ID   EFM7_CANAL              Reviewed;         262 AA.
AC   Q5A013; A0A1D8PSJ7;
DT   22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   26-APR-2005, sequence version 1.
DT   03-AUG-2022, entry version 83.
DE   RecName: Full=Protein N-terminal and lysine N-methyltransferase EFM7 {ECO:0000255|HAMAP-Rule:MF_03223};
DE            EC=2.1.1.- {ECO:0000255|HAMAP-Rule:MF_03223};
DE   AltName: Full=Elongation factor methyltransferase 7 {ECO:0000255|HAMAP-Rule:MF_03223};
GN   Name=EFM7 {ECO:0000255|HAMAP-Rule:MF_03223}; Synonyms=NNT1;
GN   OrderedLocusNames=CAALFM_CR03760WA; ORFNames=CaO19.11853, CaO19.4375;
OS   Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=237561;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SC5314 / ATCC MYA-2876;
RX   PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA   Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA   Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA   Scherer S.;
RT   "The diploid genome sequence of Candida albicans.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=SC5314 / ATCC MYA-2876;
RX   PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA   van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA   Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA   Chibana H., Nantel A., Magee P.T.;
RT   "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT   on the eight chromosomes.";
RL   Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC   STRAIN=SC5314 / ATCC MYA-2876;
RX   PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA   Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT   "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT   specific measurements and provides a simple model for repeat and indel
RT   structure.";
RL   Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
CC   -!- FUNCTION: S-adenosyl-L-methionine-dependent protein methyltransferase
CC       that trimethylates the N-terminal glycine 'Gly-2' of elongation factor
CC       1-alpha, before also catalyzing the mono- and dimethylation of 'Lys-3'.
CC       {ECO:0000255|HAMAP-Rule:MF_03223}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03223}.
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. EFM7 family. {ECO:0000255|HAMAP-Rule:MF_03223}.
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DR   EMBL; CP017630; AOW31114.1; -; Genomic_DNA.
DR   RefSeq; XP_715151.1; XM_710058.1.
DR   AlphaFoldDB; Q5A013; -.
DR   SMR; Q5A013; -.
DR   STRING; 237561.Q5A013; -.
DR   GeneID; 3643178; -.
DR   KEGG; cal:CAALFM_CR03760WA; -.
DR   CGD; CAL0000181775; orf19.11853.
DR   VEuPathDB; FungiDB:CR_03760W_A; -.
DR   eggNOG; KOG2920; Eukaryota.
DR   HOGENOM; CLU_032409_0_0_1; -.
DR   InParanoid; Q5A013; -.
DR   OMA; YQPWLLP; -.
DR   OrthoDB; 1588190at2759; -.
DR   PRO; PR:Q5A013; -.
DR   Proteomes; UP000000559; Chromosome R.
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; IBA:GO_Central.
DR   GO; GO:0018013; P:N-terminal peptidyl-glycine methylation; IEA:UniProtKB-UniRule.
DR   GO; GO:0018027; P:peptidyl-lysine dimethylation; IBA:GO_Central.
DR   Gene3D; 3.40.50.150; -; 1.
DR   HAMAP; MF_03223; Methyltr_EFM7; 1.
DR   InterPro; IPR025784; EFM7.
DR   InterPro; IPR019410; Methyltransf_16.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   PANTHER; PTHR14614; PTHR14614; 1.
DR   Pfam; PF10294; Methyltransf_16; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
DR   PROSITE; PS51560; SAM_MT_NNT1; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Methyltransferase; Reference proteome; S-adenosyl-L-methionine;
KW   Transferase.
FT   CHAIN           1..262
FT                   /note="Protein N-terminal and lysine N-methyltransferase
FT                   EFM7"
FT                   /id="PRO_0000096891"
FT   BINDING         59
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03223"
FT   BINDING         86..88
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03223"
FT   BINDING         108
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03223"
FT   BINDING         143
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03223"
FT   BINDING         171
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03223"
SQ   SEQUENCE   262 AA;  30430 MW;  4C1EAFD9320AD296 CRC64;
     MSEDEISIEG DLFEEPEGFL PERPSSHFST YKRKIPNAEP QEITMKLVGH NPLYGHLLWN
     AGIYTADYLD KHSDTLVQGK KILELGAASA LPSLVCSLNH AKEVIVTDYP DPDLLSHMEY
     SFNDLKEKTK YELSPWKVKG YIWGHDLGEL LFDEPGRKLA EEEKFDLIIL SDLVFNHSEH
     HKLLDTCRQS LKRNGGKCLV VFSPHRPYLL QDDLSFFETA KQYQFKTEKI EMVTWKPMFE
     EDEETADIRA RVYAFFLIPE WE