ID Q0SFN7_RHOJR Unreviewed; 1086 AA.
AC Q0SFN7;
DT 05-SEP-2006, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2006, sequence version 1.
DT 27-MAR-2024, entry version 110.
DE RecName: Full=RecBCD enzyme subunit RecC {ECO:0000256|HAMAP-Rule:MF_01486};
DE EC=3.1.11.5 {ECO:0000256|HAMAP-Rule:MF_01486};
DE AltName: Full=Exonuclease V subunit RecC {ECO:0000256|HAMAP-Rule:MF_01486};
DE Short=ExoV subunit RecC {ECO:0000256|HAMAP-Rule:MF_01486};
DE AltName: Full=Helicase/nuclease RecBCD subunit RecC {ECO:0000256|HAMAP-Rule:MF_01486};
GN Name=recC {ECO:0000256|HAMAP-Rule:MF_01486,
GN ECO:0000313|EMBL:ABG93649.1};
GN OrderedLocusNames=RHA1_ro01838 {ECO:0000313|EMBL:ABG93649.1};
OS Rhodococcus jostii (strain RHA1).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Rhodococcus.
OX NCBI_TaxID=101510 {ECO:0000313|EMBL:ABG93649.1, ECO:0000313|Proteomes:UP000008710};
RN [1] {ECO:0000313|Proteomes:UP000008710}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RHA1 {ECO:0000313|Proteomes:UP000008710};
RX PubMed=17030794; DOI=10.1073/pnas.0607048103;
RA McLeod M.P., Warren R.L., Hsiao W.W.L., Araki N., Myhre M., Fernandes C.,
RA Miyazawa D., Wong W., Lillquist A.L., Wang D., Dosanjh M., Hara H.,
RA Petrescu A., Morin R.D., Yang G., Stott J.M., Schein J.E., Shin H.,
RA Smailus D., Siddiqui A.S., Marra M.A., Jones S.J.M., Holt R.,
RA Brinkman F.S.L., Miyauchi K., Fukuda M., Davies J.E., Mohn W.W.,
RA Eltis L.D.;
RT "The complete genome of Rhodococcus sp. RHA1 provides insights into a
RT catabolic powerhouse.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:15582-15587(2006).
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 recognizes the wild-type Chi sequence, and when added to isolated RecB
CC increases its ATP-dependent helicase processivity. {ECO:0000256|HAMAP-
CC Rule:MF_01486}.
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_01486};
CC -!- SUBUNIT: Heterotrimer of RecB, RecC and RecD. All subunits contribute
CC to DNA-binding. {ECO:0000256|HAMAP-Rule:MF_01486}.
CC -!- SIMILARITY: Belongs to the RecC family. {ECO:0000256|HAMAP-
CC Rule:MF_01486}.
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DR EMBL; CP000431; ABG93649.1; -; Genomic_DNA.
DR RefSeq; WP_011594758.1; NC_008268.1.
DR AlphaFoldDB; Q0SFN7; -.
DR KEGG; rha:RHA1_ro01838; -.
DR PATRIC; fig|101510.16.peg.1855; -.
DR eggNOG; COG1330; Bacteria.
DR HOGENOM; CLU_007513_1_0_11; -.
DR OrthoDB; 9762834at2; -.
DR Proteomes; UP000008710; 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 Gene3D; 1.10.10.160; -; 1.
DR Gene3D; 3.40.50.10930; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR HAMAP; MF_01486; RecC; 1.
DR InterPro; IPR013986; DExx_box_DNA_helicase_dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR006697; RecC.
DR InterPro; IPR041500; RecC_C.
DR InterPro; IPR011335; Restrct_endonuc-II-like.
DR NCBIfam; TIGR01450; recC; 1.
DR PANTHER; PTHR30591; RECBCD ENZYME SUBUNIT RECC; 1.
DR PANTHER; PTHR30591:SF1; RECBCD ENZYME SUBUNIT RECC; 1.
DR Pfam; PF04257; Exonuc_V_gamma; 1.
DR Pfam; PF17946; RecC_C; 1.
DR PIRSF; PIRSF000980; RecC; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR SUPFAM; SSF52980; Restriction endonuclease-like; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_01486};
KW DNA damage {ECO:0000256|ARBA:ARBA00022763, ECO:0000256|HAMAP-
KW Rule:MF_01486};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204, ECO:0000256|HAMAP-
KW Rule:MF_01486};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|HAMAP-
KW Rule:MF_01486};
KW Exonuclease {ECO:0000256|ARBA:ARBA00022839, ECO:0000256|HAMAP-
KW Rule:MF_01486}; Helicase {ECO:0000256|HAMAP-Rule:MF_01486};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_01486};
KW Nuclease {ECO:0000256|HAMAP-Rule:MF_01486};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_01486}; Reference proteome {ECO:0000313|Proteomes:UP000008710}.
FT DOMAIN 793..1018
FT /note="RecC C-terminal"
FT /evidence="ECO:0000259|Pfam:PF17946"
SQ SEQUENCE 1086 AA; 117125 MW; 30C0BEC66296F0F7 CRC64;
MLVLHRAERS TTLASALGDV LATPLSDPFA REVVAVPAKG VERWLTQRLS TALGARPGVG
DGVAANIDFP SPTRLVDECL AAATGVSADD DPWNPSRVLW ALLGVVDDCL SEPWCAVLAK
HLGHGLPDRD PDDHRPGRRY ATASHLTDLF RSYAAQRPAM LVDWAGGRDT DGAGGPLDDD
LLWQAELWRR LREKIGSPAP AERLDSACAR LRAEPDLVEL PARLSLFGPT RLATDQIAVL
AALAVNRDVH LWLPHPSPTM WSSLSTADSV LARADDPTAL SVAHPLLSSL ARDVRELESR
LTRLDVDDLH HEGPAPRDSL LGCLQADVRD DRAPALAECT ADTSVQVHAC HGPARQVEVL
RECLLHLFED DPTLEPRDVL VMCPDVESYA PLIRAAFGQD VLGHPGHRLR VRLADRALHQ
TNPVLAVVST LLELADARVT ASQVLDLSAA APVRRRFRFG DDDLERIREW ATATGARWGI
GPRQRAAFGL GDFPQNTFTT ALDRILLGAA ADESDGEWLA LALPLDDVDS NDIDLTGRLA
EFVDRLDVAL RGLGGPQSVA DWSSALTRAL DLLVDVSAAD TWQLAQARRE LGSAMEHGGD
AVLRLSDVRA MLATRLAGRP TRANFRTGEL TVCTMVPMRS VPHRVVVLLG LDDEVFPRGV
SVDGDDVLAR NPLLGERDPR SEDRQLLLDA VMSASEKLLL FYTGADPVTG MSRPPAIPLS
ELLDAVAATV GSDALPGIVT RHPLQPFDAR NFRPEHPFSF DRAALAGARA AQHPPEPEPA
FLPAPLVPPP LGDVDLADLI AFLVHPTQAF LRQRLGLRVP DVDEDLADAL EVSPDPLARW
DLGQRMLVAR LTGVELADFR AAEWRRGTLP PFKLGESVLG GIEHAVESLV AVSGSVHVGR
AETVDVDVDL GSGRRLTGTV GGVHGSVIAT TTYSKLGPKH RLAAWAQLLA VAASDNETEW
TAVTTGRGAY SRPAWRSTLT APENALEELV RLVELRDLGL HAPLPIATGA SAAYAERRHG
GSSMEDAIEA ARKEWSSDFG DSRDRHITYV YGSSPGIDVL GDAVTIENYA RQLWAPLLAA
ETLAQP
//
