O51662 (SYT_BORBU) 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:	BB_0720

Organism

Borrelia burgdorferi (Lyme disease spirochete)

Taxonomic identifier

139 [NCBI]

Taxonomic lineage

Bacteria › Spirochaetes › Spirochaetales › Spirochaetaceae › Borrelia › Borrelia burgdorferi group

Protein attributes

Sequence length	581 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 Reference 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 – 581	581	Threonine--tRNA ligase HAMAP MF_00184		PRO_0000100945
Regions
	Region	185 – 478	294	Catalytic HAMAP MF_00184
Sites
	Metal binding	278	1	Zinc; catalytic By similarity
	Metal binding	329	1	Zinc; catalytic By similarity
	Metal binding	455	1	Zinc; catalytic By similarity

Sequences

	Sequence		Length	Mass (Da)
	O51662 [UniParc]. Last modified June 1, 1998. Version 1. Checksum: 52CEC7B50BEFC169	FASTA	581	68,172
	10 20 30 40 50 60 MSKDLDKEDI LYKKRHSIAH VMAEAVLDLF PNTKIAIGPP IKDGFYYDFE FKKQITEDSL 70 80 90 100 110 120 LDIENRMREI LKTGSSFEKE IISVEQALEI FKDEPYKIDL IKNFDLQNEV SIYKSHNFVD 130 140 150 160 170 180 LCRGPHVENM NKIDPKAFKL TSIAGAYWRG SEKNPMLTRI YGTLWNNEKE LRSYLNLREE 190 200 210 220 230 240 IKKRDHRKLG KELDLFSIHE EIGPGLVFFH PNGAKIRALI EDFWREEHSK NGYDILFTPH 250 260 270 280 290 300 IGKSWLWQTS GHLDFYKDSM FEKIEMDKSD YYLKPMNCPF HIAIYNTGKH SYRDLPFRWA 310 320 330 340 350 360 ELGTVYRYEK IGALHGMMRA RGFTQDDAHI ICTHSQVLDE IKEVLRFAIY MWSKFGFSNP 370 380 390 400 410 420 KAYLSTKPDK SVGNDSDWEM SLKVLEETLS DFEVPYEIDK GGGAFYGPKI DLKIVDSLER 430 440 450 460 470 480 EWQMSTIQFD FNLPERFNMT YTAEDGKEKR PFMIHRALLG SIERFFGILV EHYGGAFPLW 490 500 510 520 530 540 LSPVQVVIIP VNNIVEDYAI KVFNKFKNEG IRIKLDNSSS RMNAKIREYQ AKKIPYMFII 550 560 570 580 GEREATEERI SIRTRTNEQI NGMKLDEALK FILFKIRDKE I

References

[1]

"Genomic sequence of a Lyme disease spirochaete, Borrelia burgdorferi." Fraser C.M., Casjens S., Huang W.M., Sutton G.G., Clayton R.A., Lathigra R., White O., Ketchum K.A., Dodson R.J., Hickey E.K., Gwinn M.L., Dougherty B.A., Tomb J.-F., Fleischmann R.D., Richardson D.L., Peterson J.D., Kerlavage A.R., Quackenbush J. , Salzberg S.L., Hanson M., van Vugt R., Palmer N., Adams M.D., Gocayne J.D., Weidman J.F., Utterback T.R., Watthey L., McDonald L.A., Artiach P., Bowman C., Garland S.A., Fujii C., Cotton M.D., Horst K., Roberts K.M., Hatch B., Smith H.O., Venter J.C. Nature 390:580-586(1997) [PubMed: 9403685] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 35210 / B31 / CIP 102532 / DSM 4680.

+

Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE000783 Genomic DNA. Translation: AAC67076.1.
PIR	G70189.
RefSeq	NP_212854.1. NC_001318.1.
3D structure databases
ProteinModelPortal	O51662.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBBORT00000008382; EBBORP00000007712; EBBORG00000008381.
GeneID	1195574.
GenomeReviews	Gene locus BB_0720 in contig AE000783_GR.
KEGG	bbu:BB0720.
NMPDR	fig|224326.1.peg.1104.
PATRIC	20558095. VBIBorBur75917_1111.
TIGR	BB_0720.
Phylogenomic databases
GeneTree	EBGT00050000007426.
HOGENOM	HBG352811.
OMA	MIIRNIL.
PhylomeDB	O51662.
ProtClustDB	PRK12305.
Enzyme and pathway databases
BioCyc	BBUR224326:BB_0720-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. 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.
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. 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_BORBU

Accession

Primary (citable) accession number: O51662

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 2000
Last sequence update:	June 1, 1998
Last modified:	January 25, 2012
This is version 89 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program