ID G7H030_9ACTN Unreviewed; 1127 AA.
AC G7H030;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 68.
DE RecName: Full=RecBCD enzyme subunit RecB {ECO:0000256|HAMAP-Rule:MF_01485};
DE EC=3.1.11.5 {ECO:0000256|HAMAP-Rule:MF_01485};
DE AltName: Full=Exonuclease V subunit RecB {ECO:0000256|HAMAP-Rule:MF_01485};
DE Short=ExoV subunit RecB {ECO:0000256|HAMAP-Rule:MF_01485};
DE AltName: Full=Helicase/nuclease RecBCD subunit RecB {ECO:0000256|HAMAP-Rule:MF_01485};
GN Name=recB {ECO:0000256|HAMAP-Rule:MF_01485,
GN ECO:0000313|EMBL:GAB09205.1};
GN ORFNames=GOARA_033_00060 {ECO:0000313|EMBL:GAB09205.1};
OS Gordonia araii NBRC 100433.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Gordoniaceae;
OC Gordonia.
OX NCBI_TaxID=1073574 {ECO:0000313|EMBL:GAB09205.1, ECO:0000313|Proteomes:UP000035088};
RN [1] {ECO:0000313|EMBL:GAB09205.1, ECO:0000313|Proteomes:UP000035088}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 100433 {ECO:0000313|EMBL:GAB09205.1,
RC ECO:0000313|Proteomes:UP000035088};
RA Yoshida Y., Hosoyama A., Tsuchikane K., Katsumata H., Yamazaki S.,
RA Fujita N.;
RT "Whole genome shotgun sequence of Gordonia araii NBRC 100433.";
RL Submitted (NOV-2011) 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
CC contributes ATPase, 3'-5' helicase, exonuclease activity and loads RecA
CC onto ssDNA. {ECO:0000256|HAMAP-Rule:MF_01485}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=5.6.2.4;
CC Evidence={ECO:0000256|ARBA:ARBA00034618};
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_01485};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01485};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|HAMAP-Rule:MF_01485};
CC -!- SUBUNIT: Heterotrimer of RecB, RecC and RecD. All subunits contribute
CC to DNA-binding. Interacts with RecA. {ECO:0000256|HAMAP-Rule:MF_01485}.
CC -!- DOMAIN: The C-terminal domain has nuclease activity and interacts with
CC RecD. It interacts with RecA, facilitating its loading onto ssDNA.
CC {ECO:0000256|HAMAP-Rule:MF_01485}.
CC -!- DOMAIN: The N-terminal DNA-binding domain is a ssDNA-dependent ATPase
CC and has ATP-dependent 3'-5' helicase function. This domain interacts
CC with RecC. {ECO:0000256|HAMAP-Rule:MF_01485}.
CC -!- SIMILARITY: Belongs to the helicase family. UvrD subfamily.
CC {ECO:0000256|HAMAP-Rule:MF_01485}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:GAB09205.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BAEE01000033; GAB09205.1; -; Genomic_DNA.
DR RefSeq; WP_007321282.1; NZ_JABELY010000031.1.
DR AlphaFoldDB; G7H030; -.
DR STRING; 1073574.GOARA_033_00060; -.
DR OrthoDB; 9810135at2; -.
DR Proteomes; UP000035088; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
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:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IEA:UniProtKB-UniRule.
DR CDD; cd22352; RecB_C-like; 1.
DR Gene3D; 3.90.320.10; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR HAMAP; MF_01485; RecB; 1.
DR InterPro; IPR014017; DNA_helicase_UvrD-like_C.
DR InterPro; IPR000212; DNA_helicase_UvrD/REP.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR011604; PDDEXK-like_dom_sf.
DR InterPro; IPR038726; PDDEXK_AddAB-type.
DR InterPro; IPR004586; RecB.
DR InterPro; IPR011335; Restrct_endonuc-II-like.
DR InterPro; IPR014016; UvrD-like_ATP-bd.
DR PANTHER; PTHR11070:SF23; RECBCD ENZYME SUBUNIT RECB; 1.
DR PANTHER; PTHR11070; UVRD / RECB / PCRA DNA HELICASE FAMILY MEMBER; 1.
DR Pfam; PF12705; PDDEXK_1; 1.
DR Pfam; PF00580; UvrD-helicase; 1.
DR Pfam; PF13361; UvrD_C; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF52980; Restriction endonuclease-like; 1.
DR PROSITE; PS51198; UVRD_HELICASE_ATP_BIND; 1.
DR PROSITE; PS51217; UVRD_HELICASE_CTER; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_01485};
KW DNA damage {ECO:0000256|ARBA:ARBA00022763, ECO:0000256|HAMAP-
KW Rule:MF_01485};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204, ECO:0000256|HAMAP-
KW Rule:MF_01485};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|HAMAP-
KW Rule:MF_01485};
KW Exonuclease {ECO:0000256|ARBA:ARBA00022839, ECO:0000256|HAMAP-
KW Rule:MF_01485};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000256|HAMAP-Rule:MF_01485};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_01485};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_01485};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_01485};
KW Nuclease {ECO:0000256|ARBA:ARBA00022722, ECO:0000256|HAMAP-Rule:MF_01485};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_01485}.
FT DOMAIN 1..328
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51198"
FT DOMAIN 360..627
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51217"
FT REGION 1..783
FT /note="DNA-binding and helicase activity, interacts with
FT RecC"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01485"
FT REGION 802..1127
FT /note="Nuclease activity, interacts with RecD and RecA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01485"
FT REGION 848..870
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1024
FT /note="For nuclease activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01485"
FT BINDING 21..28
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
FT BINDING 885
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01485"
FT BINDING 1007
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01485"
FT BINDING 1024
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01485"
SQ SEQUENCE 1127 AA; 122585 MW; 71DC19693208B6E1 CRC64;
MTPTPFTLAD PLPTGTLVLE ASAGTGKTYA IAALAVRFIA EGTPVSRLLM ATFSNAASTE
LRDRTRARLR ECADALADLD AARAGADPLI GLLADGETQE VALRRERLLA ALSDFDAATM
ATTHTFCNRM LTVLGFLGER DQHYLLVEDV DDLARETGRD LYLKRFAGDP DPDFAFSTAE
VVARDAVRNP TAVLAPADAA SESGRTWVRF AQAVRERVRT RKRWSRLRTY DDLQGRLHEI
ITDDQWGAAA CERIRDRYEV VLVDEFQDTD PEQWEILRRC FHGHRPMVLV GDPKQSIYAF
RGAEVLSYLA AAHDADEQRD LTDNWRSDGP LVDALGAVLA DAELGDPRIA VRPVRARHAE
SRLAGTSALR LRYFNRRDFT KHTQDGTTPL VGGVRDRIID DVAADIAATL ASGATILVDD
GAGENERRIE PGDIAVLLRT NGTIEPLQRA LGGYGIATVV TGGQSVFATD AARYWWYVLQ
ALDKPSDARR VRLAALTPLL GVEPRDLDAG GDAGVGELAG DLARWARIFE DGGPAAMTSR
LIADRTVAGR VLGLVDGERL LTDLLQLASL MGEHVAETGC GLSGLVTWLG ESVADGAVAQ
QRRSSQTRRL DRDTAAVQLM TVHASKGLEF PIVYVPFGWD GVRPNRPKTF TFHDDRNVGH
LDVGGERAPG HAERKRRAEA EAAGEELRLL YVALTRARSQ VVAWWAPSTT TPGGAMHRVL
FTALNRAAAA RSGGRYPIPD AVPLTDDAGE EALLRDVAGL HPGITVEHAG TRPRPPRWRP
PAPPAHGAAL TVATFERDVD QTFRRTSYSA IVRAAHEAAH LGAVAEPETI VGSEPDDQVV
RDGEVLDEPA DDATTDTGPA DEPPSGTPSL MNGLPFGARF GTLVHEVLEN VDTSVPDRAA
HVRELCEQGA RRTAFDIDVE ALSRALDGVL TTPIGFGDLW SVAPADRLSE MDFELPLADV
GGGFDLASVA ELMRRHLRDD DPLRPYADEV AGVSDERFHG YLTGSIDSVL RVRDGDTARF
VVVDYKTNRI QPGDLVAEVF STEAMAAEMM DAHYPLQALL YSVALHRYLR WRLPGYTPEQ
HLGPVQYHFV RGMVGPETPP GCGVFQWEVP AQLVVDLSDL LAGVRDD
//
