Reviewed, UniProtKB/Swiss-Prot Q9HGQ2 (NCL1_SCHPO)

Names and origin

Protein names

Recommended name:
    tRNA (cytosine-5-)-methyltransferase ncl1
    EC=2.1.1.29

Gene names

Name:	ncl1
ORF Names:	SPAC17D4.04, SPAC458.01

Organism

Schizosaccharomyces pombe (Fission yeast) [Complete proteome]

Taxonomic identifier

4896 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces

Protein attributes

Sequence length	654 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Methylates cytosine to m5C at several positions in different tRNAs and pre-tRNAs containing intron. Able to modify tRNAs at all four positions (34, 40, 48 and 49) at which m5C has been found in tRNAs 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.

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 processing Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytosol Inferred from direct assay. Source: GeneDB_SPombe nucleolus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	tRNA (cytosine-5-)-methyltransferase activity Inferred from electronic annotation. Source: EC 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 – 654	654	tRNA (cytosine-5-)-methyltransferase ncl1		PRO_0000211824
Regions
	Region	151 – 157	7	S-adenosyl-L-methionine binding By similarity
Sites
	Active site	293	1	Nucleophile Potential
	Binding site	187	1	S-adenosyl-L-methionine By similarity
	Binding site	214	1	S-adenosyl-L-methionine By similarity
	Binding site	240	1	S-adenosyl-L-methionine By similarity
Amino acid modifications
	Modified residue	38	1	Phosphothreonine Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Q9HGQ2-1 [UniParc]. Last modified May 16, 2003. Version 2. Checksum: D7ACB93F0328C69B	FASTA	654	74,555
	10 20 30 40 50 60 MTSDYVYLLD RNENFEKYYR LQKLVTEDDF ILLKQKLTEQ LPTTFRITAS IPHATQVRDY 70 80 90 100 110 120 FIEHYYPLIE NARTEDAKIP LPVSLPWYPD GMAFMLDISK EVIRKSPHLK ALQEFLVLET 130 140 150 160 170 180 EAGDINRQES VSMVPPLLLN VESHHKVLDM CAAPGSKTAQ LLEALHKPTK KEDITTLLPS 190 200 210 220 230 240 GIVIANDSDN KRAHMLVHQI KRLNSPNVLI VNHDASFLPN FHLSSPDGKK FLKFDRILAD 250 260 270 280 290 300 VPCSGDGTFR KNIALWNEWS LKTALGLHAT QIKILMRGLQ LLEKGGRLVY STCSLNPIEN 310 320 330 340 350 360 EAVVSAVLNA TRGSVRLVDV SSELPQLKRS QGVDNWVVCD SDLNIYPSFD TLPKELYEKM 370 380 390 400 410 420 PPTLWPLPKK ELAELNIQNC LRIYPHFQNT GGFFVAVLEK YENLTSSMKT AVDDNKVFLR 430 440 450 460 470 480 EQKLPSEQAS KKRKQDTQET SSDSKLAEVK PKGKNGGNRF HELDPFVYIK EDDQALEKIY 490 500 510 520 530 540 KKFGIDEAII KKNQFFVRNV NGVPTKAIYI SNDLFRNVIE NNRNRVKFVH GGLKIFVRQD 550 560 570 580 590 600 FGSLSREIAE KNGTCVFRVQ SDGANLASHF IAESCLFHTT LSDLFILLDH EAVTIDDFPE 610 620 630 640 650 DSLFRKEYNH LDLGSTLLHV DLAKEESVIK KQVYIPLWKS VRICNVLLSN SEKR

References

[1]

"The genome sequence of Schizosaccharomyces pombe." Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M. , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P. Nature 415:871-880(2002) [PubMed: 11859360] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 38366 / 972.

[2]

"Phosphoproteome analysis of fission yeast." Wilson-Grady J.T., Villen J., Gygi S.P. J. Proteome Res. 7:1088-1097(2008) [PubMed: 18257517] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-38, MASS SPECTROMETRY.

Cross-references

Sequence databases
EMBLGenBankDDBJ	CU329670 Genomic DNA. Translation: CAC05734.1.
RefSeq	NP_594695.2.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	2542264.
KEGG	spo:SPAC17D4.04.
Organism-specific databases
GeneDB_Spombe	SPAC17D4.04.
Enzyme and pathway databases
BioCyc	SPOM-XXX-01:SPOM-XXX-01-003093-MON.
BRENDA	2.1.1.29. 653.
Gene expression databases
ArrayExpress	Q9HGQ2.
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...

Entry information

Entry name

NCL1_SCHPO

Accession

Primary (citable) accession number: Q9HGQ2
Secondary accession number(s): Q9P3W7

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 16, 2003
Last sequence update:	May 16, 2003
Last modified:	June 16, 2009
This is version 45 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)