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Database: UniProt
Entry: K1WRC4_MARBU
LinkDB: K1WRC4_MARBU
Original site: K1WRC4_MARBU 
ID   K1WRC4_MARBU            Unreviewed;       674 AA.
AC   K1WRC4;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   08-MAY-2019, entry version 32.
DE   SubName: Full=Alkaline serine protease {ECO:0000313|EMBL:EKD20175.1};
GN   ORFNames=MBM_02127 {ECO:0000313|EMBL:EKD20175.1};
OS   Marssonina brunnea f. sp. multigermtubi (strain MB_m1) (Marssonina
OS   leaf spot fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Dermateaceae; Marssonina.
OX   NCBI_TaxID=1072389 {ECO:0000313|EMBL:EKD20175.1, ECO:0000313|Proteomes:UP000006753};
RN   [1] {ECO:0000313|EMBL:EKD20175.1, ECO:0000313|Proteomes:UP000006753}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MB_m1 {ECO:0000313|EMBL:EKD20175.1,
RC   ECO:0000313|Proteomes:UP000006753};
RX   PubMed=22876864; DOI=10.1186/1471-2164-13-382;
RA   Zhu S., Cao Y.-Z., Jiang C., Tan B.-Y., Wang Z., Feng S., Zhang L.,
RA   Su X.-H., Brejova B., Vinar T., Xu M., Wang M.-X., Zhang S.-G.,
RA   Huang M.-R., Wu R., Zhou Y.;
RT   "Sequencing the genome of Marssonina brunnea reveals fungus-poplar co-
RT   evolution.";
RL   BMC Genomics 13:382-382(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};
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DR   EMBL; JH921430; EKD20175.1; -; Genomic_DNA.
DR   RefSeq; XP_007290016.1; XM_007289954.1.
DR   EnsemblFungi; EKD20175; EKD20175; MBM_02127.
DR   GeneID; 18758062; -.
DR   KEGG; mbe:MBM_02127; -.
DR   InParanoid; K1WRC4; -.
DR   KO; K01279; -.
DR   OrthoDB; 1294880at2759; -.
DR   Proteomes; UP000006753; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR   CDD; cd04056; Peptidases_S53; 1.
DR   CDD; cd11377; Pro-peptidase_S53; 1.
DR   InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
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; 1.
DR   PROSITE; PS51695; SEDOLISIN; 1.
PE   4: Predicted;
KW   Calcium {ECO:0000256|PROSITE-ProRule:PRU01032};
KW   Complete proteome {ECO:0000313|Proteomes:UP000006753};
KW   Hydrolase {ECO:0000256|PROSITE-ProRule:PRU01032};
KW   Metal-binding {ECO:0000256|PROSITE-ProRule:PRU01032};
KW   Protease {ECO:0000256|PROSITE-ProRule:PRU01032,
KW   ECO:0000313|EMBL:EKD20175.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006753};
KW   Serine protease {ECO:0000256|PROSITE-ProRule:PRU01032};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     17       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        18    674       {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5003852674.
FT   DOMAIN      237    674       Peptidase S53. {ECO:0000259|PROSITE:
FT                                PS51695}.
FT   ACT_SITE    317    317       Charge relay system.
FT                                {ECO:0000256|PROSITE-ProRule:PRU01032}.
FT   ACT_SITE    321    321       Charge relay system.
FT                                {ECO:0000256|PROSITE-ProRule:PRU01032}.
FT   ACT_SITE    592    592       Charge relay system.
FT                                {ECO:0000256|PROSITE-ProRule:PRU01032}.
FT   METAL       633    633       Calcium. {ECO:0000256|PROSITE-ProRule:
FT                                PRU01032}.
FT   METAL       634    634       Calcium; via carbonyl oxygen.
FT                                {ECO:0000256|PROSITE-ProRule:PRU01032}.
FT   METAL       652    652       Calcium; via carbonyl oxygen.
FT                                {ECO:0000256|PROSITE-ProRule:PRU01032}.
FT   METAL       654    654       Calcium. {ECO:0000256|PROSITE-ProRule:
FT                                PRU01032}.
SQ   SEQUENCE   674 AA;  73889 MW;  08281D50108B6274 CRC64;
     MLVSLSAIVA VWAGGLALEV TASPLSYSGR KKRAIPASHS LHERHLPSWE HQWSKKSRVP
     DTQILPVRIG LKQSNLEAGH DKLMEISTPG TETYGKHMTA EEIIEFFAPH QSSTEVVSEW
     LLSSGISSDR IGVSTNRQWI QFDANAAEVE TLLFAEFYLW EHRSGVHDIS TKEYHVPTHV
     REHIDYVTPG TRLRERKITA GEGNEVFKRF ESTVSARPLV TKLPGFPNPN SSVCDIYVTA
     PCTQVQYEMC NATKASPGNK LGIFESLDVH YSKKDLDIYY SSLYPNIPNG TYPEERLIDG
     AIGATEDSTI FVPIDLESGL DFNSAQPLIY PQELVLFQVD DEYYESTGNF SGFWNTFLDA
     IDGSYCTYSA YGETGDCTEE ACRDPSYPNL NPGGYTGQLQ CGVYKPTNVI SISYGATEAD
     LPDFYLKRQC NEWMKLALQG VTVVMSSGDA GVGGSICNGY SGRIFDPDFA STCPYVLSVG
     STEWDRFNAS VNPTPGQKLH EVATKRFPSG GGFSNVFGIP SYQRTAVQAY WDQKESSLGF
     RGYHHHVENG NFSSVTGGLY HHGGRGYPDV GAVGDRQVVY SNGSWWLVGG TSLSAPVWGA
     VLNLINEERI AAGKGTVGFI HPILYQHPEV FTDITVGSNP GCGSAGFPTA EGWDPVTGLG
     SPIFPKLLEL LMSI
//
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