Reviewed, UniProtKB/Swiss-Prot Q0SMD6 (SYT_BORAP)

Names and origin

Protein names

Recommended name:
    Threonyl-tRNA synthetase
    EC=6.1.1.3
Alternative name(s):
    Threonine--tRNA ligase
      Short name=ThrRS

Gene names

Name:	thrS
Ordered Locus Names:	BAPKO_0764

Organism

Borrelia afzelii (strain PKo) [Complete proteome] [HAMAP]

Taxonomic identifier

390236 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	581 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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.
Subunit structure	Homodimer By similarity.
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: HAMAP
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP binding Inferred from electronic annotation. Source: HAMAP threonine-tRNA ligase activity Inferred from electronic annotation. Source: HAMAP zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 581	581	Threonyl-tRNA synthetase HAMAP MF_00184		PRO_1000020346
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)
	Q0SMD6-1 [UniParc]. Last modified September 5, 2006. Version 1. Checksum: 3A206764A2BBEFAB	FASTA	581	68,138
	10 20 30 40 50 60 MSKDLDKEDV LYKKRHSIAH VMAEAVRDLF PNTKIAIGPP IKDGFYYDFE FKKQITEDSL 70 80 90 100 110 120 LDIENRMREI LKTGSSFEKE LISVEQALEI FKDEPYKIDL IKNFDLQNEI SIYKSHNFID 130 140 150 160 170 180 LCRGPHVDNM NKIDPKAFKL TSIAGAYWRG NEKNTMLTRI YGTLWNNEKE LRSYLNLREE 190 200 210 220 230 240 IKKRDHRKLG KELDLFSIHE EIGPGLVFFH PNGAKIRALI EDFWREEHSK NGYDILFTPH 250 260 270 280 290 300 IGKSWLWQTS GHLDFYKDSM FEKMEMDKSD YYLKPMNCPF HIAIYNTGKH SYRDLPFRWA 310 320 330 340 350 360 ELGTVYRYEK IGALHGIMRA RGFTQDDAHI ICTHSQVLDE IKEVLRFAIY MWSKFGFNSL 370 380 390 400 410 420 KAYLSTKPDK FVGNDSDWEM SLKVLEEALS GFEVPYEIDK GGGAFYGPKI DLKIVDSLER 430 440 450 460 470 480 EWQMSTIQFD FNLPERFNMT YTAEDGKEKR PFMIHRALLG SIERFFGILI EHYGGAFPLW 490 500 510 520 530 540 LSPIQAVIIP VNNAVEDYAI KVFNKFKNEG MRIKLDNTSS RMNAKIREYQ AKKIPYMFII 550 560 570 580 GEREAKEEKI SIRTRTNEQI NGLELDEALK LILLKIRDKE I

References

[1]

"Comparative genome analysis: selection pressure on the Borrelia vls cassettes is essential for infectivity." Gloeckner G., Schulte-Spechtel U., Schilhabel M., Felder M., Suehnel J., Wilske B., Platzer M. BMC Genomics 7:211-211(2006) [PubMed: 16914037] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CP000395 Genomic DNA. Translation: ABH01992.1.
RefSeq	YP_710168.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	4227063.
GenomeReviews	Gene locus BAPKO_0764 in contig CP000395_GR.
KEGG	baf:BAPKO_0764.
NMPDR	fig|390236.5.peg.774.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q0SMD6.
OMA	Q0SMD6. NTKIAIG.
Enzyme and pathway databases
BioCyc	BAFZ390236:BAPKO_0764-MON.
Family and domain databases
HAMAP	MF_00184. [Tree]
InterPro	IPR002314. aa-tRNA-synt_IIb_cons-reg. IPR006195. aa-tRNA-synth_II_cons-reg. IPR004154. Anticodon_bd. IPR002320. Thr-tRNA-synth_IIa. IPR018158. Thr-tRNA-synth_IIa_cons-reg. IPR012947. tRNA_SAD. [Graphical view]
Gene3D	G3DSA:3.40.50.800. Anticodon_bd. 1 hit.
Pfam	PF03129. HGTP_anticodon. 1 hit. PF00587. tRNA-synt_2b. 1 hit. PF07973. tRNA_SAD. 1 hit. [Graphical view]
PRINTS	PR01047. TRNASYNTHTHR.
TIGRFAMs	TIGR00418. thrS. 1 hit.
PROSITE	PS50862. AA_TRNA_LIGASE_II. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

SYT_BORAP

Accession

Primary (citable) accession number: Q0SMD6

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 15, 2008
Last sequence update:	September 5, 2006
Last modified:	June 16, 2009
This is version 24 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)