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Database: UniProt
Entry: A0A151GD02_9HYPO
LinkDB: A0A151GD02_9HYPO
Original site: A0A151GD02_9HYPO 
ID   A0A151GD02_9HYPO        Unreviewed;       283 AA.
AC   A0A151GD02;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   05-JUN-2019, entry version 11.
DE   RecName: Full=Protein N-terminal and lysine N-methyltransferase EFM7 {ECO:0000256|HAMAP-Rule:MF_03223};
DE            EC=2.1.1.- {ECO:0000256|HAMAP-Rule:MF_03223};
DE   AltName: Full=Elongation factor methyltransferase 7 {ECO:0000256|HAMAP-Rule:MF_03223};
GN   Name=EFM7 {ECO:0000256|HAMAP-Rule:MF_03223};
GN   ORFNames=DCS_06885 {ECO:0000313|EMBL:KYK54924.1};
OS   Drechmeria coniospora.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
OC   Sordariomycetes; Hypocreomycetidae; Hypocreales; Ophiocordycipitaceae;
OC   Drechmeria.
OX   NCBI_TaxID=98403 {ECO:0000313|EMBL:KYK54924.1, ECO:0000313|Proteomes:UP000076580};
RN   [1] {ECO:0000313|EMBL:KYK54924.1, ECO:0000313|Proteomes:UP000076580}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ARSEF 6962 {ECO:0000313|EMBL:KYK54924.1,
RC   ECO:0000313|Proteomes:UP000076580};
RX   PubMed=26975455; DOI=10.1038/srep23122;
RA   Zhang L., Zhou Z., Guo Q., Fokkens L., Miskei M., Pocsi I., Zhang W.,
RA   Chen M., Wang L., Sun Y., Donzelli B.G., Gibson D.M., Nelson D.R.,
RA   Luo J.G., Rep M., Liu H., Yang S., Wang J., Krasnoff S.B., Xu Y.,
RA   Molnar I., Lin M.;
RT   "Insights into Adaptations to a Near-Obligate Nematode Endoparasitic
RT   Lifestyle from the Finished Genome of Drechmeria coniospora.";
RL   Sci. Rep. 6:23122-23122(2016).
CC   -!- FUNCTION: S-adenosyl-L-methionine-dependent protein
CC       methyltransferase that trimethylates the N-terminal glycine 'Gly-
CC       2' of elongation factor 1-alpha, before also catalyzing the mono-
CC       and dimethylation of 'Lys-3'. {ECO:0000256|HAMAP-Rule:MF_03223}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03223}.
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding
CC       methyltransferase superfamily. EFM7 family. {ECO:0000256|HAMAP-
CC       Rule:MF_03223}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:KYK54924.1}.
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DR   EMBL; LAYC01000003; KYK54924.1; -; Genomic_DNA.
DR   EnsemblFungi; KYK54924; KYK54924; DCS_06885.
DR   OrthoDB; 1588190at2759; -.
DR   Proteomes; UP000076580; Chromosome 03.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0071885; F:N-terminal protein N-methyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0016279; F:protein-lysine N-methyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0018013; P:N-terminal peptidyl-glycine methylation; IEA:UniProtKB-UniRule.
DR   GO; GO:0018027; P:peptidyl-lysine dimethylation; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_03223; Methyltr_EFM7; 1.
DR   InterPro; IPR025784; EFM7.
DR   InterPro; IPR019410; Methyltransf_16.
DR   InterPro; IPR029063; SAM-dependent_MTases.
DR   Pfam; PF10294; Methyltransf_16; 1.
DR   SUPFAM; SSF53335; SSF53335; 2.
DR   PROSITE; PS51560; SAM_MT_NNT1; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000076580};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03223};
KW   Methyltransferase {ECO:0000256|HAMAP-Rule:MF_03223};
KW   Reference proteome {ECO:0000313|Proteomes:UP000076580};
KW   S-adenosyl-L-methionine {ECO:0000256|HAMAP-Rule:MF_03223};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_03223}.
FT   REGION        1     26       Disordered. {ECO:0000256|MobiDB-lite:
FT                                A0A151GD02}.
FT   REGION       81     83       S-adenosyl-L-methionine binding.
FT                                {ECO:0000256|HAMAP-Rule:MF_03223}.
FT   BINDING      55     55       S-adenosyl-L-methionine; via amide
FT                                nitrogen. {ECO:0000256|HAMAP-Rule:
FT                                MF_03223}.
FT   BINDING     103    103       S-adenosyl-L-methionine.
FT                                {ECO:0000256|HAMAP-Rule:MF_03223}.
FT   BINDING     141    141       S-adenosyl-L-methionine; via amide
FT                                nitrogen. {ECO:0000256|HAMAP-Rule:
FT                                MF_03223}.
FT   BINDING     180    180       S-adenosyl-L-methionine; via carbonyl
FT                                oxygen. {ECO:0000256|HAMAP-Rule:
FT                                MF_03223}.
SQ   SEQUENCE   283 AA;  30618 MW;  962BE722E9AEAB75 CRC64;
     MADDNFDMGG LMEDPEDYYP PSPPPTQQLF TMGQSGRPIR LHLVGSSPTE AHHLWNGAKF
     VADYFEEEPA RVRGRTVLEL GAAAGLPSLV AGILGARKVV MTDFPDPDLV ANMQKNIDEC
     GETMEPEGHL ARTIDAVGFV WGADPAPLLA RLANLDDSST MAGSTRGTAP VVKFDVLILA
     DLLFRHSEHG ALVKTIQEVM APSTASAAYV FFTSYRPWKQ DLDMGFFDVA RNAGLTVEQV
     SERKLEKPLF DGDPGDLDVQ KTVKGFVVRW AEPGSAPAAA SSE
//
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