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Database: UniProt
Entry: A0A179US09_BLAGS
LinkDB: A0A179US09_BLAGS
Original site: A0A179US09_BLAGS 
ID   A0A179US09_BLAGS        Unreviewed;       280 AA.
AC   A0A179US09;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   05-JUN-2019, entry version 10.
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=BDBG_06613 {ECO:0000313|EMBL:OAT10824.1};
OS   Blastomyces gilchristii (strain SLH14081) (Blastomyces dermatitidis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Ajellomycetaceae; Blastomyces.
OX   NCBI_TaxID=559298 {ECO:0000313|EMBL:OAT10824.1, ECO:0000313|Proteomes:UP000002038};
RN   [1] {ECO:0000313|Proteomes:UP000002038}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SLH14081 {ECO:0000313|Proteomes:UP000002038};
RX   PubMed=26439490; DOI=10.1371/journal.pgen.1005493;
RA   Munoz J.F., Gauthier G.M., Desjardins C.A., Gallo J.E., Holder J.,
RA   Sullivan T.D., Marty A.J., Carmen J.C., Chen Z., Ding L., Gujja S.,
RA   Magrini V., Misas E., Mitreva M., Priest M., Saif S., Whiston E.A.,
RA   Young S., Zeng Q., Goldman W.E., Mardis E.R., Taylor J.W.,
RA   McEwen J.G., Clay O.K., Klein B.S., Cuomo C.A.;
RT   "The dynamic genome and transcriptome of the human fungal pathogen
RT   Blastomyces and close relative Emmonsia.";
RL   PLoS Genet. 11:E1005493-E1005493(2015).
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}.
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DR   EMBL; GG657461; OAT10824.1; -; Genomic_DNA.
DR   RefSeq; XP_002623174.1; XM_002623128.1.
DR   EnsemblFungi; OAT10824; OAT10824; BDBG_06613.
DR   GeneID; 8503353; -.
DR   Proteomes; UP000002038; Unassembled WGS sequence.
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; 1.
DR   PROSITE; PS51560; SAM_MT_NNT1; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000002038};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03223};
KW   Methyltransferase {ECO:0000256|HAMAP-Rule:MF_03223,
KW   ECO:0000313|EMBL:OAT10824.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002038};
KW   S-adenosyl-L-methionine {ECO:0000256|HAMAP-Rule:MF_03223};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_03223,
KW   ECO:0000313|EMBL:OAT10824.1}.
FT   REGION        1     22       Disordered. {ECO:0000256|MobiDB-lite:
FT                                A0A179US09}.
FT   REGION       86     88       S-adenosyl-L-methionine binding.
FT                                {ECO:0000256|HAMAP-Rule:MF_03223}.
FT   COMPBIAS      1     15       Acidic. {ECO:0000256|MobiDB-lite:
FT                                A0A179US09}.
FT   BINDING      59     59       S-adenosyl-L-methionine; via amide
FT                                nitrogen. {ECO:0000256|HAMAP-Rule:
FT                                MF_03223}.
FT   BINDING     108    108       S-adenosyl-L-methionine.
FT                                {ECO:0000256|HAMAP-Rule:MF_03223}.
FT   BINDING     151    151       S-adenosyl-L-methionine; via amide
FT                                nitrogen. {ECO:0000256|HAMAP-Rule:
FT                                MF_03223}.
FT   BINDING     182    182       S-adenosyl-L-methionine; via carbonyl
FT                                oxygen. {ECO:0000256|HAMAP-Rule:
FT                                MF_03223}.
SQ   SEQUENCE   280 AA;  31628 MW;  7D5B72AEF2CCE398 CRC64;
     MDSNSENESD IEFGDIFQDP EGFLPPPKEA TFEEYTMRSG QTIKLRLVGS HPLWGFLLWN
     AGKTSADYLE DKAREWVEGR DILELGAGAG LPSLVCAILG ARTAVVTDYP DFDLVENMRI
     NAQACESLLS LGGTDGSSPK SSPLRVEGFK WGTDPETVLR HLPDDAGLGV DGRRGFDLLI
     LADVIYNHPQ HVQLITSVKQ TLKRTRDAVA FVVFTPYQPW LFEKIVAFFP RAEESGFVVT
     KVFERMMERL MFEEDPGDET LRRTVFGYEL RWKEEELDKQ
//
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