(data stored in SCRATCH zone)

SWISSPROT: B6HFD0_PENRW

ID   B6HFD0_PENRW            Unreviewed;       249 AA.
AC   B6HFD0;
DT   16-DEC-2008, integrated into UniProtKB/TrEMBL.
DT   16-DEC-2008, sequence version 1.
DT   05-JUL-2017, entry version 41.
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=Pc20g00330 {ECO:0000313|EMBL:CAP85362.1}, PCH_Pc20g00330
GN   {ECO:0000313|EMBL:CAP85362.1};
OS   Penicillium rubens (strain ATCC 28089 / DSM 1075 / NRRL 1951 /
OS   Wisconsin 54-1255) (Penicillium chrysogenum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium;
OC   Penicillium chrysogenum species complex.
OX   NCBI_TaxID=500485 {ECO:0000313|EMBL:CAP85362.1, ECO:0000313|Proteomes:UP000000724};
RN   [1] {ECO:0000313|EMBL:CAP85362.1, ECO:0000313|Proteomes:UP000000724}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin 54-1255
RC   {ECO:0000313|Proteomes:UP000000724};
RX   PubMed=18820685; DOI=10.1038/nbt.1498;
RA   van den Berg M.A., Albang R., Albermann K., Badger J.H., Daran J.-M.,
RA   Driessen A.J.M., Garcia-Estrada C., Fedorova N.D., Harris D.M.,
RA   Heijne W.H.M., Joardar V.S., Kiel J.A.K.W., Kovalchuk A., Martin J.F.,
RA   Nierman W.C., Nijland J.G., Pronk J.T., Roubos J.A.,
RA   van der Klei I.J., van Peij N.N.M.E., Veenhuis M., von Doehren H.,
RA   Wagner C., Wortman J.R., Bovenberg R.A.L.;
RT   "Genome sequencing and analysis of the filamentous fungus Penicillium
RT   chrysogenum.";
RL   Nat. Biotechnol. 26:1161-1168(2008).
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}.
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DR   EMBL; AM920435; CAP85362.1; -; Genomic_DNA.
DR   RefSeq; XP_002562597.1; XM_002562551.1.
DR   EnsemblFungi; CAP85362; CAP85362; PCH_Pc20g00330.
DR   GeneID; 8307691; -.
DR   KEGG; pcs:Pc20g00330; -.
DR   eggNOG; ENOG410ISZC; Eukaryota.
DR   eggNOG; ENOG4111PIY; LUCA.
DR   HOGENOM; HOG000187553; -.
DR   OMA; EDIHILY; -.
DR   OrthoDB; EOG092C4PYS; -.
DR   BioCyc; PCHR:PC20G00330-MONOMER; -.
DR   Proteomes; UP000000724; Contig Pc00c20.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016279; F:protein-lysine N-methyltransferase activity; IEA:UniProtKB-HAMAP.
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;
DR   PRODOM; B6HFD0.
DR   SWISS-2DPAGE; B6HFD0.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000724};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03198};
KW   Methyltransferase {ECO:0000256|HAMAP-Rule:MF_03198};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000724};
KW   S-adenosyl-L-methionine {ECO:0000256|HAMAP-Rule:MF_03198};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_03198}.
FT   REGION       95     97       S-adenosyl-L-methionine binding.
FT                                {ECO:0000256|HAMAP-Rule:MF_03198}.
FT   BINDING      68     68       S-adenosyl-L-methionine; via amide
FT                                nitrogen. {ECO:0000256|HAMAP-Rule:
FT                                MF_03198}.
FT   BINDING     119    119       S-adenosyl-L-methionine.
FT                                {ECO:0000256|HAMAP-Rule:MF_03198}.
FT   BINDING     147    147       S-adenosyl-L-methionine; via amide
FT                                nitrogen. {ECO:0000256|HAMAP-Rule:
FT                                MF_03198}.
FT   BINDING     165    165       S-adenosyl-L-methionine; via carbonyl
FT                                oxygen. {ECO:0000256|HAMAP-Rule:
FT                                MF_03198}.
SQ   SEQUENCE   249 AA;  27409 MW;  9CCB6B9E005D8229 CRC64;
     MIETPMTTPP GPELSPPSSP DGLKISESLA PPRELKAATT TDISFDGLLK EPLLLKEDLK
     DGCGGQLWPA GMALAKYLLS RHAADLSDKT IVELGAGGGL VGLAVARGCH LEQPIYITDQ
     EPMFSLMKSN IQLNNLGPNA TAAILNWGEP IPKQIPSKPN VIIAADCVYF EPAFPLLITT
     LQDLLGPNSV CYFCYKRRRR ADMRFMKMAK KAFEMELVRD DPGAEGYNRE SIFIYTIRAK
     RLDQKSETR
//

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