recD Family assigned · medium auto-curated

H37Rv Rv0629c · MTBC0 mtbc0_000662 · 575 aa · 723558–725285 (-) · RefSeq NP_215143.1

Annotation: from legacy to revised

Legacy (H37Rv / Mycobrowser)exonuclease V subunit alpha RecD
MTBC0 PGAP re-annotationexodeoxyribonuclease V subunit alpha
Revised (this work)Exodeoxyribonuclease V subunit alpha. Pfam: RecD_N (PF21185.4), AAA_30 (PF13604.13), AAA_11 (PF13086.13), UvrD-helicase (PF00580.28), AAA_19 (PF13245.13), AAA_22 (PF13401.13), NAT10_TcmA_helicase (PF05127.22), Viral_helicase1 (PF01443.25), UvrD_C_2 (PF13538.13).

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

Curated reference (UniProt)

UniProt P9WHJ1 SwissProt · reviewed · Evidence at protein level
UniProt nameRecBCD enzyme subunit RecD
EC (curated) EC 5.6.2.3
Curated functionA helicase/nuclease that prepares dsDNA breaks (DSB) for recombinational DNA repair. Binds to DSBs and unwinds DNA via a highly rapid and processive ATP-dependent bidirectional helicase activity. Holoenzyme degrades any linearized DNA that is unable to undergo homologous recombination. In the holoenzyme this subunit has ssDNA-dependent ATPase and 5'-3' helicase activity. When added to pre-assembled RecBC greatly stimulates nuclease activity and augments holoenzyme processivity. Unlike the case in E.coli, suppresses RecA-dependent homologous recombination, is instead required for single-strand .

Functional vocabulary (eggNOG-mapper, orthology transfer)

COG category L Replication, recombination and repair
Preferred namerecD
eggNOG descriptionA helicase nuclease that prepares dsDNA breaks (DSB) for recombinational DNA repair. Binds to DSBs and unwinds DNA via a highly rapid and processive ATP-dependent bidirectional helicase activity. Unwinds dsDNA until it encounters a Chi (crossover hotspot instigator) sequence from the 3' direction. Cuts ssDNA a few nucleotides 3' to the Chi site. The properties and activities of the enzyme are changed at Chi. The Chi-altered holoenzyme produces a long 3'-ssDNA overhang and facilitates RecA-binding to the ssDNA for homologous DNA recombination and repair. Holoenzyme degrades any linearized DNA that is unable to undergo homologous recombination. In the holoenzyme this subunit has ssDNA-dependent ATPase and 5'-3' helicase activity. When added to pre-assembled RecBC greatly stimulates nuclease activity and augments holoenzyme processivity. Negatively regulates the RecA-loading ability of RecBCD
Orthologous groupCOG0507
EC number EC 3.1.11.5
KEGG orthology K03581
KEGG pathways map03440
Gene Ontology (13) GO:0005575, GO:0005618, GO:0005622, GO:0005623, GO:0005737, GO:0005829, GO:0005886, GO:0016020, GO:0030312, GO:0044424, GO:0044444, GO:0044464 +1 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 0.302 · purifying
Polymorphic sites (≥ 0.1% of strains) 9 synonymous, 7 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
RecD_NPF21185.4 2.4e-0721–100 RecBCD enzyme subunit RecD, N-terminal domain
AAA_30PF13604.13 5.5e-32151–360 AAA domain
AAA_11PF13086.13 2.0e-07151–234 AAA domain
UvrD-helicasePF00580.28 3.0e-06152–243 UvrD/REP helicase N-terminal domain
AAA_19PF13245.13 6.4e-35153–304 AAA domain
AAA_22PF13401.13 2.8e-08162–298 AAA domain
NAT10_TcmA_helicasePF05127.22 3.0e-07167–285 RNA cytidine acetyltransferase NAT10/TcmA, helicase domain
Viral_helicase1PF01443.25 3.8e-05497–544 Viral superfamily 1 RNA helicase core domain
UvrD_C_2PF13538.13 1.9e-14499–545 UvrD-like helicase C-terminal domain

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

Closest characterised functional partner: recC (exonuclease V subunit gamma RecC), high confidence from genomic context alone (score 996 excluding text-mining).

PartnerProductScoreNo text-miningChannels (≥400)
Rv0631c recC exonuclease V subunit gamma RecC 999 996 ctx neighborhood:881 cooccurence:774 experimental:737 textmining:813
Rv0630c recB exonuclease V subunit beta RecB 998 996 ctx neighborhood:881 cooccurence:773 coexpression:460 experimental:510 database:540 textmining:707
Rv2793c truB tRNA pseudouridine synthase B 655 656 database:632
Rv1329c dinG ATP-dependent helicase DinG 676 606 database:537
Rv0628c hyp hypothetical protein 557 558 ctx neighborhood:554
Rv2037c transmembrane protein 514 514 ctx neighborhood:511
Rv2116 lppK lipoprotein LppK 550 508 experimental:474
Rv0002 dnaN DNA polymerase III subunit beta 549 507 experimental:474
Rv3202c adnA ATP-dependent DNA helicase 512 445
Rv2529 hyp hypothetical protein 503 443
Rv3201c adnB ATP-dependent DNA helicase 497 442
Rv0632c echA3 enoyl-CoA hydratase EchA3 432 432 ctx neighborhood:432
Rv0949 uvrD1 ATP-dependent DNA helicase UvrD 579 428
Rv1278 hyp hypothetical protein 493 427
Rv3198c uvrD2 ATP-dependent DNA helicase UvrD 458 424

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: exonuclease V subunit alpha RecD
  • MTBC0 PGAP product: exodeoxyribonuclease V subunit alpha
  • Pfam (hmmscan --cut_ga): RecD_N PF21185.4 (E=2e-07), AAA_30 PF13604.13 (E=6e-32), AAA_11 PF13086.13 (E=2e-07), UvrD-helicase PF00580.28 (E=3e-06), AAA_19 PF13245.13 (E=6e-35), AAA_22 PF13401.13 (E=3e-08), NAT10_TcmA_helicase PF05127.22 (E=3e-07), Viral_helicase1 PF01443.25 (E=4e-05), UvrD_C_2 PF13538.13 (E=2e-14)
  • (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_215143.1)
  • Domains: Pfam-A via hmmscan --cut_ga — RecD_N (PF21185.4), AAA_30 (PF13604.13), AAA_11 (PF13086.13), UvrD-helicase (PF00580.28), AAA_19 (PF13245.13), AAA_22 (PF13401.13), NAT10_TcmA_helicase (PF05127.22), Viral_helicase1 (PF01443.25), UvrD_C_2 (PF13538.13)
  • 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 COG0507
  • Curated reference: UniProt P9WHJ1 (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 — 54 functional partner(s); context anchor recC
  • Primary literature: none located yet; annotation rests on the domain/homology sources above.

Ancestral MTBC0 protein sequence

>mtbc0_000662|Rv0629c|recD
MKLTDVDFAVEASGMVRAFNQAGVLDVSDVHVAQRLCALAGESDERVALAVAVAVRALRAGSVCVDLLSIARVAGHDDLPWPDPADWLAAVRASPLLADPPVLHLYDDRLLYLDRYWREEEQVCADLLALLTSRRPAGVPDLRRLFPTGFDEQRRAAEIALSQGVTVLTGGPGTGKTTTVARLLALVAEQAELAGEPRPRIALAAPTGKAAARLAEAVRREMAKLDATDRARLGDLHAVTLHRLLGAKPGARFRQDRQNRLPHNVIVVDETSMVSLTLMARLAEAVRPGARLILVGDADQLASVEAGAVLADLVDGFSVRDDALVAQLRTSHRFGKVIGTLAEAIRAGDGDAVLGLLRSGEERIEFVDDEDPAPRLRAVLVPHALRLREAALLGASDVALATLDEHRLLCAHRDGPTGVLHWNRRVQAWLAEETGQPPWTPWYAGRPLLVTANDYGLRVYNGDTGVVLAGPTGLRAVISGASGPLDVATGRLGDVETMHAMTIHKSQGSQVDEVTVLMPQEDSRLLTRELLYTAVTRAKRKVRVVGSEASVRAAIARRAVRASGLRMRLQSTGCG