Q68XE8 (SYT_RICTY) 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:	RT0212

Organism

Rickettsia typhi (strain ATCC VR-144 / Wilmington) [Complete proteome] [HAMAP]

Taxonomic identifier

257363 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Alphaproteobacteria › Rickettsiales › Rickettsiaceae › Rickettsieae › Rickettsia › typhus group › Rickettsia typhi

Protein attributes

Sequence length	635 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-Rule MF_00184
Cofactor	Binds 1 zinc ion per subunit By similarity.
Subunit structure	Homodimer By similarity.
Subcellular location	Cytoplasm HAMAP-Rule 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 metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW threonine-tRNA ligase activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 635	635	Threonine--tRNA ligase HAMAP-Rule MF_00184		PRO_0000101039
Regions
	Region	242 – 533	292	Catalytic HAMAP-Rule MF_00184
Sites
	Metal binding	333	1	Zinc; catalytic By similarity
	Metal binding	384	1	Zinc; catalytic By similarity
	Metal binding	510	1	Zinc; catalytic By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q68XE8 [UniParc]. Last modified October 11, 2004. Version 1. Checksum: 9B0F9A0E3AA3239D	FASTA	635	72,799
	10 20 30 40 50 60 MINISFPDGS VKQFAQNITA FEIANAISMS LAKAAMVVEI NGEFKDLSTV IEHDCKLRIL 70 80 90 100 110 120 TAKDYECLEI IRHDAAHLTA AAVKELFPET QVAIGPAIEN GYYYDFARDK PFSRDDLATI 130 140 150 160 170 180 EAKMQELVKK NEKITRELWD RDKAIEFFLS IGEHYKAKII ASIPAGEQIT LYRQGNFIDL 190 200 210 220 230 240 CRGPHAPSTG FVKYFKLMKV AGAYWRGNSR NEMLQRIYGT AWATKEQLDN YLFMLEEAEK 250 260 270 280 290 300 RDHRKIGKEL DLFHFQEEAQ GMVFWHDKGW SIYNTIEQYI RKKNRKNGYI EVKTPVLVDK 310 320 330 340 350 360 SLWEASGHWA KFRCDMFTLE TDDKILALKP MNCPCHVQIF KQGIKSYRDL PLRMSEFGLC 370 380 390 400 410 420 HRNEASGALH GLMRVRSLVQ DDAHIFCAEE QITDETVRFC KLLTEVYKDF GFTDIKVKFS 430 440 450 460 470 480 DRPEIRAGND EVWDKAEHAL KTAVEKVGFI YTLNPGDGAF YGPKLEFVLT DAIGRQWQCG 490 500 510 520 530 540 TLQMDFVLPE RLDANYIAAS GEKKRPVMLH RAILGSLERF IGILIEEYAG KFPIWLAPVQ 550 560 570 580 590 600 VAIATITNDL NDYALEVQKT LIDNNIRTDI NISPDKINYK IREFSNQKIP MIAVIGKKEQ 610 620 630 ANKQVTIRKF GTTGQEILSI EQLIAMIKKE NSNYL

References

[1]

"Complete genome sequence of Rickettsia typhi and comparison with sequences of other Rickettsiae." McLeod M.P., Qin X., Karpathy S.E., Gioia J., Highlander S.K., Fox G.E., McNeill T.Z., Jiang H., Muzny D., Jacob L.S., Hawes A.C., Sodergren E., Gill R., Hume J., Morgan M., Fan G., Amin A.G., Gibbs R.A. , Hong C., Yu X.-J., Walker D.H., Weinstock G.M. J. Bacteriol. 186:5842-5855(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC VR-144 / Wilmington.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE017197 Genomic DNA. Translation: AAU03694.1.
RefSeq	YP_067176.1. NC_006142.1.
3D structure databases
ProteinModelPortal	Q68XE8.
SMR	Q68XE8. Positions 241-631.
ModBase	Search...
Protein-protein interaction databases
STRING	257363.RT0212.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAU03694; AAU03694; RT0212.
GeneID	2958589.
KEGG	rty:RT0212.
PATRIC	17909608. VBIRicTyp34752_0221.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0441.
HOGENOM	HOG000003880.
KO	K01868.
OMA	KITYKIR.
ProtClustDB	PRK00413.
Enzyme and pathway databases
BioCyc	RTYP257363:GJEQ-224-MONOMER.
Family and domain databases
Gene3D	3.10.20.30. 1 hit. 3.40.50.800. 1 hit.
HAMAP	MF_00184. Thr_tRNA_synth.
InterPro	IPR002314. aa-tRNA-synt_IIb_cons-dom. IPR006195. aa-tRNA-synth_II. IPR004154. Anticodon-bd. IPR012675. Beta-grasp_dom. IPR004095. TGS. IPR012676. TGS-like. IPR002320. Thr-tRNA-ligase_IIa. IPR018163. Thr/Ala-tRNA-synth_IIc_edit. IPR012947. tRNA_SAD. [Graphical view]
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.
SMART	SM00863. tRNA_SAD. 1 hit. [Graphical view]
SUPFAM	SSF52954. Anticodon_bd. 1 hit. SSF81271. TGS-like. 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_RICTY

Accession

Primary (citable) accession number: Q68XE8

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 30, 2005
Last sequence update:	October 11, 2004
Last modified:	May 1, 2013
This is version 60 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program