Reviewed, UniProtKB/Swiss-Prot Q0VRK1 (SYD_ALCBS)

Names and origin

Protein names

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

Gene names

Name:	aspS
Ordered Locus Names:	ABO_0749

Organism

Alcanivorax borkumensis (strain SK2 / ATCC 700651 / DSM 11573) [Complete proteome] [HAMAP]

Taxonomic identifier

393595 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Oceanospirillales › Alcanivoracaceae › Alcanivorax

Protein attributes

Sequence length	587 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 MF_00044
Subunit structure	Homodimer By similarity. HAMAP MF_00044
Subcellular location	Cytoplasm By similarity HAMAP 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 – 587	587	Aspartyl-tRNA synthetase HAMAP MF_00044		PRO_1000006630

Sequences

	Sequence		Length	Mass (Da)
	Q0VRK1-1 [UniParc]. Last modified September 5, 2006. Version 1. Checksum: 991D56D498DD71AC	FASTA	587	65,330
	10 20 30 40 50 60 MRSHYCGDLR ASHDGETVEL CGWVSRRRDH GGVIFLDLRD RNGLVQVVFD PDTVDAFALA 70 80 90 100 110 120 DKVRSEYVVR LSGRVRMRDE SVRNNKMATG DIEVLGKELT ILNEAETPPF ELDAHSAAGE 130 140 150 160 170 180 EVRLKYRYMD LRRPDVLKNF QFRSRLTHVV RAFLEGEGFM DVETPILTRA TPEGARDYLV 190 200 210 220 230 240 PSRTHPGSFF ALPQSPQLFK QLLMVAGFDR YYQIAKCFRD EDLRADRQPE FTQIDLEASF 250 260 270 280 290 300 VEEEDIMGIT ERMVRSVFKE LLSVDLPDFP RMPFSEAMQR FGSDKPDLRI ALELIDIADL 310 320 330 340 350 360 LAGVDFKVFS GPANDPKGRV AAMRVPGGCS LSRKDIDGYT KFVSIYGAKG LAYIKVNDLA 370 380 390 400 410 420 AGAEGLQSPI LKFLTEDAIK GILERTGAET GDLIFFGADK AKIVNEALGA LRVKVGHDLN 430 440 450 460 470 480 LVEGEWAPLW VVDFPMFEED EGQYHALHHP FTMPSCSAEE LKSNPGEALS RAYDMVLNGT 490 500 510 520 530 540 ELGGGSIRIH SPAMQRTVFE ALGISDEEAE EKFGFLLDGL KYGAPPHGGL AFGLDRMVML 550 560 570 580 MTGCESIRDV IAFPKTQTAA CTMTNAPSPV DNKQLREVGV QVRKEEG

References

[1]

"Genome sequence of the ubiquitous hydrocarbon-degrading marine bacterium Alcanivorax borkumensis." Schneiker S., Martins dos Santos V.A.P., Bartels D., Bekel T., Brecht M., Buhrmester J., Chernikova T.N., Denaro R., Ferrer M., Gertler C., Goesmann A., Golyshina O.V., Kaminski F., Khachane A.N., Lang S., Linke B., McHardy A.C., Meyer F. , Nechitaylo T., Puehler A., Regenhardt D., Rupp O., Sabirova J.S., Selbitschka W., Yakimov M.M., Timmis K.N., Vorhoelter F.-J., Weidner S., Kaiser O., Golyshin P.N. Nat. Biotechnol. 24:997-1004(2006) [PubMed: 16878126] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	AM286690 Genomic DNA. Translation: CAL16197.1.
RefSeq	YP_692469.1.
3D structure databases
SMR	Q0VRK1. Positions 1-584.
ModBase	Search...
Protein-protein interaction databases
STRING	Q0VRK1.
Genome annotation databases
GeneID	4213839.
GenomeReviews	Gene locus ABO_0749 in contig AM286690_GR.
KEGG	abo:ABO_0749.
NMPDR	fig|393595.12.peg.752.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0173.
HOGENOM	HBG396032.
OMA	PLFEYDE.
PhylomeDB	Q0VRK1.
Enzyme and pathway databases
BioCyc	ABOR393595:ABO_0749-MONOMER.
Family and domain databases
HAMAP	MF_00044_B. Asp_tRNA_synth_B. [Tree]
InterPro	IPR004364. aa-tRNA-synt_II. IPR018150. aa-tRNA-synt_II-like. IPR006195. aa-tRNA-synth_II_cons-dom. IPR002312. Asp-tRNA-synth_IIb. IPR020564. Asp-tRNA-synth_IIb_bac-type. IPR004524. Asp-tRNA-synth_IIb_bac/mt. IPR018153. Asp-tRNA-synth_IIb_C_bac/mt. IPR004115. GAD_dom. 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. PTHR22594:SF5. AspS_bac. 1 hit.
Pfam	PF02938. GAD. 1 hit. 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...

Entry information

Entry name

SYD_ALCBS

Accession

Primary (citable) accession number: Q0VRK1

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 15, 2008
Last sequence update:	September 5, 2006
Last modified:	February 9, 2010
This is version 35 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)