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Database: UniProt
Entry: A0A1I7SFF4_BURXY
LinkDB: A0A1I7SFF4_BURXY
Original site: A0A1I7SFF4_BURXY 
ID   A0A1I7SFF4_BURXY        Unreviewed;       236 AA.
AC   A0A1I7SFF4;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   RecName: Full=Protein-lysine N-methyltransferase BXYJ_LOCUS3081 {ECO:0000256|HAMAP-Rule:MF_03188};
DE            EC=2.1.1.- {ECO:0000256|HAMAP-Rule:MF_03188};
GN   ORFNames=BXYJ_LOCUS3081 {ECO:0000313|EMBL:CAD5213540.1};
OS   Bursaphelenchus xylophilus (Pinewood nematode worm) (Aphelenchoides
OS   xylophilus).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Tylenchina; Tylenchomorpha; Aphelenchoidea; Aphelenchoididae;
OC   Bursaphelenchus.
OX   NCBI_TaxID=6326 {ECO:0000313|Proteomes:UP000095284, ECO:0000313|WBParaSite:BXY_1176600.1};
RN   [1] {ECO:0000313|WBParaSite:BXY_1176600.1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (NOV-2016) to UniProtKB.
RN   [2] {ECO:0000313|EMBL:CAG9092730.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Ka4C1 {ECO:0000313|EMBL:CAD5213540.1};
RA   Kikuchi T.;
RL   Submitted (AUG-2020) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: S-adenosyl-L-methionine-dependent protein-lysine N-
CC       methyltransferase that methylates elongation factor 1-alpha.
CC       {ECO:0000256|HAMAP-Rule:MF_03188}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03188}.
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. EFM4 family. {ECO:0000256|HAMAP-Rule:MF_03188}.
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DR   EMBL; CAJFDI010000002; CAD5213540.1; -; Genomic_DNA.
DR   EMBL; CAJFCV020000002; CAG9092730.1; -; Genomic_DNA.
DR   WBParaSite; BXY_1176600.1; BXY_1176600.1; BXY_1176600.
DR   eggNOG; KOG1271; Eukaryota.
DR   Proteomes; UP000095284; Unplaced.
DR   Proteomes; UP000582659; Unassembled WGS sequence.
DR   Proteomes; UP000659654; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016279; F:protein-lysine N-methyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   CDD; cd02440; AdoMet_MTases; 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   HAMAP; MF_03188; Methyltr_EFM4; 1.
DR   InterPro; IPR026635; Efm4/METTL10.
DR   InterPro; IPR025714; Methyltranfer_dom.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   PANTHER; PTHR12843:SF5; EEF1A LYSINE METHYLTRANSFERASE 2; 1.
DR   PANTHER; PTHR12843; PROTEIN-LYSINE N-METHYLTRANSFERASE METTL10; 1.
DR   Pfam; PF13847; Methyltransf_31; 1.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_03188};
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|HAMAP-
KW   Rule:MF_03188}; Reference proteome {ECO:0000313|Proteomes:UP000659654};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691, ECO:0000256|HAMAP-
KW   Rule:MF_03188};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_03188}.
FT   DOMAIN          67..196
FT                   /note="Methyltransferase"
FT                   /evidence="ECO:0000259|Pfam:PF13847"
SQ   SEQUENCE   236 AA;  26717 MW;  E32CF6D6AF448C5B CRC64;
     MPSTSENPLN VDFECSKLGT KEYWDQRYAQ DLETFRDCGE EGEIWFGKTA ENRIIKFVRE
     NVPQSAAILD LGCANGSILR KLFYKGYRNL FGVDYSETAI RLAKECVEND EDVDSPESFQ
     FETVDLTSPD ALPDSLKAKF DSLMDKGTWD AISLGSNPSD LIHRYVQCLS ALFNDETEGN
     QYFVIISCNF TVEELTDFFT KDGRFEVHAE LPNTNTFCFG GKVGKTTSGM AFKRIR
//
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