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Database: UniProt
Entry: A0A0C3JTG4_PISTI
LinkDB: A0A0C3JTG4_PISTI
Original site: A0A0C3JTG4_PISTI 
ID   A0A0C3JTG4_PISTI        Unreviewed;       575 AA.
AC   A0A0C3JTG4;
DT   01-APR-2015, integrated into UniProtKB/TrEMBL.
DT   01-APR-2015, sequence version 1.
DT   16-JAN-2019, entry version 18.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KIO12423.1};
GN   ORFNames=M404DRAFT_125005 {ECO:0000313|EMBL:KIO12423.1};
OS   Pisolithus tinctorius Marx 270.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina;
OC   Agaricomycetes; Agaricomycetidae; Boletales; Sclerodermatineae;
OC   Pisolithaceae; Pisolithus.
OX   NCBI_TaxID=870435 {ECO:0000313|EMBL:KIO12423.1, ECO:0000313|Proteomes:UP000054217};
RN   [1] {ECO:0000313|EMBL:KIO12423.1, ECO:0000313|Proteomes:UP000054217}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Marx 270 {ECO:0000313|EMBL:KIO12423.1,
RC   ECO:0000313|Proteomes:UP000054217};
RG   DOE Joint Genome Institute;
RA   Kuo A., Kohler A., Costa M.D., Nagy L.G., Floudas D., Copeland A.,
RA   Barry K.W., Cichocki N., Veneault-Fourrey C., LaButti K.,
RA   Lindquist E.A., Lipzen A., Lundell T., Morin E., Murat C., Sun H.,
RA   Tunlid A., Henrissat B., Grigoriev I.V., Hibbett D.S., Martin F.,
RA   Nordberg H.P., Cantor M.N., Hua S.X.;
RL   Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000054217}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Marx 270 {ECO:0000313|Proteomes:UP000054217};
RG   DOE Joint Genome Institute;
RG   Mycorrhizal Genomics Consortium;
RA   Kohler A., Kuo A., Nagy L.G., Floudas D., Copeland A., Barry K.W.,
RA   Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A.,
RA   Lipzen A., Lundell T., Morin E., Murat C., Riley R., Ohm R., Sun H.,
RA   Tunlid A., Henrissat B., Grigoriev I.V., Hibbett D.S., Martin F.;
RT   "Evolutionary Origins and Diversification of the Mycorrhizal
RT   Mutualists.";
RL   Submitted (JAN-2015) 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; KN831947; KIO12423.1; -; Genomic_DNA.
DR   EnsemblFungi; KIO12423; KIO12423; M404DRAFT_125005.
DR   OrthoDB; 1294880at2759; -.
DR   Proteomes; UP000054217; 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; 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:UP000054217};
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:UP000054217};
KW   Serine protease {ECO:0000256|PROSITE-ProRule:PRU01032};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     18       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        19    575       {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5002175510.
FT   DOMAIN      197    574       Peptidase S53. {ECO:0000259|PROSITE:
FT                                PS51695}.
FT   ACT_SITE    273    273       Charge relay system.
FT                                {ECO:0000256|PROSITE-ProRule:PRU01032}.
FT   ACT_SITE    277    277       Charge relay system.
FT                                {ECO:0000256|PROSITE-ProRule:PRU01032}.
FT   ACT_SITE    491    491       Charge relay system.
FT                                {ECO:0000256|PROSITE-ProRule:PRU01032}.
FT   METAL       533    533       Calcium. {ECO:0000256|PROSITE-ProRule:
FT                                PRU01032}.
FT   METAL       534    534       Calcium; via carbonyl oxygen.
FT                                {ECO:0000256|PROSITE-ProRule:PRU01032}.
FT   METAL       552    552       Calcium; via carbonyl oxygen.
FT                                {ECO:0000256|PROSITE-ProRule:PRU01032}.
FT   METAL       554    554       Calcium. {ECO:0000256|PROSITE-ProRule:
FT                                PRU01032}.
SQ   SEQUENCE   575 AA;  63263 MW;  535A9A79B0451C82 CRC64;
     MRSLSLLLLH LVVTLANATS YKDCQFKIKE SIVAPPRGWV EHAPAPPNHI LELRIALPQP
     YFPLLEKHLW EVSDPTHKRY GDYLSKEETE VFLAPYPHTV DTVSEWLASY GIYEEHLFRS
     SAQDWVTARV PVSLAEEMLD TKYHIYRHSE TDEYIVRTTS YSLPEVLHEH IQFIQPTTMF
     ARFKAFKSTM HWTTAPSITP TCLRQLYNAV GYETSATNGN QIGITGYLEQ YVNNDDLQQF
     FETYAPAACG SNYTLVSING GQNNQSVAAA GEEADLDSQY AFGLTYPTPG TFYTTAGSPP
     FDPDARTPNN TNEPYSYWLE YVLSAENLPQ TISTSYGDDE QTVPESYANR VCTGFAALGT
     RGVSITFSSG DIGVGDGDSN PETQKCFSND GRNATMFIPA FPAACPYVTT VGGTAYIPET
     AASFSSGGFS NYFSRPSYQD EAVSEYLSKL PPGTYEGLYN PDGRAYPDVS AQSEWFMIAY
     QGKFTYIGGT SASSPTFASI ISMLNDARIS AGKKSLGFLN PWLYSVGYAG LNDITTGNNP
     GCGTEGFNAT TGWDPVTGLG TPNFEKLKDL ALQLP
//
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