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Protein

Proline--tRNA ligase

Gene

proS

Organism
Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H) (Methanobacterium thermoautotrophicum)
Status
Reviewed-Annotation score: Annotation score: 4 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). Can inadvertently accommodate and process cysteine.1 Publication

Catalytic activityi

ATP + L-proline + tRNA(Pro) = AMP + diphosphate + L-prolyl-tRNA(Pro).UniRule annotation1 Publication

Kineticsi

  1. KM=0.26 mM for proline (at 60 degrees Celsius)2 Publications
  2. KM=0.05 mM for cysteine (at 60 degrees Celsius)2 Publications
  3. KM=4.1 µM for tRNA(Pro) (at 50 degrees Celsius)2 Publications
  4. KM=2.2 µM for tRNA(Pro) (at 50 degrees Celsius in the presence of LeuRS)2 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei117 – 1171Proline1 Publication
    Binding sitei119 – 1191Proline1 Publication
    Binding sitei148 – 1481ATP1 Publication
    Binding sitei148 – 1481Proline1 Publication
    Binding sitei150 – 1501ATP1 Publication
    Binding sitei232 – 2321ATP1 Publication
    Binding sitei235 – 2351ATP1 Publication
    Binding sitei237 – 2371Proline1 Publication
    Binding sitei269 – 2691ATP1 Publication
    Metal bindingi436 – 4361Zinc; structural1 Publication
    Metal bindingi441 – 4411Zinc; structural1 Publication
    Metal bindingi464 – 4641Zinc; structural1 Publication
    Metal bindingi467 – 4671Zinc; structural1 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, Metal-binding, Nucleotide-binding, Zinc

    Enzyme and pathway databases

    BioCyciMTHE187420:GJNM-611-MONOMER.
    SABIO-RKO26708.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Proline--tRNA ligaseUniRule annotationCurated (EC:6.1.1.15UniRule annotation1 Publication)
    Alternative name(s):
    Prolyl-tRNA synthetase1 PublicationUniRule annotation
    Short name:
    ProRS1 PublicationUniRule annotation
    Gene namesi
    Name:proS
    Ordered Locus Names:MTH_611
    OrganismiMethanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H) (Methanobacterium thermoautotrophicum)
    Taxonomic identifieri187420 [NCBI]
    Taxonomic lineageiArchaeaEuryarchaeotaMethanobacteriaMethanobacterialesMethanobacteriaceaeMethanothermobacter
    Proteomesi
    • UP000005223 Componenti: Chromosome

    Subcellular locationi

    • Cytoplasm UniRule annotation

    GO - Cellular componenti

    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 482482Proline--tRNA ligasePRO_0000139352Add
    BLAST

    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. Interacts with LeuRS, which enhances tRNA(Pro) aminoacylation.3 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    leuSO275523EBI-7963357,EBI-7963108

    Protein-protein interaction databases

    IntActiO26708. 1 interaction.
    MINTiMINT-6664518.
    STRINGi187420.MTH611.

    Structurei

    Secondary structure

    1
    482
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi20 – 3011Combined sources
    Beta strandi33 – 353Combined sources
    Helixi48 – 6518Combined sources
    Turni66 – 683Combined sources
    Beta strandi76 – 794Combined sources
    Helixi80 – 834Combined sources
    Helixi87 – 926Combined sources
    Turni93 – 964Combined sources
    Beta strandi99 – 1035Combined sources
    Beta strandi106 – 1149Combined sources
    Beta strandi116 – 1183Combined sources
    Helixi119 – 12911Combined sources
    Turni133 – 1353Combined sources
    Beta strandi138 – 14710Combined sources
    Turni156 – 1583Combined sources
    Beta strandi161 – 17515Combined sources
    Helixi176 – 19621Combined sources
    Beta strandi202 – 2054Combined sources
    Turni208 – 2103Combined sources
    Beta strandi216 – 2249Combined sources
    Beta strandi230 – 24011Combined sources
    Helixi242 – 2476Combined sources
    Beta strandi250 – 2523Combined sources
    Beta strandi254 – 2563Combined sources
    Beta strandi258 – 2603Combined sources
    Beta strandi262 – 2687Combined sources
    Helixi271 – 2799Combined sources
    Beta strandi283 – 2875Combined sources
    Turni290 – 2923Combined sources
    Beta strandi296 – 3016Combined sources
    Beta strandi304 – 3074Combined sources
    Helixi308 – 32316Combined sources
    Turni324 – 3263Combined sources
    Beta strandi329 – 3313Combined sources
    Helixi338 – 34710Combined sources
    Beta strandi351 – 3566Combined sources
    Helixi358 – 3614Combined sources
    Turni362 – 3643Combined sources
    Beta strandi365 – 3739Combined sources
    Beta strandi376 – 3805Combined sources
    Turni381 – 3833Combined sources
    Helixi384 – 40825Combined sources
    Beta strandi411 – 4133Combined sources
    Helixi417 – 42711Combined sources
    Beta strandi429 – 4357Combined sources
    Helixi439 – 44911Combined sources
    Beta strandi452 – 4587Combined sources
    Turni465 – 4673Combined sources
    Beta strandi473 – 4786Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1NJ1X-ray2.55A1-481[»]
    1NJ2X-ray3.11A1-481[»]
    1NJ5X-ray2.80A1-481[»]
    1NJ6X-ray2.85A1-481[»]
    ProteinModelPortaliO26708.
    SMRiO26708. Positions 19-472.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO26708.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni346 – 37631Interaction with tRNABy similarityAdd
    BLAST

    Domaini

    Consists of three domains: the N-terminal catalytic domain, the anticodon-binding domain and the C-terminal extension. The C-terminal extension binds a zinc ion, which probably plays a non-essential structural role in stabilizing the fold of C-terminal domain.

    Sequence similaritiesi

    Belongs to the class-II aminoacyl-tRNA synthetase family. ProS type 3 subfamily.UniRule annotationCurated

    Phylogenomic databases

    eggNOGiarCOG00402. Archaea.
    COG0442. LUCA.
    KOiK01881.
    OMAiVYWGKAY.

    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.
    InterProiIPR002314. aa-tRNA-synt_IIb.
    IPR006195. aa-tRNA-synth_II.
    IPR004154. Anticodon-bd.
    IPR002316. Pro-tRNA-ligase_IIa.
    IPR004499. Pro-tRNA-ligase_IIa_arc-type.
    IPR016061. Pro-tRNA_ligase_II_C.
    IPR017449. Pro-tRNA_synth_II.
    IPR033721. ProRS_core_arch_euk.
    [Graphical view]
    PANTHERiPTHR11451:SF6. PTHR11451:SF6. 1 hit.
    PfamiPF03129. HGTP_anticodon. 1 hit.
    PF09180. ProRS-C_1. 1 hit.
    PF00587. tRNA-synt_2b. 1 hit.
    [Graphical view]
    PRINTSiPR01046. TRNASYNTHPRO.
    SMARTiSM00946. ProRS-C_1. 1 hit.
    [Graphical view]
    SUPFAMiSSF52954. SSF52954. 1 hit.
    SSF64586. SSF64586. 1 hit.
    TIGRFAMsiTIGR00408. proS_fam_I. 1 hit.
    PROSITEiPS50862. AA_TRNA_LIGASE_II. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    O26708-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MQKPIKKDPN RYHGEKMTEF SEWFHNILEE AEIIDQRYPV KGMHVWMPHG
    60 70 80 90 100
    FMIRKNTLKI LRRILDRDHE EVLFPLLVPE DELAKEAIHV KGFEDEVYWV
    110 120 130 140 150
    THGGLSKLQR KLALRPTSET VMYPMFALWV RSHTDLPMRF YQVVNTFRYE
    160 170 180 190 200
    TKHTRPLIRV REITTFKEAH TIHATASEAE EQVERAVEIY KEFFNSLGIP
    210 220 230 240 250
    YLITRRPPWD KFPGSEYTVA FDTLMPDGKT LQIGTVHNLG QTFARTFEIK
    260 270 280 290 300
    FETPEGDHEY VHQTCYGLSD RVIASVIAIH GDESGLCLPP DVAAHQVVIV
    310 320 330 340 350
    PIIFKKAAEE VMEACRELRS RLEAAGFRVH LDDRDIRAGR KYYEWEMRGV
    360 370 380 390 400
    PLRVEIGPRD LEKGAAVISR RDTGEKVTAD LQGIEETLRE LMKDILENLR
    410 420 430 440 450
    TRAWERMESE IREAETLEEA SRIVDEKRGI ISFMWCGEEE CGMDVEEKVR
    460 470 480
    VDILGIQEEG SGTCINCGRE APTGLTLPEH IS
    Length:482
    Mass (Da):55,806
    Last modified:January 1, 1998 - v1
    Checksum:i57D81ED7E9496BAA
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AE000666 Genomic DNA. Translation: AAB85117.1.
    PIRiC69181.

    Genome annotation databases

    EnsemblBacteriaiAAB85117; AAB85117; MTH_611.
    KEGGimth:MTH_611.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AE000666 Genomic DNA. Translation: AAB85117.1.
    PIRiC69181.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1NJ1X-ray2.55A1-481[»]
    1NJ2X-ray3.11A1-481[»]
    1NJ5X-ray2.80A1-481[»]
    1NJ6X-ray2.85A1-481[»]
    ProteinModelPortaliO26708.
    SMRiO26708. Positions 19-472.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    IntActiO26708. 1 interaction.
    MINTiMINT-6664518.
    STRINGi187420.MTH611.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAB85117; AAB85117; MTH_611.
    KEGGimth:MTH_611.

    Phylogenomic databases

    eggNOGiarCOG00402. Archaea.
    COG0442. LUCA.
    KOiK01881.
    OMAiVYWGKAY.

    Enzyme and pathway databases

    BioCyciMTHE187420:GJNM-611-MONOMER.
    SABIO-RKO26708.

    Miscellaneous databases

    EvolutionaryTraceiO26708.

    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.
    InterProiIPR002314. aa-tRNA-synt_IIb.
    IPR006195. aa-tRNA-synth_II.
    IPR004154. Anticodon-bd.
    IPR002316. Pro-tRNA-ligase_IIa.
    IPR004499. Pro-tRNA-ligase_IIa_arc-type.
    IPR016061. Pro-tRNA_ligase_II_C.
    IPR017449. Pro-tRNA_synth_II.
    IPR033721. ProRS_core_arch_euk.
    [Graphical view]
    PANTHERiPTHR11451:SF6. PTHR11451:SF6. 1 hit.
    PfamiPF03129. HGTP_anticodon. 1 hit.
    PF09180. ProRS-C_1. 1 hit.
    PF00587. tRNA-synt_2b. 1 hit.
    [Graphical view]
    PRINTSiPR01046. TRNASYNTHPRO.
    SMARTiSM00946. ProRS-C_1. 1 hit.
    [Graphical view]
    SUPFAMiSSF52954. SSF52954. 1 hit.
    SSF64586. SSF64586. 1 hit.
    TIGRFAMsiTIGR00408. proS_fam_I. 1 hit.
    PROSITEiPS50862. AA_TRNA_LIGASE_II. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Entry informationi

    Entry nameiSYP_METTH
    AccessioniPrimary (citable) accession number: O26708
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 15, 1998
    Last sequence update: January 1, 1998
    Last modified: September 7, 2016
    This is version 126 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

    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.