Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Proline--tRNA ligase

Gene

proS

Organism
Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440) (Methanococcus jannaschii)
Status
Reviewed-Annotation score: -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). Can inadvertently accommodate and process non-cognate amino acids such as cysteine and alanine.4 Publications

Caution

Was originally (PubMed:10642548, PubMed:10869184 and PubMed:11141055) thought to have both prolyl- and cysteinyl-tRNA synthetase activities (ProCysRS). However, recent biochemical and structural studies show that ProRS misaminoacylates tRNA(Pro) with cysteine but is unable to aminoacylate tRNA(Cys). These conflicting results may be due to the fact that much of the previous work was done with unfractionated tRNA.Curated
According to PubMed:12130658, ProRS is unable to edit the misacylated Cys-tRNA(Pro) and Ala-tRNA(Pro), whereas according to PubMed:11408489, it hydrolyzes Ala-AMP and Ala-tRNA(Pro) by 'pretransfer' and 'posttransfer' editing activities, respectively.Curated

Catalytic activityi

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

Enzyme regulationi

Inhibited by high concentrations of prolinamide.

Kineticsi

  1. KM=0.28 mM for proline (at 60 degrees Celsius)3 Publications
  2. KM=0.09 mM for cysteine (at 60 degrees Celsius)3 Publications

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Binding sitei101ProlineBy similarity1
    Binding sitei103ProlineBy similarity1
    Binding sitei132ATPBy similarity1
    Binding sitei132ProlineBy similarity1
    Binding sitei134ATPBy similarity1
    Binding sitei216ATPBy similarity1
    Binding sitei219ATPBy similarity1
    Binding sitei221ProlineBy similarity1
    Binding sitei253ATPBy similarity1
    Binding sitei255ATPBy similarity1

    GO - Molecular functioni

    GO - Biological processi

    Keywordsi

    Molecular functionAminoacyl-tRNA synthetase, Ligase
    Biological processProtein biosynthesis
    LigandATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciMJAN243232:G1GKE-1343-MONOMER
    BRENDAi6.1.1.15 3260
    SABIO-RKiQ58635

    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:MJ1238
    OrganismiMethanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440) (Methanococcus jannaschii)
    Taxonomic identifieri243232 [NCBI]
    Taxonomic lineageiArchaeaEuryarchaeotaMethanococciMethanococcalesMethanocaldococcaceaeMethanocaldococcus
    Proteomesi
    • UP000000805 Componenti: Chromosome

    Subcellular locationi

    GO - Cellular componenti

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00001393511 – 455Proline--tRNA ligaseAdd BLAST455

    Proteomic databases

    PRIDEiQ58635

    Interactioni

    Subunit structurei

    Homodimer. The dimer is functionally asymmetric: only one of the two active sites at a time is able to form prolyl-adenylate, and only one tRNA molecule binds per dimer.2 Publications

    Protein-protein interaction databases

    STRINGi243232.MJ_1238

    Structurei

    Secondary structure

    1455
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Helixi3 – 13Combined sources11
    Helixi31 – 50Combined sources20
    Beta strandi60 – 63Combined sources4
    Helixi64 – 70Combined sources7
    Beta strandi72 – 74Combined sources3
    Helixi75 – 80Combined sources6
    Beta strandi82 – 98Combined sources17
    Beta strandi100 – 102Combined sources3
    Helixi103 – 111Combined sources9
    Beta strandi124 – 128Combined sources5
    Turni140 – 142Combined sources3
    Beta strandi150 – 159Combined sources10
    Helixi160 – 181Combined sources22
    Beta strandi186 – 190Combined sources5
    Beta strandi200 – 208Combined sources9
    Beta strandi214 – 224Combined sources11
    Helixi226 – 230Combined sources5
    Beta strandi234 – 236Combined sources3
    Beta strandi240 – 244Combined sources5
    Beta strandi246 – 252Combined sources7
    Helixi255 – 264Combined sources10
    Beta strandi278 – 285Combined sources8
    Helixi292 – 307Combined sources16
    Beta strandi312 – 314Combined sources3
    Helixi321 – 330Combined sources10
    Beta strandi334 – 339Combined sources6
    Helixi341 – 345Combined sources5
    Beta strandi348 – 353Combined sources6
    Turni354 – 356Combined sources3
    Beta strandi359 – 363Combined sources5
    Helixi367 – 393Combined sources27
    Beta strandi394 – 396Combined sources3
    Helixi402 – 408Combined sources7
    Turni409 – 412Combined sources4
    Beta strandi414 – 419Combined sources6
    Helixi422 – 424Combined sources3
    Helixi427 – 433Combined sources7
    Beta strandi437 – 442Combined sources6
    Beta strandi444 – 452Combined sources9

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1NJ8X-ray3.20A/B/C/D2-455[»]
    ProteinModelPortaliQ58635
    SMRiQ58635
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ58635

    Family & Domainsi

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni329 – 359Interaction with tRNABy similarityAdd BLAST31

    Domaini

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

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiarCOG00402 Archaea
    COG0442 LUCA
    InParanoidiQ58635
    KOiK01881
    OMAiEVYWVTH
    OrthoDBiPOG093Z01RZ
    PhylomeDBiQ58635

    Family and domain databases

    CDDicd00778 ProRS_core_arch_euk, 1 hit
    Gene3Di3.30.110.30, 1 hit
    3.40.50.800, 1 hit
    HAMAPiMF_01571 Pro_tRNA_synth_type3, 1 hit
    InterProiView protein in InterPro
    IPR002314 aa-tRNA-synt_IIb
    IPR006195 aa-tRNA-synth_II
    IPR004154 Anticodon-bd
    IPR036621 Anticodon-bd_dom_sf
    IPR002316 Pro-tRNA-ligase_IIa
    IPR004499 Pro-tRNA-ligase_IIa_arc-type
    IPR017449 Pro-tRNA_synth_II
    IPR015264 Pro-tRNA_synth_II_arc
    IPR033721 ProRS_core_arch_euk
    PfamiView protein in Pfam
    PF03129 HGTP_anticodon, 1 hit
    PF09181 ProRS-C_2, 1 hit
    PF00587 tRNA-synt_2b, 1 hit
    PRINTSiPR01046 TRNASYNTHPRO
    SUPFAMiSSF64586 SSF64586, 1 hit
    TIGRFAMsiTIGR00408 proS_fam_I, 1 hit
    PROSITEiView protein in PROSITE
    PS50862 AA_TRNA_LIGASE_II, 1 hit

    Sequencei

    Sequence statusi: Complete.

    Q58635-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MEFSEWYSDI LEKAEIYDVR YPIKGCGVYL PYGFKIRRYT FEIIRNLLDE
    60 70 80 90 100
    SGHDEALFPM LIPEDLLAKE AEHIKGFEDE VYWVTHGGKT QLDVKLALRP
    110 120 130 140 150
    TSETPIYYMM KLWVKVHTDL PIKIYQIVNT FRYETKHTRP LIRLREIMTF
    160 170 180 190 200
    KEAHTAHSTK EEAENQVKEA ISIYKKFFDT LGIPYLISKR PEWDKFPGAE
    210 220 230 240 250
    YTMAFDTIFP DGRTMQIATV HNLGQNFSKT FEIIFETPTG DKDYAYQTCY
    260 270 280 290 300
    GISDRVIASI IAIHGDEKGL ILPPIVAPIQ VVIVPLIFKG KEDIVMEKAK
    310 320 330 340 350
    EIYEKLKGKF RVHIDDRDIR PGRKFNDWEI KGVPLRIEVG PKDIENKKIT
    360 370 380 390 400
    LFRRDTMEKF QVDETQLMEV VEKTLNNIME NIKNRAWEKF ENFITILEDI
    410 420 430 440 450
    NPDEIKNILS EKRGVILVPF KEEIYNEELE EKVEATILGE TEYKGNKYIA

    IAKTY
    Length:455
    Mass (Da):53,309
    Last modified:November 1, 1996 - v1
    Checksum:i3D155A36AFE0CC3B
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    L77117 Genomic DNA Translation: AAB99242.1
    PIRiE64454
    RefSeqiWP_010870750.1, NC_000909.1

    Genome annotation databases

    EnsemblBacteriaiAAB99242; AAB99242; MJ_1238
    GeneIDi1452134
    KEGGimja:MJ_1238

    Similar proteinsi

    Entry informationi

    Entry nameiSYP_METJA
    AccessioniPrimary (citable) accession number: Q58635
    Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: November 1, 1996
    Last modified: May 23, 2018
    This is version 128 of the entry and version 1 of the sequence. See complete history.
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

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

    Cookie policy

    We would like to use anonymized google analytics cookies to gather statistics on how uniprot.org is used in aggregate. Learn more

    UniProt is an ELIXIR core data resource
    Main funding by: National Institutes of Health