Reviewed, UniProtKB/Swiss-Prot B7I688 (SYT_ACIB5)

Names and origin

Protein names

Recommended name:
    Threonyl-tRNA synthetase
    EC=6.1.1.3
Alternative name(s):
    Threonine--tRNA ligase
      Short name=ThrRS

Gene names

Name:	thrS
Ordered Locus Names:	AB57_0695

Organism

Acinetobacter baumannii (strain AB0057) [Complete proteome] [HAMAP]

Taxonomic identifier

480119 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Moraxellaceae › Acinetobacter

Protein attributes

Sequence length	640 AA.
Sequence status	Complete.
Protein existence	Inferred from homology.

General annotation (Comments)

Catalytic activity	ATP + L-threonine + tRNA(Thr) = AMP + diphosphate + L-threonyl-tRNA(Thr). HAMAP MF_00184
Cofactor	Binds 1 zinc ion per subunit By similarity. HAMAP MF_00184
Subunit structure	Homodimer By similarity. HAMAP MF_00184
Subcellular location	Cytoplasm By similarity HAMAP MF_00184.
Sequence similarities	Belongs to the class-II aminoacyl-tRNA synthetase family.

Ontologies

Keywords
Biological process	Protein biosynthesis
Cellular component	Cytoplasm
Ligand	ATP-binding Metal-binding Nucleotide-binding Zinc
Molecular function	Aminoacyl-tRNA synthetase Ligase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	threonyl-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 threonine-tRNA ligase activity Inferred from electronic annotation. Source: HAMAP zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 640	640	Threonyl-tRNA synthetase HAMAP MF_00184		PRO_1000199520
Regions
	Region	242 – 533	292	Catalytic HAMAP MF_00184
Sites
	Metal binding	333	1	Zinc; catalytic By similarity
	Metal binding	384	1	Zinc; catalytic By similarity
	Metal binding	510	1	Zinc; catalytic By similarity

Sequences

	Sequence		Length	Mass (Da)
	B7I688-1 [UniParc]. Last modified February 10, 2009. Version 1. Checksum: F21FB415DFF22418	FASTA	640	73,179
	10 20 30 40 50 60 MPIITLPNGD QKSFDHPVSV MEVAQSIGPG LAKNTVAGRV NDRLVDACDL ITEDSTLQII 70 80 90 100 110 120 TPKDEEGLEI IRHSCAHLVG HAVKQLFPEA KMVIGPVIEE GFYYDIWMPR PFTLDDMAAI 130 140 150 160 170 180 EERMKKLIDQ DYDVIKKMTP RDEVIKVFTD RGEEYKLRLV EDMPEEKAMG LYYHQEYVDM 190 200 210 220 230 240 CRGPHVPNTK FLKSFKLTKI SGAYWRGDAK NEQLQRIYGT AWADKKQLAA YIKRIEEAEK 250 260 270 280 290 300 RDHRKIGKAL DLFHMQEEAP GMVFWHANGW TIYQVLEQYM RKVQQDNGYQ EIKTPQIVDF 310 320 330 340 350 360 TLWEKSGHAA NYVENMFTTH SESRNYAVKP MNCPCHVQVF NQGLKSYRDL PIRLAEFGSC 370 380 390 400 410 420 HRNEPSGSLH GIMRVRGFTQ DDAHIFCTKE QIGKEVADFI KLTLDVYKDF GFEEVQMKLS 430 440 450 460 470 480 TRPEKRVGDD ALWDLAEKSL ADALDAAGLE WELQPGEGAF YGPKIEFSLK DCLGRVWQCG 490 500 510 520 530 540 TIQCDFNLPV RLDASYVTEE NERDQPVMLH RAILGSFERF IGILIEHYAG FMPPWLSPVQ 550 560 570 580 590 600 ACVMNITDSQ AEASEQVVAK LKENGLRAIS DLRNEKIGFK IRERTLERIP YLLVLGDREV 610 620 630 640 EEGTVNVRTR SGKNLGTMSV DAFIDLVKSA VAERGRYIVE

References

[1]

"Comparative genome sequence analysis of multidrug-resistant Acinetobacter baumannii." Adams M.D., Goglin K., Molyneaux N., Hujer K.M., Lavender H., Jamison J.J., MacDonald I.J., Martin K.M., Russo T., Campagnari A.A., Hujer A.M., Bonomo R.A., Gill S.R. J. Bacteriol. 190:8053-8064(2008) [PubMed: 18931120] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP001182 Genomic DNA. Translation: ACJ40115.1.
RefSeq	YP_002318098.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	7043581.
GenomeReviews	Gene locus AB57_0695 in contig CP001182_GR.
KEGG	abn:AB57_0695.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG352811.
OMA	ELELFMF.
Family and domain databases
HAMAP	MF_00184_B. Thr_tRNA_synth_B. [Tree]
InterPro	IPR002314. aa-tRNA-synt_IIb_cons-dom. IPR006195. aa-tRNA-synth_II_cons-dom. IPR004154. Anticodon_bd. IPR012675. b-grasp_ferredoxin-like. IPR004095. TGS. IPR012676. TGS-like. IPR002320. Thr-tRNA-synth_IIa. IPR018158. Thr-tRNA-synth_IIa_cons-reg. IPR018163. Thr/Ala-tRNA-synth_IIc_edit. IPR012947. tRNA_SAD. [Graphical view]
Gene3D	G3DSA:3.40.50.800. Anticodon_bd. 1 hit. G3DSA:3.10.20.30. Ferredoxin_fold. 1 hit.
Pfam	PF03129. HGTP_anticodon. 1 hit. PF02824. TGS. 1 hit. PF00587. tRNA-synt_2b. 1 hit. PF07973. tRNA_SAD. 1 hit. [Graphical view]
PRINTS	PR01047. TRNASYNTHTHR.
SMART	SM00863. tRNA_SAD. 1 hit. [Graphical view]
TIGRFAMs	TIGR00418. thrS. 1 hit.
PROSITE	PS50862. AA_TRNA_LIGASE_II. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

SYT_ACIB5

Accession

Primary (citable) accession number: B7I688

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 14, 2009
Last sequence update:	February 10, 2009
Last modified:	February 9, 2010
This is version 11 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)