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Database: UniProt
Entry: M2RE35_CERS8
LinkDB: M2RE35_CERS8
Original site: M2RE35_CERS8 
ID   M2RE35_CERS8            Unreviewed;       653 AA.
AC   M2RE35;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   11-DEC-2019, entry version 21.
DE   RecName: Full=BPL/LPL catalytic domain-containing protein {ECO:0000259|PROSITE:PS51733};
GN   ORFNames=CERSUDRAFT_114980 {ECO:0000313|EMBL:EMD37081.1};
OS   Ceriporiopsis subvermispora (strain B) (White-rot fungus) (Gelatoporia
OS   subvermispora).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Polyporales; Gelatoporiaceae; Gelatoporia.
OX   NCBI_TaxID=914234 {ECO:0000313|EMBL:EMD37081.1, ECO:0000313|Proteomes:UP000016930};
RN   [1] {ECO:0000313|EMBL:EMD37081.1, ECO:0000313|Proteomes:UP000016930}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B {ECO:0000313|EMBL:EMD37081.1,
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., St John F.J.,
RA   Vanden Wymelenberg A., Sabat G., Splinter BonDurant S., Syed K.,
RA   Yadav J.S., Doddapaneni H., Subramanian V., Lavin J.L., Oguiza J.A.,
RA   Perez G., Pisabarro A.G., Ramirez L., Santoyo F., Master E., Coutinho P.M.,
RA   Henrissat B., Lombard V., Magnuson J.K., Kuees U., Hori C., Igarashi K.,
RA   Samejima M., Held B.W., Barry K.W., LaButti K.M., Lapidus A.,
RA   Lindquist E.A., Lucas S.M., Riley R., Salamov A.A., Hoffmeister D.,
RA   Schwenk D., Hadar Y., Yarden O., de Vries R.P., Wiebenga A., Stenlid J.,
RA   Eastwood D., Grigoriev I.V., Berka R.M., Blanchette R.A., Kersten P.,
RA   Martinez A.T., Vicuna R., 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).
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DR   EMBL; KB445797; EMD37081.1; -; Genomic_DNA.
DR   EnsemblFungi; EMD37081; EMD37081; CERSUDRAFT_114980.
DR   OrthoDB; 1392751at2759; -.
DR   Proteomes; UP000016930; Unassembled WGS sequence.
DR   GO; GO:0004077; F:biotin-[acetyl-CoA-carboxylase] ligase activity; IEA:InterPro.
DR   GO; GO:0006464; P:cellular protein modification process; IEA:InterPro.
DR   CDD; cd16442; BPL; 1.
DR   Gene3D; 3.40.50.880; -; 1.
DR   InterPro; IPR019197; Biotin-prot_ligase_N.
DR   InterPro; IPR004408; Biotin_CoA_COase_ligase.
DR   InterPro; IPR004143; BPL_LPL_catalytic.
DR   InterPro; IPR029062; Class_I_gatase-like.
DR   Pfam; PF03099; BPL_LplA_LipB; 1.
DR   Pfam; PF09825; BPL_N; 1.
DR   TIGRFAMs; TIGR00121; birA_ligase; 1.
DR   PROSITE; PS51733; BPL_LPL_CATALYTIC; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000016930}.
FT   DOMAIN          369..568
FT                   /note="BPL/LPL catalytic"
FT                   /evidence="ECO:0000259|PROSITE:PS51733"
SQ   SEQUENCE   653 AA;  70547 MW;  358DFC635A9C6070 CRC64;
     MNVLVYSGPE VLDTSLSQTL QTLRSLLVPN YAIQTINTQA ISSQPWASNC AMLVLPACRA
     ALVPAAPFTS ALKAYVEHGG VLLAFGAGAR RQARQAFTGE TLEARMARMN VGASSVAALR
     FVDRASGTLE VTLPGHGEES LRVYQLEAKD RSTAEGIVMA GKAEITDATD WKGAEVLARY
     GDGRTNPVAG VCCPVGEGKL ALWTALIDHC LAEEPVKSLV TQSNDHASLD LAAAESQRLV
     LLQTSLTALG LRLPSNESSV ARPLPQFLTC VPTKPDIVER IAAALSIKEL EKGPHVLQDD
     NDTFQFHAAS EGPKLLEEAR TSHSSADPST WQPKHVVICT GGHIPLKDDT PLFDIATYYT
     ELEASRRKYV GPACPEPWGV GEALLYGEVV TSTQTMLDKN PRLMSLLPTP LLSLATHQLA
     GRGRGGNVWI SPAGCLQFSL LLYVPMQTLP TYRVVFVQYL FGLAVVEACR DAGVLGKLGD
     RVRLKWPNDI YAVLDNGEKR KIGGVLVNTS FNGGAVEVII GCGLNVLNPP PITSLQQMVP
     PDMDTKLSIE RTAAVIMAKF EEMWVTFLTN RGSFAPFMDL YLERWLHSDQ LVTLTTTNPP
     QQVRIVGITP NHGLLRTMPE RDGWSGGGTG EFIDLQPDGN SFDLMAGLIK SKS
//
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