Reviewed, UniProtKB/Swiss-Prot Q1LT63 (SYN_BAUCH)

Names and origin

Protein names

Recommended name:
    Asparaginyl-tRNA synthetase
    EC=6.1.1.22
Alternative name(s):
    Asparagine--tRNA ligase
      Short name=AsnRS

Gene names

Name:	asnS
Ordered Locus Names:	BCI_0408

Organism

Baumannia cicadellinicola subsp. Homalodisca coagulata [Complete proteome] [HAMAP]

Taxonomic identifier

374463 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Candidatus Baumannia

Protein attributes

Sequence length	467 AA.
Sequence status	Complete.
Protein existence	Inferred from homology.

General annotation (Comments)

Catalytic activity	ATP + L-asparagine + tRNA(Asn) = AMP + diphosphate + L-asparaginyl-tRNA(Asn). HAMAP MF_00534
Subunit structure	Homodimer By similarity. HAMAP MF_00534
Subcellular location	Cytoplasm HAMAP MF_00534.
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	asparaginyl-tRNA aminoacylation Inferred from electronic annotation. Source: HAMAP 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: HAMAP asparagine-tRNA ligase activity Inferred from electronic annotation. Source: HAMAP aspartate-tRNA ligase activity Inferred from electronic annotation. Source: InterPro 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 – 467	467	Asparaginyl-tRNA synthetase HAMAP MF_00534		PRO_1000051380

Sequences

	Sequence		Length	Mass (Da)
	Q1LT63-1 [UniParc]. Last modified May 30, 2006. Version 1. Checksum: 79F9BDE893AFFDF6	FASTA	467	53,150
	10 20 30 40 50 60 MIILPIAKIL QGIILAADHE VIVQGWVRTR RDSKAGISFL SIYDGSCLDS LQVIINHDLP 70 80 90 100 110 120 NYKSDVLHLT TGCSVVITGS IVTSIGVGQH FEIQAKNIKV LGWVKNPETY PITAKKHSLE 130 140 150 160 170 180 FLREVAHLRP RTNIIGAVTR VRHTLAQAIH RFMHIEGFFW VSTPLITTFN CEGAGEMFRV 190 200 210 220 230 240 STLDLENLPY TSKGKINYEK DFFGKEAFLT VSGQLNGESY ACALSKIYTF GPTFRAENSN 250 260 270 280 290 300 TSRHLAEFWM VEPEVAFANL TDIAILAEKM LKYIFNAILI ERVDDINFFA EQINKNIIKR 310 320 330 340 350 360 LEQFISSNFA QIDYTEAIDI LQNCKQKFDH TVFWGMDLFA EHERYLADKH FQAPVVVTNY 370 380 390 400 410 420 PKDIKAFYMR INDDGKTVAA MDVLAPGIGE IIGGSQREER LAKLDQRLAD RGLNIEDYWW 430 440 450 460 YRDLRSYGTV PHSGFGLGLE RLMIYITGMH NIRDVIPFPR NPRQASF

References

[1]

"Metabolic complementarity and genomics of the dual bacterial symbiosis of sharpshooters." Wu D., Daugherty S.C., Van Aken S.E., Pai G.H., Watkins K.L., Khouri H., Tallon L.J., Zaborsky J.M., Dunbar H.E., Tran P.L., Moran N.A., Eisen J.A. PLoS Biol. 4:1079-1092(2006) [PubMed: 16729848] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000238 Genomic DNA. Translation: ABF13990.1.
RefSeq	YP_588851.1.
3D structure databases
SMR	Q1LT63. Positions 18-465.
ModBase	Search...
Protein-protein interaction databases
STRING	Q1LT63.
Genome annotation databases
GeneID	4056737.
GenomeReviews	Gene locus BCI_0408 in contig CP000238_GR.
KEGG	bci:BCI_0408.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0017.
HOGENOM	HBG745843.
OMA	LQKKRHS.
PhylomeDB	Q1LT63.
Family and domain databases
HAMAP	MF_00534. Asn_tRNA_synth. [Tree]
InterPro	IPR004364. aa-tRNA-synt_II. IPR018150. aa-tRNA-synt_II-like. IPR006195. aa-tRNA-synth_II_cons-dom. IPR004522. Asn-tRNA-synth_IIb. IPR002312. Asp-tRNA-synth_IIb. 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	TIGR00457. asnS. 1 hit.
PROSITE	PS50862. AA_TRNA_LIGASE_II. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

SYN_BAUCH

Accession

Primary (citable) accession number: Q1LT63

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 15, 2008
Last sequence update:	May 30, 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)