ID D3SAR5_THISK Unreviewed; 679 AA.
AC D3SAR5;
DT 20-APR-2010, integrated into UniProtKB/TrEMBL.
DT 20-APR-2010, sequence version 1.
DT 27-MAR-2024, entry version 80.
DE RecName: Full=RecBCD enzyme subunit RecD {ECO:0000256|HAMAP-Rule:MF_01487};
DE EC=3.1.11.5 {ECO:0000256|HAMAP-Rule:MF_01487};
DE AltName: Full=Exonuclease V subunit RecD {ECO:0000256|HAMAP-Rule:MF_01487};
DE Short=ExoV subunit RecD {ECO:0000256|HAMAP-Rule:MF_01487};
DE AltName: Full=Helicase/nuclease RecBCD subunit RecD {ECO:0000256|HAMAP-Rule:MF_01487};
GN Name=recD {ECO:0000256|HAMAP-Rule:MF_01487};
GN OrderedLocusNames=TK90_1623 {ECO:0000313|EMBL:ADC72120.1};
OS Thioalkalivibrio sp. (strain K90mix).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales;
OC Ectothiorhodospiraceae; Thioalkalivibrio.
OX NCBI_TaxID=396595 {ECO:0000313|EMBL:ADC72120.1, ECO:0000313|Proteomes:UP000009099};
RN [1] {ECO:0000313|Proteomes:UP000009099}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K90mix {ECO:0000313|Proteomes:UP000009099};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA Pitluck S., Foster B., Sun H., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Ivanova N., Sorokin D.Y., Muyzer G., Woyke T.;
RT "Complete sequence of chromosome of Thioalkalivibrio sp. K90mix.";
RL Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ADC72120.1, ECO:0000313|Proteomes:UP000009099}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K90mix {ECO:0000313|EMBL:ADC72120.1,
RC ECO:0000313|Proteomes:UP000009099};
RX PubMed=22675584; DOI=10.4056/sigs.2315092;
RA Muyzer G., Sorokin D.Y., Mavromatis K., Lapidus A., Foster B., Sun H.,
RA Ivanova N., Pati A., D'haeseleer P., Woyke T., Kyrpides N.C.;
RT "Complete genome sequence of Thioalkalivibrio sp. K90mix.";
RL Stand. Genomic Sci. 5:341-355(2011).
CC -!- FUNCTION: A helicase/nuclease that prepares dsDNA breaks (DSB) for
CC recombinational DNA repair. Binds to DSBs and unwinds DNA via a highly
CC rapid and processive ATP-dependent bidirectional helicase activity.
CC Unwinds dsDNA until it encounters a Chi (crossover hotspot instigator)
CC sequence from the 3' direction. Cuts ssDNA a few nucleotides 3' to the
CC Chi site. The properties and activities of the enzyme are changed at
CC Chi. The Chi-altered holoenzyme produces a long 3'-ssDNA overhang and
CC facilitates RecA-binding to the ssDNA for homologous DNA recombination
CC and repair. Holoenzyme degrades any linearized DNA that is unable to
CC undergo homologous recombination. In the holoenzyme this subunit has
CC ssDNA-dependent ATPase and 5'-3' helicase activity. When added to pre-
CC assembled RecBC greatly stimulates nuclease activity and augments
CC holoenzyme processivity. Negatively regulates the RecA-loading ability
CC of RecBCD. {ECO:0000256|HAMAP-Rule:MF_01487}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Exonucleolytic cleavage (in the presence of ATP) in either
CC 5'- to 3'- or 3'- to 5'-direction to yield 5'-
CC phosphooligonucleotides.; EC=3.1.11.5; Evidence={ECO:0000256|HAMAP-
CC Rule:MF_01487};
CC -!- SUBUNIT: Heterotrimer of RecB, RecC and RecD. All subunits contribute
CC to DNA-binding. {ECO:0000256|HAMAP-Rule:MF_01487}.
CC -!- SIMILARITY: Belongs to the RecD family. {ECO:0000256|HAMAP-
CC Rule:MF_01487}.
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DR EMBL; CP001905; ADC72120.1; -; Genomic_DNA.
DR RefSeq; WP_012983001.1; NC_013889.1.
DR AlphaFoldDB; D3SAR5; -.
DR STRING; 396595.TK90_1623; -.
DR KEGG; tkm:TK90_1623; -.
DR eggNOG; COG0507; Bacteria.
DR HOGENOM; CLU_007524_1_2_6; -.
DR OrthoDB; 9803432at2; -.
DR Proteomes; UP000009099; Chromosome.
DR GO; GO:0009338; C:exodeoxyribonuclease V complex; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003678; F:DNA helicase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008854; F:exodeoxyribonuclease V activity; IEA:UniProtKB-EC.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IEA:UniProtKB-UniRule.
DR CDD; cd17933; DEXSc_RecD-like; 1.
DR CDD; cd18809; SF1_C_RecD; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 3.
DR Gene3D; 1.10.10.1020; RecBCD complex, subunit RecD, N-terminal domain; 1.
DR HAMAP; MF_01487; RecD; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR006344; RecD.
DR InterPro; IPR049550; RecD_N.
DR InterPro; IPR041851; RecD_N_sf.
DR InterPro; IPR027785; UvrD-like_helicase_C.
DR NCBIfam; TIGR01447; recD; 1.
DR PANTHER; PTHR43788; DNA2/NAM7 HELICASE FAMILY MEMBER; 1.
DR PANTHER; PTHR43788:SF6; RECBCD ENZYME SUBUNIT RECD; 1.
DR Pfam; PF13245; AAA_19; 1.
DR Pfam; PF21185; RecD_N; 1.
DR Pfam; PF13538; UvrD_C_2; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_01487}; DNA damage {ECO:0000256|HAMAP-Rule:MF_01487};
KW DNA repair {ECO:0000256|HAMAP-Rule:MF_01487};
KW DNA-binding {ECO:0000256|HAMAP-Rule:MF_01487};
KW Exonuclease {ECO:0000256|HAMAP-Rule:MF_01487};
KW Helicase {ECO:0000256|HAMAP-Rule:MF_01487};
KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_01487, ECO:0000313|EMBL:ADC72120.1};
KW Nuclease {ECO:0000256|HAMAP-Rule:MF_01487};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_01487}.
FT DOMAIN 40..133
FT /note="RecBCD enzyme subunit RecD N-terminal"
FT /evidence="ECO:0000259|Pfam:PF21185"
FT DOMAIN 607..653
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13538"
FT BINDING 205..212
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01487"
SQ SEQUENCE 679 AA; 73295 MW; 3E69FE559A93B754 CRC64;
MTAERALQDT GALLDLLGEW EHAGWVRGVD RVLVRFLREQ VPAAPPLTLL LAALTSHQAG
RGHVCLDLDG LLEAPDRMLS LPPEGAERGL PRPSDVLRGL DRAALDTALE GHRICGVDAD
AGTPLVRAQD RLYLRRYREA ERRIGEAVAG RLREQPAWRE GLDADVLRTW LDRLFGPADE
ADGEPDWQRL ACILAAGSGF SVITGGPGTG KTYTVLQLLA LLQGLQGEGE PLRIRLAAPT
GKAAARLNAS VAGAVDALGL ERFPGGVRLR AAIPREVVTL HRLLGARPDT RRFRHDARNP
LPVDVLVVDE ASMVDLELMA SLMVAVPAHA RLVLLGDRDQ LASVEAGAVL GELCARADGG
HYTPQTAAWL REVAGLELPA GYVDEDGRAL DQHVAMLRRS RRFGADSGIG RLAAAVNDGT
AEVTGHPGED VYAAVLQGPD DPALLRRVLD GAGHADAAPF GVVRYLEHLT AGRPASRDAR
GTWEEWARGT LREHGRFQLL CAVREGPWGV DRMNRRVAGA LTARGVLQAE GVWYEGRPVI
VTRNDYALGL INGDIGVTLR VPAWLARGDA EPGADDATET ALRVAFVAAD GHVRWMIPQR
LESVETAFAL TVHKSQGSEF EHVAFLLPPP ESPLLTRELA YTAITRASGW LSLFEPQAGV
LQQASRQPTR RSGGLRTWL
//
