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Database: UniProt
Entry: M2QTD6_CERS8
LinkDB: M2QTD6_CERS8
Original site: M2QTD6_CERS8 
ID   M2QTD6_CERS8            Unreviewed;       652 AA.
AC   M2QTD6;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   05-JUN-2019, entry version 26.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EMD35310.1};
GN   ORFNames=CERSUDRAFT_116113 {ECO:0000313|EMBL:EMD35310.1};
OS   Ceriporiopsis subvermispora (strain B) (White-rot fungus) (Gelatoporia
OS   subvermispora).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina;
OC   Agaricomycetes; Polyporales; Gelatoporiaceae; Gelatoporia.
OX   NCBI_TaxID=914234 {ECO:0000313|EMBL:EMD35310.1, ECO:0000313|Proteomes:UP000016930};
RN   [1] {ECO:0000313|EMBL:EMD35310.1, ECO:0000313|Proteomes:UP000016930}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B {ECO:0000313|EMBL:EMD35310.1,
RC   ECO:0000313|Proteomes:UP000016930};
RX   PubMed=22434909; DOI=10.1073/pnas.1119912109;
RA   Fernandez-Fueyo E., Ruiz-Duenas F.J., Ferreira P., Floudas D.,
RA   Hibbett D.S., Canessa P., Larrondo L.F., James T.Y., Seelenfreund D.,
RA   Lobos S., Polanco R., Tello M., Honda Y., Watanabe T., Watanabe T.,
RA   Ryu J.S., Kubicek C.P., Schmoll M., Gaskell J., Hammel K.E.,
RA   St John F.J., Vanden Wymelenberg A., Sabat G., Splinter BonDurant S.,
RA   Syed K., Yadav J.S., Doddapaneni H., Subramanian V., Lavin J.L.,
RA   Oguiza J.A., Perez G., Pisabarro A.G., Ramirez L., Santoyo F.,
RA   Master E., Coutinho P.M., Henrissat B., Lombard V., Magnuson J.K.,
RA   Kuees U., Hori C., Igarashi K., Samejima M., Held B.W., Barry K.W.,
RA   LaButti K.M., Lapidus A., Lindquist E.A., Lucas S.M., Riley R.,
RA   Salamov A.A., Hoffmeister D., Schwenk D., Hadar Y., Yarden O.,
RA   de Vries R.P., Wiebenga A., Stenlid J., Eastwood D., Grigoriev I.V.,
RA   Berka R.M., Blanchette R.A., Kersten P., Martinez A.T., Vicuna R.,
RA   Cullen D.;
RT   "Comparative genomics of Ceriporiopsis subvermispora and Phanerochaete
RT   chrysosporium provide insight into selective ligninolysis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:5458-5463(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; KB445800; EMD35310.1; -; Genomic_DNA.
DR   MEROPS; S53.007; -.
DR   EnsemblFungi; EMD35310; EMD35310; CERSUDRAFT_116113.
DR   OrthoDB; 1294880at2759; -.
DR   Proteomes; UP000016930; 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   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:UP000016930};
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:UP000016930};
KW   Serine protease {ECO:0000256|PROSITE-ProRule:PRU01032};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     25       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        26    652       {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5004023741.
FT   DOMAIN      238    651       Peptidase S53. {ECO:0000259|PROSITE:
FT                                PS51695}.
FT   REGION      184    208       Disordered. {ECO:0000256|MobiDB-lite:
FT                                M2QTD6}.
FT   ACT_SITE    317    317       Charge relay system.
FT                                {ECO:0000256|PROSITE-ProRule:PRU01032}.
FT   ACT_SITE    321    321       Charge relay system.
FT                                {ECO:0000256|PROSITE-ProRule:PRU01032}.
FT   ACT_SITE    567    567       Charge relay system.
FT                                {ECO:0000256|PROSITE-ProRule:PRU01032}.
FT   METAL       610    610       Calcium. {ECO:0000256|PROSITE-ProRule:
FT                                PRU01032}.
FT   METAL       611    611       Calcium; via carbonyl oxygen.
FT                                {ECO:0000256|PROSITE-ProRule:PRU01032}.
FT   METAL       629    629       Calcium; via carbonyl oxygen.
FT                                {ECO:0000256|PROSITE-ProRule:PRU01032}.
FT   METAL       631    631       Calcium. {ECO:0000256|PROSITE-ProRule:
FT                                PRU01032}.
SQ   SEQUENCE   652 AA;  69495 MW;  A54916D01474F56A CRC64;
     MAFLRRLLLA VVVSVIAVAA SPLSARVFHD DPRVPPGYKV LRRAAPHTVL PFRVGLKQSN
     IDSIESFLLD VSHPESPNYG KHWTAAQVAE TFRPSSESVG TVHNWLTESG VDASRIKLSA
     SGAWVQANVT IAEAERLLEA EYYIYEHEAT ESRHIACGQG YTLPADVAPH VDIVLPTVHF
     DAKHRGRRSM KRSESGPGDA AGSSGRPVSD AVIQKLDANT LEFAQDADTS ELANCDKNIT
     LACLRVLYNF PEFPKPASSS NRTIGIVEYT PQAYTPEDLD NFFKTYSPSQ VGERPNEVDI
     DGGTIHVNST NSNSFGESNL DLQYAMGLLG TSQDVILYQN GDLVEGASFD NFLDALDGSF
     CTFEGGDDPS QDSIYPDPFP GGFTGPENCG GAPLAHVIST SYGTNEASLT PAYAQRQCAE
     YAKLGLMGTT VLYSSGDEGV SGHGELCIAP NGTEVAGSGA FNPTFPGVCP FVTSVGATQV
     NPGASVHDPE SSCQQVIFPG GGFSNVFALP EYQKTAVQTY LTKFPPPYPP TQFNSTGRSR
     GFPDISANGA NYIVSILGEF AHVFGTSCAT PVSAAFIAAI NDARAAHNKS SVGFINPTLY
     SSAFKNAFND ITNGTNPGCG TEGFAARPGW DPLTGLGTPN VEKWLQLFLE LP
//
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