Q2SVD8 (SYT_BURTA) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Threonine--tRNA ligase
EC=6.1.1.3

Alternative name(s):
Threonyl-tRNA synthetase
Short name=ThrRS

Gene names

Name:	thrS
Ordered Locus Names:	BTH_I2595

Organism

Burkholderia thailandensis (strain E264 / ATCC 700388 / DSM 13276 / CIP 106301) [Complete proteome] [HAMAP]

Taxonomic identifier

271848 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Burkholderiaceae › Burkholderia › pseudomallei group

Protein attributes

Sequence length	635 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 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: InterPro
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW threonine-tRNA ligase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 635	635	Threonine--tRNA ligase HAMAP MF_00184		PRO_1000020359
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)
	Q2SVD8 [UniParc]. Last modified January 24, 2006. Version 1. Checksum: 9EA5167EB6CB586C	FASTA	635	72,297
	10 20 30 40 50 60 MVSIRLPDGS IRQYEHPVTV AEVAASIGPG LAKAALGGKL DGELVDTSAL IDRDASLAIV 70 80 90 100 110 120 TDKDADGLDI IRHSTAHLLA YAVKELHPDA QVTIGPVIDN GFYYDFSYHR PFTPEDLEAI 130 140 150 160 170 180 EKRMQELAKR DEPVTRRVVS RDEAVSYFRS IGEKYKAEII ESIPASDEIK LYSHGGFTDL 190 200 210 220 230 240 CRGPHVPSTG KLKVFKLMKV AGAYWRGDSK NEQLQRIYGT AWTKKEDQDA YLHMLEEAEK 250 260 270 280 290 300 RDHRKLGKQL DLFHIQEEAP GMVFWHPKGW TLWQRVEQYM RRRLDAAGYL EIKTPMIMDR 310 320 330 340 350 360 SLWEASGHWQ NYRENMFTTE SEKRDYAIKP MNCPGHVQVF KHGLRSYRDL PLRYAEFGSC 370 380 390 400 410 420 HRNEASGALH GLMRVRGFVQ DDAHIFCTED QINSEAIAFN KLAMSVYEDF GFDRIDIKLS 430 440 450 460 470 480 LRPEQRMGSD ETWDHAEEGL RNALKACGLE WEELPGEGAF YGPKIEYHIK DALGRSWQCG 490 500 510 520 530 540 TLQLDMMLPE RLGAEYVAED NSRRRPVMLH RAIVGSMERF LGILIEHHAG AMPAWLAPFH 550 560 570 580 590 600 AVVLNIAESQ AEYAQTVVQS LQKQGLRVSA DLRNEKISYK IREHTLEKVP YLLVVGDKER 610 620 630 EAQTVAVRAR GGVDLGVMPV EAFVERLRED IQAFK

References

[1]

"Bacterial genome adaptation to niches: divergence of the potential virulence genes in three Burkholderia species of different survival strategies." Kim H.S., Schell M.A., Yu Y., Ulrich R.L., Sarria S.H., Nierman W.C., DeShazer D. BMC Genomics 6:174-174(2005) [PubMed: 16336651] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: E264 / ATCC 700388 / DSM 13276 / CIP 106301.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000086 Genomic DNA. Translation: ABC37600.1.
RefSeq	YP_443111.1. NC_007651.1.
3D structure databases
ProteinModelPortal	Q2SVD8.
SMR	Q2SVD8. Positions 241-633.
ModBase	Search...
Protein-protein interaction databases
STRING	Q2SVD8.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	3848822.
GenomeReviews	Gene locus BTH_I2595 in contig CP000086_GR.
KEGG	bte:BTH_I2595.
PATRIC	19308338. VBIBurTha36512_5450.
TIGR	BTH_I2595.
Phylogenomic databases
eggNOG	COG0441.
HOGENOM	HBG352811.
OMA	VGSDALW.
ProtClustDB	PRK00413.
Enzyme and pathway databases
BioCyc	BTHA271848:BTH_I2595-MONOMER.
Family and domain databases
HAMAP	MF_00184. Thr_tRNA_synth. [Tree]
InterPro	IPR002314. aa-tRNA-synt_IIb_cons-dom. IPR006195. aa-tRNA-synth_II. IPR004154. Anticodon-bd. IPR012675. Beta-grasp_ferredoxin-type. IPR004095. TGS. IPR012676. TGS-like. IPR002320. Thr-tRNA-synth_IIa. 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.
KO	K01868.
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]
SUPFAM	SSF52954. Anticodon_bd. 1 hit. SSF81271. TGS-like. 1 hit. SSF55186. Thr/Ala-tRNA-synth_IIc_edit. 1 hit.
TIGRFAMs	TIGR00418. ThrS. 1 hit.
PROSITE	PS50862. AA_TRNA_LIGASE_II. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

SYT_BURTA

Accession

Primary (citable) accession number: Q2SVD8

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 15, 2008
Last sequence update:	January 24, 2006
Last modified:	January 25, 2012
This is version 52 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program