Q2YT75 (SYD_STAAB) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Aspartate--tRNA ligase
EC=6.1.1.12

Alternative name(s):
Aspartyl-tRNA synthetase
Short name=AspRS

Gene names

Name:	aspS
Ordered Locus Names:	SAB1499c

Organism

Staphylococcus aureus (strain bovine RF122 / ET3-1) [Complete proteome] [HAMAP]

Taxonomic identifier

273036 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Firmicutes › Bacilli › Bacillales › Staphylococcaceae › Staphylococcus › Staphylococcus aureus

Protein attributes

Sequence length	588 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Catalytic activity	ATP + L-aspartate + tRNA(Asp) = AMP + diphosphate + L-aspartyl-tRNA(Asp). HAMAP-Rule MF_00044
Subunit structure	Homodimer By similarity. HAMAP-Rule MF_00044
Subcellular location	Cytoplasm By similarity HAMAP-Rule MF_00044.
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
Technical term	Complete proteome
Gene Ontology (GO)
Biological_process	aspartyl-tRNA aminoacylation Inferred from electronic annotation. Source: HAMAP
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	ATP binding Inferred from electronic annotation. Source: HAMAP aspartate-tRNA ligase activity Inferred from electronic annotation. Source: HAMAP 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 – 588	588	Aspartate--tRNA ligase HAMAP-Rule MF_00044		PRO_0000235560

Sequences

	Sequence		Length	Mass (Da)
	Q2YT75 [UniParc]. Last modified December 20, 2005. Version 1. Checksum: 38A6F2C4BF9E9E9B	FASTA	588	66,599
	10 20 30 40 50 60 MSKRTTYCGL VTEAFLGQEI TLKGWVNNRR DLGGLIFVDL RDREGIVQVV FNPAFSEEAL 70 80 90 100 110 120 KIAETVRSEY VVEVQGTVTK RDPETVNPKI KTGQVEVQVT NIKVINKSET PPFSINEENV 130 140 150 160 170 180 NVDENIRLKY RYLDLRRQEL AQTFKMRHQI TRSIRQYLDD EGFFDIETPV LTKSTPEGAR 190 200 210 220 230 240 DYLVPSRVHD GEFYALPQSP QLFKQLLMIS GFDKYYQIVK CFRDEDLRAD RQPEFTQVDI 250 260 270 280 290 300 EMSFVDQEDV MQMGEEMLKK VVKEVKGVEI NGAFPRMTYK EAMRRYGSDK PDTRFEMELI 310 320 330 340 350 360 DVSQLGRDMD FKVFKDTVEN DGEIKAIVAK GAAEQYTRKD MDALTEFVNI YGAKGLAWVK 370 380 390 400 410 420 VVEDGLTGPI GRFFETENVE TLLTLTGAEA GDLVMFVADK PNVVAQSLGA LRVKLAKELG 430 440 450 460 470 480 LIDETKLNFL WVTDWPLLEY DEDAKRYVAA HHPFTSPKEA DIAKLGTAPE EAEANAYDIV 490 500 510 520 530 540 LNGYELGGGS IRIHDGELQE KMFEVLGFTK EQAQEQFGFL LDAFKYGAPP HGGIALGLDR 550 560 570 580 LVMLLTNRTN LRDTIAFPKT ASATCLLTNA PGEVSDKQLE ELSLRIRH

References

[1]	"Molecular correlates of host specialization in Staphylococcus aureus." Herron-Olson L., Fitzgerald J.R., Musser J.M., Kapur V. PLoS ONE 2:E1120-E1120(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: bovine RF122 / ET3-1.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AJ938182 Genomic DNA. Translation: CAI81188.1.
RefSeq	YP_416969.1. NC_007622.1.
3D structure databases
ProteinModelPortal	Q2YT75.
SMR	Q2YT75. Positions 4-586.
ModBase	Search...
Protein-protein interaction databases
STRING	273036.SAB1499c.
Proteomic databases
PRIDE	Q2YT75.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	CAI81188; CAI81188; SAB1499c.
GeneID	3794960.
KEGG	sab:SAB1499c.
PATRIC	19523887. VBIStaAur92441_1592.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0173.
HOGENOM	HOG000275159.
KO	K01876.
OMA	QEWAKQR.
ProtClustDB	PRK00476.
Enzyme and pathway databases
BioCyc	SAUR273036:GJVS-1521-MONOMER.
Family and domain databases
Gene3D	2.40.50.140. 1 hit. 3.30.1360.30. 1 hit.
HAMAP	MF_00044_B. Asp_tRNA_synth_B.
InterPro	IPR004364. aa-tRNA-synt_II. IPR018150. aa-tRNA-synt_II-like. IPR006195. aa-tRNA-synth_II. IPR004524. Asp-tRNA-ligase_IIb_bac/mt. IPR002312. Asp/Asn-tRNA-synth_IIb. IPR004115. GAD_dom. IPR012340. NA-bd_OB-fold. IPR004365. NA-bd_OB_tRNA-helicase. [Graphical view]
PANTHER	PTHR22594. PTHR22594. 1 hit. PTHR22594:SF5. PTHR22594:SF5. 1 hit.
Pfam	PF02938. GAD. 1 hit. PF00152. tRNA-synt_2. 1 hit. PF01336. tRNA_anti. 1 hit. [Graphical view]
PRINTS	PR01042. TRNASYNTHASP.
SUPFAM	SSF50249. Nucleic_acid_OB. 1 hit. SSF55261. SSF55261. 1 hit.
TIGRFAMs	TIGR00459. aspS_bact. 1 hit.
PROSITE	PS50862. AA_TRNA_LIGASE_II. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

SYD_STAAB

Accession

Primary (citable) accession number: Q2YT75

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 16, 2006
Last sequence update:	December 20, 2005
Last modified:	May 1, 2013
This is version 60 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program