ID A0A026WAQ9_OOCBI Unreviewed; 491 AA.
AC A0A026WAQ9;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE RecName: Full=Protein-lysine N-methyltransferase X777_07142 {ECO:0000256|HAMAP-Rule:MF_03188};
DE EC=2.1.1.- {ECO:0000256|HAMAP-Rule:MF_03188};
GN ORFNames=X777_07142 {ECO:0000313|EMBL:EZA52761.1};
OS Ooceraea biroi (Clonal raider ant) (Cerapachys biroi).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Dorylinae; Ooceraea.
OX NCBI_TaxID=2015173 {ECO:0000313|EMBL:EZA52761.1, ECO:0000313|Proteomes:UP000053097};
RN [1] {ECO:0000313|EMBL:EZA52761.1, ECO:0000313|Proteomes:UP000053097}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=24508170; DOI=10.1016/j.cub.2014.01.018;
RA Oxley P.R., Ji L., Fetter-Pruneda I., McKenzie S.K., Li C., Hu H.,
RA Zhang G., Kronauer D.J.;
RT "The genome of the clonal raider ant Cerapachys biroi.";
RL Curr. Biol. 24:451-458(2014).
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; KK107321; EZA52761.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A026WAQ9; -.
DR STRING; 2015173.A0A026WAQ9; -.
DR EnsemblMetazoa; XM_011343166.3; XP_011341468.2; LOC105281728.
DR Proteomes; UP000053097; 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:UP000053097};
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 62..191
FT /note="Methyltransferase"
FT /evidence="ECO:0000259|Pfam:PF13847"
SQ SEQUENCE 491 AA; 55240 MW; CAAD42CFA2DD4A89 CRC64;
MTEQENGELT PSDLGTLEFW ENAYEHELDN FRGHGDVGEI WFGAANSRKI VRWIATKLDL
NKESDKIIDV GCGNAMTLVE LAKEGFTNLM GVDYSEKAVD LARMVLNDND LPNVKLEVCD
ILDNTLPHDF KVVHDKGTYD AISLNPENPT EKRQKYIENI CRILLPRGYL VLTSCNWTKE
ELLKHFTNLA TGLYDTCEET IQCSTYLLSG AKCINKVCVC GPGYYYLHGL YEKCKQDVDC
YVNADFEASV CDNGICKCTP GFYQREYRTC RREGKKDGDE CTINNDCTFD NAICTEFVCK
ASQVEEAIEL ASDAMLTTNN SDANEGSPRT CIRRYSCDDY ICMIPLEIRV DGNCMTNEDC
RALGNAVCSP IGTCRCDRAH FASATGTECI PELGEPCQES QKGYIEKSFC RKGRWSCSSD
TVASKNNREC LEVLGETCMN HNECYESVKQ IQEKKIICKN GKCACDWGWN EWNSSVCVKH
PEAAAFYLNS K
//
