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Database: UniProt
Entry: R7SNY1_DICSQ
LinkDB: R7SNY1_DICSQ
Original site: R7SNY1_DICSQ 
ID   R7SNY1_DICSQ            Unreviewed;       564 AA.
AC   R7SNY1;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   16-JAN-2019, entry version 30.
DE   SubName: Full=Family S53 protease-like protein {ECO:0000313|EMBL:EJF57638.1};
GN   ORFNames=DICSQDRAFT_157239 {ECO:0000313|EMBL:EJF57638.1};
OS   Dichomitus squalens (strain LYAD-421) (Western red white-rot fungus).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina;
OC   Agaricomycetes; Polyporales; Polyporaceae; Dichomitus.
OX   NCBI_TaxID=732165 {ECO:0000313|EMBL:EJF57638.1};
RN   [1] {ECO:0000313|EMBL:EJF57638.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LYAD-421 SS1 {ECO:0000313|EMBL:EJF57638.1};
RX   PubMed=22745431; DOI=10.1126/science.1221748;
RA   Floudas D., Binder M., Riley R., Barry K., Blanchette R.A.,
RA   Henrissat B., Martinez A.T., Otillar R., Spatafora J.W., Yadav J.S.,
RA   Aerts A., Benoit I., Boyd A., Carlson A., Copeland A., Coutinho P.M.,
RA   de Vries R.P., Ferreira P., Findley K., Foster B., Gaskell J.,
RA   Glotzer D., Gorecki P., Heitman J., Hesse C., Hori C., Igarashi K.,
RA   Jurgens J.A., Kallen N., Kersten P., Kohler A., Kues U., Kumar T.K.,
RA   Kuo A., LaButti K., Larrondo L.F., Lindquist E., Ling A., Lombard V.,
RA   Lucas S., Lundell T., Martin R., McLaughlin D.J., Morgenstern I.,
RA   Morin E., Murat C., Nagy L.G., Nolan M., Ohm R.A., Patyshakuliyeva A.,
RA   Rokas A., Ruiz-Duenas F.J., Sabat G., Salamov A., Samejima M.,
RA   Schmutz J., Slot J.C., St John F., Stenlid J., Sun H., Sun S.,
RA   Syed K., Tsang A., Wiebenga A., Young D., Pisabarro A., Eastwood D.C.,
RA   Martin F., Cullen D., Grigoriev I.V., Hibbett D.S.;
RT   "The Paleozoic origin of enzymatic lignin decomposition reconstructed
RT   from 31 fungal genomes.";
RL   Science 336:1715-1719(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; JH719447; EJF57638.1; -; Genomic_DNA.
DR   RefSeq; XP_007369610.1; XM_007369548.1.
DR   EnsemblFungi; EJF57638; EJF57638; DICSQDRAFT_157239.
DR   GeneID; 18837744; -.
DR   KEGG; dsq:DICSQDRAFT_157239; -.
DR   KO; K01279; -.
DR   OMA; QVHETRE; -.
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; 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.
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   ECO:0000313|EMBL:EJF57638.1};
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    564       {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5004444301.
FT   DOMAIN      208    564       Peptidase S53. {ECO:0000259|PROSITE:
FT                                PS51695}.
FT   ACT_SITE    284    284       Charge relay system.
FT                                {ECO:0000256|PROSITE-ProRule:PRU01032}.
FT   ACT_SITE    288    288       Charge relay system.
FT                                {ECO:0000256|PROSITE-ProRule:PRU01032}.
FT   ACT_SITE    480    480       Charge relay system.
FT                                {ECO:0000256|PROSITE-ProRule:PRU01032}.
FT   METAL       523    523       Calcium. {ECO:0000256|PROSITE-ProRule:
FT                                PRU01032}.
FT   METAL       524    524       Calcium; via carbonyl oxygen.
FT                                {ECO:0000256|PROSITE-ProRule:PRU01032}.
FT   METAL       542    542       Calcium; via carbonyl oxygen.
FT                                {ECO:0000256|PROSITE-ProRule:PRU01032}.
FT   METAL       544    544       Calcium. {ECO:0000256|PROSITE-ProRule:
FT                                PRU01032}.
SQ   SEQUENCE   564 AA;  58444 MW;  4461B41ACFA33D6E CRC64;
     MFSKALVVIC FAAVALGKPV ARSLQVHETR EQVPAAFSLA GPASPDTMLN LRIALVSSDM
     AGLEKALYDV STPGSALYGQ HLSKEEVEQF VAPTSETVDA VTSWLKENDV EAAKASPAGD
     WLSISIPVSK ANELFDANFS VFTHSKTGTQ SIRTLTYSIP TDLKNKLDFV HPTTVFAQPF
     SGPQFHTPIL TPAVNVTSDA VPSSCGSTIT PACLQALYGI PTTSNAISSN VLGVSGFIDQ
     FAQKADLKSF LSRLRTDLPS TTTFTLQTLD GGENPQSASD AGIEANLDIQ YTVGVASKVP
     VNFISVGDNN QDGINGFLDI IQFLLNESTP PTVLTTSYGF NEPDLTSSVA NNLCNAYMQL
     GARGTSILFA SGDGGVSGSQ SQSCTTFIPT FPSGCPFLTS VGATTGITET AADFSSGGFS
     AIFSQPSYQS SAVSTYLTAL GSTNSGKFTK TGRAFPDVSA QGENVEIADG GEFGTVDGTS
     CSSPIFASVI ALLNDNRAAA GKAPLGFLNP FLYSAAGTAA LNDVTTGSNP GCNTNGFPAK
     AGWDPVTGLG TPNFAKLLSA TANL
//
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