Q57D65 (SYT_BRUAB) 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:	BruAb1_1076

Organism

Brucella abortus biovar 1 (strain 9-941) [Complete proteome] [HAMAP]

Taxonomic identifier

262698 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Brucellaceae › Brucella

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 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 – 658	658	Threonine--tRNA ligase HAMAP MF_00184		PRO_0000100947
Regions
	Region	246 – 548	303	Catalytic HAMAP 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)
	Q57D65 [UniParc]. Last modified May 10, 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]

"Completion of the genome sequence of Brucella abortus and comparison to the highly similar genomes of Brucella melitensis and Brucella suis." Halling S.M., Peterson-Burch B.D., Bricker B.J., Zuerner R.L., Qing Z., Li L.-L., Kapur V., Alt D.P., Olsen S.C. J. Bacteriol. 187:2715-2726(2005) [PubMed: 15805518] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 9-941.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE017223 Genomic DNA. Translation: AAX74419.1.
RefSeq	YP_221780.1. NC_006932.1.
3D structure databases
ProteinModelPortal	Q57D65.
SMR	Q57D65. Positions 245-646.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	3339847.
GenomeReviews	Gene locus BruAb1_1076 in contig AE017223_GR.
KEGG	bmb:BruAb1_1076.
PATRIC	17823831. VBIBruAbo15061_1139.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG352811.
OMA	VGSDALW.
PhylomeDB	Q57D65.
ProtClustDB	PRK00413.
Enzyme and pathway databases
BioCyc	BABO262698:BRUAB1_1076-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. 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. 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_BRUAB

Accession

Primary (citable) accession number: Q57D65

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 30, 2005
Last sequence update:	May 10, 2005
Last modified:	January 25, 2012
This is version 45 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program