argS Resolved · high auto-curated

H37Rv Rv1292 · MTBC0 mtbc0_001384 · 550 aa · 1455418–1457070 (+) · RefSeq NP_215808.1

Annotation: from legacy to revised

Legacy (H37Rv / Mycobrowser)arginine--tRNA ligase
MTBC0 PGAP re-annotationarginine--tRNA ligase
Revised (this work)Arginine--tRNA ligase. Pfam: Arg_tRNA_synt_N (PF03485.22), tRNA-synt_1d (PF00750.26), tRNA-synt_1 (PF00133.29), DALR_1 (PF05746.22).

Auto-curated: this verdict and function were generated by rules from PGAP + Pfam + Foldseek and have not been hand-reviewed.

Curated reference (UniProt)

UniProt P9WFW5 SwissProt · reviewed · Evidence at protein level
UniProt nameArginine--tRNA ligase
EC (curated) EC 6.1.1.19

Functional vocabulary (eggNOG-mapper, orthology transfer)

COG category J Translation, ribosomal structure and biogenesis
Preferred nameargS
eggNOG descriptionArginyl-tRNA synthetase
Orthologous groupCOG0018
EC number EC 6.1.1.19
KEGG orthology K01887
KEGG pathways map00970
KEGG modules M00359, M00360
Gene Ontology (63) GO:0003674, GO:0003824, GO:0004812, GO:0004814, GO:0005575, GO:0005622, GO:0005623, GO:0005737, GO:0005829, GO:0005886, GO:0006082, GO:0006139 +51 more

Orthology-based transfer (eggNOG 5.0.2, diamond). EC/KO/GO/CAZy are computed annotations, not manual curation; cross-check against the primary literature before treating a specific reaction as established.

Conservation & selection (intra-MTBC, 145 209 strains)

pN/pS 0.448 · purifying
Polymorphic sites (≥ 0.1% of strains) 6 synonymous, 8 missense, 0 nonsense, 0 frameshift

pN/pS from segregating SNPs (singletons removed) normalised by possible sites. Low pN/pS = purifying selection (a strong signal that a "hypothetical" is a real, constrained gene). A high pN/pS is ambiguous: relaxed constraint or positive selection (drug resistance, antigenic variation) inflate it; e.g. rpoB/katG/pncA score high here for resistance, not loss of function. A clonal disruption (one allele over a clade) suggests lineage pseudogenisation; a convergent one (many independent alleles) is typical of resistance loss-of-function.

Domains (Pfam, hmmscan --cut_ga)

PfamAccessioni-EvalueResiduesDescription
Arg_tRNA_synt_NPF03485.22 7.0e-2313–93 Arginyl tRNA synthetase N terminal domain
tRNA-synt_1dPF00750.26 1.0e-16120–390 tRNA synthetases class I (R), catalytic domain
tRNA-synt_1PF00133.29 4.5e-05327–412 tRNA synthetases class I (I, L, M and V)
DALR_1PF05746.22 1.5e-35429–550 DALR anticodon binding domain

Functional interaction network (STRING v12, guilt-by-association)

Closest characterised functional partner: lysA (diaminopimelate decarboxylase), high confidence from genomic context alone (score 903 excluding text-mining).

PartnerProductScoreNo text-miningChannels (≥400)
Rv3396c guaA GMP synthase 988 980 coexpression:979 textmining:432
Rv2992c gltS glutamate--tRNA ligase 995 967 coexpression:432 experimental:844 database:546 textmining:881
Rv1536 ileS isoleucine--tRNA ligase 993 958 coexpression:513 experimental:788 database:597 textmining:851
Rv1007c metS methionine--tRNA ligase 962 947 experimental:814 database:571
Rv2845c proS proline--tRNA ligase 957 940 coexpression:704 experimental:512 database:597
Rv0041 leuS leucine--tRNA ligase 994 919 coexpression:411 experimental:675 database:597 textmining:940
Rv1293 lysA diaminopimelate decarboxylase 912 903 ctx neighborhood:882
Rv1295 thrC threonine synthase 906 903 ctx neighborhood:882
Rv1294 thrA homoserine dehydrogenase 896 891 ctx neighborhood:881
Rv3598c lysS lysine--tRNA ligase 887 835 coexpression:452 experimental:462
Rv1650 pheT phenylalanine--tRNA ligase subunit beta 920 815 coexpression:708 textmining:588
Rv1640c lysX bifunctional lysine--tRNA ligase/phosphatidylglycerol lysyltransferase 859 811 coexpression:450 experimental:462
Rv1699 pyrG CTP synthase 813 800 coexpression:783
Rv1017c prsA ribose-phosphate pyrophosphokinase 778 769 coexpression:702
Rv1296 thrB homoserine kinase 746 745 ctx neighborhood:731

STRING combines evidence channels (neighborhood, fusion, cooccurrence, coexpression, experimental, database, text-mining) into a 0–1000 score. The ctx badge marks edges carried by the genomic-context channels (conserved neighborhood, fusion, phylogenetic co-occurrence), which are independent of orthology and structure and the strongest signal for an unknown gene. The no text-mining column recomputes the score from data alone, so a link that does not depend on the literature is visible. Association is a function hypothesis, not proof: corroborate with the operon context and the primary literature before assigning a function.

Evidence

  • Legacy H37Rv annotation: arginine--tRNA ligase
  • MTBC0 PGAP product: arginine--tRNA ligase
  • Pfam (hmmscan --cut_ga): Arg_tRNA_synt_N PF03485.22 (E=7e-23), tRNA-synt_1d PF00750.26 (E=1e-16), tRNA-synt_1 PF00133.29 (E=5e-05), DALR_1 PF05746.22 (E=1e-35)
  • (auto-curated by rules from PGAP + Pfam + Foldseek; not hand-reviewed)

Sources

  • Ancestral sequence & coordinates: Harrison LB et al. (2024), An imputed ancestral reference genome for the MTBC, doi:10.1101/2023.09.07.556366
  • Product annotation: NCBI PGAP on MTBC0; legacy from H37Rv NC_000962.3 (RefSeq NP_215808.1)
  • Domains: Pfam-A via hmmscan --cut_ga — Arg_tRNA_synt_N (PF03485.22), tRNA-synt_1d (PF00750.26), tRNA-synt_1 (PF00133.29), DALR_1 (PF05746.22)
  • Sequence-level signal: ESM Atlas (EvolutionaryScale × BioHub) — exploratory
  • Controlled vocabulary: eggNOG-mapper 2.1.12 (Cantalapiedra et al. 2021, doi:10.1093/molbev/msab293), eggNOG 5.0 DB (Huerta-Cepas et al. 2019) — OG COG0018
  • Curated reference: UniProt P9WFW5 (SwissProt, reviewed; Evidence at protein level)
  • Intra-MTBC selection: pN/pS and disruption from SPDI variants of 145 209 MTBC strains (this work, local collection vs H37Rv NC_000962.3)
  • Interaction network: STRING v12.0 (Szklarczyk et al. 2023, doi:10.1093/nar/gkac1000), taxon 83332, CC-BY 4.0 — 118 functional partner(s); context anchor lysA
  • Primary literature: none located yet; annotation rests on the domain/homology sources above.

Ancestral MTBC0 protein sequence

>mtbc0_001384|Rv1292|argS
MTPADLAELLKATAAAVLAERGLDASALPQMVTVERPRIPEHGDYASNLAMQLAKKVGTNPRELAGWLAEALTKVDGIASAEVAGPGFINMRLETAAQAKVVTSVIDAGHSYGHSLLLAGRKVNLEFVSANPTGPIHIGGTRWAAVGDALGRLLTTQGADVVREYYFNDHGAQIDRFANSLIAAAKGEPTPQDGYAGSYITNIAEQVLQKAPDALSLPDAELRETFRAIGVDLMFDHIKQSLHEFGTDFDVYTHEDSMHTGGRVENAIARLRETGNIYEKDGATWLRTSAFGDDKDRVVIKSDGKPAYIAGDLAYYLDKRQRGFDLCIYMLGADHHGYIARLKAAAAAFGDDPATVEVLIGQMVNLVRDGQPVRMSKRAGTVLTLDDLVEAIGVDAARYSLIRSSVDTAIDIDLALWSSASNENPVYYVQYAHARLSALARNAAELALIPDTNHLELLNHDKEGTLLRTLGEFPRVLETAASLREPHRVCRYLEDLAGDYHRFYDSCRVLPQGDEQPTDLHTARLALCQATRQVIANGLAIIGVTAPERM