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Proline--tRNA ligase (Thioalkalivibrio sulfidiphilus HL-EbGr7)

Protein
Dates
  • Create:
    2017-04-15
  • Modify:
    2025-01-18
Description
Please note that Proline--tRNA ligase (Thioalkalivibrio sulfidiphilus HL-EbGr7) does not have data or annotation in PubChem. However, annotations from external sources are available.
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.

1 Names and Identifiers

1.1 Synonyms

  • Proline--tRNA ligase
  • EC 6.1.1.15
  • Prolyl-tRNA synthetase
  • ProRS

1.2 Other Identifiers

1.2.1 RefSeq Accession

1.2.2 UniProt ID

1.2.3 Enzyme Commission (EC) Number

1.2.4 InterPro Protein

2 Sequence

>sp|B8GPP4|SYP_THISH Proline--tRNA ligase (Run BLAST)

MRATRFPLATLKETPADAEVISHQLMLRAGMIRRLASGLYSWTPLGLRVLRKVEGLVRDEMDRAGALELLMPAVQPAELWQESGRWEQYGPELLRLKDRHMREFCFGPTHEEVITDYVRREVKSYRQLPVNYYQIQTKFRDEIRPRFGVMRAREFLMKDAYSFHVDEDSLKETYARMHEAYTRIFTRCGLDFRAVLADTGSIGGNASHEFHVLADSGEDAIAFSDVSDYAANVELAEAVAPATERAAPGEAMRLVDTPNARTIADLVEQHGLAIEKTVKTLVVAAAEGAEAPLIALLVRGDHELNAIKAEKLPQVASPLRMATEEEIRAAIGAGPGSLGPVNLPIPCVVDRAVALMSDFGAGANIDGKHYFGINWERDLALPPVADLRNVVAGDPSPDGQGSLQIRRGIEVGHIFQLGRKYSEAMGATVLDEQGRSLVVTMGCYGIGVSRVVAAAIEQNHDAQGIIWPEALAPFTVALCPINAQKSQRLREAADALYERLLNAGFEVFYDDRGLRPGAMFADMELIGIPHRLVLGERGLDAGEIEYKGRRDTDTTQVALDGVLDFLRQRMNAAH

3 Domains

3.1 CDD Domains

3.2 InterPro Domains

4 Biochemical Reactions

5 Literature

5.1 Consolidated References

6 Information Sources

  1. NCBI Protein
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    NCBI Website and Data Usage Policies and Disclaimers
    https://www.ncbi.nlm.nih.gov/home/about/policies/
  2. PubChem
  3. InterPro
    LICENSE
    All of the InterPro, Pfam, PRINTS and SFLD downloadable data provided on the InterPro website is freely available under CC0 1.0 Universal (CC0 1.0) Public Domain Dedication.
    https://www.ebi.ac.uk/interpro/about/license/
  4. NCBI Conserved Domains (CDD)
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    https://www.ncbi.nlm.nih.gov/home/about/policies/
  5. UniProt
    LICENSE
    We have chosen to apply the Creative Commons Attribution (CC BY 4.0, http://creativecommons.org/licenses/by/4.0/) License to all copyrightable parts of our databases.
    https://www.uniprot.org/help/license
  6. Rhea - annotated reactions database
    LICENSE
    Rhea has chosen to apply the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/). This means that you are free to copy, distribute, display and make commercial use of the database in all legislations, provided you credit (cite) Rhea.
    https://www.rhea-db.org/help/license-disclaimer
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