EFNMT_DANRE
ID EFNMT_DANRE Reviewed; 690 AA.
AC A5WVX1; Q567H9;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 1.
DT 03-AUG-2022, entry version 70.
DE RecName: Full=eEF1A lysine and N-terminal methyltransferase {ECO:0000250|UniProtKB:Q8N6R0};
DE AltName: Full=Methyltransferase-like protein 13 {ECO:0000250|UniProtKB:Q8N6R0};
DE Includes:
DE RecName: Full=eEF1A lysine methyltransferase {ECO:0000250|UniProtKB:Q8N6R0};
DE EC=2.1.1.- {ECO:0000250|UniProtKB:Q8N6R0};
DE Includes:
DE RecName: Full=eEF1A N-terminal methyltransferase {ECO:0000250|UniProtKB:Q8N6R0};
DE EC=2.1.1.- {ECO:0000250|UniProtKB:Q8N6R0};
GN Name=mettl13; Synonyms=eef1aknmt {ECO:0000250|UniProtKB:Q8N6R0};
GN ORFNames=si:dkey-19f21.2, zgc:152769;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-440.
RC TISSUE=Olfactory epithelium;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Dual methyltransferase that catalyzes methylation of
CC elongation factor 1-alpha (eef1a1 and eef1a2) at two different
CC positions, and is therefore involved in the regulation of mRNA
CC translation. Via its C-terminus, methylates the N-terminus of eef1a1
CC and eef1a2. Via its N-terminus dimethylates lysine residues of eef1a1
CC and eef1a2. {ECO:0000250|UniProtKB:Q8N6R0}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-lysyl-[protein] + S-adenosyl-L-methionine = H(+) + N(6)-
CC methyl-L-lysyl-[protein] + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:51736, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:13053,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:61929;
CC Evidence={ECO:0000250|UniProtKB:Q8N6R0};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=N(6)-methyl-L-lysyl-[protein] + S-adenosyl-L-methionine = H(+)
CC + N(6),N(6)-dimethyl-L-lysyl-[protein] + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:54196, Rhea:RHEA-COMP:13053, Rhea:RHEA-COMP:13827,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:61929, ChEBI:CHEBI:61976;
CC Evidence={ECO:0000250|UniProtKB:Q8N6R0};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=N-terminal glycyl-L-lysyl-L-glutamyl-[protein] + 3 S-adenosyl-
CC L-methionine = 3 H(+) + N-terminal N,N,N-trimethyl-glycyl-L-lysyl-L-
CC glutamyl-[protein] + 3 S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:58440, Rhea:RHEA-COMP:15140, Rhea:RHEA-COMP:15143,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:142597, ChEBI:CHEBI:142600;
CC Evidence={ECO:0000250|UniProtKB:Q8N6R0};
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CT563248; CAN88294.1; -; Genomic_DNA.
DR EMBL; BC093167; AAH93167.1; -; mRNA.
DR AlphaFoldDB; A5WVX1; -.
DR SMR; A5WVX1; -.
DR STRING; 7955.ENSDARP00000026819; -.
DR PaxDb; A5WVX1; -.
DR PeptideAtlas; A5WVX1; -.
DR ZFIN; ZDB-GENE-060929-60; mettl13.
DR eggNOG; KOG2352; Eukaryota.
DR InParanoid; A5WVX1; -.
DR PhylomeDB; A5WVX1; -.
DR PRO; PR:A5WVX1; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.150; -; 2.
DR InterPro; IPR041698; Methyltransf_25.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR Pfam; PF13649; Methyltransf_25; 1.
DR SUPFAM; SSF53335; SSF53335; 2.
PE 2: Evidence at transcript level;
KW Methyltransferase; Multifunctional enzyme; Reference proteome; Transferase.
FT CHAIN 1..690
FT /note="eEF1A lysine and N-terminal methyltransferase"
FT /id="PRO_0000310762"
FT REGION 427..451
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 437
FT /note="N -> K (in Ref. 2; AAH93167)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 690 AA; 76025 MW; A7AD078D7188BDF7 CRC64;
MSLLPRTAEE FSSADYWERF FRKRGEKAFE WYGDYNSLCG VLHKYIKPRD KVLVVGCGNS
ELSEQLYDVG YRQLTNIDIS ETVVSHMNQR NAERRPDLSF QQLDATQTGF ESGSFQVTLD
KGTLDAMASE EDGALAGRML AEVGRVLAVG GRYVCITLAQ EHVIKLAVEH FVKGWAVRVH
CLTGQQNEES DSSFALPVFV LVCTKFRQAP PFAVLELCQG EDGAPARLAS VEELLSAVKE
RQAYNLMLHK LKGGTDSSST PSLTLCHAAS GRPRYTLTIQ DGPPSAKTPR SNHFAIFIVP
QGRESDWLYG SAEGRAQLAS SAKFRRLVIV AMHRDQEYED MQAVQSELSP VVMELAPPGM
PANQQVPFLS VGGDLGWREV IGRGLSALTG EYSVEDVRGE DGYLYRRLIF MNNSQLVQSE
SRLQSAAAAS SASKKKNKKK AKQPASTGAK DRSVDRGFLC CTHHEVMVAG LAMLGMDAIN
NKDQPVSVLL VGLGGGGLPQ FVRDFVPCAR VEVVELDPVV LDVAQTWFGF QIDDRLKVTL
GDGLDHITTL ESEGERYFDV IMFDVDSKDT TLGMSCPPPA FVETSLLKKV YSLLSPRGLF
MLNLVCRDSA LRKSVLDRVH SVFPCVFSRG IEGEVNEVLL CCRSSGEHKP HTVPQTLQQT
AKDLQKTLRA NSQTAPQIDI TAMLNDLKVV
