ID   MET23_XENLA             Reviewed;         234 AA.
AC   Q6DJF8;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   03-AUG-2022, entry version 64.
DE   RecName: Full=Histone-arginine methyltransferase METTL23 {ECO:0000305};
DE            EC=2.1.1.319 {ECO:0000250|UniProtKB:A2AA28};
DE   AltName: Full=Methyltransferase-like protein 23 {ECO:0000305};
GN   Name=mettl23;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Eye;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Histone methyltransferase that dimethylates histone H3 at
CC       'Arg-17', forming asymmetric dimethylarginine (H3R17me2a), leading to
CC       activate transcription via chromatin remodeling.
CC       {ECO:0000250|UniProtKB:A2AA28}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-arginyl-[protein] + 2 S-adenosyl-L-methionine = 2 H(+) +
CC         N(omega),N(omega)-dimethyl-L-arginyl-[protein] + 2 S-adenosyl-L-
CC         homocysteine; Xref=Rhea:RHEA:48096, Rhea:RHEA-COMP:10532, Rhea:RHEA-
CC         COMP:11991, ChEBI:CHEBI:15378, ChEBI:CHEBI:29965, ChEBI:CHEBI:57856,
CC         ChEBI:CHEBI:59789, ChEBI:CHEBI:61897; EC=2.1.1.319;
CC         Evidence={ECO:0000250|UniProtKB:A2AA28};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48097;
CC         Evidence={ECO:0000250|UniProtKB:A2AA28};
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:A2AA28}. Cytoplasm
CC       {ECO:0000250|UniProtKB:A2AA28}.
CC   -!- SIMILARITY: Belongs to the methyltransferase superfamily. METTL23
CC       family. {ECO:0000305}.
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DR   EMBL; BC075221; AAH75221.1; -; mRNA.
DR   RefSeq; NP_001086389.1; NM_001092920.1.
DR   AlphaFoldDB; Q6DJF8; -.
DR   SMR; Q6DJF8; -.
DR   MaxQB; Q6DJF8; -.
DR   DNASU; 444818; -.
DR   GeneID; 444818; -.
DR   KEGG; xla:444818; -.
DR   CTD; 444818; -.
DR   OMA; LMQDHTI; -.
DR   OrthoDB; 1588190at2759; -.
DR   Proteomes; UP000186698; Chromosome 9_10S.
DR   Bgee; 444818; Expressed in brain and 19 other tissues.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0035642; F:histone methyltransferase activity (H3-R17 specific); ISS:UniProtKB.
DR   GO; GO:0035242; F:protein-arginine omega-N asymmetric methyltransferase activity; IEA:RHEA.
DR   GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR   GO; GO:0034971; P:histone H3-R17 methylation; ISS:UniProtKB.
DR   Gene3D; 3.40.50.150; -; 1.
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.
PE   2: Evidence at transcript level;
KW   Chromatin regulator; Cytoplasm; Methyltransferase; Nucleus;
KW   Reference proteome; S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..234
FT                   /note="Histone-arginine methyltransferase METTL23"
FT                   /id="PRO_0000321523"
SQ   SEQUENCE   234 AA;  26502 MW;  B085645E21C48514 CRC64;
     MGEENEQRIG ERVYEFLRRE GKDEQKMRVT IPEVLNCQYG MYVWPCAVVL AQYLWYHRKN
     LADKRVLEVG AGVSLPGILA AKCGAKVILS DSAEMPQCLE NCRRSCKMNN IVGVPVIGLT
     WGEVSPDLLD LPPIDIILGS DVFYEPKDFE DILLTVRFLM ERMPQAEFWT TYQVRSADWS
     VEALLCKWNL KCTNVPLKTF DADNECLAGS ELPGRHTVQM MIITLDRKGA GHTG