Reviewed, UniProtKB/Swiss-Prot P56881 (SYT_THET8)

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:	TTHA1875

Organism

Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579) [Complete proteome] [HAMAP]

Taxonomic identifier

300852 [NCBI]

Taxonomic lineage

Bacteria › Deinococcus-Thermus › Deinococci › Thermales › Thermaceae › Thermus

Protein attributes

Sequence length	659 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

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. HAMAP MF_00184
Subunit structure	Homodimer. HAMAP MF_00184
Subcellular location	Cytoplasm. HAMAP MF_00184
Domain	The C-terminal domain recognizes the anticodon bases. 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 Direct protein sequencing
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 – 659	659	Threonyl-tRNA synthetase HAMAP MF_00184		PRO_0000101075
Regions
	Region	234 – 548	315	Catalytic HAMAP MF_00184
	Compositional bias	338 – 341	4	Poly-Glu HAMAP MF_00184
Sites
	Metal binding	349	1	Zinc; catalytic By similarity
	Metal binding	400	1	Zinc; catalytic By similarity
	Metal binding	529	1	Zinc; catalytic By similarity
Experimental info
	Sequence conflict	42	1	E → T AA sequence Ref.3

Sequences

	Sequence		Length	Mass (Da)
	P56881-1 [UniParc]. Last modified May 30, 2000. Version 1. Checksum: 1993A1BEF1151FF4	FASTA	659	75,537
	10 20 30 40 50 60 MTVYLPDGKP LELPEGATAK DVARALGEGW ERRAVGAIVD GELYDLLKPL PQGAKVRLLT 70 80 90 100 110 120 EKDPEFQTLF RHTLAHVLAQ AVKEFFREKG YDPESVRLGV GPVIEKGFYY DIEAPEPLSD 130 140 150 160 170 180 EDLPAIEAKM REILKRDLPL RRFVLSREEA LARYRGKDPY KTELVLEIPE GEEISFYQQG 190 200 210 220 230 240 DEAYGFTDLC RGPHVPSTGR IPPHFKLTHV AGAYWRGDEN RPMLQRVYGV AFRTAEELKE 250 260 270 280 290 300 YLWQLEEAKK RDHRRLGREL ELFLIDPLVG KGLVLWLPKG NVVREELMAF MREEQVRRGY 310 320 330 340 350 360 QLVTTPHIGS LELYKTSGHY PYYAESQFPP ISFKERGEEE EYLLKPMNCP HHIRIYAYRK 370 380 390 400 410 420 RSYRELPLRL AEFGTVYRYE KAGELLGLTR VRGFTQDDAH IFCTPEEVKG EFLGVLDLVL 430 440 450 460 470 480 KVFATLGLKD YRARIGVRDP KSDKYVGDEA KWALAERQIE EAAAEAGLRY TVEEGDAAFY 490 500 510 520 530 540 GPKLDFVVKD ALGREWQLGT IQVDYNLPER FGLTYVGKDG EEHRPVMLHR APFGSLERFI 550 560 570 580 590 600 GILIEHFAGD FPLWLAPVQA VVVPVSEKQE DYAREVAGRL KEAGLRAEAD TRPERMQARI 610 620 630 640 650 RDAEVQKVPY ILVVGEREKA EGAVSVRRRK KGNLGTMPLA AFLEGALREY RERRLEPVF

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Sequence analysis and modular organization of threonyl-tRNA synthetase from Thermus thermophilus and its interrelation with threonyl-tRNA synthetases of other origins." Cura V., Moras D., Kern D. Eur. J. Biochem. 267:379-393(2000) [PubMed: 10632708] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Complete genome sequence of Thermus thermophilus HB8." Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T., Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S. Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]	"Threonyl-tRNA synthetase from Thermus thermophilus: purification and some structural and kinetic properties." Zheltonosova J., Melnikova E., Garber M., Reinbolt J., Kern D., Ehresmann C., Ehresmann B. Biochimie 76:71-77(1994) [PubMed: 8031907] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-45, CHARACTERIZATION.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AJ250953 Genomic DNA. Translation: CAB65483.1. AP008226 Genomic DNA. Translation: BAD71698.1.
RefSeq	YP_145141.1.
3D structure databases
HSSP	HSSP built from PDB template 1EVL based on UniProtKB P00955.
ModBase	Search...
Protein-protein interaction databases
STRING	P56881.
Genome annotation databases
GeneID	3168147.
GenomeReviews	Gene locus TTHA1875 in contig AP008226_GR.
KEGG	ttj:TTHA1875.
NMPDR	fig|300852.3.peg.1418.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	P56881.
OMA	HIGNIEL.
Enzyme and pathway databases
BioCyc	TTHE300852:TTHA1875-MON.
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_THET8

Accession

Primary (citable) accession number: P56881
Secondary accession number(s): Q5SH55

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	May 30, 2000
Last modified:	November 3, 2009
This is version 62 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)