Reviewed, UniProtKB/Swiss-Prot Q1LT04 (SYT_BAUCH)

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:	BCI_0472

Organism

Baumannia cicadellinicola subsp. Homalodisca coagulata [Complete proteome] [HAMAP]

Taxonomic identifier

374463 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Candidatus Baumannia

Protein attributes

Sequence length	642 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 – 642	642	Threonyl-tRNA synthetase HAMAP MF_00184		PRO_1000020344
Regions
	Region	243 – 534	292	Catalytic HAMAP MF_00184
Sites
	Metal binding	334	1	Zinc; catalytic By similarity
	Metal binding	385	1	Zinc; catalytic By similarity
	Metal binding	511	1	Zinc; catalytic By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q1LT04-1 [UniParc]. Last modified May 30, 2006. Version 1. Checksum: B6B1324B5BB2914E	FASTA	642	75,086
	10 20 30 40 50 60 MPVITITNGL QLTFQKPVSS LEIAKYISSN CEQNCIASYL NNRLVDAVDL IMQDSKLDII 70 80 90 100 110 120 TAEDKAGLDI LRCSCNHLLG HAIKQLWPEA KMTIGKIIDK GFYYDIDLEH KLQPEDIDAL 130 140 150 160 170 180 EKCMHTLANK NYNIVKKYVS WQQAREIFQA NGEIYKVAIL DDNINQHTLV ALYYYEEYVD 190 200 210 220 230 240 MCRGPHAPNI RFCHHFKLQK TSITYWRNND KNKKLQRIYG TAWGTDMQLK CYLQSLQEVK 250 260 270 280 290 300 KRDHRKIGQQ LDLYHIQEEA PGMVFWHVDG WIIFRELETF IRSKLQTYKY QEVKSPVMID 310 320 330 340 350 360 RTLWEQTGHW SNYAEHIFTT SSENREYCIK PMNCPGHVQI FNQQINSYRD LPLRMAEFGS 370 380 390 400 410 420 CYRNEPSGSL HGLMRVRNFT QDDAHIFCTE EQVCDEINNN IKMLYEVYHT FGFKKILVNL 430 440 450 460 470 480 STRPAHRIGN DKIWDKAEQD LATTLTNNGI LFKYNVGAGA FYGPKIEFTL LDSFDRAWQC 490 500 510 520 530 540 GTIQLDFSLP SRLKAFYINK NNQRLVPVMI HRAILGSLER FIGILIEEYA GFFPTWLAPT 550 560 570 580 590 600 QVVLMNISDN QSNYVIQLMQ KLSTANIRAK IDLRNEKIGF KIREHTLRRV PYMLICGDQE 610 620 630 640 IKMGKVTIRT RYGKNLGMFE MNNFIEKLQH EINHRNLSQI EK

References

[1]

"Metabolic complementarity and genomics of the dual bacterial symbiosis of sharpshooters." Wu D., Daugherty S.C., Van Aken S.E., Pai G.H., Watkins K.L., Khouri H., Tallon L.J., Zaborsky J.M., Dunbar H.E., Tran P.L., Moran N.A., Eisen J.A. PLoS Biol. 4:1079-1092(2006) [PubMed: 16729848] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CP000238 Genomic DNA. Translation: ABF13851.1.
RefSeq	YP_588910.1.
3D structure databases
SMR	Q1LT04. Positions 242-642.
ModBase	Search...
Protein-protein interaction databases
STRING	Q1LT04.
Genome annotation databases
GeneID	4056409.
GenomeReviews	Gene locus BCI_0472 in contig CP000238_GR.
KEGG	bci:BCI_0472.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q1LT04.
OMA	QDEAPGM.
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. 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. 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_BAUCH

Accession

Primary (citable) accession number: Q1LT04

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 15, 2008
Last sequence update:	May 30, 2006
Last modified:	November 3, 2009
This is version 31 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)