Reviewed, UniProtKB/Swiss-Prot Q9W4M9 (NSUN2_DROME)

Names and origin

Protein names

Recommended name:
    tRNA (cytosine-5-)-methyltransferase CG6133
    EC=2.1.1.29

Gene names

ORF Names:

CG6133

Organism

Drosophila melanogaster (Fruit fly) [Complete proteome]

Taxonomic identifier

7227 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Ephydroidea › Drosophilidae › Drosophila › Sophophora

Protein attributes

Sequence length	746 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at transcript level.

General annotation (Comments)

Function	RNA methyltransferase that methylates tRNAs. Methylates cytosine to 5-methylcytosine (m5C) at position 34 of intron-containing tRNA(Leu)(CAA) precursors By similarity.
Catalytic activity	S-adenosyl-L-methionine + tRNA = S-adenosyl-L-homocysteine + tRNA containing 5-methylcytosine.
Subcellular location	Nucleus › nucleolus By similarity.
Sequence similarities	Belongs to the methyltransferase superfamily. RsmB/NOP family. TRM4 subfamily.
Sequence caution	The sequence CAA21831.1 differs from that shown. Reason: Frameshift at position 709.

Ontologies

Keywords
Biological process	tRNA processing
Cellular component	Nucleus
Ligand	RNA-binding S-adenosyl-L-methionine tRNA-binding
Molecular function	Methyltransferase Transferase
PTM	Phosphoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	tRNA methylation Inferred from sequence or structural similarity. Source: UniProtKB
Cellular component	cytoplasm Inferred from sequence or structural similarity. Source: UniProtKB nucleolus Inferred from sequence or structural similarity. Source: UniProtKB
Molecular function	tRNA (cytosine-5-)-methyltransferase activity Inferred from sequence or structural similarity. Source: UniProtKB tRNA binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 746	746	tRNA (cytosine-5-)-methyltransferase CG6133		PRO_0000289228
Regions
	Region	184 – 190	7	S-adenosyl-L-methionine binding By similarity
Sites
	Active site	323	1	Nucleophile Potential
	Binding site	216	1	S-adenosyl-L-methionine By similarity
	Binding site	243	1	S-adenosyl-L-methionine By similarity
	Binding site	270	1	S-adenosyl-L-methionine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9W4M9-1 [UniParc]. Last modified May 1, 2000. Version 1. Checksum: 5178D0D26097C5F0	FASTA	746	84,162
	10 20 30 40 50 60 MGRNQKQNFF AARKRQKREN GPKRTDRQAQ PYEEIKRDNA FFIKYYQLQK ICATDEEWTQ 70 80 90 100 110 120 FLASIRDNLP TTFRVTGFKD EAKALLSIIE TQLFTEYVRA VAELHQKAPE DVERPLCLPW 130 140 150 160 170 180 YPNGLAYQLH LTRKDIRRSE PLYRLHNFLI VETTAGGISR QEAVSMIPPI VLDVRPTDKV 190 200 210 220 230 240 LDMCAAPGSK TAQLIEALHA APEEHKIPPG FVLANDVDNN RCYMLVHQAK RLNSPCLLVT 250 260 270 280 290 300 NHDSSVFPNL VTTKPDGSKA ILKFDKILCD VPCSGDGTLR KNPDIWLKWN LAQAYNLHGI 310 320 330 340 350 360 QYRIVRRGAE MLEVGGRLVY STCSLNPIEN EAVLQRIIKD ADGALELVDA GHLVPGLKYK 370 380 390 400 410 420 PGMTDWKLAT KEVDQIFTRF EEVPESLHTI IRPGMFPLPA DEMAKIGLEK CLRVLPHLQD 430 440 450 460 470 480 SGGFFVAVLE KRRQLSFEKN DVVELVKLNE TAKQPAAEPQ VDADGKPIEE KSVPWGPQRK 490 500 510 520 530 540 KRRLHGYKED PYVFFGENDP DYQAIKEFYQ LDESLSQRCL LTRCVTEKKK NIYYCSEPIR 550 560 570 580 590 600 DLVLNNENNI KIINTGVKTF VRCENRHTVH PFRLAQEGLQ TSNAFMGASR RIQVEREDLV 610 620 630 640 650 660 MMLNCTDPTQ PPSTHELKKE TQERCKELGV GSCILKYVDQ RFTLYTVGWR GTSSLRAYVQ 670 680 690 700 710 720 KDETIHILRL LGADLSKFET NKYEDARVAA AAAADAEVGK SAEAEADSSG DGDATESTFS 730 740 GSGAIDVTVA AETTGTPMDT EVVATS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The genome sequence of Drosophila melanogaster." Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D. , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C. Science 287:2185-2195(2000) [PubMed: 10731132] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Berkeley.
[2]	"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review." Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E. Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed: 12537572] [Abstract] Cited for: GENOME REANNOTATION.
[3]	"From sequence to chromosome: the tip of the X chromosome of D. melanogaster." Benos P.V., Gatt M.K., Ashburner M., Murphy L., Harris D., Barrell B.G., Ferraz C., Vidal S., Brun C., Demailles J., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Borkova D., Minana B. , Kafatos F.C., Louis C., Siden-Kiamos I., Bolshakov S., Papagiannakis G., Spanos L., Cox S., Madueno E., de Pablos B., Modolell J., Peter A., Schoettler P., Werner M., Mourkioti F., Beinert N., Dowe G., Schaefer U., Jaeckle H., Bucheton A., Callister D.M., Campbell L.A., Darlamitsou A., Henderson N.S., McMillan P.J., Salles C., Tait E.A., Valenti P., Saunders R.D.C., Glover D.M. Science 287:2220-2222(2000) [PubMed: 10731137] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Oregon-R.
[4]	"A Drosophila full-length cDNA resource." Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., Celniker S.E. Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed: 12537569] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Berkeley. Tissue: Embryo.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AE014298 Genomic DNA. Translation: AAF45921.1. AL033125 Genomic DNA. Translation: CAA21831.1. Frameshift. AY061496 mRNA. Translation: AAL29044.1.
RefSeq	NP_652007.1.
UniGene	Dm.3580
3D structure databases
HSSP	HSSP built from PDB template 1IXK based on UniProtKB O50082.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9W4M9. 1 interaction.
Proteomic databases
PRIDE	Q9W4M9.
Genome annotation databases
Ensembl	FBgn0026079. Drosophila melanogaster. [Contig view]
GeneID	45064.
KEGG	dme:Dmel_CG6133.
NMPDR	fig|7227.3.peg.16443.
Organism-specific databases
FlyBase	FBgn0026079. CG6133.
Phylogenomic databases
OMA	Q9W4M9. SMPWNKR.
Enzyme and pathway databases
BRENDA	2.1.1.29. 48.
Gene expression databases
ArrayExpress	Q9W4M9.
Family and domain databases
InterPro	IPR001678. Fmu/NOL1/Nop2p. IPR018314. Fmu/NOL1/Nop2p_CS. [Graphical view]
Pfam	PF01189. Nol1_Nop2_Fmu. 2 hits. [Graphical view]
PROSITE	PS01153. NOL1_NOP2_SUN. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	837913.

Entry information

Entry name

NSUN2_DROME

Accession

Primary (citable) accession number: Q9W4M9
Secondary accession number(s): O97427

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 29, 2007
Last sequence update:	May 1, 2000
Last modified:	June 16, 2009
This is version 53 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

Drosophila annotation project