(data stored in ACNUC7421 zone)

SWISSPROT: Q4WNI7_ASPFU

ID   Q4WNI7_ASPFU            Unreviewed;       256 AA.
AC   Q4WNI7;
DT   05-JUL-2005, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2005, sequence version 1.
DT   11-DEC-2019, entry version 65.
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=AFUA_4G05890 {ECO:0000313|EMBL:EAL90197.1};
OS   Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS   A1100) (Aspergillus fumigatus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=330879 {ECO:0000313|EMBL:EAL90197.1, ECO:0000313|Proteomes:UP000002530};
RN   [1] {ECO:0000313|EMBL:EAL90197.1, ECO:0000313|Proteomes:UP000002530}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100
RC   {ECO:0000313|Proteomes:UP000002530};
RX   PubMed=16372009; DOI=10.1038/nature04332;
RA   Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA   Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J., Bowyer P.,
RA   Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.,
RA   Fedorova N., Fedorova N., Feldblyum T.V., Fischer R., Fosker N., Fraser A.,
RA   Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA   Griffith-Jones S., Gwilliam R., Haas B., Haas H., Harris D., Horiuchi H.,
RA   Huang J., Humphray S., Jimenez J., Keller N., Khouri H., Kitamoto K.,
RA   Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafon A., Latge J.P.,
RA   Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L., Mohamoud Y.,
RA   Molina M., Monod M., Mouyna I., Mulligan S., Murphy L., O'Neil S.,
RA   Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L., Quail M.A.,
RA   Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U., Renauld H.,
RA   Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M., Ronning C.M.,
RA   Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C., Saunders D.,
RA   Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F., Turner G.,
RA   Vazquez de Aldana C.R., Weidman J., White O., Woodward J., Yu J.H.,
RA   Fraser C., Galagan J.E., Asai K., Machida M., Hall N., Barrell B.,
RA   Denning D.W.;
RT   "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT   Aspergillus fumigatus.";
RL   Nature 438:1151-1156(2005).
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 methyltransferase
CC       superfamily. METTL21 family. EFM6 subfamily. {ECO:0000256|HAMAP-
CC       Rule:MF_03198}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EAL90197.1}.
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DR   EMBL; AAHF01000005; EAL90197.1; -; Genomic_DNA.
DR   RefSeq; XP_752235.1; XM_747142.1.
DR   STRING; 746128.CADAFUBP00006123; -.
DR   EnsemblFungi; EAL90197; EAL90197; AFUA_4G05890.
DR   GeneID; 3509418; -.
DR   KEGG; afm:AFUA_4G05890; -.
DR   EuPathDB; FungiDB:Afu4g05890; -.
DR   HOGENOM; HOG000187553; -.
DR   InParanoid; Q4WNI7; -.
DR   KO; K21804; -.
DR   OMA; KAMVLNW; -.
DR   OrthoDB; 1494909at2759; -.
DR   Proteomes; UP000002530; Chromosome 4.
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;
DR   PRODOM; Q4WNI7.
DR   SWISS-2DPAGE; Q4WNI7.
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03198};
KW   Methyltransferase {ECO:0000256|HAMAP-Rule:MF_03198};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002530};
KW   S-adenosyl-L-methionine {ECO:0000256|HAMAP-Rule:MF_03198};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_03198}.
FT   REGION          97..99
FT                   /note="S-adenosyl-L-methionine binding"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03198"
FT   BINDING         70
FT                   /note="S-adenosyl-L-methionine; via amide nitrogen"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03198"
FT   BINDING         122
FT                   /note="S-adenosyl-L-methionine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03198"
FT   BINDING         150
FT                   /note="S-adenosyl-L-methionine; via amide nitrogen"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03198"
FT   BINDING         168
FT                   /note="S-adenosyl-L-methionine; via carbonyl oxygen"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03198"
SQ   SEQUENCE   256 AA;  28497 MW;  2B737D9FD10220A7 CRC64;
     MGAKILPMEA TIPDKPSSPN LVAAFDVSEH LVPVRELKPA GNTLVSFDGL LEEPLILKED
     LKEGCGGQLW PAGIVLAKYL LRQHRNNLSN KTIVELGAGG GLVGLAVARG CDVGPCPIYI
     TDQEPMLHLM KTNIELNNLS TAVAATVLNW GERLPDCIPT HPEIVLAADC VYFEPAFPLL
     ISTLQDLLGP ESVCYFCFKR RRRADLRFMK AAKRVFDIKE VRDDPEADTY RRENIFLYSL
     RLRFRPENGS LRAIKE
//

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