A1R0E4 (SYT_BORT9) 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:	BT0720

Organism

Borrelia turicatae (strain 91E135) [Complete proteome] [HAMAP]

Taxonomic identifier

314724 [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_1000199531
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)
	A1R0E4 [UniParc]. Last modified April 14, 2009. Version 1. Checksum: 8EB4EF500E28DE87	FASTA	583	68,226
	10 20 30 40 50 60 MSEKLDKEDV LYKKRHSIAH VMAEAVIELF PNTKIAIGPP IKDGFYYDFD FEKHIIEDDL 70 80 90 100 110 120 LLIEQKMREI LKTGSSFVKE VITKEQALML FKDEPYKIDL IHELDIADEI SIYKSHNFTD 130 140 150 160 170 180 LCKGPHIDNM GKIDPKAFKL ISIAGAYWRG DEKNKMLTRI YGTLWNNEKD LKAYLKLREE 190 200 210 220 230 240 IKRRDHRKLG RELDLFSVHE EIGPGLIFFH PSGARIRALI EDFWREEHFK NGYDILFTPH 250 260 270 280 290 300 VGKSWLWETS GHLDFYKESM FEKMEMDKSN YYVKPMNCPF HIAIYNTGRH SYRDLPFRWA 310 320 330 340 350 360 ELGTVYRYEK VGALHGTMRV RGFTQDDAHI ICTYDQVKFE VQEVLRFALY MWNKFGFTAL 370 380 390 400 410 420 KAYLSTKPEK SVGDEDDWIM SVKVLKEALI NLGIDYDIDE GGGAFYGPKI DLKIIDSLGR 430 440 450 460 470 480 EWQMSTIQFD FNLPARFKMT YTAEDGKERQ PFMIHRALLG SIERFFGILV EHYGGAFPVW 490 500 510 520 530 540 LAPLQVVIIP VNNIVEEYAL EVLSRFKKEG IRIKLDNDCN MRMNAKIRQY QSQKVPYMFI 550 560 570 580 VGEKEVVEGK ISIRTRTNEQ INGLELKEAL EFVKLKVSNK EIL

References

[1]

"The genome sequence of Borrelia hermsii and Borrelia turicatae: comparative analysis of two agents of endemic N. America relapsing fever." Porcella S.F., Raffel S.J., Schrumpf M.E., Montgomery B., Smith T., Schwan T.G. Submitted (DEC-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 91E135.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000049 Genomic DNA. Translation: AAX18036.1.
RefSeq	YP_945706.1. NC_008710.1.
3D structure databases
ProteinModelPortal	A1R0E4.
ModBase	Search...
Protein-protein interaction databases
STRING	A1R0E4.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBBORT00000000123; EBBORP00000000123; EBBORG00000000123.
GeneID	4642891.
GenomeReviews	Gene locus BT0720 in contig CP000049_GR.
KEGG	btu:BT0720.
PATRIC	20573165. VBIBorTur92789_0706.
Organism-specific databases
CMR	Search...
Phylogenomic databases
GeneTree	EBGT00050000007426.
OMA	MVHRALY.
ProtClustDB	PRK12305.
Enzyme and pathway databases
BioCyc	BTUR314724:BT0720-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_BORT9

Accession

Primary (citable) accession number: A1R0E4

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 28, 2009
Last sequence update:	April 14, 2009
Last modified:	January 25, 2012
This is version 28 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program