Reviewed, UniProtKB/Swiss-Prot B6YQ95 (SYT_AZOPC)

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:	CFPG_104

Organism

Azobacteroides pseudotrichonymphae genomovar. CFP2 [Complete proteome] [HAMAP]

Taxonomic identifier

511995 [NCBI]

Taxonomic lineage

Bacteria › Bacteroidetes › Bacteroidia › Bacteroidales › Candidatus Azobacteroides

Protein attributes

Sequence length	648 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 By similarity.
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 – 648	648	Threonyl-tRNA synthetase HAMAP MF_00184		PRO_1000098541
Regions
	Region	243 – 542	300	Catalytic HAMAP MF_00184
Sites
	Metal binding	338	1	Zinc; catalytic By similarity
	Metal binding	389	1	Zinc; catalytic By similarity
	Metal binding	519	1	Zinc; catalytic By similarity

Sequences

	Sequence		Length	Mass (Da)
	B6YQ95-1 [UniParc]. Last modified January 20, 2009. Version 1. Checksum: EDB53D0B221280A7	FASTA	648	75,185
	10 20 30 40 50 60 MIKITFPNTS ARNYAIGTTP MQIAESISCR LAEEILSANV NGEMWDLSRP INENASVKLY 70 80 90 100 110 120 KWEDFEGKRT FWHSSAHLLA ESLQELYPNI HFGMGPAIEN GFYYDVDLGD GVVIKDVDLV 130 140 150 160 170 180 TIEKKMQELA SKKLSISRQN VTKQNALELF GKKGETYKIE LISKLEDGKI TVYTQGNFTD 190 200 210 220 230 240 LCRGPHLPNT SYIKAIKLTS VARAYWKGDE SRKQLTRIYG ISFPKKEELS EYLALMEKAK 250 260 270 280 290 300 KRDHRRIGKE MELFTFSHKV GRGLPLWLPK GTQLRLRLED FLKRIQKKYG YQQVITPHIG 310 320 330 340 350 360 NKTLYIASGH YAKYGKDSFQ PIHTPELGEE FLLKPMNCPH HCEIYKAFLR SYKELPLRLA 370 380 390 400 410 420 EFGTVYRYER SGELQGLTRV RGFTQDDAHI FCSPEQVKEE LIKVIDIVRV IFCALNFNDY 430 440 450 460 470 480 EVQISLRDLN NRIKYIGSEE NWKNSEGAII EVCQEKKIKA KIKLGEAAFY GPKLDFMVKD 490 500 510 520 530 540 ALGRNWQLGT IQVDYNLPER FELEYVGADN QKHRPVMIHR APFGSMERFV AVMIEHTGGK 550 560 570 580 590 600 FPLWLVSDQV VILPVSENYN QYAEEIAKEF HKRDIRVTID KRNEKVGRKI RDNELKKIPY 610 620 630 640 LLIIGEKERR NSEISVRKHG KENIGIMKVT EFAEFLKKEV ERQMSQWQ

References

[1]

"Genome of an endosymbiont coupling N2 fixation to cellulolysis within RT protist cells in termite gut." Hongoh Y., Sharma V.K., Prakash T., Noda S., Toh H., Taylor T.D., Kudo T., Sakaki Y., Toyoda A., Hattori M., Ohkuma M. Science 322:1108-1109(2008) [PubMed: 19008447] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	AP010656 Genomic DNA. Translation: BAG83367.1.
RefSeq	YP_002308778.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	7039217.
GenomeReviews	Gene locus CFPG_104 in contig AP010656_GR.
KEGG	aps:CFPG_104.
Organism-specific databases
CMR	Search...
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_AZOPC

Accession

Primary (citable) accession number: B6YQ95

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 24, 2009
Last sequence update:	January 20, 2009
Last modified:	June 16, 2009
This is version 7 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)