ID   K2S0E3_MACPH            Unreviewed;       641 AA.
AC   K2S0E3;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   18-JAN-2017, entry version 20.
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   -!- 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   -!- SIMILARITY: Contains 1 peptidase S53 domain. {ECO:0000256|PROSITE-
CC       ProRule:PRU01032}.
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; EOG092C24LG; -.
DR   Proteomes; UP000007129; Unassembled WGS sequence.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   CDD; cd04056; Peptidases_S53; 1.
DR   CDD; cd11377; Pro-peptidase_S53; 1.
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   Calcium {ECO:0000256|PROSITE-ProRule:PRU01032};
KW   Complete proteome {ECO:0000313|Proteomes:UP000007129};
KW   Hydrolase {ECO:0000256|PROSITE-ProRule:PRU01032,
KW   ECO:0000256|SAAS:SAAS00066207};
KW   Metal-binding {ECO:0000256|PROSITE-ProRule:PRU01032};
KW   Protease {ECO:0000256|PROSITE-ProRule:PRU01032,
KW   ECO:0000256|SAAS:SAAS00066236};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007129};
KW   Serine protease {ECO:0000256|PROSITE-ProRule:PRU01032,
KW   ECO:0000256|SAAS:SAAS00066164}; 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}.
FT   ACT_SITE    293    293       Charge relay system.
FT                                {ECO:0000256|PROSITE-ProRule:PRU01032}.
FT   ACT_SITE    297    297       Charge relay system.
FT                                {ECO:0000256|PROSITE-ProRule:PRU01032}.
FT   ACT_SITE    558    558       Charge relay system.
FT                                {ECO:0000256|PROSITE-ProRule:PRU01032}.
FT   METAL       599    599       Calcium. {ECO:0000256|PROSITE-ProRule:
FT                                PRU01032}.
FT   METAL       600    600       Calcium; via carbonyl oxygen.
FT                                {ECO:0000256|PROSITE-ProRule:PRU01032}.
FT   METAL       618    618       Calcium; via carbonyl oxygen.
FT                                {ECO:0000256|PROSITE-ProRule:PRU01032}.
FT   METAL       620    620       Calcium. {ECO:0000256|PROSITE-ProRule:
FT                                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
//