NSUN2_CHICK
ID NSUN2_CHICK Reviewed; 796 AA.
AC Q5ZLV4;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 82.
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}; ORFNames=RCJMB04_4l11;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=CB; TISSUE=Bursa of Fabricius;
RX PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA Hayashizaki Y., Buerstedde J.-M.;
RT "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT function analysis.";
RL Genome Biol. 6:R6.1-R6.9(2005).
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; AJ719630; CAG31289.1; -; mRNA.
DR RefSeq; NP_001026175.1; NM_001031004.1.
DR AlphaFoldDB; Q5ZLV4; -.
DR SMR; Q5ZLV4; -.
DR STRING; 9031.ENSGALP00000021294; -.
DR PaxDb; Q5ZLV4; -.
DR PRIDE; Q5ZLV4; -.
DR GeneID; 420938; -.
DR KEGG; gga:420938; -.
DR CTD; 54888; -.
DR VEuPathDB; HostDB:geneid_420938; -.
DR eggNOG; KOG2198; Eukaryota.
DR InParanoid; Q5ZLV4; -.
DR OrthoDB; 911098at2759; -.
DR PhylomeDB; Q5ZLV4; -.
DR PRO; PR:Q5ZLV4; -.
DR Proteomes; UP000000539; Unplaced.
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..796
FT /note="RNA cytosine-C(5)-methyltransferase NSUN2"
FT /id="PRO_0000289225"
FT REGION 1..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 435..501
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 707..796
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 451..465
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 468..488
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 707..756
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 775..796
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 321
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01023"
FT BINDING 184..190
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01023"
FT BINDING 215
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01023"
FT BINDING 242
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01023"
FT BINDING 268
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01023"
SQ SEQUENCE 796 AA; 90845 MW; F2C352922B62D9AD CRC64;
MGRRARDRRR QLQPQQRRER SGGGGGGGDD QAGWAGGYPE IVKENELFER YYREQRIVPD
GEWDAFMAAL REPLPATLRI TGYKSHAREI LHCLKEKYFR ELQHLEVDGQ KVEMPQALSW
YPEELAWHTN LSRKILRKSP QLERFHQFLV SETECGNISR QEAVSMIPPL LLNVNPDHKI
LDMCAAPGSK TAQLIEMLHA DMNVPFPKGF VIANDVDNKR CYLLVHQAKR LNSPCIMVVN
HDASSIPNLQ VDVDGRKETL FYDRILCDVP CSGDGTMRKN IDVWKKWTTQ NSLQLHGLQL
RIATRGVEQL AEGGRMVYST CSLNPIENEA VIASLLEKSQ GALELADVSS ELPGLKRMPG
ITKWKVMLKD GQWFEEWKDV PSNRQTQIRP TMFPIKEEEK LKAMNLERCI RILPHHQNTG
GFFVAVLIKK SPMPWNKRQP KVHQKLPGKT EDTEVTATNA GDGSEDATEK PTLAEDEEPK
KVQELQNSDT EQSKKGVCGP PPSKKMKLFG FKEDPFVFLP EDDPLFLPIQ KFYALDPSFP
KMNLLTRTQE GKKRQLYMVS KELRNVLLNN SEKMKVINTG IKVWSRNSDG EQFGCAFRLA
QEGIYTLYPF IHARIVNVCI EDVKILLTQE NPFLSKFSSE TQRKVKDMAM GSIVLKYEPD
PEKPDDLQCP IVLCGWQGKT SLRAFVPKNE RLHYLRMMGV EVFKAKRKEG ESEGKTEEEV
QCRPAQTEEG MDVEDKERDA VTKMEAEIDE ESPRSPVESS AMEIENKSED SDQCSKNTNS
HINQESKDMN TNNVKD
