Reviewed, UniProtKB/Swiss-Prot Q6FEH6 (SYD_ACIAD)

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:	ACIAD0609

Organism

Acinetobacter sp. (strain ADP1) [Complete proteome] [HAMAP]

Taxonomic identifier

62977 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Moraxellaceae › Acinetobacter

Protein attributes

Sequence length	592 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 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 – 592	592	Aspartyl-tRNA synthetase HAMAP MF_00044		PRO_0000110815

Sequences

	Sequence		Length	Mass (Da)
	Q6FEH6-1 [UniParc]. Last modified March 29, 2005. Version 2. Checksum: 7815E9258286C572	FASTA	592	66,646
	10 20 30 40 50 60 MMRTHYCGSL TEAQIDQTVT LCGWVHRRRD HGGVIFLDMR DRDGLVQVVI DPDTPEAFAT 70 80 90 100 110 120 ADKVRSEFVL KITGRVRRRY EGTENSNMVS GQIEVLGKEI EVLAQSETPP FPLNDDNINI 130 140 150 160 170 180 SEEHRLKYRF LDIRRPEMLD RLRFRSKVTN LIRNYLDDHG FLDVETPILT RATPEGARDY 190 200 210 220 230 240 LVPSRVQNGS FYALPQSPQL FKQLLMVGGI DRYYQIAKCF RDEDLRADRQ PEFTQIDIET 250 260 270 280 290 300 SFLNDDDIMD LMEGMTVKLF DELLGIKFDK FQRMPYSEAM RDYASDKPDL RIPLKLVDVA 310 320 330 340 350 360 DLMQDVEFKV FAGPAKDPKG RIAALRVPGA GALPRSAIDE YTKFVGIYGA KGLAYIKVNE 370 380 390 400 410 420 IEKGVEGLQS PIVKFIEPIV MQLLERVGAE NGDIVFFGAD KAKVVNDAMG ALRVKIGHDL 430 440 450 460 470 480 KLVTCEWAPL WVVDFPMFEE TDDGKWTSVH HPFTLPKSSV EDVKANPGEA LSVAYDMVLN 490 500 510 520 530 540 GTEVGGGSLR IYTLEMQKAI FEALGISDEE AEEKFSFLLN ALRYGAPPHG GLAFGLDRLI 550 560 570 580 590 MLMTGASSIR DVIAFPKTKT AECPLTQAPA PVEANQLRDL GIRLREQPKK ED

References

[1]

"Unique features revealed by the genome sequence of Acinetobacter sp. ADP1, a versatile and naturally transformation competent bacterium." Barbe V., Vallenet D., Fonknechten N., Kreimeyer A., Oztas S., Labarre L., Cruveiller S., Robert C., Duprat S., Wincker P., Ornston L.N., Weissenbach J., Marliere P., Cohen G.N., Medigue C. Nucleic Acids Res. 32:5766-5779(2004) [PubMed: 15514110] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	CR543861 Genomic DNA. Translation: CAG67532.1. Different initiation.
RefSeq	YP_045354.1.
3D structure databases
SMR	Q6FEH6. Positions 2-585.
ModBase	Search...
Protein-protein interaction databases
STRING	Q6FEH6.
Genome annotation databases
GeneID	2880676.
GenomeReviews	Gene locus ACIAD0609 in contig CR543861_GR.
KEGG	aci:ACIAD0609.
NMPDR	fig|62977.3.peg.204.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0173.
HOGENOM	HBG396032.
PhylomeDB	Q6FEH6.
Enzyme and pathway databases
BioCyc	ASP62977:ACIAD0609-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_ACIAD

Accession

Primary (citable) accession number: Q6FEH6

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 29, 2005
Last sequence update:	March 29, 2005
Last modified:	February 9, 2010
This is version 43 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

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