Q2YQ07 (SYT_BRUA2) 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:	BAB1_1093

Organism

Brucella abortus (strain 2308) [Complete proteome] [HAMAP]

Taxonomic identifier

359391 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Brucellaceae › Brucella › Brucella abortus

Protein attributes

Sequence length	658 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-Rule MF_00184
Cofactor	Binds 1 zinc ion per subunit By similarity.
Subunit structure	Homodimer By similarity.
Subcellular location	Cytoplasm HAMAP-Rule 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 metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW threonine-tRNA ligase activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 658	658	Threonine--tRNA ligase HAMAP-Rule MF_00184		PRO_1000020350
Regions
	Region	246 – 548	303	Catalytic HAMAP-Rule MF_00184
Sites
	Metal binding	343	1	Zinc; catalytic By similarity
	Metal binding	394	1	Zinc; catalytic By similarity
	Metal binding	525	1	Zinc; catalytic By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q2YQ07 [UniParc]. Last modified December 20, 2005. Version 1. Checksum: AAFC0CF2C38225BC	FASTA	658	74,603
	10 20 30 40 50 60 MSNTVSLQFP DGSVREYDAS MTGAALAESI SKSLAKKAVA YAVDGTVRDL SDPLGASGKL 70 80 90 100 110 120 EIITREDPRA LELIRHDTAH VLAEAVQELF PGTQVTIGPV IENGFYYDFA RNEPFTLDDL 130 140 150 160 170 180 PVIEKKMREI IQRNKPFTKE VWSREKAKQV FSDKGESYKV ELVDAIPAGQ DLKIYYQGDW 190 200 210 220 230 240 FDLCRGPHMA STGQIGNSFK LMKVAGAYWR GDANNPMLTR IYGTAFANDN DLQAYLHMLE 250 260 270 280 290 300 EAEKRDHRRL GREMDLFHFQ EEGPGVVFWH AKGWKMFQNL VSYMRRRLDS HGYQEVNTPQ 310 320 330 340 350 360 VLDKSLWETS GHWGWYRDNM FKVTVAGDDT DDDRVFALKP MNCPGHVQIF KHGLKSYRDL 370 380 390 400 410 420 PIKLAEFGNV HRYEPSGALH GLMRVRGFTQ DDAHIFCTEE QMAAECLHIN DLILSVYKDF 430 440 450 460 470 480 GFEEITIKLS TRPEKRVGSD ELWDRAESVM MTVLEQIRQQ SNNIKTGILP GEGAFYGPKF 490 500 510 520 530 540 EYTLKDAIGR EWQCGTTQVD FNLPERFGAF YIGADSEKKQ PVMIHRAICG SMERFLGILI 550 560 570 580 590 600 ENFAGHMPLW FAPVQVVVAT ITSDADEYAK EAAAKLKAAG LQVVTDLRNE KINYKVREHS 610 620 630 640 650 LQKVPVILVC GKREAEEKTV NMRRLGSRDQ ESMTLDEAIA RLCEEATPPD LLRLKNAG

References

[1]

"Whole-genome analyses of speciation events in pathogenic Brucellae." Chain P.S., Comerci D.J., Tolmasky M.E., Larimer F.W., Malfatti S.A., Vergez L.M., Aguero F., Land M.L., Ugalde R.A., Garcia E. Infect. Immun. 73:8353-8361(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 2308.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AM040264 Genomic DNA. Translation: CAJ11049.1.
RefSeq	YP_414489.1. NC_007618.1.
3D structure databases
ProteinModelPortal	Q2YQ07.
SMR	Q2YQ07. Positions 245-646.
ModBase	Search...
Protein-protein interaction databases
STRING	359391.BAB1_1093.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	CAJ11049; CAJ11049; BAB1_1093.
GeneID	3787745.
KEGG	bmf:BAB1_1093.
PATRIC	17845134. VBIBruMel86222_1138.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0441.
HOGENOM	HOG000003880.
KO	K01868.
OMA	KITYKIR.
ProtClustDB	PRK00413.
Enzyme and pathway databases
BioCyc	BMEL359391:GJOQ-1113-MONOMER.
Family and domain databases
Gene3D	3.10.20.30. 1 hit. 3.40.50.800. 1 hit.
HAMAP	MF_00184. Thr_tRNA_synth.
InterPro	IPR002314. aa-tRNA-synt_IIb_cons-dom. IPR006195. aa-tRNA-synth_II. IPR004154. Anticodon-bd. IPR012675. Beta-grasp_dom. IPR012676. TGS-like. IPR002320. Thr-tRNA-ligase_IIa. IPR018163. Thr/Ala-tRNA-synth_IIc_edit. IPR012947. tRNA_SAD. [Graphical view]
Pfam	PF03129. HGTP_anticodon. 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_BRUA2

Accession

Primary (citable) accession number: Q2YQ07

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 15, 2008
Last sequence update:	December 20, 2005
Last modified:	May 1, 2013
This is version 62 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program