Reviewed, UniProtKB/Swiss-Prot P15179 (SYDM_YEAST)

Names and origin

Protein names

Recommended name:
    Aspartyl-tRNA synthetase, mitochondrial
    EC=6.1.1.12
Alternative name(s):
    Aspartate--tRNA ligase
      Short name=AspRS

Gene names

Name:	MSD1
Ordered Locus Names:	YPL104W
ORF Names:	LPG5W

Organism

Saccharomyces cerevisiae (Baker's yeast) [Complete proteome]

Taxonomic identifier

4932 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length	658 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Catalytic activity	ATP + L-aspartate + tRNA(Asp) = AMP + diphosphate + L-aspartyl-tRNA(Asp).
Subcellular location	Mitochondrion matrix.
Miscellaneous	Present with 1550 molecules/cell in log phase SD medium. Ref.3
Sequence similarities	Belongs to the class-II aminoacyl-tRNA synthetase family.

Ontologies

Keywords
Biological process	Protein biosynthesis
Cellular component	Mitochondrion
Ligand	ATP-binding Nucleotide-binding
Molecular function	Aminoacyl-tRNA synthetase Ligase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	mitochondrial aspartyl-tRNA aminoacylation Ref.1 Inferred from mutant phenotype. Source: SGD
Cellular component	mitochondrial matrix Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW aspartate-tRNA ligase activity Ref.1 Inferred from mutant phenotype. Source: SGD nucleic acid binding Inferred from electronic annotation. Source: InterPro protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
PHR1	P05066	1	EBI-18659,EBI-13385

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 658	658	Aspartyl-tRNA synthetase, mitochondrial		PRO_0000111015

Sequences

	Sequence		Length	Mass (Da)
	P15179-1 [UniParc]. Last modified April 1, 1990. Version 1. Checksum: 664081ED6DE24964	FASTA	658	75,461
	10 20 30 40 50 60 MLARSRVCLQ TITRRLADFP EANAIKKKFL FRKDTSTIKQ LKGLSSGQKI VLNGWIEQKP 70 80 90 100 110 120 KRVGKNLIFG LLRDSNGDII QLVDNKSLLK GFTLEDVVQA VGILSLKRKL SNEDADEYEV 130 140 150 160 170 180 QLEDITVLNA SNKKPAQMQD FKLSAIYPPE FRYLQLRNPK YQDFLKKRSS ISKEIRNSFN 190 200 210 220 230 240 NFDFTEVETP MLFKATPEGA REFLVPTRTK RSDGKPSFYA LDQSPQQYKQ LLMASGVNKY 250 260 270 280 290 300 YQMARCFRDE DLRADRQPEF TQVDMEMAFA NSEDVMKIIE KTVSGVWSKF SKKRGLLTLD 310 320 330 340 350 360 SKGTLVPAKK ENGTVSIFRM TYEQAMTSYG IDKPDLRAPD LKIINLGEFN AFSHLNKKFP 370 380 390 400 410 420 VFEVIILRSA FSNMEEYKER WSFLTNNSNY NYRVPIVLPI ENDEQANSNW FENFHAIATF 430 440 450 460 470 480 ENPHLITKFL KLKKGDIVCG CTREPNHSIF ENPTPLGRLR QLVLQSEHGK NIYHAVNKDV 490 500 510 520 530 540 ASWIVDFPLF SPVIIEDKSG KKEKLAYPEY EKDRLCSTHH PFTMVKLKDY EKLEKTPEKC 550 560 570 580 590 600 LGRHYDLVVN GVELGGGSTR IHDPRLQDYI FEDILKIDNA YELFGHLLNA FDMGTPPHAG 610 620 630 640 650 FAIGFDRMCA MICETESIRD VIAFPKSITG ADLVVKSPSV IPESILEPYN IKYSNSKK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Homology of aspartyl- and lysyl-tRNA synthetases." Gampel A., Tzagoloff A. Proc. Natl. Acad. Sci. U.S.A. 86:6023-6027(1989) [PubMed: 2668951] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI." Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W., Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D., Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E., Churcher C.M. , Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H., DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N., Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K., Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M., Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A., Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S., Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D., Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S., Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B., Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A., Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R., Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A., Vo D.H., Hani J. Nature 387:103-105(1997) [PubMed: 9169875] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[3]	"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: 14562106] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	M26020 Genomic DNA. Translation: AAA35137.1. M24418 Genomic DNA. Translation: AAA35173.1. U43281 Genomic DNA. Translation: AAB68196.1.
PIR	SYBYDM. S61963.
RefSeq	NP_015221.1.
3D structure databases
HSSP	HSSP built from PDB template 1BBW based on UniProtKB P13030.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP:6339N.
IntAct	P15179. 6 interactions.
STRING	P15179.
Proteomic databases
PRIDE	P15179.
Genome annotation databases
Ensembl	YPL104W; YPL104W; YPL104W; Saccharomyces cerevisiae. [Genome view]
GeneID	856000.
GenomeReviews	Gene locus YPL104W in contig U00094_GR.
KEGG	sce:YPL104W.
NMPDR	fig|4932.3.peg.6353.
Organism-specific databases
CYGD	YPL104w.
SGD	S000006025. MSD1.
Phylogenomic databases
HOGENOM	P15179.
OMA	VDRRRDH.
Enzyme and pathway databases
BRENDA	6.1.1.12. 250.
Gene expression databases
ArrayExpress	P15179.
Genevestigator	P15179.
GermOnline	YPL104W. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR004364. aa-tRNA-synt_II. IPR018150. aa-tRNA-synt_II-like. IPR006195. aa-tRNA-synth_II_cons-reg. IPR002312. Asp-tRNA-synth_IIb. IPR004524. Asp-tRNA-synth_IIb_bac/mt. IPR018153. Asp-tRNA-synth_IIb_C_bac/mt. IPR012340. NA-bd_OB-fold. IPR004365. NA_bd_OB_tRNA-helicase. [Graphical view]
Gene3D	G3DSA:2.40.50.140. OB_NA_bd_sub. 1 hit.
PANTHER	PTHR22594. aa-tRNA-synt_II. 1 hit. PTHR22594:SF5. AspS_bac. 1 hit.
Pfam	PF00152. tRNA-synt_2. 1 hit. PF01336. tRNA_anti. 1 hit. [Graphical view]
PRINTS	PR01042. TRNASYNTHASP.
TIGRFAMs	TIGR00459. aspS_bact. 1 hit.
PROSITE	PS50862. AA_TRNA_LIGASE_II. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	980869.

Entry information

Entry name

SYDM_YEAST

Accession

Primary (citable) accession number: P15179

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1990
Last sequence update:	April 1, 1990
Last modified:	November 3, 2009
This is version 95 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)