GenomeNet

Database: UniProt
Entry: B8P3X1_POSPM
LinkDB: B8P3X1_POSPM
Original site: B8P3X1_POSPM 
ID   B8P3X1_POSPM            Unreviewed;       249 AA.
AC   B8P3X1;
DT   03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   03-MAR-2009, sequence version 1.
DT   05-JUN-2019, entry version 34.
DE   RecName: Full=Protein-lysine N-methyltransferase EFM6 {ECO:0000256|HAMAP-Rule:MF_03198};
DE            EC=2.1.1.- {ECO:0000256|HAMAP-Rule:MF_03198};
DE   AltName: Full=Elongation factor methyltransferase 6 {ECO:0000256|HAMAP-Rule:MF_03198};
GN   Name=EFM6 {ECO:0000256|HAMAP-Rule:MF_03198};
GN   ORFNames=POSPLDRAFT_93483 {ECO:0000313|EMBL:EED84419.1};
OS   Postia placenta (strain ATCC 44394 / Madison 698-R) (Brown rot fungus)
OS   (Poria monticola).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina;
OC   Agaricomycetes; Polyporales; Dacryobolaceae; Postia.
OX   NCBI_TaxID=561896 {ECO:0000313|Proteomes:UP000001743};
RN   [1] {ECO:0000313|EMBL:EED84419.1, ECO:0000313|Proteomes:UP000001743}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 44394 / Madison 698-R {ECO:0000313|Proteomes:UP000001743};
RX   PubMed=19193860; DOI=10.1073/pnas.0809575106;
RA   Martinez D., Challacombe J., Morgenstern I., Hibbett D., Schmoll M.,
RA   Kubicek C.P., Ferreira P., Ruiz-Duenas F.J., Martinez A.T.,
RA   Kersten P., Hammel K.E., Vanden Wymelenberg A., Gaskell J.,
RA   Lindquist E., Sabat G., Splinter BonDurant S., Larrondo L.F.,
RA   Canessa P., Vicuna R., Yadav J., Doddapaneni H., Subramanian V.,
RA   Pisabarro A.G., Lavin J.L., Oguiza J.A., Master E., Henrissat B.,
RA   Coutinho P.M., Harris P., Magnuson J.K., Baker S.E., Bruno K.,
RA   Kenealy W., Hoegger P.J., Kuees U., Ramaiya P., Lucas S., Salamov A.,
RA   Shapiro H., Tu H., Chee C.L., Misra M., Xie G., Teter S., Yaver D.,
RA   James T., Mokrejs M., Pospisek M., Grigoriev I.V., Brettin T.,
RA   Rokhsar D., Berka R., Cullen D.;
RT   "Genome, transcriptome, and secretome analysis of wood decay fungus
RT   Postia placenta supports unique mechanisms of lignocellulose
RT   conversion.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:1954-1959(2009).
CC   -!- FUNCTION: S-adenosyl-L-methionine-dependent protein-lysine N-
CC       methyltransferase that methylates elongation factor 1-alpha.
CC       {ECO:0000256|HAMAP-Rule:MF_03198}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03198}.
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding
CC       methyltransferase superfamily. METTL21 family. EFM6 subfamily.
CC       {ECO:0000256|HAMAP-Rule:MF_03198}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   EMBL; EQ966250; EED84419.1; -; Genomic_DNA.
DR   RefSeq; XP_002470394.1; XM_002470349.1.
DR   EnsemblFungi; EED84419; EED84419; POSPLDRAFT_93483.
DR   KEGG; ppl:POSPLDRAFT_93483; -.
DR   InParanoid; B8P3X1; -.
DR   KO; K21804; -.
DR   OMA; HILYIRK; -.
DR   Proteomes; UP000001743; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016279; F:protein-lysine N-methyltransferase activity; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_03198; Methyltr_EFM6; 1.
DR   InterPro; IPR033684; EFM6.
DR   InterPro; IPR019410; Methyltransf_16.
DR   InterPro; IPR029063; SAM-dependent_MTases.
DR   Pfam; PF10294; Methyltransf_16; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000001743};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03198};
KW   Methyltransferase {ECO:0000256|HAMAP-Rule:MF_03198};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001743};
KW   S-adenosyl-L-methionine {ECO:0000256|HAMAP-Rule:MF_03198};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_03198}.
FT   REGION       17     36       Disordered. {ECO:0000256|MobiDB-lite:
FT                                B8P3X1}.
FT   REGION      102    104       S-adenosyl-L-methionine binding.
FT                                {ECO:0000256|HAMAP-Rule:MF_03198}.
FT   BINDING      75     75       S-adenosyl-L-methionine; via amide
FT                                nitrogen. {ECO:0000256|HAMAP-Rule:
FT                                MF_03198}.
FT   BINDING     124    124       S-adenosyl-L-methionine.
FT                                {ECO:0000256|HAMAP-Rule:MF_03198}.
FT   BINDING     152    152       S-adenosyl-L-methionine; via amide
FT                                nitrogen. {ECO:0000256|HAMAP-Rule:
FT                                MF_03198}.
FT   BINDING     168    168       S-adenosyl-L-methionine; via carbonyl
FT                                oxygen. {ECO:0000256|HAMAP-Rule:
FT                                MF_03198}.
SQ   SEQUENCE   249 AA;  27292 MW;  45623A4FF2A72185 CRC64;
     MADLLREENL DDLDPLRHLR GSADADDADD TDLVPAQPPS ILDQTIELTF PSDPSETVSI
     TLAVDASPGC GGIAWPAGEV LSRYIARKGP AYFKDKTVLE LGSGTGLVGL VAAKLGAPRV
     WLTDQAPLLA TMRRNTALNG LAPPVRVAEL NWGAPLPLLP RPDVVLAADC VYFEPAFPLL
     VRTLAALVPR DAPGPDADVL FCYKKRRKAD RRFFALLRKE FTWTEVLDDP DRDVYAREAI
     SLLRLSRRR
//
DBGET integrated database retrieval system