Reviewed, UniProtKB/Swiss-Prot Q3SYZ4 (SYDC_BOVIN)

Names and origin

Protein names

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

Gene names

Name:

DARS

Organism

Bos taurus (Bovine)

Taxonomic identifier

9913 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos

Protein attributes

Sequence length	501 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level.

General annotation (Comments)

Function	Catalyzes the specific attachment of an amino acid to its cognate tRNA in a 2 step reaction: the amino acid (AA) is first activated by ATP to form AA-AMP and then transferred to the acceptor end of the tRNA.
Catalytic activity	ATP + L-aspartate + tRNA(Asp) = AMP + diphosphate + L-aspartyl-tRNA(Asp).
Subunit structure	Homodimer; also part of a multisubunit complex that groups AIMP1, AIMP2, EEF1A1 and tRNA ligases for Arg, Asp, Glu, Gln, Ile, Leu, Lys, Met and Pro By similarity.
Subcellular location	Cytoplasm By similarity.
Sequence similarities	Belongs to the class-II aminoacyl-tRNA synthetase family.

Ontologies

Keywords
Biological process	Protein biosynthesis
Cellular component	Cytoplasm
Ligand	ATP-binding Nucleotide-binding
Molecular function	Aminoacyl-tRNA synthetase Ligase
PTM	Acetylation Phosphoprotein
Gene Ontology (GO)
Biological process	aspartyl-tRNA aminoacylation Inferred from electronic annotation. Source: InterPro
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW aspartate-tRNA ligase activity Inferred from electronic annotation. Source: EC 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
	Chain	1 – 501	501	Aspartyl-tRNA synthetase, cytoplasmic		PRO_0000245022
Regions
	Region	411 – 415	5	Binding site for the 3'-end of tRNA Potential
Amino acid modifications
	Modified residue	74	1	N6-acetyllysine By similarity
	Modified residue	238	1	Phosphoserine By similarity
	Modified residue	249	1	Phosphoserine By similarity
	Modified residue	374	1	N6-acetyllysine By similarity
	Modified residue	500	1	Phosphothreonine; by PKA Potential

Sequences

	Sequence		Length	Mass (Da)
	Q3SYZ4-1 [UniParc]. Last modified October 11, 2005. Version 1. Checksum: A8E00861B2C3E607	FASTA	501	57,036
	10 20 30 40 50 60 MPSANASRRS QEKPREIMDA AEDYAKERYG VSSMIQSQEK PDRVLVRISD LTVQKAGEVV 70 80 90 100 110 120 WVRARVHTSR AKGKQCFLVL RQQQFNVQAL VAVGDHASKQ MVKFAANINK ESIVDVEGVV 130 140 150 160 170 180 RKVNQKIGSC TQQDVELHVQ KIYVISSAEP RLPLQLDDAV RPEVEGEEEG RATVNQDTRL 190 200 210 220 230 240 DNRVIDLRTS TSQAIFRLQS GICHPFRETL TNKGFVEIQT PKIISAASEG GANVFTVSYF 250 260 270 280 290 300 KNNAYLAQSP QLYKQMCICA DFEKVFCIGP VFRAEDSNTH RHLTEFVGLD IEMAFNYHYH 310 320 330 340 350 360 EVVEEIADTL VQIFKGLQKR FQTEIQTVNK QFPCEPFKFL EPTLRLEYCE ALAMLREAGI 370 380 390 400 410 420 EMGDEEDLST PNEKLLGRLV KEKYDTDFYI LDKYPLAVRP FYTMPDPRNP KQSNSYDMFM 430 440 450 460 470 480 RGEEILSGAQ RIHDPQLVTE RALHHGIDLE KIKAYIDSFR FGAPPHAGGG IGLERVTMLF 490 500 LGLHNVRQTS MFPRDPKRLT P

References

[1]	NIH - Mammalian Gene Collection (MGC) project Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Crossbred X Angus. Tissue: Ileum.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BC103319 mRNA. Translation: AAI03320.1.
IPI	IPI00715362.
RefSeq	NP_001030257.1.
UniGene	Bt.48837
3D structure databases
SMR	Q3SYZ4. Positions 22-501.
ModBase	Search...
Protein-protein interaction databases
STRING	Q3SYZ4.
Genome annotation databases
Ensembl	ENSBTAT00000013123; ENSBTAP00000013123; ENSBTAG00000009949; Bos taurus. [Genome view]
GeneID	510162.
KEGG	bta:510162.
Organism-specific databases
CTD	510162.
Phylogenomic databases
eggNOG	maNOG08209.
HOVERGEN	Q3SYZ4.
InParanoid	Q3SYZ4.
PhylomeDB	Q3SYZ4.
Enzyme and pathway databases
BRENDA	6.1.1.12. 251.
Family and domain databases
InterPro	IPR004364. aa-tRNA-synt_II. IPR018150. aa-tRNA-synt_II-like. IPR006195. aa-tRNA-synth_II_cons-dom. IPR002312. Asp-tRNA-synth_IIb. IPR004523. Asp-tRNA-synth_IIb_arc/euk. IPR012340. NA-bd_OB-fold. IPR016027. NA-bd_OB-fold-like. 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.
Pfam	PF00152. tRNA-synt_2. 1 hit. PF01336. tRNA_anti. 1 hit. [Graphical view]
PRINTS	PR01042. TRNASYNTHASP.
TIGRFAMs	TIGR00458. aspS_arch. 1 hit.
PROSITE	PS50862. AA_TRNA_LIGASE_II. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

SYDC_BOVIN

Accession

Primary (citable) accession number: Q3SYZ4

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 11, 2006
Last sequence update:	October 11, 2005
Last modified:	February 9, 2010
This is version 34 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)