B5RMR3 (SYT_BORDL) 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:	BDU_723

Organism

Borrelia duttonii (strain Ly) [Complete proteome] [HAMAP]

Taxonomic identifier

412419 [NCBI]

Taxonomic lineage

Bacteria › Spirochaetes › Spirochaetales › Spirochaetaceae › Borrelia

Protein attributes

Sequence length	583 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: 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 – 583	583	Threonine--tRNA ligase HAMAP MF_00184		PRO_1000098543
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)
	B5RMR3 [UniParc]. Last modified November 4, 2008. Version 1. Checksum: 5B2DABF4CD53B568	FASTA	583	68,508
	10 20 30 40 50 60 MGEKLDKDSI LYKKRHSIAH VMAEAVLELF PNTKIAIGPP IKDGFYYDFD FEKHISEDDL 70 80 90 100 110 120 LLIEHKMREI LKTGSPFIRE VITREQALVL FKDEPYKIDL IQNFDVTDEI TIYKSHKFTD 130 140 150 160 170 180 LCRGPHVDNM NKLDPKAFKL TSIAGAYWRG DERNKMLSRI YGTLWNNEKD LKAYLKLQEE 190 200 210 220 230 240 IKKRDHRKLG RELNLFSVHD EIGPGLIFFH PHGARIRALI ENFWREEHFK NGYDILFTPH 250 260 270 280 290 300 IGKSWLWETS GHLDFYKESM FEKIEMDRSD YYVKPMNCPF HIAIYNTDKH SYRDLPFRWA 310 320 330 340 350 360 ELGTVYRYEK IGAIHGTMRV RGFTQDDAHI ICTYEQVNFE VREVLRFAID MWNKFGFTNL 370 380 390 400 410 420 KAYLSTKPEK AVGDDDDWQM AVKVLEKALI DFNIDFDIDE GGGAFYGPKI DLKIIDSLGR 430 440 450 460 470 480 AWQMSTIQFD FNLPVRFKMT YTAEDGKEKR PFMIHRALLG SIERFFGILV EHYGGAFPVW 490 500 510 520 530 540 LAPLQVVIIP VNSIVEEYAL EVLSRFQNEG IRIKFDNYCN MRMNAKIRQY QSKKVPYMFI 550 560 570 580 IGEREVVEGK ISIRTRTNEQ INGLELKEAL EFVKLKISNK EIL

References

[1]

"The genome of Borrelia recurrentis, the agent of deadly louse-borne relapsing fever, is a degraded subset of tick-borne Borrelia duttonii." Lescot M., Audic S., Robert C., Nguyen T.T., Blanc G., Cutler S.J., Wincker P., Couloux A., Claverie J.-M., Raoult D., Drancourt M. PLoS Genet. 4:E1000185-E1000185(2008) [PubMed: 18787695] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Ly.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000976 Genomic DNA. Translation: ACH93649.1.
RefSeq	YP_002222355.1. NC_011229.1.
3D structure databases
ProteinModelPortal	B5RMR3.
ModBase	Search...
Protein-protein interaction databases
STRING	B5RMR3.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBBORT00000001066; EBBORP00000001028; EBBORG00000001066.
GeneID	6917949.
GenomeReviews	Gene locus BDU_723 in contig CP000976_GR.
KEGG	bdu:BDU_723.
PATRIC	20563564. VBIBorDut9941_0730.
Organism-specific databases
CMR	Search...
Phylogenomic databases
GeneTree	EBGT00050000007426.
HOGENOM	HBG352811.
OMA	MIIRNIL.
ProtClustDB	PRK12305.
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_BORDL

Accession

Primary (citable) accession number: B5RMR3

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 24, 2009
Last sequence update:	November 4, 2008
Last modified:	January 25, 2012
This is version 30 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program