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Database: UniProt
Entry: B0CPZ8_LACBS
LinkDB: B0CPZ8_LACBS
Original site: B0CPZ8_LACBS 
ID   B0CPZ8_LACBS            Unreviewed;       651 AA.
AC   B0CPZ8;
DT   26-FEB-2008, integrated into UniProtKB/TrEMBL.
DT   26-FEB-2008, sequence version 1.
DT   08-MAY-2019, entry version 47.
DE   SubName: Full=Predicted protein {ECO:0000313|EMBL:EDR15501.1};
GN   ORFNames=LACBIDRAFT_301946 {ECO:0000313|EMBL:EDR15501.1};
OS   Laccaria bicolor (strain S238N-H82 / ATCC MYA-4686) (Bicoloured
OS   deceiver) (Laccaria laccata var. bicolor).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina;
OC   Agaricomycetes; Agaricomycetidae; Agaricales; Tricholomataceae;
OC   Laccaria.
OX   NCBI_TaxID=486041 {ECO:0000313|Proteomes:UP000001194};
RN   [1] {ECO:0000313|EMBL:EDR15501.1, ECO:0000313|Proteomes:UP000001194}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S238N-H82 / ATCC MYA-4686 {ECO:0000313|Proteomes:UP000001194};
RX   PubMed=18322534; DOI=10.1038/nature06556;
RA   Martin F., Aerts A., Ahren D., Brun A., Danchin E.G.J., Duchaussoy F.,
RA   Gibon J., Kohler A., Lindquist E., Pereda V., Salamov A.,
RA   Shapiro H.J., Wuyts J., Blaudez D., Buee M., Brokstein P.,
RA   Canbaeck B., Cohen D., Courty P.E., Coutinho P.M., Delaruelle C.,
RA   Detter J.C., Deveau A., DiFazio S., Duplessis S.,
RA   Fraissinet-Tachet L., Lucic E., Frey-Klett P., Fourrey C.,
RA   Feussner I., Gay G., Grimwood J., Hoegger P.J., Jain P., Kilaru S.,
RA   Labbe J., Lin Y.C., Legue V., Le Tacon F., Marmeisse R., Melayah D.,
RA   Montanini B., Muratet M., Nehls U., Niculita-Hirzel H.,
RA   Oudot-Le Secq M.P., Peter M., Quesneville H., Rajashekar B., Reich M.,
RA   Rouhier N., Schmutz J., Yin T., Chalot M., Henrissat B., Kuees U.,
RA   Lucas S., Van de Peer Y., Podila G.K., Polle A., Pukkila P.J.,
RA   Richardson P.M., Rouze P., Sanders I.R., Stajich J.E., Tunlid A.,
RA   Tuskan G., Grigoriev I.V.;
RT   "The genome of Laccaria bicolor provides insights into mycorrhizal
RT   symbiosis.";
RL   Nature 452:88-92(2008).
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; DS547091; EDR15501.1; -; Genomic_DNA.
DR   RefSeq; XP_001873709.1; XM_001873674.1.
DR   MEROPS; S53.007; -.
DR   EnsemblFungi; EDR15501; EDR15501; LACBIDRAFT_301946.
DR   GeneID; 6068982; -.
DR   KEGG; lbc:LACBIDRAFT_301946; -.
DR   eggNOG; ENOG410IFW0; Eukaryota.
DR   eggNOG; COG4934; LUCA.
DR   InParanoid; B0CPZ8; -.
DR   KO; K01279; -.
DR   OrthoDB; 1294880at2759; -.
DR   Proteomes; UP000001194; 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; 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   Complete proteome {ECO:0000313|Proteomes:UP000001194};
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:UP000001194};
KW   Serine protease {ECO:0000256|PROSITE-ProRule:PRU01032};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     16       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        17    651       {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5002746891.
FT   DOMAIN      221    650       Peptidase S53. {ECO:0000259|PROSITE:
FT                                PS51695}.
FT   ACT_SITE    298    298       Charge relay system.
FT                                {ECO:0000256|PROSITE-ProRule:PRU01032}.
FT   ACT_SITE    302    302       Charge relay system.
FT                                {ECO:0000256|PROSITE-ProRule:PRU01032}.
FT   ACT_SITE    566    566       Charge relay system.
FT                                {ECO:0000256|PROSITE-ProRule:PRU01032}.
FT   METAL       609    609       Calcium. {ECO:0000256|PROSITE-ProRule:
FT                                PRU01032}.
FT   METAL       610    610       Calcium; via carbonyl oxygen.
FT                                {ECO:0000256|PROSITE-ProRule:PRU01032}.
FT   METAL       628    628       Calcium; via carbonyl oxygen.
FT                                {ECO:0000256|PROSITE-ProRule:PRU01032}.
FT   METAL       630    630       Calcium. {ECO:0000256|PROSITE-ProRule:
FT                                PRU01032}.
SQ   SEQUENCE   651 AA;  71573 MW;  48BD999D6AB09C10 CRC64;
     MRSSLILLCL LGSALSAPQS FTHVVHERRT AEPMDWVSSR RLERDFMVPM RIGLTQNNLH
     SLGDMLMAVS QPDSPDYGNH WTATDLVKTF APSTETIDEV SKWLVESGIA RDRLHLSLDQ
     GWIQVNATAV EVEELLKTEY YVFTHPSGQE QISCSDYSVP DHVQSHIDLI IPTVHFSSRP
     TTMAHRKRYG GVGSPDVKNG PFRSDQAITL EKSDLQNCDK YITLDCLRVL YGIKYKPRAT
     RRNSFGIVEF TPQSYIPSDL DLFFKNFVPN LVGSRPKLES IDGGMLQFNM TGFDYNGESN
     LDLEYAMGLV NPQKVTLLQT GDEIVGASFN TWLDAVDGTY CTHKGGDDPN FDPVYPHGPP
     GYTGPKACGI IKPPHVISIS YGYNEVDLTR KYAQRQCNEY GKVFSKPIIT GMFSLTTSML
     QLGLMGSSVF YSSGDNGVAG NGNQCVNPST GQLDPKGTVF TPSFPGGCPW VTSVGATQIN
     PGSSVYAPES ACEQVIFSGG GFSNYFSIPD YQCEQVDHYL KKHTSQYTSA QFNNSGSARA
     FPDVAANGAN YVVAINGEFY LVYGTSASSP VFASMISMIN DARIHMGRKP VGFINPMIYS
     HKFKSAFNDI TTGNNPGCGT QGFSATKGWD PVTGLGTPRF QQLLEMFKRL P
//
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