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A0JXC7 (SYT_ARTS2) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 44. 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:Arth_2317
OrganismArthrobacter sp. (strain FB24) [Complete proteome] [HAMAP]
Taxonomic identifier290399 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesMicrococcineaeMicrococcaceaeArthrobacter

Protein attributes

Sequence length669 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 – 669669Threonine--tRNA ligase HAMAP MF_00184
PRO_1000020338

Regions

Region260 – 566307Catalytic HAMAP MF_00184

Sites

Metal binding3651Zinc; catalytic By similarity
Metal binding4161Zinc; catalytic By similarity
Metal binding5431Zinc; catalytic By similarity

Sequences

Sequence LengthMass (Da)Tools
A0JXC7 [UniParc].

Last modified December 12, 2006. Version 1.
Checksum: 21BE16FDEBC45439

FASTA66974,930
        10         20         30         40         50         60 
MSDAQQITLI VDGEETKVTT GTTGAELFFE RRDVVVARVN GELKDLDQPL PEGADIEGVT 

        70         80         90        100        110        120 
IDSPDGLNVL RHSTAHVMAQ AVQQLRPDAK LGIGPYITDG FYFDFDVAEP FTPEDLKALE 

       130        140        150        160        170        180 
KMMLKIINQN QKFVRRVVSE DEAREAMKNE PYKLELLGKK NNAADAGEGV NVEVGAGDIT 

       190        200        210        220        230        240 
IYDNVDRKSG DSVWCDLCRG PHLPNTKLIS NAFALTRSSA AYWLGNQNNQ QLQRIYGTAW 

       250        260        270        280        290        300 
PTKDALKAYQ ERIAEAERRD HRKLGAELDL FSFPDELGSG LPVFHPKGGI IRKAMEDYSR 

       310        320        330        340        350        360 
QRHVDAGYDF VYTPHITKGH LYEVSGHLDW YKEGMFPAMH IDAELNEDGT VRKPGQDYYL 

       370        380        390        400        410        420 
KPMNCPMHNL IFRSRGRSYR ELPLRLFEFG SVYRYEKSGV VHGLTRVRGM TQDDAHIYCT 

       430        440        450        460        470        480 
REQMKDELTT TLNFVLGLLK DYGLDDFYLE LSTKNEDKFV GDDATWDEAT RTLAEVAEAS 

       490        500        510        520        530        540 
GLELIPDPGG AAFYGPKISV QAKDALGRTW QMSTIQLDFN LPERFELEFQ AADGTRQRPV 

       550        560        570        580        590        600 
MIHRALFGSV ERFMGVLTEH YAGAFPAWLA PVQVVGIPVA EAFNDYMFDV VDQLKAVGIR 

       610        620        630        640        650        660 
AEVDISSDRF PKKIRTASKD KIPFVLIAGG EDAEAGAVSF RFRDGSQDNG VPVAEAVQRI 


VEAVRNRTS 

« Hide

References

[1]"Complete sequence of chromosome 1 of Arthrobacter sp. FB24."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Chertkov O., Thompson S., Brettin T., Bruce D., Han C., Tapia R., Gilna P. expand/collapse author list , Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Beasley F., Chen W., Jerke K., Nakatsu C.H., Richardson P.
Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: FB24.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000454 Genomic DNA. Translation: ABK03697.1.
RefSeqYP_831797.1. NC_008541.1.

3D structure databases

ProteinModelPortalA0JXC7.
ModBaseSearch...

Protein-protein interaction databases

STRINGA0JXC7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4445360.
GenomeReviewsGene locus Arth_2317 in contig CP000454_GR.
KEGGart:Arth_2317.
PATRIC20999977. VBIArtSp72239_2686.
TIGRArth_2317.

Phylogenomic databases

eggNOGCOG0441.
HOGENOMHBG352811.
OMAGRKWQLG.
ProtClustDBPRK00413.

Enzyme and pathway databases

BioCycASP1667:ARTH_2317-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.
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.
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.
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_ARTS2
AccessionPrimary (citable) accession number: A0JXC7
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: December 12, 2006
Last modified: January 25, 2012
This is version 44 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