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Database: UniProt
Entry: A0A167DFE9_9PEZI
LinkDB: A0A167DFE9_9PEZI
Original site: A0A167DFE9_9PEZI 
ID   A0A167DFE9_9PEZI        Unreviewed;       603 AA.
AC   A0A167DFE9;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   16-JAN-2019, entry version 12.
DE   SubName: Full=Tripeptidyl peptidase a {ECO:0000313|EMBL:KZL83801.1};
GN   ORFNames=CI238_08186 {ECO:0000313|EMBL:KZL83801.1}, CSPAE12_10542
GN   {ECO:0000313|EMBL:OHW90895.1};
OS   Colletotrichum incanum.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
OC   Sordariomycetes; Hypocreomycetidae; Glomerellales; Glomerellaceae;
OC   Colletotrichum.
OX   NCBI_TaxID=1573173 {ECO:0000313|EMBL:KZL83801.1, ECO:0000313|Proteomes:UP000076584};
RN   [1] {ECO:0000313|EMBL:KZL83801.1, ECO:0000313|Proteomes:UP000076584}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MAFF 238704 {ECO:0000313|EMBL:KZL83801.1,
RC   ECO:0000313|Proteomes:UP000076584};
RA   Hacquard S., Kracher B., Hiruma K., Weinman A., Muench P.,
RA   Garrido Oter R., Ver Loren van Themaat E., Dallerey J.-F., Damm U.,
RA   Henrissat B., Lespinet O., Thon M., Kemen E., McHardy A.C.,
RA   Schulze-Lefert P., O'Connell R.J.;
RT   "Survival trade-offs in plant roots during colonization by closely
RT   related pathogenic and mutualistic fungi.";
RL   Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:OHW90895.1, ECO:0000313|Proteomes:UP000179819}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MAFF238712 {ECO:0000313|EMBL:OHW90895.1,
RC   ECO:0000313|Proteomes:UP000179819};
RX   PubMed=27189990; DOI=10.1093/gbe/evw089;
RA   Gan P., Narusaka M., Kumakura N., Tsushima A., Takano Y., Narusaka Y.,
RA   Shirasu K.;
RT   "Genus-Wide Comparative Genome Analyses of Colletotrichum Species
RT   Reveal Specific Gene Family Losses and Gains during Adaptation to
RT   Specific Infection Lifestyles.";
RL   Genome Biol. Evol. 8:1467-1481(2016).
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; LFIW01001066; KZL83801.1; -; Genomic_DNA.
DR   EMBL; KV842145; OHW90895.1; -; Genomic_DNA.
DR   EnsemblFungi; KZL83801; KZL83801; CI238_08186.
DR   EnsemblFungi; OHW90895; OHW90895; CSPAE12_10542.
DR   OrthoDB; 1294880at2759; -.
DR   Proteomes; UP000076584; Unassembled WGS sequence.
DR   Proteomes; UP000179819; 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   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   Complete proteome {ECO:0000313|Proteomes:UP000076584,
KW   ECO:0000313|Proteomes:UP000179819};
KW   Hydrolase {ECO:0000256|PROSITE-ProRule:PRU01032};
KW   Metal-binding {ECO:0000256|PROSITE-ProRule:PRU01032};
KW   Protease {ECO:0000256|PROSITE-ProRule:PRU01032};
KW   Reference proteome {ECO:0000313|Proteomes:UP000076584};
KW   Serine protease {ECO:0000256|PROSITE-ProRule:PRU01032};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     19       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        20    603       {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5007885193.
FT   DOMAIN      207    603       Peptidase S53. {ECO:0000259|PROSITE:
FT                                PS51695}.
FT   ACT_SITE    281    281       Charge relay system.
FT                                {ECO:0000256|PROSITE-ProRule:PRU01032}.
FT   ACT_SITE    285    285       Charge relay system.
FT                                {ECO:0000256|PROSITE-ProRule:PRU01032}.
FT   ACT_SITE    503    503       Charge relay system.
FT                                {ECO:0000256|PROSITE-ProRule:PRU01032}.
FT   METAL       545    545       Calcium. {ECO:0000256|PROSITE-ProRule:
FT                                PRU01032}.
FT   METAL       546    546       Calcium; via carbonyl oxygen.
FT                                {ECO:0000256|PROSITE-ProRule:PRU01032}.
FT   METAL       581    581       Calcium; via carbonyl oxygen.
FT                                {ECO:0000256|PROSITE-ProRule:PRU01032}.
FT   METAL       583    583       Calcium. {ECO:0000256|PROSITE-ProRule:
FT                                PRU01032}.
SQ   SEQUENCE   603 AA;  64491 MW;  2FF94817BE2BD7A8 CRC64;
     MTFLKALVAL AVVFPVIDAR LMSRAANFAQ GVQMVNMAAD DQQISLQIGI KLQNIEKLEP
     MLRDVSDPDS PNYGKYLTAA QVNDMFKPAE ASVAAIQTWL AKENVSDVSY TDGGRFVNFA
     TDVATANRIL GASFAYYDVQ GTMKLRTKEY SVPDAMTQHV ELITPTTYFG STKADPAFTN
     AELPPMPAPL VGRQAPGPGA ATNCSKVFTP TCFELAYNYG AYQADPAAGS RVGFASFLNQ
     SARQDDLTAF LNRFQLPAQK FTSVLVNGGQ DHQDPAGEIG EANLDAQVMA ATVKTLPITQ
     YLTGGKPPLT PNLRSPTQAD NQNEPFLDFY QFMMTQENAQ IPQVLSVSYG DDEQTVPIEY
     ATRVCNLIGM MGLRGVSILE SSGDTGVGAP CRANDASNAP QFTPQFPATC PYITSVGGTQ
     AFGPEITWVA SGSGFSNYFK QAWYQEGAVN QYLQTGISPE TKAYYQPFAN FSGRGFPDIS
     AHSASPPFPI VNANKLVGTG GTSASAPLVA GLVGLLNDAR IRAGQPTMGF MNPWLYKRGF
     KGLTDVNTGV AKGCGGVDLQ SGKPLQGAGV IPFATWNGTQ GWDPVTGLGL PNFEEMKTIA
     LMK
//
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