ID I3YAG6_THIV6 Unreviewed; 766 AA.
AC I3YAG6;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 27-MAR-2024, entry version 53.
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=Thivi_2027 {ECO:0000313|EMBL:AFL73984.1};
OS Thiocystis violascens (strain ATCC 17096 / DSM 198 / 6111) (Chromatium
OS violascens).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC Thiocystis.
OX NCBI_TaxID=765911 {ECO:0000313|EMBL:AFL73984.1, ECO:0000313|Proteomes:UP000006062};
RN [1] {ECO:0000313|EMBL:AFL73984.1, ECO:0000313|Proteomes:UP000006062}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 17096 / DSM 198 / 6111
RC {ECO:0000313|Proteomes:UP000006062};
RG US DOE Joint Genome Institute;
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Ovchinnikova G., Teshima H., Detter J.C., Han C., Tapia R.,
RA Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Vogl K., Liu Z.,
RA Frigaard N.-U., Bryant D., Woyke T.;
RT "Complete sequence of Thiocystis violascens DSM 198.";
RL Submitted (JUN-2012) to the EMBL/GenBank/DDBJ databases.
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; CP003154; AFL73984.1; -; Genomic_DNA.
DR RefSeq; WP_014778440.1; NC_018012.1.
DR AlphaFoldDB; I3YAG6; -.
DR STRING; 765911.Thivi_2027; -.
DR KEGG; tvi:Thivi_2027; -.
DR eggNOG; COG0507; Bacteria.
DR HOGENOM; CLU_007524_1_2_6; -.
DR OrthoDB; 9803432at2; -.
DR Proteomes; UP000006062; 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, ECO:0000313|EMBL:AFL73984.1};
KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_01487, ECO:0000313|EMBL:AFL73984.1};
KW Nuclease {ECO:0000256|HAMAP-Rule:MF_01487};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_01487}; Reference proteome {ECO:0000313|Proteomes:UP000006062}.
FT DOMAIN 35..132
FT /note="RecBCD enzyme subunit RecD N-terminal"
FT /evidence="ECO:0000259|Pfam:PF21185"
FT DOMAIN 684..729
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13538"
FT BINDING 227..234
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01487"
SQ SEQUENCE 766 AA; 82955 MW; F0E6D43492424CB0 CRC64;
MDTRTSHPFA LSGVEGFAPV EAEDLLARLR AWADAGALRA LDLALTRFIH RHGPETDTAV
LLAVALTSER NGHGHVCLDL AGARERPDAL LTRLRDDVDT AAEVRADLSA LLRGLTLADW
VGRLSRSPAV HNRLDRDATD DAASPLVLEG TPARPLLYLR RYWRYESRIL DGIRARLDQR
LELPETDLRA LLDALFVVDQ DAASDPCDWQ KIACALAARS AFAIVTGGPG TGKTTTVVRL
LALLQGLAIG RGQPPLRIRL AAPTGKAAAR LNESIAARVA DLPLDAVPNG EQVRREIPTE
VTTLHRLLGS IPDSRHFRHH AGHPLPADLV VVDEASMVDV EMMARLLEAL RPDARLILLG
DKDQLASVEA GAVLGDLCQR ARAAHYLPVT RDWLRRVTGA TIPDTYLDDA GEPLDQAIVM
LRKSYRFKPE GGIGALAALV NDDRRHDDTP ERQPPTARLS AVLSLFERQR SVSDGKLGRI
DAIQLRDTGS PEFAALVRDG YRAYLTRMRD EDPGDDATRD ALDRWARAVL KAQEGFQLLT
ALRQGPWGVE GLNRRIVEVL KDAGLLSGGD ALGTAGADRH WFAGRPVLVT RNDYGLHLMN
GDIGITLALP LAPRGVEGPA LSGVAGPVLS GVAGPVLSGV EGAELGGQEI GARRRVLRVA
FPAGDGSGGI RWILPSRLQA VETVFAMTVH KSQGSEFDHT VLILPDTSNP VLTRELVYTG
ITRSRHAFTL LYREPSVLGD ALERRVRRVS GIGLSRGQTL DECNDA
//
