E4WGS9 (E4WGS9_RHOE1) Unreviewed, UniProtKB/TrEMBL

Names and origin

Protein names

Recommended name:
Threonine--tRNA ligase HAMAP-Rule MF_00184
EC=6.1.1.3 HAMAP-Rule MF_00184

Alternative name(s):
Threonyl-tRNA synthetase HAMAP-Rule MF_00184

Gene names

Name:	thrS HAMAP-Rule MF_00184 EMBL CBH48133.1
Ordered Locus Names:	REQ_20750 EMBL CBH48133.1

Organism

Rhodococcus equi (strain 103S) (Corynebacterium equi) [Complete proteome] [HAMAP]

Taxonomic identifier

685727 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Actinobacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Nocardiaceae › Rhodococcus › Corynebacterium equii

Protein attributes

Sequence length	683 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 SAAS SAAS002320
Cofactor	Binds 1 zinc ion per subunit By similarity. HAMAP-Rule MF_00184
Subunit structure	Homodimer By similarity. HAMAP-Rule MF_00184
Subcellular location	Cytoplasm By similarity HAMAP-Rule MF_00184.
Sequence similarities	Belongs to the class-II aminoacyl-tRNA synthetase family. RuleBase RU003746 HAMAP-Rule MF_00184

Ontologies

Keywords
Biological process	Protein biosynthesis HAMAP-Rule MF_00184 SAAS SAAS002320
Cellular component	Cytoplasm HAMAP-Rule MF_00184 SAAS SAAS002320
Ligand	ATP-binding HAMAP-Rule MF_00184 SAAS SAAS002320 Metal-binding HAMAP-Rule MF_00184 Nucleotide-binding Zinc HAMAP-Rule MF_00184
Molecular function	Aminoacyl-tRNA synthetase HAMAP-Rule MF_00184 SAAS SAAS002320 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
Regions
	Region	262 – 568	307	Catalytic By similarity HAMAP-Rule MF_00184
Sites
	Metal binding	367	1	Zinc; catalytic By similarity HAMAP-Rule MF_00184
	Metal binding	418	1	Zinc; catalytic By similarity HAMAP-Rule MF_00184
	Metal binding	545	1	Zinc; catalytic By similarity HAMAP-Rule MF_00184

Sequences

	Sequence		Length	Mass (Da)
	E4WGS9 [UniParc]. Last modified February 8, 2011. Version 1. Checksum: 2FDF288A2137C772	FASTA	683	76,392
	10 20 30 40 50 60 MTTPASVTPA ARVQVPAGTT AGTAVRDAGL PGKGPDAIVV VRDADGNLKD LSWTPDVDVE 70 80 90 100 110 120 VEAVAADTED GRSVIRHSAA HVLAQAVQQE FPEAKLGIGP PIKDGFYYDF QVERPFTPED 130 140 150 160 170 180 LAKLEKRMKK IVKDAQRFSR RVVEDLEDAR TELANEPFKL ELIDDKSGID DPEVMEVGGG 190 200 210 220 230 240 ELTIYDNLNP RTGEVIWKDL CRGPHIPTTK YIPAFKITRS SAAYWRGDQS REDLQRIYGT 250 260 270 280 290 300 AWESTEALDQ HLELLAEAER RDHRKLGAEL DLFSFPDELG SGLPVFHPKG GIIRQEMENY 310 320 330 340 350 360 SRKRHVEEGY EFVYSPHITK GHLYEVSGHL DWYKDGMFPA MHIDEELNED GTVRKPGQDY 370 380 390 400 410 420 YLKPMNCPMH NLVFGSRGRS YRELPLRLFE FGSVYRYEKS GVVHGLTRVR GMTQDDAHIY 430 440 450 460 470 480 CTKEQMRDEL TTTLKFVLGL LKDYGLDDFY LELSTKNPDK FVGDDALWEE ATETLREVGE 490 500 510 520 530 540 ASGLNLVPDP GGAAFYGPKI SVQVQDALGR SWQMSTIQLD FNLPERFDLE YTGSDGTKQR 550 560 570 580 590 600 PVMIHRALFG SIERFFGVLT EHYAGAFPAW LAPVQVVGIP VAEAFEDHLF DVVKQLKAAG 610 620 630 640 650 660 VRAEVDVSDD RMQKKIRNHT TQKVPFMLLA GERDVEAGAV SFRFRDGTQV NGVPVADAVE 670 680 TIVAWIGRRE NASPTAELVG GAQ

References

[1]

"The genome of a pathogenic rhodococcus: cooptive virulence underpinned by key gene acquisitions." Letek M., Gonzalez P., Macarthur I., Rodriguez H., Freeman T.C., Valero-Rello A., Blanco M., Buckley T., Cherevach I., Fahey R., Hapeshi A., Holdstock J., Leadon D., Navas J., Ocampo A., Quail M.A., Sanders M., Scortti M.M. , Prescott J.F., Fogarty U., Meijer W.G., Parkhill J., Bentley S.D., Vazquez-Boland J.A. PLoS Genet. 6:E1001145-E1001145(2010) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 103S.

Cross-references

Sequence databases
EMBL GenBank DDBJ	FN563149 Genomic DNA. Translation: CBH48133.1.
RefSeq	YP_004006818.1. NC_014659.1.
3D structure databases
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	CBH48133; CBH48133; REQ_20750.
GeneID	9964783.
KEGG	req:REQ_20750.
PATRIC	42661577. VBIRhoEqu141084_2073.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HOG000003880.
KO	K01868.
OMA	MYSPMDI.
Enzyme and pathway databases
BioCyc	REQU685727:GHKP-4479-MONOMER.
Family and domain databases
Gene3D	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. IPR002320. Thr-tRNA-ligase_IIa. IPR018163. Thr/Ala-tRNA-synth_IIc_edit. IPR012947. tRNA_SAD. [Graphical view]
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

E4WGS9_RHOE1

Accession

Primary (citable) accession number: E4WGS9

Entry history

Integrated into UniProtKB/TrEMBL:	February 8, 2011
Last sequence update:	February 8, 2011
Last modified:	May 1, 2013
This is version 18 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)