ID A0A1A1WD76_9MYCO Unreviewed; 1089 AA.
AC A0A1A1WD76;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 32.
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 ORFNames=A5730_17370 {ECO:0000313|EMBL:OBF04803.1};
OS Mycobacterium sp. ACS4054.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=1834119 {ECO:0000313|EMBL:OBF04803.1, ECO:0000313|Proteomes:UP000091876};
RN [1] {ECO:0000313|EMBL:OBF04803.1, ECO:0000313|Proteomes:UP000091876}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ACS4054 {ECO:0000313|EMBL:OBF04803.1,
RC ECO:0000313|Proteomes:UP000091876};
RA Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL Submitted (JUN-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
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}.
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:OBF04803.1}.
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DR EMBL; LZHV01000058; OBF04803.1; -; Genomic_DNA.
DR RefSeq; WP_067902823.1; NZ_LZHV01000058.1.
DR AlphaFoldDB; A0A1A1WD76; -.
DR STRING; 1834119.A5730_17370; -.
DR OrthoDB; 9762834at2; -.
DR Proteomes; UP000091876; 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:0000724; P:double-strand break repair via homologous recombination; IEA:UniProtKB-UniRule.
DR Gene3D; 1.10.10.160; -; 1.
DR Gene3D; 1.10.10.990; -; 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}.
FT DOMAIN 793..1019
FT /note="RecC C-terminal"
FT /evidence="ECO:0000259|Pfam:PF17946"
SQ SEQUENCE 1089 AA; 119832 MW; 553FDE979A9C8CB7 CRC64;
MSLHLHRAER TDLLADGLGA LLANPPTDPF AEELVLVPAR GVERWLSQRL SHVLGRARGG
DGVCGGVAFR SPGSLIAELT GTADEDPWSA DAMAWPLLRV IDCSLDEPWC RTLATHLGHF
APTETEAELR LGRRYAVARR LAGLFASYAR QRPRLLADWL AGDTGDLDPD LAWQPELWRA
LVAAVPADPP HIRHQAAVAR LRDGRTGLPE RLSLFGHTRL ARTDIELLDA VSARHELHLW
LPHPSDQLWR ALADTRGTIP RRLDTSHRGV GHPLLATLGR DLRELQRGLP ADPQTDEYLP
GPDRPDTLLG WLQSDIAANA VRPQGRNLAS TDRSVQVHNC HGPARQVDVL REVLLGLLQD
DPTLEPRDIL VMCPDIETYA PLIVADFGLG DVVHGAHPAH RLRVRLADRS PLQTNPLLGI
ASQLLALAGS RATASEVLDF AEAAPVRARF GFTDDDLEAI TRWVRQANIR WGFDQEHRRP
YHVDFVHNTW RFGIDRVLAG VAMSDDSHAW IDATLPLDDV SSNRVQLAGQ FAEFVARLQR
VVDSLTGARP LRDWLAALAG GIDLLTQVDD ADSWQAGQLQ REFAATLADA GVRADTVLRL
PDIRALLDGR LAGRPTRANF RTGTLTVCTM VPMRSVPHRV VCLVGLDDGV FPRLGVVDGD
DALARDPMTG DRDIRSEDRQ LLLDAIGAAT EKLVVTYTGA NEYSGQARPP AVPLAELLDT
LDITTMGKVR DRVVVAHPLQ PFDVRNVIPG GLVPEVPFSF DPTVLRAARV ASGERRDAPK
FISGPLPPAP ADDVIVADLV AFFKDPVKGF FRALEFTLPR DVDGVQDAMP VDLDGLEEWT
VGDRMLGDML RGWAPDDARQ AEWRRGTLPP GQLGWRAATE IRDQAALLAA AAREHRRADA
RAYDVDIDLG GGRRLTGTVS PVYGERLVSV TYSRLDGRHL LESWIPLLAL TAHDPGRDWS
AVCIGRRKRG TAPRVEALGR PHDDAAAALR ELVAIYDAGR REPIPLPVKT SYAWAAARHC
GDDPLREAEH RWKWEREEPA HLRAWGKNAR LADLMRPVRP GEECDGEDNR LGAYAARVWL
PMLCAEGKP
//
