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; CC Evidence={ECO:0000256|PROSITE-ProRule:PRU01032}; CC Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000256|PROSITE- CC ProRule:PRU01032}; CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space CC {ECO:0000256|ARBA:ARBA00004239}. 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: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 AlphaFoldDB; K2S0E3; -. DR STRING; 1126212.K2S0E3; -. DR MEROPS; S53.007; -. DR VEuPathDB; FungiDB:MPH_12775; -. DR eggNOG; ENOG502QTN1; Eukaryota. DR HOGENOM; CLU_013783_4_0_1; -. DR InParanoid; K2S0E3; -. DR OrthoDB; 1405251at2759; -. DR Proteomes; UP000007129; Unassembled WGS sequence. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule. DR GO; GO:0008240; F:tripeptidyl-peptidase activity; IEA:TreeGrafter. DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW. DR CDD; cd04056; Peptidases_S53; 1. DR CDD; cd11377; Pro-peptidase_S53; 1. DR FunFam; 3.40.50.200:FF:000015; Tripeptidyl peptidase A; 1. DR Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1. DR InterPro; IPR000209; Peptidase_S8/S53_dom. DR InterPro; IPR036852; Peptidase_S8/S53_dom_sf. DR InterPro; IPR015366; S53_propep. DR InterPro; IPR030400; Sedolisin_dom. DR InterPro; IPR050819; Tripeptidyl-peptidase_I. DR PANTHER; PTHR14218; PROTEASE S8 TRIPEPTIDYL PEPTIDASE I CLN2; 1. DR PANTHER; PTHR14218:SF19; SERINE PROTEASE AORO, PUTATIVE (AFU_ORTHOLOGUE AFUA_6G10250)-RELATED; 1. DR Pfam; PF00082; Peptidase_S8; 1. DR Pfam; PF09286; Pro-kuma_activ; 1. DR SMART; SM00944; Pro-kuma_activ; 1. DR SUPFAM; SSF54897; Protease propeptides/inhibitors; 1. DR SUPFAM; SSF52743; Subtilisin-like; 1. DR PROSITE; PS51695; SEDOLISIN; 1. PE 4: Predicted; KW Calcium {ECO:0000256|ARBA:ARBA00022837, ECO:0000256|PROSITE- KW ProRule:PRU01032}; Hydrolase {ECO:0000256|PROSITE-ProRule:PRU01032}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE- KW ProRule:PRU01032}; Protease {ECO:0000256|PROSITE-ProRule:PRU01032}; KW Reference proteome {ECO:0000313|Proteomes:UP000007129}; KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE- KW ProRule:PRU01032}; Signal {ECO:0000256|SAM:SignalP}; KW Zymogen {ECO:0000256|ARBA:ARBA00023145}. FT SIGNAL 1..18 FT /evidence="ECO:0000256|SAM:SignalP" FT CHAIN 19..641 FT /note="tripeptidyl-peptidase II" FT /evidence="ECO:0000256|SAM:SignalP" FT /id="PRO_5003867203" FT DOMAIN 214..640 FT /note="Peptidase S53" FT /evidence="ECO:0000259|PROSITE:PS51695" FT ACT_SITE 293 FT /note="Charge relay system" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01032" FT ACT_SITE 297 FT /note="Charge relay system" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01032" FT ACT_SITE 558 FT /note="Charge relay system" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01032" FT BINDING 599 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01032" FT BINDING 600 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01032" FT BINDING 618 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01032" FT BINDING 620 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01032" 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 //