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Database: UniProt
Entry: R7SQ21_DICSQ
LinkDB: R7SQ21_DICSQ
Original site: R7SQ21_DICSQ 
ID   R7SQ21_DICSQ            Unreviewed;       642 AA.
AC   R7SQ21;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   08-MAY-2019, entry version 32.
DE   SubName: Full=Subtilisin-like protein {ECO:0000313|EMBL:EJF57850.1};
GN   ORFNames=DICSQDRAFT_149462 {ECO:0000313|EMBL:EJF57850.1};
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:EJF57850.1};
RN   [1] {ECO:0000313|EMBL:EJF57850.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LYAD-421 SS1 {ECO:0000313|EMBL:EJF57850.1};
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; JH719443; EJF57850.1; -; Genomic_DNA.
DR   RefSeq; XP_007369347.1; XM_007369285.1.
DR   MEROPS; S53.007; -.
DR   EnsemblFungi; EJF57850; EJF57850; DICSQDRAFT_149462.
DR   GeneID; 18836837; -.
DR   KEGG; dsq:DICSQDRAFT_149462; -.
DR   KO; K01279; -.
DR   OMA; FPGGCPW; -.
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   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   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     18       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        19    642       {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5004444272.
FT   DOMAIN      230    641       Peptidase S53. {ECO:0000259|PROSITE:
FT                                PS51695}.
FT   ACT_SITE    307    307       Charge relay system.
FT                                {ECO:0000256|PROSITE-ProRule:PRU01032}.
FT   ACT_SITE    311    311       Charge relay system.
FT                                {ECO:0000256|PROSITE-ProRule:PRU01032}.
FT   ACT_SITE    557    557       Charge relay system.
FT                                {ECO:0000256|PROSITE-ProRule:PRU01032}.
FT   METAL       600    600       Calcium. {ECO:0000256|PROSITE-ProRule:
FT                                PRU01032}.
FT   METAL       601    601       Calcium; via carbonyl oxygen.
FT                                {ECO:0000256|PROSITE-ProRule:PRU01032}.
FT   METAL       619    619       Calcium; via carbonyl oxygen.
FT                                {ECO:0000256|PROSITE-ProRule:PRU01032}.
FT   METAL       621    621       Calcium. {ECO:0000256|PROSITE-ProRule:
FT                                PRU01032}.
SQ   SEQUENCE   642 AA;  68988 MW;  303501D9B7F21EC9 CRC64;
     MRLFSLTWAF ALATLAIAAP SITRRSNLVV HEKRAQEPRD WVLTRRLEPS AVLPMRFGLT
     QSNLHKVEEM LMSVSHPSSP TYGQHFTAKE IVDTFAPSTD TIERVVEWLT DSGIDRSRLK
     LSKSKGWIEV DATVEEAETL INAEYHVYTH PETGAQQIGC HSYSVPEDIR EHIDLIKPTV
     HFLHRVPTPN QLRKRSFERP STHIKQGPKL KADTSPLATV PQDLSTCDEE ITLDCLRALY
     SIDYTPVSTD TNTFGILEFT PQAFLQSDLD MFFANFSPSQ VGTAPILISI DGGVDQTDDT
     GFDFNGESDL DLQYAFGLTN PQPILLLQTG DLVEGASFDN WLDAVDASFC TFEGGDDPTQ
     DGIYPDPLPG GFNGPASCGI LTPPFVTSTS YGQDEASVTA AYAQRQCTEY AKLGMLGTTV
     LYSSGDDGVA GGGGVCLDGN GQPARRGGVQ FNPDFPVTCP FVTGVGATQI NPGSTVNDPE
     GACEQVIFSG GGFSNFFEMP DYQATAVTSF LTNHPPPFTG EQFNNSGVAR GFPDLSANGL
     VHVLPVAGEF ELVFGTSCSS PVVGSMITLI NDARIAAGKG PVGFINPAIY TDEFQAAFND
     ITTGGNQGCG TPGFTATEGW DPVTGVGTPN LSKLMPLFLA LP
//
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