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A1USJ2 (SYT_BARBK) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 42. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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:BARBAKC583_0641
OrganismBartonella bacilliformis (strain ATCC 35685 / KC583) [Complete proteome] [HAMAP]
Taxonomic identifier360095 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBartonellaceaeBartonella

Protein attributes

Sequence length658 AA.
Sequence statusComplete.
Protein existenceInferred 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. HAMAP MF_00184

Subunit structure

Homodimer By similarity. HAMAP MF_00184

Subcellular location

Cytoplasm HAMAP MF_00184.

Sequence similarities

Belongs to the class-II aminoacyl-tRNA synthetase family.

Ontologies

Keywords
   Biological processProtein biosynthesis
   Cellular componentCytoplasm
   LigandATP-binding
Metal-binding
Nucleotide-binding
Zinc
   Molecular functionAminoacyl-tRNA synthetase
Ligase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processthreonyl-tRNA aminoacylation

Inferred from electronic annotation. Source: InterPro

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

threonine-tRNA ligase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 658658Threonine--tRNA ligase HAMAP MF_00184
PRO_1000020343

Regions

Region246 – 549304Catalytic HAMAP MF_00184

Sites

Metal binding3431Zinc; catalytic By similarity
Metal binding3941Zinc; catalytic By similarity
Metal binding5261Zinc; catalytic By similarity

Sequences

Sequence LengthMass (Da)Tools
A1USJ2 [UniParc].

Last modified February 6, 2007. Version 1.
Checksum: DE4236DD7882B76D

FASTA65875,863
        10         20         30         40         50         60 
MSFSISLSFP DGSQRDFPAE ITGLELAESI SKSLAKKAIA YSLNGVIRDL LDPLEQSGQV 

        70         80         90        100        110        120 
EIITRDDPRA LQLIRHSCAH VLAEAVQELF PETQVTIGPV IENGFYYDFA RQQPFTLEDL 

       130        140        150        160        170        180 
NTIEKKMREI IQRNKFFKKE IWSREKAKKI FSDKGELYKV ELIDAIPEDQ DLKIYYQGDW 

       190        200        210        220        230        240 
FDLCRGPHVP STGQIGNAFK LMKVAGAYWR GDANNPMLTR IYGTAFSNEN ALKAYLNMLE 

       250        260        270        280        290        300 
EAEKRDHRRL GREMDLFHFQ EEGPGMIFWH PKGWKMFQNL VSYMRRRLDE HKYDEVNAPQ 

       310        320        330        340        350        360 
VLDKSLWETS GHWGWYQENM FKTIPATNDW NDEHVYALKP MNCPGHVQIF KHGLKSYRDL 

       370        380        390        400        410        420 
PIRLAEFGLL HRYEPSGSLH GLMRVRSFTQ DDAHVFCTDE QLADECLKIN DLILSTYADF 

       430        440        450        460        470        480 
GFEEIILKLS TRPEKRVGSD ELWDHAENIM MSVLKTIEKE AKGRIKTSIL QGEGAFYGPK 

       490        500        510        520        530        540 
FEYTLKDAIG REWQCGTTQV DFNLPERFEV FYINRDSEKC QPVMIHRAIF GSMERFLGIL 

       550        560        570        580        590        600 
IENFAGHMPL WLAPQQIVVT TITSEANEYA EKITAKLKAS GLSAVSDLRS EKINYKIREH 

       610        620        630        640        650 
SLQKVPVILV CGKRESETNS VNMRRLGSMN QISLPIDQAI KQLTNEAIPP DLRRFMNS 

« Hide

References

[1]Hendrix L., Mohamoud Y., Radune D., Shvartsbeyn A., Daugherty S., Dodson R., Durkin A.S., Harkins D., Huot H., Kothari S.P., Madupu R., Li J., Nelson W.C., Shrivastava S., Giglio M.G., Haft D., Selengut J., Fraser-Ligget C., Seshadri R.
Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 35685 / KC583.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000524 Genomic DNA. Translation: ABM44590.1.
RefSeqYP_988945.1. NC_008783.1.

3D structure databases

ProteinModelPortalA1USJ2.
SMRA1USJ2. Positions 245-653.
ModBaseSearch...

Protein-protein interaction databases

STRINGA1USJ2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4684002.
GenomeReviewsGene locus BARBAKC583_0641 in contig CP000524_GR.
KEGGbbk:BARBAKC583_0641.
NMPDRfig|360095.3.peg.321.
PATRIC20537569. VBIBarBac6912_0625.
TIGRBARBAKC583_0641.

Phylogenomic databases

eggNOGCOG0441.
HOGENOMHBG352811.
OMAVGSDALW.
ProtClustDBPRK00413.

Enzyme and pathway databases

BioCycBBAC360095:BARBAKC583_0641-MONOMER.

Family and domain databases

HAMAPMF_00184. Thr_tRNA_synth.
[Tree]
InterProIPR002314. aa-tRNA-synt_IIb_cons-dom.
IPR006195. aa-tRNA-synth_II.
IPR004154. Anticodon-bd.
IPR012675. Beta-grasp_ferredoxin-type.
IPR004095. TGS.
IPR012676. TGS-like.
IPR002320. Thr-tRNA-synth_IIa.
IPR018163. Thr/Ala-tRNA-synth_IIc_edit.
IPR012947. tRNA_SAD.
[Graphical view]
Gene3DG3DSA:3.40.50.800. Anticodon_bd. 1 hit.
G3DSA:3.10.20.30. Ferredoxin_fold. 1 hit.
KOK01868.
PfamPF03129. HGTP_anticodon. 1 hit.
PF02824. TGS. 1 hit.
PF00587. tRNA-synt_2b. 1 hit.
PF07973. tRNA_SAD. 1 hit.
[Graphical view]
PRINTSPR01047. TRNASYNTHTHR.
SMARTSM00863. tRNA_SAD. 1 hit.
[Graphical view]
SUPFAMSSF52954. Anticodon_bd. 1 hit.
SSF81271. TGS-like. 1 hit.
SSF55186. Thr/Ala-tRNA-synth_IIc_edit. 1 hit.
TIGRFAMsTIGR00418. ThrS. 1 hit.
PROSITEPS50862. AA_TRNA_LIGASE_II. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYT_BARBK
AccessionPrimary (citable) accession number: A1USJ2
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: February 6, 2007
Last modified: January 25, 2012
This is version 42 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries

SIMILARITY comments

Index of protein domains and families