Q6BQD2 (LCMT1_DEBHA) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Leucine carboxyl methyltransferase 1
EC=2.1.1.233

Alternative name(s):
Protein phosphatase methyltransferase 1
[Phosphatase 2A protein]-leucine-carboxy methyltransferase 1

Gene names

Name:	PPM1
Ordered Locus Names:	DEHA2E06094g

Organism

Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / JCM 1990 / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii) [Complete proteome]

Taxonomic identifier

284592 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Saccharomycotina › Saccharomycetes › Saccharomycetales › Debaryomycetaceae › Debaryomyces › Debaryomyces hansenii › Debaryomyces hansenii var. hansenii

Protein attributes

Sequence length	369 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Methylates the carboxyl group of the C-terminal leucine residue of protein phosphatase 2A catalytic subunits to form alpha-leucine ester residues By similarity.
Catalytic activity	S-adenosyl-L-methionine + [phosphatase 2A protein]-leucine = S-adenosyl-L-homocysteine + [phosphatase 2A protein]-leucine methyl ester.
Sequence similarities	Belongs to the methyltransferase superfamily. LCMT family.

Ontologies

Keywords
Ligand	S-adenosyl-L-methionine
Molecular function	Methyltransferase Transferase
Technical term	Complete proteome
Gene Ontology (GO)
Molecular_function	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 – 369	369	Leucine carboxyl methyltransferase 1		PRO_0000226127
Regions
	Region	187 – 188	2	S-adenosyl-L-methionine binding By similarity
Sites
	Binding site	84	1	S-adenosyl-L-methionine By similarity
	Binding site	108	1	S-adenosyl-L-methionine; via carbonyl oxygen By similarity
	Binding site	132	1	S-adenosyl-L-methionine By similarity
	Binding site	215	1	S-adenosyl-L-methionine; via carbonyl oxygen By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q6BQD2 [UniParc]. Last modified December 16, 2008. Version 2. Checksum: 67A1F2B3AE0E40A1	FASTA	369	42,526
	10 20 30 40 50 60 MISPQEKQDK VIRATDLDAL SCRYSANNKS YFSKPDPFID SLISSYKMHL PLCTGYTNMS 70 80 90 100 110 120 ANRTLRSVFN EQKLPLINRG TYLRTESIDV ITQEFIKEFK KCQVISLGGG SDTRCFRILE 130 140 150 160 170 180 EHGEDVRYCE IDFHESVKIK KLAIINDKKL ADIVKYDEES QSITSKEEFA RLESNIHTEN 190 200 210 220 230 240 YHLIGYDLRE LTGALDSGAI LEYVDTSLPT LILSECVLCY LNPKENERII EFWKNAFASK 250 260 270 280 290 300 ALLALLIYEP MSLNDAFGTT MTHNLSNRGI NLLTFNEYPN LEARYKFLSE KCQSSNVKLT 310 320 330 340 350 360 DMSNVGGYDS DNTTKAWINS KDLARINRLE LVDEIEEIRL LLKHYCLCYC EFSHSPSLKT INKWKWILE

References

[1]

"Genome evolution in yeasts." Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I., de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L., Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S. , Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J., Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E., Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C., Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M., Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S., Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F., Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M., Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M., Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J., Wincker P., Souciet J.-L. Nature 430:35-44(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 36239 / CBS 767 / JCM 1990 / NBRC 0083 / IGC 2968.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CR382137 Genomic DNA. Translation: CAG87815.2.
RefSeq	XP_459588.2. XM_459588.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	4959.Q6BQD2.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	2901885.
KEGG	dha:DEHA2E06094g.
Phylogenomic databases
eggNOG	NOG329644.
HOGENOM	HOG000205368.
OMA	ECVLVYI.
OrthoDB	EOG4ZW8MC.
Family and domain databases
InterPro	IPR007213. LCM_MeTrfase. IPR021121. LCM_MeTrfase_euk. IPR016651. Leu_CO_MeTrfase_LCTM1. [Graphical view]
PANTHER	PTHR13600. PTHR13600. 1 hit.
Pfam	PF04072. LCM. 1 hit. [Graphical view]
PIRSF	PIRSF016305. LCM_mtfrase. 1 hit.
ProtoNet	Search...

Entry information

Entry name

LCMT1_DEBHA

Accession

Primary (citable) accession number: Q6BQD2

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 7, 2006
Last sequence update:	December 16, 2008
Last modified:	May 1, 2013
This is version 47 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program