O05947 (SYT_RICPR) 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:	RP221

Organism

Rickettsia prowazekii (strain Madrid E) [Reference proteome] [HAMAP]

Taxonomic identifier

272947 [NCBI]

Taxonomic lineage

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

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 Reference 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_0000101038
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)
	O05947 [UniParc]. Last modified July 1, 1997. Version 1. Checksum: B000D1514AF729D5	FASTA	635	72,677
	10 20 30 40 50 60 MINISFPDGS VKQFAQNITA FEIVNAISMS LAKAAIVVEI NGELKDLSTV IENDCKLRIL 70 80 90 100 110 120 TAQDYECLEI IRHDAAHLTA EAVKELFPET QVTIGPAIEN GYYYDFARDK PFSIDDLANI 130 140 150 160 170 180 EAKMQELSKK NEKITRELWD RDKAVEFFLS IGEHYKAKII ASIPEGEPIT LYRQGNFIDL 190 200 210 220 230 240 CRGPHSPSTG FVKHFKLMKV AGAYWRGNSR NEMLQRIYGT AWATKEQLDN YLFMLEEAEK 250 260 270 280 290 300 RDHRKIGKEL DLFHFQEEAQ GMVFWHDKGW SIYNTIEQYI RKKIRKNGYI EVKTPVLVDK 310 320 330 340 350 360 SLWEASGHWA KFRCDMFTLE TDDKTLALKP MNCPCHVQIF KQGIKSYRDL PLRMSEFGLC 370 380 390 400 410 420 HRNEASGALH GLMRVRSLVQ DDAHIFCAEE QITDETVRFC KLLTEVYKDF GFTDIKVKFS 430 440 450 460 470 480 DRSEICAGND EVWDKAENAL KTAIEKAGFI YTLNPGEAAF YGPKIEFVLT DAIGRQWQCG 490 500 510 520 530 540 TLQMDFVLPE RLDANYIAAS GEKKRPVMLH RAILGSLERF IGILIEEYAG KFPIWLAPVQ 550 560 570 580 590 600 VAIATITNDL NDYALEVQKT LIDNGVRTDI NISPDKINYK IREFSNQKIP IIAVIGKQEQ 610 620 630 ANKQVTIRKL GTIEQEILSI EQLIAMIKKE NSNYL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Genomic rearrangements during evolution of the obligate intracellular parasite Rickettsia prowazekii as inferred from an analysis of 52015 bp nucleotide sequence." Andersson J.O., Andersson S.G.E. Microbiology 143:2783-2795(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: Madrid E.
[2]	"The genome sequence of Rickettsia prowazekii and the origin of mitochondria." Andersson S.G.E., Zomorodipour A., Andersson J.O., Sicheritz-Ponten T., Alsmark U.C.M., Podowski R.M., Naeslund A.K., Eriksson A.-S., Winkler H.H., Kurland C.G. Nature 396:133-140(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Madrid E.

Cross-references

Sequence databases
EMBL GenBank DDBJ	Y11780 Genomic DNA. Translation: CAA72469.1. AJ235270 Genomic DNA. Translation: CAA14684.1.
PIR	E71733.
RefSeq	NP_220607.1. NC_000963.1.
3D structure databases
ProteinModelPortal	O05947.
SMR	O05947. Positions 241-631.
ModBase	Search...
Protein-protein interaction databases
STRING	272947.RP221.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	CAA14684; CAA14684; CAA14684.
GeneID	883948.
KEGG	rpr:RP221.
PATRIC	17901202. VBIRicPro72556_0229.
Phylogenomic databases
eggNOG	COG0441.
HOGENOM	HOG000003880.
KO	K01868.
OMA	KITYKIR.
ProtClustDB	PRK00413.
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_RICPR

Accession

Primary (citable) accession number: O05947

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	July 1, 1997
Last modified:	May 1, 2013
This is version 91 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program