P32048 (SYKM_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Lysine--tRNA ligase, mitochondrial
EC=6.1.1.6

Alternative name(s):
Lysyl-tRNA synthetase
Short name=LysRS

Gene names

Name:	MSK1
Ordered Locus Names:	YNL073W
ORF Names:	N2364

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces › Saccharomyces cerevisiae

Protein attributes

Sequence length	576 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Catalytic activity	ATP + L-lysine + tRNA(Lys) = AMP + diphosphate + L-lysyl-tRNA(Lys).
Subcellular location	Mitochondrion matrix.
Miscellaneous	Present with 2280 molecules/cell in log phase SD medium.
Sequence similarities	Belongs to the class-II aminoacyl-tRNA synthetase family.

Ontologies

Keywords
Biological process	Protein biosynthesis
Cellular component	Mitochondrion
Domain	Transit peptide
Ligand	ATP-binding Nucleotide-binding
Molecular function	Aminoacyl-tRNA synthetase Ligase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	mitochondrial lysyl-tRNA aminoacylation Inferred from mutant phenotype Ref.1. Source: SGD tRNA import into mitochondrion Inferred from direct assay PubMed 17560369. Source: SGD
Cellular_component	mitochondrial matrix Inferred from electronic annotation. Source: UniProtKB-SubCell mitochondrion Inferred from direct assay PubMed 14576278PubMed 16823961Ref.1. Source: SGD
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW lysine-tRNA ligase activity Inferred from mutant phenotype Ref.1. Source: SGD nucleic acid binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 30	30	Mitochondrion Potential
	Chain	31 – 576	546	Lysine--tRNA ligase, mitochondrial		PRO_0000035812
Amino acid modifications
	Modified residue	9	1	Phosphoserine Ref.7

Sequences

	Sequence		Length	Mass (Da)
	P32048 [UniParc]. Last modified February 1, 1996. Version 3. Checksum: E3C440EEF86BB46E	FASTA	576	66,128
	10 20 30 40 50 60 MNVLLKRRSL TFAPRWLWCK CRSSRSRPYS LAHAVDTSKM EATRRNGQIV KDLGRYYPSM 70 80 90 100 110 120 SESALHDLCQ EYKEVTIADF NERFLGNPAT LHHEDNPNLL LSINGRIKSI RFSGQKIVFI 130 140 150 160 170 180 DLYNGSSGLK NDTQLQLIVN YNKIGGSSED KANFSEYMNF LKKGDYIKAL GYPGFSQSRV 190 200 210 220 230 240 KMLSLICNKL PIVLSVSQLP LPSRLNDETK IKSNRVVDYQ LNGTQTLLVR ARIIKLLRKF 250 260 270 280 290 300 LDDRNFVEVE TPILSSKSNG AMAKPFITSS KDFDHLELRI APELWLKRLI ISGLQKVYEI 310 320 330 340 350 360 GKVFRNEGID STHNAEFSTL EFYETYMSMD DIVTRTEDLF KFLITNLQKF FQDTRLPVPK 370 380 390 400 410 420 TFSELHLALS ENNWKFRKVE FLPTLNKELG IDLMNSGLDI NKPSELLKAL PKDIAKKYFP 430 440 450 460 470 480 SADNTGQLSS LQILNKLSDV FLEQRHCQST LPTVIYHQPA ILSPLAKTDP QNKQVTKRFE 490 500 510 520 530 540 VFIKGKEYIN AYEEENCPQL QLQKFLQQKQ INELTGNKTE TLSPVIDYQY VETMKYGMPP 550 560 570 VGGFGLGIDR LCMLFCDKKR IEEVLPFGCV DDVNRQ

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Structure and evolution of a group of related aminoacyl-tRNA synthetases." Gatti D., Tzagoloff A. J. Mol. Biol. 218:557-568(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	Tzagoloff A. Submitted (JAN-1994) to the EMBL/GenBank/DDBJ databases Cited for: SEQUENCE REVISION.
[3]	"Sequencing a cosmid clone of Saccharomyces cerevisiae chromosome XIV reveals 12 new open reading frames (ORFs) and an ancient duplication of six ORFs." Poehlmann R., Philippsen P. Yeast 12:391-402(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 96604 / S288c / FY1679.
[4]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its evolutionary implications." Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K., Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K., Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M., Beinhauer J.D., Boskovic J., Buitrago M.J. , Bussereau F., Coster F., Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F., Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C., Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A., Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H., Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L., Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R., Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D., Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A., Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C., Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F., Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G., Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M., Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J. Nature 387:93-98(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 96604 / S288c / FY1679.
[5]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[6]	"Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[7]	"A multidimensional chromatography technology for in-depth phosphoproteome analysis." Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H. Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-9, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X57360 Genomic DNA. Translation: CAA40634.1. Sequence problems. X86470 Genomic DNA. Translation: CAA60187.1. Z71349 Genomic DNA. Translation: CAA95947.1. BK006947 Genomic DNA. Translation: DAA10472.1.
PIR	S14834.
RefSeq	NP_014326.1. NM_001182911.1.
3D structure databases
ProteinModelPortal	P32048.
SMR	P32048. Positions 74-567.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-5319N.
IntAct	P32048. 2 interactions.
MINT	MINT-518945.
STRING	4932.YNL073W.
Proteomic databases
PaxDb	P32048.
PeptideAtlas	P32048.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YNL073W; YNL073W; YNL073W.
GeneID	855651.
KEGG	sce:YNL073W.
Organism-specific databases
CYGD	YNL073w.
SGD	S000005017. MSK1.
Phylogenomic databases
eggNOG	COG1190.
HOGENOM	HOG000236577.
KO	K04567.
OMA	AYEEENC.
OrthoDB	EOG4GJ2XG.
Gene expression databases
Genevestigator	P32048.
GermOnline	YNL073W. Saccharomyces cerevisiae.
Family and domain databases
Gene3D	2.40.50.140. 1 hit.
InterPro	IPR004364. aa-tRNA-synt_II. IPR018150. aa-tRNA-synt_II-like. IPR006195. aa-tRNA-synth_II. IPR002313. Lys-tRNA-ligase_II. IPR018149. Lys-tRNA-synth_II_C. IPR012340. NA-bd_OB-fold. IPR004365. NA-bd_OB_tRNA-helicase. [Graphical view]
PANTHER	PTHR22594. PTHR22594. 1 hit. PTHR22594:SF4. PTHR22594:SF4. 1 hit.
Pfam	PF00152. tRNA-synt_2. 1 hit. PF01336. tRNA_anti. 1 hit. [Graphical view]
PRINTS	PR00982. TRNASYNTHLYS.
SUPFAM	SSF50249. Nucleic_acid_OB. 1 hit.
TIGRFAMs	TIGR00499. lysS_bact. 1 hit.
PROSITE	PS50862. AA_TRNA_LIGASE_II. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	979899.

Entry information

Entry name

SYKM_YEAST

Accession

Primary (citable) accession number: P32048
Secondary accession number(s): D6W1A6

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1993
Last sequence update:	February 1, 1996
Last modified:	May 1, 2013
This is version 121 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program