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Database: UniProt
Entry: N4VVW3_COLOR
LinkDB: N4VVW3_COLOR
Original site: N4VVW3_COLOR 
ID   N4VVW3_COLOR            Unreviewed;       585 AA.
AC   N4VVW3;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   05-JUN-2019, entry version 23.
DE   SubName: Full=Tripeptidyl peptidase {ECO:0000313|EMBL:ENH88122.1};
GN   ORFNames=Cob_03765 {ECO:0000313|EMBL:ENH88122.1};
OS   Colletotrichum orbiculare (strain 104-T / ATCC 96160 / CBS 514.97 /
OS   LARS 414 / MAFF 240422) (Cucumber anthracnose fungus) (Colletotrichum
OS   lagenarium).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
OC   Sordariomycetes; Hypocreomycetidae; Glomerellales; Glomerellaceae;
OC   Colletotrichum.
OX   NCBI_TaxID=1213857 {ECO:0000313|EMBL:ENH88122.1};
RN   [1] {ECO:0000313|EMBL:ENH88122.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=MAFF 240422 {ECO:0000313|EMBL:ENH88122.1};
RA   Gan P., Ikeda K., Irieda H., Narusaka M., O'Connell R.J., Narusaka Y.,
RA   Takano Y., Kubo Y., Shirasu K.;
RT   "Genome analysis of Colletotrichum orbiculare and Colletotrichum
RT   gloeosporioides.";
RL   Submitted (AUG-2012) to the EMBL/GenBank/DDBJ databases.
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; KB725671; ENH88122.1; -; Genomic_DNA.
DR   MEROPS; S53.010; -.
DR   EnsemblFungi; ENH88122; ENH88122; Cob_03765.
DR   OrthoDB; 1294880at2759; -.
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   Gene3D; 3.40.50.200; -; 1.
DR   InterPro; IPR000209; Peptidase_S8/S53_dom.
DR   InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR   InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR   InterPro; IPR015366; S53_propep.
DR   InterPro; IPR030400; Sedolisin_dom.
DR   Pfam; PF00082; Peptidase_S8; 1.
DR   Pfam; PF09286; Pro-kuma_activ; 1.
DR   SMART; SM00944; Pro-kuma_activ; 1.
DR   SUPFAM; SSF52743; SSF52743; 1.
DR   PROSITE; PS51695; SEDOLISIN; 1.
DR   PROSITE; PS00138; SUBTILASE_SER; 1.
PE   4: Predicted;
KW   Calcium {ECO:0000256|PROSITE-ProRule:PRU01032};
KW   Hydrolase {ECO:0000256|PROSITE-ProRule:PRU01032};
KW   Metal-binding {ECO:0000256|PROSITE-ProRule:PRU01032};
KW   Protease {ECO:0000256|PROSITE-ProRule:PRU01032};
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    585       {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5004123559.
FT   DOMAIN      203    585       Peptidase S53. {ECO:0000259|PROSITE:
FT                                PS51695}.
FT   REGION      306    325       Disordered. {ECO:0000256|MobiDB-lite:
FT                                N4VVW3}.
FT   ACT_SITE    283    283       Charge relay system.
FT                                {ECO:0000256|PROSITE-ProRule:PRU01032}.
FT   ACT_SITE    287    287       Charge relay system.
FT                                {ECO:0000256|PROSITE-ProRule:PRU01032}.
FT   ACT_SITE    498    498       Charge relay system.
FT                                {ECO:0000256|PROSITE-ProRule:PRU01032}.
FT   METAL       541    541       Calcium. {ECO:0000256|PROSITE-ProRule:
FT                                PRU01032}.
FT   METAL       542    542       Calcium; via carbonyl oxygen.
FT                                {ECO:0000256|PROSITE-ProRule:PRU01032}.
FT   METAL       565    565       Calcium; via carbonyl oxygen.
FT                                {ECO:0000256|PROSITE-ProRule:PRU01032}.
FT   METAL       567    567       Calcium. {ECO:0000256|PROSITE-ProRule:
FT                                PRU01032}.
SQ   SEQUENCE   585 AA;  63608 MW;  C78B7346E42059CB CRC64;
     MMRSSWAALL LSGFALGQPT NGGHVLHESV AQLPQGWRRV AAADNVLAVK LSIALKQPGL
     SELKARLEVT SDPSHVEYGS HVSRDVMKRF QEPAAAAYDA VSSWLQAYDI QDYSLDGAWV
     RLNTTVGKAN RLLDCKFAEY QFDDETPVLR ATEYYLPTRV SDLVDFVYPV SQFVNKPPRR
     RDTIEESVKV KRQSTMPQSC WSYTTPDCIV DLYNITYFPP DGPSPTEFGI AGFLEEYPNV
     PTLQNFLASY SPQRNRTGFT PKYDLAVESV NGGNATTEGG GVEALLDIQY SMPFIQPMNA
     TYFSTGGRGP EVDEQGAEKP AGESGNEPWI EFLEALLARE SIPHVISVSY TDDEQMVPLP
     YARRVCDLFM QVAARGVSVV VASGDGGAGS TAGKQCVSND GNKTSKFIPT FPVDCPYVTS
     VGATGNYAPA EPAWYSSGGF SEYFERPAWQ DAQARAYIER INGSHAGWYA PGGRGIPDIS
     AIGSRFLMQP GWTQKGTSAS TPVVAAMIAL ANDKRMRQGK PSLGFLNPLL YSDKVRAAID
     DVKSGSSGSC AIGDQIETGW EATEGWDPAT GLGTLNFAKF IEALE
//
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