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UniProtKB/Swiss-Prot entry A1V3R3

[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name SYT_BURMS
Primary accession number A1V3R3
Secondary accession numbers None
Integrated into Swiss-Prot on January 15, 2008
Sequence was last modified on February 6, 2007 (Sequence version 1)
Annotations were last modified on    November 4, 2008 (Entry version 15)
Name and origin of the protein
Protein name Threonyl-tRNA synthetase
Synonyms EC 6.1.1.3
Threonine--tRNA ligase
ThrRS
Gene name
Name: thrS
OrderedLocusNames: BMASAVP1_A1539
From
Burkholderia mallei (strain SAVP1) [TaxID: 320388] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; Burkholderiaceae; Burkholderia.
Protein existence 3: Inferred from homology;
References
[1]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DeShazer D., Woods D.E., Nierman W.C.;
Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
CP000526; ABM52129.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq YP_992866.1; -.
3D structure databases
ModBase A1V3R3.
Ontologies
GO
GO:0005737; Cellular component: cytoplasm (inferred from electronic annotation from HAMAP).
GO:0005524; Molecular function: ATP binding (inferred from electronic annotation from HAMAP).
GO:0004829; Molecular function: threonine-tRNA ligase activity (inferred from electronic annotation from HAMAP).
GO:0008270; Molecular function: zinc ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0006435; Biological process: threonyl-tRNA aminoacylation (inferred from electronic annotation from HAMAP).
QuickGo view.
Family and domain databases
HAMAP MF_00184; -; 1.
PBIL [Tree]
InterPro IPR002314; aa-tRNA-synt_IIb.
IPR006195; aa-tRNA-synth_II.
IPR004154; Anticodon_bd.
IPR012675; b-grasp_ferredoxin-like.
IPR004095; TGS.
IPR002320; Thr-tRNA-synth_IIa.
IPR012947; tRNA_SAD.
Graphical view of domain structure.
Gene3D G3DSA:3.40.50.800; Anticodon_bd; 1.
G3DSA:3.10.20.30; Ferredoxin_fold; 1.
Pfam PF03129; HGTP_anticodon; 1.
PF02824; TGS; 1.
PF00587; tRNA-synt_2b; 1.
PF07973; tRNA_SAD; 1.
Pfam graphical view of domain structure.
PRINTS PR01047; TRNASYNTHTHR.
TIGRFAMs TIGR00418; thrS; 1.
PROSITE PS50862; AA_TRNA_LIGASE_II; 1.
PROSITE graphical view of domain structure (profiles).
Genome annotation databases
GeneID 4681248; -.
GenomeReviews CP000526_GR; BMASAVP1_A1539.
KEGG bmv:BMASAVP1_A1539; -.
TIGR BMASAVP1_A1539; -.
Other
ProtoNet A1V3R3.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Cytoplasm; Ligase; Metal-binding; Nucleotide-binding; Protein biosynthesis; Zinc.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   635  635     Threonyl-tRNA synthetase. PRO_1000020354
REGION   242   533  292     Catalytic. 
METAL   333   333        Zinc; catalytic (By similarity). 
METAL   384   384        Zinc; catalytic (By similarity). 
METAL   510   510        Zinc; catalytic (By similarity). 
Sequence information
Length: 635 AA [This is the length of the unprocessed precursor] Molecular weight: 72265 Da [This is the MW of the unprocessed precursor] CRC64: 6AA2BEB8B94C0344 [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MVSIRLPDGS VRQYEHPVTV AEVAASIGPG LAKAALGGKL DGELVDTSAL IDRDASLAIV 

        70         80         90        100        110        120 
TDKDADGLDI IRHSTAHLLA YAVKELHPDA QVTIGPVIDN GFYYDFSYHR PFTPEDLEAI 

       130        140        150        160        170        180 
EKRMQELAKR DEPVTRRVVS RDEAVSYFRS IGEKYKAEII ESIPASDEIK LYSHGSFTDL 

       190        200        210        220        230        240 
CRGPHVPSTG KLKVFKLMKV AGAYWRGDSK NEQLQRIYGT AWTRKEDQDA YLHMLEEAEK 

       250        260        270        280        290        300 
RDHRKLGKQL DLFHIQEEAP GMVFWHPKGW TLWQQVEQYM RRRLDAAGYL EIKTPMIMDR 

       310        320        330        340        350        360 
SLWEASGHWQ NYRENMFTTE SEKRDYAIKP MNCPGHVQVF KHGLRSYRDL PLRYAEFGSC 

       370        380        390        400        410        420 
HRNEASGALH GLMRVRGFVQ DDAHIFCTED QINSEAIAFN KLAMSVYEDF GFDRIDIKLS 

       430        440        450        460        470        480 
LRPEQRMGSD ETWDHAEEGL RNALKACGLE WEELPGEGAF YGPKIEYHIK DALGRSWQCG 

       490        500        510        520        530        540 
TLQLDMMLPE RLGAEYVAED NSRRRPVMLH RAIVGSMERF LGILIEHHAG AMPVWLAPAH 

       550        560        570        580        590        600 
AVVLNIAESQ AEYARTVAQS LQKQGLRVSA DLRNEKISYK IREHTLEKVP YLLVVGDKER 

       610        620        630 
EAQTVAVRAR GGVDLGVMPV EAFVERLRED IQAFK
A1V3R3 in FASTA format

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