ID A0A1H4BAT4_ALKAM Unreviewed; 705 AA.
AC A0A1H4BAT4;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
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 ORFNames=SAMN04488051_103262 {ECO:0000313|EMBL:SEA45227.1};
OS Alkalimonas amylolytica.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alkalimonas.
OX NCBI_TaxID=152573 {ECO:0000313|EMBL:SEA45227.1, ECO:0000313|Proteomes:UP000198773};
RN [1] {ECO:0000313|EMBL:SEA45227.1, ECO:0000313|Proteomes:UP000198773}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.3430 {ECO:0000313|EMBL:SEA45227.1,
RC ECO:0000313|Proteomes:UP000198773};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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; FNRM01000003; SEA45227.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H4BAT4; -.
DR STRING; 152573.SAMN04488051_103262; -.
DR OrthoDB; 9803432at2; -.
DR Proteomes; UP000198773; Unassembled WGS sequence.
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:0004842; F:ubiquitin-protein transferase activity; IEA:InterPro.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IEA:UniProtKB-UniRule.
DR GO; GO:0016567; P:protein ubiquitination; IEA:InterPro.
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; IPR041851; RecD_N_sf.
DR InterPro; IPR003613; Ubox_domain.
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; PF13538; UvrD_C_2; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS51698; U_BOX; 1.
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:SEA45227.1};
KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_01487};
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:UP000198773}.
FT DOMAIN 1..27
FT /note="U-box"
FT /evidence="ECO:0000259|PROSITE:PS51698"
FT BINDING 212..219
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01487"
SQ SEQUENCE 705 AA; 76130 MW; 6B292C15E39DF391 CRC64;
MSAQSLTPTL PTLLQQAEDW CQAGLIRSLD WMLAQFFSRQ LPELTELELL AVLLCSEAHG
RGHVCLDIGA VLLQSKVKAP AGRSELWQQA DAELKQYLSA HSGQDWLQAL QGSALVASQL
PGQQAHTRAN APFVLAGSAQ KPLLYMRRYW QYEQLIAAEI TRRLQPEAPL AVDRVAPLLQ
GLFPAHKRAA PFDWQMAACA LALRSRFAII TGGPGTGKTT TVLKLLALLQ GLQLTGQQKP
LQILLAAPTG KAAARLNESI AQSLQQLDVS ALPLPDPGQL KAWLPTRVQT LHRLLGARPD
SRHFKHQRQN PLAADVVVVD EASMVDVELM AALVQALPAD CRLYLLGDKD QLASVEAGSV
LGDLCRFAEA GSYRPGTVAY LQQLCAAAIP ERYVAAEDAP ALAQVTAMLR HSYRFTEGGA
IHRLATLVNR GGTTDDGARV DGNELEGAGD ACSAVTTIKA IAAEPNSPVQ LLQQSMSAVS
TGTSASTAMP FSDALKALLL TGYRPYLTAV AAFAPEAETA QRNQTALQIL ALQRNFQLLG
AVREGDWGVQ GLNARIERLL ARHGLIRPEG LAWYPGRPVL MTRNDYQVQL MNGDIGVCLP
VQEQGETVLR VAFLDGEGGI RWVLPSRLHS AETVFAMTVH KSQGSEFQHT ALLLPASSSP
VLTRELLYTG ITRAKTTFSL IYDNEAVLAS TITQRVQRAS GIALL
//
