NSUN2_DROME
ID NSUN2_DROME Reviewed; 746 AA.
AC Q9W4M9; O97427;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=tRNA (cytosine(34)-C(5))-methyltransferase;
DE EC=2.1.1.203 {ECO:0000269|PubMed:22541559};
DE AltName: Full=NOP2/Sun domain family member 2 ortholog {ECO:0000303|PubMed:22541559};
GN Name=Nsun2 {ECO:0000303|PubMed:22541559, ECO:0000312|FlyBase:FBgn0026079};
GN ORFNames=CG6133 {ECO:0000312|FlyBase:FBgn0026079};
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Oregon-R;
RX PubMed=10731137; DOI=10.1126/science.287.5461.2220;
RA Benos P.V., Gatt M.K., Ashburner M., Murphy L., Harris D., Barrell B.G.,
RA Ferraz C., Vidal S., Brun C., Demailles J., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Borkova D., Minana B., Kafatos F.C.,
RA Louis C., Siden-Kiamos I., Bolshakov S., Papagiannakis G., Spanos L.,
RA Cox S., Madueno E., de Pablos B., Modolell J., Peter A., Schoettler P.,
RA Werner M., Mourkioti F., Beinert N., Dowe G., Schaefer U., Jaeckle H.,
RA Bucheton A., Callister D.M., Campbell L.A., Darlamitsou A., Henderson N.S.,
RA McMillan P.J., Salles C., Tait E.A., Valenti P., Saunders R.D.C.,
RA Glover D.M.;
RT "From sequence to chromosome: the tip of the X chromosome of D.
RT melanogaster.";
RL Science 287:2220-2222(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [5]
RP FUNCTION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=22541559; DOI=10.1016/j.ajhg.2012.03.021;
RA Abbasi-Moheb L., Mertel S., Gonsior M., Nouri-Vahid L., Kahrizi K.,
RA Cirak S., Wieczorek D., Motazacker M.M., Esmaeeli-Nieh S., Cremer K.,
RA Weissmann R., Tzschach A., Garshasbi M., Abedini S.S., Najmabadi H.,
RA Ropers H.H., Sigrist S.J., Kuss A.W.;
RT "Mutations in NSUN2 cause autosomal-recessive intellectual disability.";
RL Am. J. Hum. Genet. 90:847-855(2012).
CC -!- FUNCTION: RNA methyltransferase that methylates tRNAs. Methylates
CC cytosine to 5-methylcytosine (m5C) at position 34 of intron-containing
CC tRNA(Leu)(CAA) precursors. Required for short-term memory.
CC {ECO:0000269|PubMed:22541559}.
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:0000269|PubMed:22541559};
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus
CC {ECO:0000250|UniProtKB:Q08J23}.
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed during embryonic
CC development. Some enrichment is observed in the proventriculus area of
CC the foregut and in the hindgut. {ECO:0000269|PubMed:22541559}.
CC -!- DEVELOPMENTAL STAGE: Expressed maternally and zygotically. Expressed
CC during embryonic development. {ECO:0000269|PubMed:22541559}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. RsmB/NOP family. TRM4 subfamily. {ECO:0000255|PROSITE-
CC ProRule:PRU01023}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA21831.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AE014298; AAF45921.1; -; Genomic_DNA.
DR EMBL; AL033125; CAA21831.1; ALT_FRAME; Genomic_DNA.
DR EMBL; AY061496; AAL29044.1; -; mRNA.
DR RefSeq; NP_652007.1; NM_143750.3.
DR AlphaFoldDB; Q9W4M9; -.
DR SMR; Q9W4M9; -.
DR BioGRID; 69457; 22.
DR IntAct; Q9W4M9; 2.
DR STRING; 7227.FBpp0070637; -.
DR PaxDb; Q9W4M9; -.
DR PRIDE; Q9W4M9; -.
DR EnsemblMetazoa; FBtr0070669; FBpp0070637; FBgn0026079.
DR GeneID; 45064; -.
DR KEGG; dme:Dmel_CG6133; -.
DR UCSC; CG6133-RA; d. melanogaster.
DR CTD; 54888; -.
DR FlyBase; FBgn0026079; Nsun2.
DR VEuPathDB; VectorBase:FBgn0026079; -.
DR eggNOG; KOG2198; Eukaryota.
DR GeneTree; ENSGT00940000153665; -.
DR HOGENOM; CLU_005316_4_3_1; -.
DR InParanoid; Q9W4M9; -.
DR OMA; QLFTEYV; -.
DR OrthoDB; 911098at2759; -.
DR PhylomeDB; Q9W4M9; -.
DR BRENDA; 2.1.1.203; 1994.
DR BioGRID-ORCS; 45064; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 45064; -.
DR PRO; PR:Q9W4M9; -.
DR Proteomes; UP000000803; Chromosome X.
DR Bgee; FBgn0026079; Expressed in embryonic/larval proventriculus (Drosophila) and 25 other tissues.
DR Genevisible; Q9W4M9; DM.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005730; C:nucleolus; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:FlyBase.
DR GO; GO:0008168; F:methyltransferase activity; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; IMP:FlyBase.
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:0001510; P:RNA methylation; ISS:FlyBase.
DR GO; GO:0007614; P:short-term memory; IMP:FlyBase.
DR GO; GO:0030488; P:tRNA methylation; IMP:FlyBase.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR018314; Fmu/NOL1/Nop2p_CS.
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; PS01153; NOL1_NOP2_SUN; 1.
DR PROSITE; PS51686; SAM_MT_RSMB_NOP; 1.
PE 2: Evidence at transcript level;
KW Methyltransferase; Nucleus; Phosphoprotein; Reference proteome;
KW RNA-binding; S-adenosyl-L-methionine; Transferase; tRNA processing;
KW tRNA-binding.
FT CHAIN 1..746
FT /note="tRNA (cytosine(34)-C(5))-methyltransferase"
FT /id="PRO_0000289228"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 454..475
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 701..746
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 12..30
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 711..746
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 323
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 216
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01023"
FT BINDING 243
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 746 AA; 84162 MW; 5178D0D26097C5F0 CRC64;
MGRNQKQNFF AARKRQKREN GPKRTDRQAQ PYEEIKRDNA FFIKYYQLQK ICATDEEWTQ
FLASIRDNLP TTFRVTGFKD EAKALLSIIE TQLFTEYVRA VAELHQKAPE DVERPLCLPW
YPNGLAYQLH LTRKDIRRSE PLYRLHNFLI VETTAGGISR QEAVSMIPPI VLDVRPTDKV
LDMCAAPGSK TAQLIEALHA APEEHKIPPG FVLANDVDNN RCYMLVHQAK RLNSPCLLVT
NHDSSVFPNL VTTKPDGSKA ILKFDKILCD VPCSGDGTLR KNPDIWLKWN LAQAYNLHGI
QYRIVRRGAE MLEVGGRLVY STCSLNPIEN EAVLQRIIKD ADGALELVDA GHLVPGLKYK
PGMTDWKLAT KEVDQIFTRF EEVPESLHTI IRPGMFPLPA DEMAKIGLEK CLRVLPHLQD
SGGFFVAVLE KRRQLSFEKN DVVELVKLNE TAKQPAAEPQ VDADGKPIEE KSVPWGPQRK
KRRLHGYKED PYVFFGENDP DYQAIKEFYQ LDESLSQRCL LTRCVTEKKK NIYYCSEPIR
DLVLNNENNI KIINTGVKTF VRCENRHTVH PFRLAQEGLQ TSNAFMGASR RIQVEREDLV
MMLNCTDPTQ PPSTHELKKE TQERCKELGV GSCILKYVDQ RFTLYTVGWR GTSSLRAYVQ
KDETIHILRL LGADLSKFET NKYEDARVAA AAAADAEVGK SAEAEADSSG DGDATESTFS
GSGAIDVTVA AETTGTPMDT EVVATS
