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Q5SM45

- SYR_THET8

UniProt

Q5SM45 - SYR_THET8

Protein

Arginine--tRNA ligase

Gene

argS

Organism
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Status
Reviewed - Annotation score: 2 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 67 (01 Oct 2014)
      Sequence version 1 (21 Dec 2004)
      Previous versions | rss
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    Functioni

    Catalytic activityi

    ATP + L-arginine + tRNA(Arg) = AMP + diphosphate + L-arginyl-tRNA(Arg).UniRule annotation

    GO - Molecular functioni

    1. arginine-tRNA ligase activity Source: UniProtKB-HAMAP
    2. ATP binding Source: UniProtKB-HAMAP

    GO - Biological processi

    1. arginyl-tRNA aminoacylation Source: UniProtKB-HAMAP

    Keywords - Molecular functioni

    Aminoacyl-tRNA synthetase, Ligase

    Keywords - Biological processi

    Protein biosynthesis

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciTTHE300852:GH8R-102-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Arginine--tRNA ligaseUniRule annotation (EC:6.1.1.19UniRule annotation)
    Alternative name(s):
    Arginyl-tRNA synthetaseUniRule annotation
    Short name:
    ArgRSUniRule annotation
    Gene namesi
    Name:argSUniRule annotation
    Ordered Locus Names:TTHA0098
    OrganismiThermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
    Taxonomic identifieri300852 [NCBI]
    Taxonomic lineageiBacteriaDeinococcus-ThermusDeinococciThermalesThermaceaeThermus
    ProteomesiUP000000532: Chromosome

    Subcellular locationi

    Cytoplasm UniRule annotation

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 592592Arginine--tRNA ligasePRO_0000242112Add
    BLAST

    Interactioni

    Subunit structurei

    Monomer.UniRule annotation

    Protein-protein interaction databases

    STRINGi300852.TTHA0098.

    Structurei

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1IQ0X-ray2.30A1-592[»]
    1IR4model-A1-592[»]
    ProteinModelPortaliQ5SM45.
    SMRiQ5SM45. Positions 1-592.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ5SM45.

    Family & Domainsi

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi112 – 12211"HIGH" regionAdd
    BLAST

    Sequence similaritiesi

    Belongs to the class-I aminoacyl-tRNA synthetase family.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG0018.
    HOGENOMiHOG000247213.
    KOiK01887.
    OMAiNFERNSA.
    OrthoDBiEOG6JB13C.
    PhylomeDBiQ5SM45.

    Family and domain databases

    Gene3Di1.10.730.10. 1 hit.
    3.30.1360.70. 1 hit.
    3.40.50.620. 1 hit.
    HAMAPiMF_00123. Arg_tRNA_synth.
    InterProiIPR001412. aa-tRNA-synth_I_CS.
    IPR001278. Arg-tRNA-ligase.
    IPR005148. Arg-tRNA-synth_N.
    IPR008909. DALR_anticod-bd.
    IPR014729. Rossmann-like_a/b/a_fold.
    IPR009080. tRNAsynth_1a_anticodon-bd.
    [Graphical view]
    PANTHERiPTHR11956. PTHR11956. 1 hit.
    PfamiPF03485. Arg_tRNA_synt_N. 1 hit.
    PF05746. DALR_1. 1 hit.
    PF00750. tRNA-synt_1d. 2 hits.
    [Graphical view]
    PRINTSiPR01038. TRNASYNTHARG.
    SMARTiSM01016. Arg_tRNA_synt_N. 1 hit.
    SM00836. DALR_1. 1 hit.
    [Graphical view]
    SUPFAMiSSF47323. SSF47323. 1 hit.
    SSF55190. SSF55190. 1 hit.
    PROSITEiPS00178. AA_TRNA_LIGASE_I. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q5SM45-1 [UniParc]FASTAAdd to Basket

    « Hide

    MLRRALEEAI AQALKEMGVP VRLKVARAPK DKPGDYGVPL FALAKELRKP    50
    PQAIAQELKD RLPLPEFVEE AVPVGGYLNF RLRTEALLRE ALRPKAPFPR 100
    RPGVVLVEHT SVNPNKELHV GHLRNIALGD AIARILAYAG REVLVLNYID 150
    DTGRQAAETL FALRHYGLTW DGKEKYDHFA GRAYVRLHQD PEYERLQPAI 200
    EEVLHALERG ELREEVNRIL LAQMATMHAL NARYDLLVWE SDIVRAGLLQ 250
    KALALLEQSP HVFRPREGKY AGALVMDASP VIPGLEDPFF VLLRSNGTAT 300
    YYAKDIAFQF WKMGILEGLR FRPYENPYYP GLRTSAPEGE AYTPKAEETI 350
    NVVDVRQSHP QALVRAALAL AGYPALAEKA HHLAYETVLL EGRQMSGRKG 400
    LAVSVDEVLE EATRRARAIV EEKNPDHPDK EEAARMVALG AIRFSMVKTE 450
    PKKQIDFRYQ EALSFEGDTG PYVQYAHARA HSILRKAGEW GAPDLSQATP 500
    YERALALDLL DFEEAVLEAA EERTPHVLAQ YLLDLAASWN AYYNARENGQ 550
    PATPVLTAPE GLRELRLSLV QSLQRTLATG LDLLGIPAPE VM 592
    Length:592
    Mass (Da):66,227
    Last modified:December 21, 2004 - v1
    Checksum:iBA300E5F28F672E6
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AP008226 Genomic DNA. Translation: BAD69921.1.
    RefSeqiYP_143364.1. NC_006461.1.

    Genome annotation databases

    EnsemblBacteriaiBAD69921; BAD69921; BAD69921.
    GeneIDi3169614.
    KEGGittj:TTHA0098.
    PATRICi23955127. VBITheThe93045_0096.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AP008226 Genomic DNA. Translation: BAD69921.1 .
    RefSeqi YP_143364.1. NC_006461.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1IQ0 X-ray 2.30 A 1-592 [» ]
    1IR4 model - A 1-592 [» ]
    ProteinModelPortali Q5SM45.
    SMRi Q5SM45. Positions 1-592.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 300852.TTHA0098.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai BAD69921 ; BAD69921 ; BAD69921 .
    GeneIDi 3169614.
    KEGGi ttj:TTHA0098.
    PATRICi 23955127. VBITheThe93045_0096.

    Phylogenomic databases

    eggNOGi COG0018.
    HOGENOMi HOG000247213.
    KOi K01887.
    OMAi NFERNSA.
    OrthoDBi EOG6JB13C.
    PhylomeDBi Q5SM45.

    Enzyme and pathway databases

    BioCyci TTHE300852:GH8R-102-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei Q5SM45.

    Family and domain databases

    Gene3Di 1.10.730.10. 1 hit.
    3.30.1360.70. 1 hit.
    3.40.50.620. 1 hit.
    HAMAPi MF_00123. Arg_tRNA_synth.
    InterProi IPR001412. aa-tRNA-synth_I_CS.
    IPR001278. Arg-tRNA-ligase.
    IPR005148. Arg-tRNA-synth_N.
    IPR008909. DALR_anticod-bd.
    IPR014729. Rossmann-like_a/b/a_fold.
    IPR009080. tRNAsynth_1a_anticodon-bd.
    [Graphical view ]
    PANTHERi PTHR11956. PTHR11956. 1 hit.
    Pfami PF03485. Arg_tRNA_synt_N. 1 hit.
    PF05746. DALR_1. 1 hit.
    PF00750. tRNA-synt_1d. 2 hits.
    [Graphical view ]
    PRINTSi PR01038. TRNASYNTHARG.
    SMARTi SM01016. Arg_tRNA_synt_N. 1 hit.
    SM00836. DALR_1. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47323. SSF47323. 1 hit.
    SSF55190. SSF55190. 1 hit.
    PROSITEi PS00178. AA_TRNA_LIGASE_I. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "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].
      Strain: HB8 / ATCC 27634 / DSM 579.

    Entry informationi

    Entry nameiSYR_THET8
    AccessioniPrimary (citable) accession number: Q5SM45
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 27, 2006
    Last sequence update: December 21, 2004
    Last modified: October 1, 2014
    This is version 67 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Aminoacyl-tRNA synthetases
      List of aminoacyl-tRNA synthetase entries
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3