P40999 (PMT1M_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
tRNA (cytosine(38)-C(5))-methyltransferase
EC=2.1.1.204

Alternative name(s):
DNA (cytosine-5)-methyltransferase-like protein 2
Short name=Dnmt2
M.SpomI
SpIM.SpoI

Gene names

Name:	pmt1
ORF Names:	SPBC19C2.02

Organism

Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) [Reference proteome]

Taxonomic identifier

284812 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces › Schizosaccharomyces pombe

Protein attributes

Sequence length	330 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Specifically methylates cytosine 38 in the anticodon loop of tRNA(Asp). Can also methylate cytosine 38 in tRNA(Glu), albeit to a lower level, but not tRNA(Lys). Pmt1-dependent tRNA methylation is induced by nitrogen limitation and depends on the nutrient-sensing protein kinase sck2. Does not have DNA-methylation activity. Ref.5
Catalytic activity	S-adenosyl-L-methionine + cytosine38 in tRNA = S-adenosyl-L-homocysteine + 5-methylcytosine38 in tRNA.
Subcellular location	Cytoplasm. Nucleus Ref.4.
Induction	Constitutively expressed at protein and RNA levels. Ref.5
Sequence similarities	Belongs to the C5-methyltransferase family.
Caution	Was originally thought not to have cytosine-5 methyltransferase activity, and this was attributed to the insertion of a Ser residue between the Pro-Cys motif found at the active site of C5 MTases (Ref.3). When this serine is deleted it becomes catalytically active and recognizes and methylates the sequence CC[AT]GG. This was in agreement with S.pombe lacking m5C DNA-methylation. However, it has later been shown that it has tRNA-methyltransferase activity despite this sequence variation (Ref.5).

Ontologies

Keywords
Biological process	tRNA processing
Cellular component	Cytoplasm Nucleus
Ligand	RNA-binding S-adenosyl-L-methionine
Molecular function	Methyltransferase Transferase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	tRNA methylation in response to nitrogen starvation Inferred from mutant phenotype Ref.5. Source: PomBase
Cellular_component	cytosol Inferred from direct assay Ref.4. Source: PomBase nucleus Inferred from direct assay Ref.4. Source: PomBase
Molecular_function	RNA binding Inferred from electronic annotation. Source: UniProtKB-KW methyltransferase activity 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 – 330	330	tRNA (cytosine(38)-C(5))-methyltransferase		PRO_0000088042
Sites
	Active site	81	1	By similarity
Experimental info
	Mutagenesis	81	1	C → A: Loss of methyltransferase activity. Ref.5

Sequences

	Sequence		Length	Mass (Da)
	P40999 [UniParc]. Last modified February 1, 1995. Version 1. Checksum: 50A7121FA7CF58A1	FASTA	330	37,976
	10 20 30 40 50 60 MLSTKRLRVL ELYSGIGGMH YALNLANIPA DIVCAIDINP QANEIYNLNH GKLAKHMDIS 70 80 90 100 110 120 TLTAKDFDAF DCKLWTMSPS CQPFTRIGNR KDILDPRSQA FLNILNVLPH VNNLPEYILI 130 140 150 160 170 180 ENVQGFEESK AAEECRKVLR NCGYNLIEGI LSPNQFNIPN SRSRWYGLAR LNFKGEWSID 190 200 210 220 230 240 DVFQFSEVAQ KEGEVKRIRD YLEIERDWSS YMVLESVLNK WGHQFDIVKP DSSSCCCFTR 250 260 270 280 290 300 GYTHLVQGAG SILQMSDHEN THEQFERNRM ALQLRYFTAR EVARLMGFPE SLEWSKSNVT 310 320 330 EKCMYRLLGN SINVKVVSYL ISLLLEPLNF

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The fission yeast gene pmt1+ encodes a DNA methyltransferase homologue." Wilkinson C.R.M., Bartlett R., Nurse P., Bird A.P. Nucleic Acids Res. 23:203-210(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], CHARACTERIZATION. Strain: 972 / ATCC 24843.
[2]	"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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 972 / ATCC 24843.
[3]	"Activation of a yeast pseudo DNA methyltransferase by deletion of a single amino acid." Pinarbasi E., Elliott J., Hornby D.P. J. Mol. Biol. 257:804-813(1996) [PubMed] [Europe PMC] [Abstract] Cited for: CHARACTERIZATION.
[4]	"ORFeome cloning and global analysis of protein localization in the fission yeast Schizosaccharomyces pombe." Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S., Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S., Yoshida M. Nat. Biotechnol. 24:841-847(2006) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[5]	"Pmt1, a Dnmt2 homolog in Schizosaccharomyces pombe, mediates tRNA methylation in response to nutrient signaling." Becker M., Muller S., Nellen W., Jurkowski T.P., Jeltsch A., Ehrenhofer-Murray A.E. Nucleic Acids Res. 40:11648-11658(2012) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, MUTAGENESIS OF CYS-81, INDUCTION.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X82444 Genomic DNA. Translation: CAA57824.1. CU329671 Genomic DNA. Translation: CAB52029.1.
PIR	S53990.
RefSeq	NP_595687.1. NM_001021584.2.
3D structure databases
ProteinModelPortal	P40999.
ModBase	Search...
Protein-protein interaction databases
STRING	4896.SPBC19C2.02-1.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	SPBC19C2.02.1; SPBC19C2.02.1:pep; SPBC19C2.02.
GeneID	2540766.
KEGG	spo:SPBC19C2.02.
Organism-specific databases
PomBase	SPBC19C2.02.
Phylogenomic databases
eggNOG	COG0270.
HOGENOM	HOG000265038.
KO	K15336.
OMA	RLMSFPE.
OrthoDB	EOG4M3DJS.
Family and domain databases
InterPro	IPR018117. C5_DNA_meth_AS. IPR001525. C5_MeTfrase. [Graphical view]
PANTHER	PTHR10629. PTHR10629. 1 hit.
Pfam	PF00145. DNA_methylase. 1 hit. [Graphical view]
PRINTS	PR00105. C5METTRFRASE.
TIGRFAMs	TIGR00675. dcm. 1 hit.
PROSITE	PS00094. C5_MTASE_1. False negative. PS00095. C5_MTASE_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	20801885.

Entry information

Entry name

PMT1M_SCHPO

Accession

Primary (citable) accession number: P40999

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1995
Last sequence update:	February 1, 1995
Last modified:	May 1, 2013
This is version 88 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program