NSUN2_XENTR
ID NSUN2_XENTR Reviewed; 798 AA.
AC Q28E61;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 04-APR-2006, sequence version 1.
DT 03-AUG-2022, entry version 73.
DE RecName: Full=RNA cytosine-C(5)-methyltransferase NSUN2 {ECO:0000305};
DE EC=2.1.1.- {ECO:0000250|UniProtKB:Q08J23};
DE AltName: Full=NOL1/NOP2/Sun domain family member 2 {ECO:0000250|UniProtKB:Q08J23};
DE AltName: Full=mRNA cytosine C(5)-methyltransferase {ECO:0000305};
DE EC=2.1.1.- {ECO:0000250|UniProtKB:Q08J23};
DE AltName: Full=tRNA cytosine C(5)-methyltransferase {ECO:0000305};
DE EC=2.1.1.- {ECO:0000250|UniProtKB:Q08J23};
DE EC=2.1.1.203 {ECO:0000250|UniProtKB:Q08J23};
GN Name=nsun2 {ECO:0000250|UniProtKB:Q08J23};
GN ORFNames=TEgg048n02.1 {ECO:0000303|Ref.1};
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Egg;
RG Sanger Xenopus tropicalis EST/cDNA project;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: RNA cytosine C(5)-methyltransferase that methylates cytosine
CC to 5-methylcytosine (m5C) in various RNAs, such as tRNAs, mRNAs and
CC some long non-coding RNAs (lncRNAs). Involved in various processes,
CC such as epidermal stem cell differentiation, testis differentiation and
CC maternal to zygotic transition during early development: acts by
CC increasing protein synthesis; cytosine C(5)-methylation promoting tRNA
CC stability and preventing mRNA decay. Methylates cytosine to 5-
CC methylcytosine (m5C) at positions 34 and 48 of intron-containing
CC tRNA(Leu)(CAA) precursors, and at positions 48, 49 and 50 of
CC tRNA(Gly)(GCC) precursors. tRNA methylation is required generation of
CC RNA fragments derived from tRNAs (tRFs). Also mediates C(5)-methylation
CC of mitochondrial tRNAs. Catalyzes cytosine C(5)-methylation of mRNAs,
CC leading to stabilize them and prevent mRNA decay. Cytosine C(5)-
CC methylation of mRNAs also regulates mRNA export. Also mediates cytosine
CC C(5)-methylation of non-coding RNAs, such as vault RNAs (vtRNAs),
CC promoting their processing into regulatory small RNAs. Required for
CC proper spindle assembly and chromosome segregation, independently of
CC its methyltransferase activity. {ECO:0000250|UniProtKB:Q08J23}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=cytidine(48) in tRNA + S-adenosyl-L-methionine = 5-
CC methylcytidine(48) in tRNA + H(+) + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:42948, Rhea:RHEA-COMP:10293, Rhea:RHEA-COMP:10297,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:74483, ChEBI:CHEBI:82748;
CC Evidence={ECO:0000250|UniProtKB:Q08J23};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42949;
CC Evidence={ECO:0000250|UniProtKB:Q08J23};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=cytidine(49) in tRNA + S-adenosyl-L-methionine = 5-
CC methylcytidine(49) in tRNA + H(+) + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:42952, Rhea:RHEA-COMP:10294, Rhea:RHEA-COMP:10385,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:74483, ChEBI:CHEBI:82748;
CC Evidence={ECO:0000250|UniProtKB:Q08J23};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42953;
CC Evidence={ECO:0000250|UniProtKB:Q08J23};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=cytidine(50) in tRNA + S-adenosyl-L-methionine = 5-
CC methylcytidine(50) in tRNA + H(+) + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:61488, Rhea:RHEA-COMP:15838, Rhea:RHEA-COMP:15839,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:74483, ChEBI:CHEBI:82748;
CC Evidence={ECO:0000250|UniProtKB:Q08J23};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61489;
CC Evidence={ECO:0000250|UniProtKB:Q08J23};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=cytidine(34) in tRNA precursor + S-adenosyl-L-methionine = 5-
CC methylcytidine(34) in tRNA precursor + H(+) + S-adenosyl-L-
CC homocysteine; Xref=Rhea:RHEA:42940, Rhea:RHEA-COMP:10291, Rhea:RHEA-
CC COMP:10295, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:74483, ChEBI:CHEBI:82748; EC=2.1.1.203;
CC Evidence={ECO:0000250|UniProtKB:Q08J23};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42941;
CC Evidence={ECO:0000250|UniProtKB:Q08J23};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a cytidine in mRNA + S-adenosyl-L-methionine = a 5-
CC methylcytidine in mRNA + H(+) + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:61464, Rhea:RHEA-COMP:15145, Rhea:RHEA-COMP:15826,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:74483, ChEBI:CHEBI:82748;
CC Evidence={ECO:0000250|UniProtKB:Q08J23};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61465;
CC Evidence={ECO:0000250|UniProtKB:Q08J23};
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus
CC {ECO:0000250|UniProtKB:Q08J23}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q08J23}. Mitochondrion
CC {ECO:0000250|UniProtKB:Q08J23}. Cytoplasm, cytoskeleton, spindle
CC {ECO:0000250|UniProtKB:Q08J23}. Secreted, extracellular exosome
CC {ECO:0000250|UniProtKB:Q1HFZ0}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. RsmB/NOP family. TRM4 subfamily. {ECO:0000255|PROSITE-
CC ProRule:PRU01023}.
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DR EMBL; CR848434; CAJ83692.1; -; mRNA.
DR RefSeq; NP_001015962.1; NM_001015962.2.
DR RefSeq; XP_012820119.1; XM_012964665.2.
DR RefSeq; XP_012820120.1; XM_012964666.2.
DR AlphaFoldDB; Q28E61; -.
DR SMR; Q28E61; -.
DR STRING; 8364.ENSXETP00000059424; -.
DR PaxDb; Q28E61; -.
DR PRIDE; Q28E61; -.
DR Ensembl; ENSXETT00000062642; ENSXETP00000059424; ENSXETG00000001732.
DR GeneID; 548716; -.
DR KEGG; xtr:548716; -.
DR CTD; 54888; -.
DR Xenbase; XB-GENE-962623; nsun2.
DR eggNOG; KOG2198; Eukaryota.
DR InParanoid; Q28E61; -.
DR OrthoDB; 911098at2759; -.
DR Proteomes; UP000008143; Chromosome 6.
DR Proteomes; UP000790000; Unplaced.
DR Bgee; ENSXETG00000001732; Expressed in ovary and 12 other tissues.
DR ExpressionAtlas; Q28E61; baseline.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0070062; C:extracellular exosome; ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005819; C:spindle; IEA:UniProtKB-SubCell.
DR GO; GO:0008168; F:methyltransferase activity; IBA:GO_Central.
DR GO; GO:0062152; F:mRNA (cytidine-5-)-methyltransferase activity; ISS:UniProtKB.
DR GO; GO:0016428; F:tRNA (cytosine-5-)-methyltransferase activity; ISS:UniProtKB.
DR GO; GO:0000049; F:tRNA binding; IBA:GO_Central.
DR GO; GO:0080009; P:mRNA methylation; ISS:UniProtKB.
DR GO; GO:0010793; P:regulation of mRNA export from nucleus; ISS:UniProtKB.
DR GO; GO:2000736; P:regulation of stem cell differentiation; ISS:UniProtKB.
DR GO; GO:0001510; P:RNA methylation; IBA:GO_Central.
DR GO; GO:0030488; P:tRNA methylation; ISS:UniProtKB.
DR GO; GO:0036416; P:tRNA stabilization; ISS:UniProtKB.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR001678; MeTrfase_RsmB/NOP2.
DR InterPro; IPR023267; RCMT.
DR InterPro; IPR023270; RCMT_NCL1.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR22808; PTHR22808; 1.
DR Pfam; PF01189; Methyltr_RsmB-F; 1.
DR PRINTS; PR02008; RCMTFAMILY.
DR PRINTS; PR02011; RCMTNCL1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR PROSITE; PS51686; SAM_MT_RSMB_NOP; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; Cytoskeleton; Methyltransferase; Mitochondrion; Nucleus;
KW Phosphoprotein; Reference proteome; RNA-binding; S-adenosyl-L-methionine;
KW Secreted; Transferase; tRNA processing; tRNA-binding.
FT CHAIN 1..798
FT /note="RNA cytosine-C(5)-methyltransferase NSUN2"
FT /id="PRO_0000289227"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 476..499
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 723..798
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 14..30
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 485..499
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 723..751
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 323
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01023"
FT BINDING 186..192
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01023"
FT BINDING 217
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01023"
FT BINDING 244
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01023"
FT BINDING 270
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01023"
SQ SEQUENCE 798 AA; 91020 MW; 3F79B94FBDED8AA8 CRC64;
MGRRNRRNRQ RHQRSTEQRS PAEEEQRRKA REQAAWECGY PEIIKENKLF EHYYQELKIV
PDGEWDKFMA SLREPLPATI RITGYKSHAK EILHCLKEKY FKELQDIEVD GQKIEAPQPL
SWYPEELAWH TNLSRKIIRK SPELEKFHQF LVNETESGNI SRQEAVSMIP PVLLKVQPHH
KILDMCAAPG SKTAQIIEML HADMNVPFPE GFVIANDVDN KRCYLLVHQA KRLNSPCIMV
VNHDASSIPR LLVENNGSRE VLYYDRILCD VPCSGDGTLR KNIDVWKKWT TLNSLQLHGL
QIRIATRGVE QLAEGGRMVY STCSLNPVED EAVIASLLDK SEGSLELADV ASEIPGLKWM
PGITQWKVMT KEGHWYEKWE DIPTSRHTQI RPTMFPPKDE EKLKSMNLNR CMRILPHHQN
TGGFFVAVLI KKAPMPWNKR QPKLQRRPPV SACDASIAVA PELVKAVTEN SAGMADEPAV
DTENGETKPC TNQSDSSKTD IVCCPPPSKK MKLFGFKEDP FVFVSEDDPI FDPIQTFYAL
DPSFPKKNLL TRTQEGKKRQ LYMVSKELRN VLLHNSEKMK VINTGIKVLC RNNDGEQYGC
AYRLAQEGIY TLYPFINARI VTVSIEDIKV LLTQENPFLS KFSKETQKQA NNFDMGSIVL
KYEPDPQEPE TLQCPIVLCG WRGKTSIRSF VPKNERLHYL RMMGVEVFKE KAEVLEKKPV
EGKACDEEHI DEKMDIDGAK EESKELSGNE SGDDEDPKEE DVIDRGVLEH VALKNTSAIP
ASVEDQAEDA SVSKESVD
