Reviewed, UniProtKB/Swiss-Prot Q9K866 (SYT_BACHD)

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:	BH3141

Organism

Bacillus halodurans [Complete proteome] [HAMAP]

Taxonomic identifier

86665 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length	645 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 – 645	645	Threonyl-tRNA synthetase HAMAP MF_00184		PRO_0000100937
Regions
	Region	247 – 544	298	Catalytic HAMAP MF_00184
Sites
	Metal binding	340	1	Zinc; catalytic By similarity
	Metal binding	391	1	Zinc; catalytic By similarity
	Metal binding	521	1	Zinc; catalytic By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9K866-1 [UniParc]. Last modified October 1, 2000. Version 1. Checksum: 2F47BE51A4FA573C	FASTA	645	73,852
	10 20 30 40 50 60 MADMINITFP DGAVKEFPKG TTTAEIAGSI SPGLKKKALA GMLDGTLLDL NTPIEQDGTI 70 80 90 100 110 120 TIVTPESDEA LEVLRHSTAH VMAQALKRLF KDRNVKLGVG PVIEGGFYYD VDMDESLTPE 130 140 150 160 170 180 DLPKIEKEMK KIIGENLPIE RVVVSREEAL ARYEEVGDPY KIELINDLPE DETITIYEQG 190 200 210 220 230 240 EFFDLCRGVH VPSTGKLKEF KLLNLAGAYW RGDSSNKMLQ RIYGTAFFKK ADLDEHLRLL 250 260 270 280 290 300 EEAKERDHRK LGKELGIFAL SQKVGQGLPL WLPKGATIRR IIERYIVDKE EKLGYQHVYT 310 320 330 340 350 360 PVLASSELYK TSGHWDHYKD DMFPTMEMEN EELVLRPMNC PHHMMVYKTE MRSYRQLPLR 370 380 390 400 410 420 IAELGLMHRY EMSGAVSGLQ RVRGMTLNDA HIFCRPDQIK DEFVRVVRLI QAVYEDFGLK 430 440 450 460 470 480 NYSFRLSYRD PEDKEKYFDD DNMWNKAQGM LKEAMDELEL EYFEAEGEAA FYGPKLDVQV 490 500 510 520 530 540 RTALGKDETL STVQLDFLLP ERFDLTYVGE DGQPHRPVVV HRGVVSTMER FVAFLLEEYK 550 560 570 580 590 600 GAFPTWLAPV QVQVIPVSPE AHLEYAKNVQ ETLQQAGIRV EIDERDEKIG YKIREAQMQK 610 620 630 640 IPYMLVLGDK EVEANGVNVR KYGEKDSSSM GLDEFVRHVA REAKK

References

[1]

"Complete genome sequence of the alkaliphilic bacterium Bacillus halodurans and genomic sequence comparison with Bacillus subtilis." Takami H., Nakasone K., Takaki Y., Maeno G., Sasaki R., Masui N., Fuji F., Hirama C., Nakamura Y., Ogasawara N., Kuhara S., Horikoshi K. Nucleic Acids Res. 28:4317-4331(2000) [PubMed: 11058132] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC BAA-125 / C-125 / DSM 18197 / FERM 7344 / JCM 9153.

Cross-references

Sequence databases
EMBLGenBankDDBJ	BA000004 Genomic DNA. Translation: BAB06860.1.
PIR	E84042.
RefSeq	NP_244007.1.
3D structure databases
HSSP	HSSP built from PDB template 1EVL based on UniProtKB P00955.
ModBase	Search...
Genome annotation databases
GeneID	890593.
GenomeReviews	Gene locus BH3141 in contig BA000004_GR.
KEGG	bha:BH3141.
NMPDR	fig|272558.1.peg.3141.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q9K866.
OMA	IQLDFML.
Enzyme and pathway databases
BioCyc	BHAL272558:BH3141-MON.
BRENDA	6.1.1.3. 191865.
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. IPR012675. b-grasp_ferredoxin-like. IPR004095. TGS. 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. G3DSA:3.10.20.30. Ferredoxin_fold. 1 hit.
Pfam	PF03129. HGTP_anticodon. 1 hit. PF02824. TGS. 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_BACHD

Accession

Primary (citable) accession number: Q9K866

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 23, 2002
Last sequence update:	October 1, 2000
Last modified:	November 3, 2009
This is version 56 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)