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Protein

Proline--tRNA ligase

Gene

proS

Organism
Aquifex aeolicus (strain VF5)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the attachment of proline to tRNA(Pro) in a two-step reaction: proline is first activated by ATP to form Pro-AMP and then transferred to the acceptor end of tRNA(Pro). As ProRS can inadvertently accommodate and process non-cognate amino acids such as alanine and cysteine, to avoid such errors it has two additional distinct editing activities against alanine. One activity is designated as 'pretransfer' editing and involves the tRNA(Pro)-independent hydrolysis of activated Ala-AMP. The other activity is designated 'posttransfer' editing and involves deacylation of mischarged Ala-tRNA(Pro). The misacylated Cys-tRNA(Pro) is not edited by ProRS.

Catalytic activityi

ATP + L-proline + tRNA(Pro) = AMP + diphosphate + L-prolyl-tRNA(Pro).

Kineticsi

  1. KM=0.06 mM for proline (at 60 degrees Celsius)1 Publication
  2. KM=0.05 mM for cysteine (at 60 degrees Celsius)1 Publication

    GO - Molecular functioni

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Aminoacyl-tRNA synthetase, Ligase

    Keywords - Biological processi

    Protein biosynthesis

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciAAEO224324:GJBH-269-MONOMER.
    SABIO-RKO66690.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Proline--tRNA ligase (EC:6.1.1.15)
    Alternative name(s):
    Prolyl-tRNA synthetase
    Short name:
    ProRS
    Gene namesi
    Name:proS
    Ordered Locus Names:aq_365
    OrganismiAquifex aeolicus (strain VF5)
    Taxonomic identifieri224324 [NCBI]
    Taxonomic lineageiBacteriaAquificaeAquificalesAquificaceaeAquifex
    Proteomesi
    • UP000000798 Componenti: Chromosome

    Subcellular locationi

    GO - Cellular componenti

    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 570570Proline--tRNA ligasePRO_0000248226Add
    BLAST

    Proteomic databases

    PRIDEiO66690.

    Interactioni

    Subunit structurei

    Homodimer.By similarity

    Protein-protein interaction databases

    STRINGi224324.aq_365.

    Structurei

    3D structure databases

    ProteinModelPortaliO66690.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domaini

    Consists of three domains: the N-terminal catalytic domain, the editing domain and the C-terminal anticodon-binding domain.By similarity

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiENOG4105C90. Bacteria.
    COG0442. LUCA.
    HOGENOMiHOG000076893.
    InParanoidiO66690.
    KOiK01881.
    OMAiIQPAELW.
    OrthoDBiEOG6TTVMR.

    Family and domain databases

    Gene3Di3.40.50.800. 1 hit.
    3.90.960.10. 1 hit.
    HAMAPiMF_01569. Pro_tRNA_synth_type1.
    InterProiIPR002314. aa-tRNA-synt_IIb.
    IPR006195. aa-tRNA-synth_II.
    IPR004154. Anticodon-bd.
    IPR002316. Pro-tRNA-ligase_IIa.
    IPR004500. Pro-tRNA-synth_IIa_bac-type.
    IPR023717. Pro-tRNA-Synthase_IIa_type1.
    IPR007214. YbaK/aa-tRNA-synth-assoc-dom.
    [Graphical view]
    PANTHERiPTHR11451:SF3. PTHR11451:SF3. 2 hits.
    PfamiPF03129. HGTP_anticodon. 1 hit.
    PF00587. tRNA-synt_2b. 1 hit.
    PF04073. tRNA_edit. 1 hit.
    [Graphical view]
    PRINTSiPR01046. TRNASYNTHPRO.
    SUPFAMiSSF52954. SSF52954. 1 hit.
    SSF55826. SSF55826. 1 hit.
    TIGRFAMsiTIGR00409. proS_fam_II. 1 hit.
    PROSITEiPS50862. AA_TRNA_LIGASE_II. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    O66690-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MRWSRYFLYT EKEEPKEAEA PSHRLLLKAG FIKQVSAGIY ELLPPAYKVL
    60 70 80 90 100
    KKVESIIRKE MDRSGAQELL LTVLNPKELW EETGRWETYG EELFKLKDRN
    110 120 130 140 150
    GREYCLGPTH EEEITDLVRR VVRSYRQLPV ILYQIQVKFR DEKRPRFGLI
    160 170 180 190 200
    RAREFIMKDA YSFDTDDMSA MISYEAMKFA YQRIFNKLRL NVIMAEADVG
    210 220 230 240 250
    QIGGKMSHEF IAFTDYGEAK VAYCENCGYA ANAEIVPLPK PEEEKEEEKP
    260 270 280 290 300
    MEKVHTPNVH TIEELSKFLD VHPSKIMKAV LYIVNEKEPV LVLIRGDREI
    310 320 330 340 350
    DENKLEKVLG TDNFRLATDE EVQELLGTKK GFIGIFNLPE NIKVLWDNSL
    360 370 380 390 400
    YGVKNLVVAL NEPDWHYINV NPGRDFQYGE FVDVAEVREG DPCPKCGSPL
    410 420 430 440 450
    KVRRGLELGH IFLLGTRYSE PMKAYFTDRD GKEKPIIMGC YGIGVSRILA
    460 470 480 490 500
    ALVEQYHDDK GIKWPTPVAP FELDIILLNT KDEEMKNVAE KLYLEAEEKG
    510 520 530 540 550
    IDVIFDDREE SPGFKFADAD LVGFPYRIVV GKKVKEGKVE VQSRHTGEKW
    560 570
    DVEIEKAIDF VKEKIEEDKK
    Length:570
    Mass (Da):65,873
    Last modified:August 1, 1998 - v1
    Checksum:i6B12F0FA016DAE14
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AE000657 Genomic DNA. Translation: AAC06648.1.
    PIRiF70332.
    RefSeqiNP_213250.1. NC_000918.1.
    WP_010880188.1. NC_000918.1.

    Genome annotation databases

    EnsemblBacteriaiAAC06648; AAC06648; aq_365.
    GeneIDi1193016.
    KEGGiaae:aq_365.
    PATRICi20958318. VBIAquAeo85532_0295.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AE000657 Genomic DNA. Translation: AAC06648.1.
    PIRiF70332.
    RefSeqiNP_213250.1. NC_000918.1.
    WP_010880188.1. NC_000918.1.

    3D structure databases

    ProteinModelPortaliO66690.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi224324.aq_365.

    Proteomic databases

    PRIDEiO66690.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAC06648; AAC06648; aq_365.
    GeneIDi1193016.
    KEGGiaae:aq_365.
    PATRICi20958318. VBIAquAeo85532_0295.

    Phylogenomic databases

    eggNOGiENOG4105C90. Bacteria.
    COG0442. LUCA.
    HOGENOMiHOG000076893.
    InParanoidiO66690.
    KOiK01881.
    OMAiIQPAELW.
    OrthoDBiEOG6TTVMR.

    Enzyme and pathway databases

    BioCyciAAEO224324:GJBH-269-MONOMER.
    SABIO-RKO66690.

    Family and domain databases

    Gene3Di3.40.50.800. 1 hit.
    3.90.960.10. 1 hit.
    HAMAPiMF_01569. Pro_tRNA_synth_type1.
    InterProiIPR002314. aa-tRNA-synt_IIb.
    IPR006195. aa-tRNA-synth_II.
    IPR004154. Anticodon-bd.
    IPR002316. Pro-tRNA-ligase_IIa.
    IPR004500. Pro-tRNA-synth_IIa_bac-type.
    IPR023717. Pro-tRNA-Synthase_IIa_type1.
    IPR007214. YbaK/aa-tRNA-synth-assoc-dom.
    [Graphical view]
    PANTHERiPTHR11451:SF3. PTHR11451:SF3. 2 hits.
    PfamiPF03129. HGTP_anticodon. 1 hit.
    PF00587. tRNA-synt_2b. 1 hit.
    PF04073. tRNA_edit. 1 hit.
    [Graphical view]
    PRINTSiPR01046. TRNASYNTHPRO.
    SUPFAMiSSF52954. SSF52954. 1 hit.
    SSF55826. SSF55826. 1 hit.
    TIGRFAMsiTIGR00409. proS_fam_II. 1 hit.
    PROSITEiPS50862. AA_TRNA_LIGASE_II. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: VF5.
    2. "Cysteine activation is an inherent in vitro property of prolyl-tRNA synthetases."
      Ahel I., Stathopoulos C., Ambrogelly A., Sauerwald A., Toogood H., Hartsch T., Soell D.
      J. Biol. Chem. 277:34743-34748(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROLINE AND CYSTEINE ACTIVATION, POSTTRANSFER EDITING ACTIVITY, KINETIC PARAMETERS.

    Entry informationi

    Entry nameiSYP_AQUAE
    AccessioniPrimary (citable) accession number: O66690
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 5, 2006
    Last sequence update: August 1, 1998
    Last modified: June 8, 2016
    This is version 102 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

    Complete proteome, Reference proteome

    Documents

    1. Aminoacyl-tRNA synthetases
      List of aminoacyl-tRNA synthetase entries
    2. SIMILARITY comments
      Index of protein domains and families

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.