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Protein

Proline--tRNA ligase

Gene

proS

Organism
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Status
Reviewed-Annotation score: Annotation score: 5 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.2 Publications

Catalytic activityi

ATP + L-proline + tRNA(Pro) = AMP + diphosphate + L-prolyl-tRNA(Pro).UniRule annotation2 Publications

Kineticsi

  1. KM=0.15 mM for proline (at 60 degrees Celsius)1 Publication
  2. KM=0.02 mM for cysteine (at 60 degrees Celsius)1 Publication

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Binding sitei111Proline1 Publication1
    Binding sitei113Proline1 Publication1
    Binding sitei142ATP1 Publication1
    Binding sitei142Proline1 Publication1
    Binding sitei153ATP1 Publication1
    Binding sitei225ATP1 Publication1
    Binding sitei228ATP1 Publication1
    Binding sitei230Proline1 Publication1
    Binding sitei262ATP1 Publication1
    Binding sitei264ATP1 Publication1
    Metal bindingi427Zinc; structural2 Publications1
    Metal bindingi432Zinc; structural2 Publications1
    Metal bindingi458Zinc; structural2 Publications1
    Metal bindingi461Zinc; structural2 Publications1

    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

    BRENDAi6.1.1.15. 2305.
    SABIO-RKQ5SM28.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Proline--tRNA ligaseUniRule annotationCurated (EC:6.1.1.15UniRule annotation2 Publications)
    Alternative name(s):
    Prolyl-tRNA synthetase1 PublicationUniRule annotation
    Short name:
    ProRS1 PublicationUniRule annotation
    Gene namesi
    Name:proS
    Ordered Locus Names:TTHA0115
    OrganismiThermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
    Taxonomic identifieri300852 [NCBI]
    Taxonomic lineageiBacteriaDeinococcus-ThermusDeinococciThermalesThermaceaeThermus
    Proteomesi
    • UP000000532 Componenti: Chromosome

    Subcellular locationi

    • Cytoplasm UniRule annotation

    GO - Cellular componenti

    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Mutagenesisi477Y → A: Slightly reduces the aminoacylation activity. 1 Publication1
    Mutagenesisi477Y → F: Little change in the aminoacylation activity. 1 Publication1

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00002482291 – 477Proline--tRNA ligaseAdd BLAST477

    Interactioni

    Subunit structurei

    Homodimer. Only one tRNA molecule binds per dimer.2 Publications

    Protein-protein interaction databases

    STRINGi300852.TTHA0115.

    Structurei

    Secondary structure

    1477
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Helixi10 – 24Combined sources15
    Beta strandi27 – 30Combined sources4
    Beta strandi37 – 39Combined sources3
    Helixi41 – 60Combined sources20
    Beta strandi70 – 74Combined sources5
    Helixi81 – 87Combined sources7
    Helixi88 – 90Combined sources3
    Beta strandi92 – 108Combined sources17
    Helixi113 – 123Combined sources11
    Helixi127 – 129Combined sources3
    Beta strandi132 – 141Combined sources10
    Turni149 – 151Combined sources3
    Beta strandi154 – 167Combined sources14
    Helixi168 – 190Combined sources23
    Beta strandi195 – 198Combined sources4
    Turni201 – 203Combined sources3
    Beta strandi208 – 217Combined sources10
    Beta strandi223 – 233Combined sources11
    Helixi235 – 239Combined sources5
    Beta strandi243 – 245Combined sources3
    Beta strandi251 – 253Combined sources3
    Beta strandi255 – 262Combined sources8
    Helixi264 – 273Combined sources10
    Beta strandi278 – 280Combined sources3
    Turni283 – 285Combined sources3
    Beta strandi289 – 294Combined sources6
    Turni298 – 300Combined sources3
    Helixi301 – 317Combined sources17
    Beta strandi322 – 324Combined sources3
    Beta strandi328 – 330Combined sources3
    Helixi332 – 341Combined sources10
    Beta strandi345 – 350Combined sources6
    Helixi352 – 356Combined sources5
    Beta strandi359 – 364Combined sources6
    Turni365 – 367Combined sources3
    Beta strandi371 – 373Combined sources3
    Helixi374 – 376Combined sources3
    Helixi377 – 402Combined sources26
    Beta strandi404 – 406Combined sources3
    Helixi410 – 416Combined sources7
    Turni417 – 419Combined sources3
    Beta strandi420 – 424Combined sources5
    Helixi430 – 440Combined sources11
    Beta strandi443 – 451Combined sources9
    Turni459 – 461Combined sources3
    Beta strandi471 – 474Combined sources4

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1H4QX-ray3.00A/B1-477[»]
    1H4SX-ray2.85A/B1-477[»]
    1H4TX-ray2.90A/B/C/D1-477[»]
    1HC7X-ray2.43A/B/C/D1-477[»]
    ProteinModelPortaliQ5SM28.
    SMRiQ5SM28.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ5SM28.

    Family & Domainsi

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni340 – 369Interaction with tRNAAdd BLAST30

    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

    eggNOGiENOG4107R1M. Bacteria.
    COG0442. LUCA.
    HOGENOMiHOG000167538.
    KOiK01881.
    OMAiVYWGKAY.
    PhylomeDBiQ5SM28.

    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.

    Q5SM28-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MAKEKGLTPQ SQDFSEWYLE VIQKAELADY GPVRGTIVVR PYGYAIWENI
    60 70 80 90 100
    QQVLDRMFKE TGHQNAYFPL FIPMSFLRKE AEHVEGFSPE LAVVTHAGGE
    110 120 130 140 150
    ELEEPLAVRP TSETVIGYMW SKWIRSWRDL PQLLNQWGNV VRWEMRTRPF
    160 170 180 190 200
    LRTSEFLWQE GHTAHATREE AEEEVRRMLS IYARLAREYA AIPVIEGLKT
    210 220 230 240 250
    EKEKFAGAVY TTTIEALMKD GKALQAGTSH YLGENFARAF DIKFQDRDLQ
    260 270 280 290 300
    VKYVHTTSWG LSWRFIGAII MTHGDDRGLV LPPRLAPIQV VIVPIYKDES
    310 320 330 340 350
    RERVLEAAQG LRQALLAQGL RVHLDDRDQH TPGYKFHEWE LKGVPFRVEL
    360 370 380 390 400
    GPKDLEGGQA VLASRLGGKE TLPLAALPEA LPGKLDAFHE ELYRRALAFR
    410 420 430 440 450
    EDHTRKVDTY EAFKEAVQEG FALAFHCGDK ACERLIQEET TATTRCVPFE
    460 470
    AEPEEGFCVR CGRPSAYGKR VVFAKAY
    Length:477
    Mass (Da):54,488
    Last modified:December 21, 2004 - v1
    Checksum:i6AA477F1EC4D12F5
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AF384553 Genomic DNA. Translation: AAK62359.1.
    AP008226 Genomic DNA. Translation: BAD69938.1.
    RefSeqiWP_011227720.1. NC_006461.1.
    YP_143381.1. NC_006461.1.

    Genome annotation databases

    EnsemblBacteriaiBAD69938; BAD69938; BAD69938.
    GeneIDi3169620.
    KEGGittj:TTHA0115.
    PATRICi23955165. VBITheThe93045_0113.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AF384553 Genomic DNA. Translation: AAK62359.1.
    AP008226 Genomic DNA. Translation: BAD69938.1.
    RefSeqiWP_011227720.1. NC_006461.1.
    YP_143381.1. NC_006461.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1H4QX-ray3.00A/B1-477[»]
    1H4SX-ray2.85A/B1-477[»]
    1H4TX-ray2.90A/B/C/D1-477[»]
    1HC7X-ray2.43A/B/C/D1-477[»]
    ProteinModelPortaliQ5SM28.
    SMRiQ5SM28.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi300852.TTHA0115.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiBAD69938; BAD69938; BAD69938.
    GeneIDi3169620.
    KEGGittj:TTHA0115.
    PATRICi23955165. VBITheThe93045_0113.

    Phylogenomic databases

    eggNOGiENOG4107R1M. Bacteria.
    COG0442. LUCA.
    HOGENOMiHOG000167538.
    KOiK01881.
    OMAiVYWGKAY.
    PhylomeDBiQ5SM28.

    Enzyme and pathway databases

    BRENDAi6.1.1.15. 2305.
    SABIO-RKQ5SM28.

    Miscellaneous databases

    EvolutionaryTraceiQ5SM28.

    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_THET8
    AccessioniPrimary (citable) accession number: Q5SM28
    Secondary accession number(s): Q93N97
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 5, 2006
    Last sequence update: December 21, 2004
    Last modified: November 2, 2016
    This is version 95 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.