NSUN2_XENLA
ID NSUN2_XENLA Reviewed; 698 AA.
AC Q4V7N2;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 70.
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};
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=Egg;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JUN-2005) 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; BC097814; AAH97814.1; -; mRNA.
DR RefSeq; NP_001084513.1; NM_001091044.1.
DR AlphaFoldDB; Q4V7N2; -.
DR SMR; Q4V7N2; -.
DR BioGRID; 100882; 1.
DR DNASU; 414460; -.
DR GeneID; 414460; -.
DR KEGG; xla:414460; -.
DR CTD; 414460; -.
DR Xenbase; XB-GENE-962628; nsun2.S.
DR Proteomes; UP000186698; Chromosome 6S.
DR Bgee; 414460; Expressed in egg cell and 19 other tissues.
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:0005819; C:spindle; IEA:UniProtKB-SubCell.
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; IEA:UniProtKB-KW.
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: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..698
FT /note="RNA cytosine-C(5)-methyltransferase NSUN2"
FT /id="PRO_0000289226"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 472..496
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 12..28
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 479..496
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 319
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01023"
FT BINDING 182..188
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01023"
FT BINDING 213
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01023"
FT BINDING 240
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01023"
FT BINDING 266
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01023"
SQ SEQUENCE 698 AA; 80051 MW; 3AD1F0DEF6CCBB43 CRC64;
MGRKNRRNRQ RRTEQRSPAE EERRKAREQA AWEGGYPEII KENKLFEHYY QELKIVPDGE
WDKFMDALRE PLPATIRITG YKSHAKEILH CLKEKYFKEL PDIEVDGQKI EAPQPLSWYP
EELAWHTNLS RKIIRKSPEL EKFHQFLVSE TESGNISRQE AVSMIPPVLL NVQPHHKILD
MCAAPGSKTA QIIEMLHADM NVPFPEGFVI ANDVDNKRCY LLVHQAKRLN SPCIMVVNHD
ASSIPRLLIE NNGSREVLYY DRILCDVPCS GDGTMRKNID VWKKWTTLNS LQLHGLQIRI
ATRGVEQLAE GGRMVYSTCS LNPVEDEAVI VSLLDKSEGS LELADVASEL PGLKWMPGIT
QWRVMTKEGQ WFEKWEDVPT SRHTQIRPTM FPLKDEEKLK SMNLNRCMRI LPHHQNTGGF
FVAVLIKKAP MPWNKRQPKL QRRPPVSVCD ASVAPEIVKA VADISAIADE PAVDAENGET
KPCTNQSGSS KTDSVCCPPP SKKMKLFGFK EDPFVFLSED DPIFEPIQKF YALDPSFPKK
NLLTRTQEGK KRQLYMVSKE LRNVLLHNSE KMKVINTGIK VLCRNNDGEQ YGCAYRLAQE
GIYSLYPFIN ARILTVSVED IKVLLTQENP FLSKFSKETQ KQANNLDMGS IVLKYEPDPQ
QPETLQCPIV LCGWRGKTSI RSFVFFLHRI NLVQWIFI
