ID A0A257EFB9_9BURK Unreviewed; 1197 AA.
AC A0A257EFB9;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
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:OYU12089.1};
GN ORFNames=CFE38_09770 {ECO:0000313|EMBL:OYU12089.1};
OS Comamonadaceae bacterium PBBC1.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae.
OX NCBI_TaxID=2015580 {ECO:0000313|EMBL:OYU12089.1, ECO:0000313|Proteomes:UP000216161};
RN [1] {ECO:0000313|EMBL:OYU12089.1, ECO:0000313|Proteomes:UP000216161}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PBBC1 {ECO:0000313|EMBL:OYU12089.1};
RA Kojadinovic M., Villain A., Puppo C., Fon Sing S., Prioretti L., Hubert P.,
RA Gregori G., Zhang Y., Sassi J.-F., Claverie J.-M., Blanc G., Gontero B.;
RT "A metagenomic investigation of the 'star' freshwater diatom Asterionella
RT formosa and its bacterial cohort.";
RL Submitted (JUN-2017) 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:OYU12089.1}.
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DR EMBL; NKIP01000007; OYU12089.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A257EFB9; -.
DR Proteomes; UP000216161; 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 877..1117
FT /note="RecC C-terminal"
FT /evidence="ECO:0000259|Pfam:PF17946"
FT REGION 832..861
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 843..861
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1197 AA; 132250 MW; E7CFBF212A687015 CRC64;
MTTSSIVPGF LALHSHRSEV LAETLSAWLM RQPLAALEQE VVLVQSNGMA EWIKMALAGQ
GGPGGGVCAA TRVELPSRFL WRTYRQVLGA SNVPPDSPLD KLPMTWRLMA LLPACVGDPV
FQPVAGYLRG KRPEPEPERL LQLASRLADL FDQYQIYRPD WLQDWAEGRD VLRRQSGQPV
RPDDKAGLLP EDQRWQAELW RRVLATLTDA EKQATRPALH LRALALLQSG QALASPVARR
VSVFGMSHMP SQLLDMLAAL SAHSQVLLAV PNPCQHHWGD IMDGRDALRA ERRRHAYKKD
NLSTVDFEQM HLHAPTLLAA WGRQGRDFIR QLDAFDDLQA AQERHPGVRL DLFDDAPGAD
GRRLLTQLQN RIRDLKSSQE PVEAALDSSD DSLVFKVAHS PVRELEVLHD QLLLWFHAQP
EVSPRDVVVM VPDIEVMAPA IRAVFGQYKR GDARFIPYDI ADLGAQATSP LIHAVEWLLA
LPQQRSRMSE WVALLEVPAL AARFGLKPEQ LPTLTRWMVG SGIRWGLSAP HRAGLGLDTC
ADDNSALFGV QRMLMGYACG ADPVPDAPGL AGIDPYAEVG GLDAELAGAL AHLLQALMDW
WQQCASEATP LQWAQRGRAL LAALFKAQDD TDRNALSALD QALNDWTRSA DQADFAQAVP
LTVARAAWME ALKVPKLEQR FRAGGVTFCT LMPMRAIPFA RVCLLGMNDA DYPRRSPRAD
FDLLGLPGLS RPGDRSRRDD DRQLMLEALL SARRTLYVSW SGRSVRNNSE QPPSVLVSQL
RDEIDALWGE GTAKRLTTVH PLQPFSRQYF EQDSTLQTFA LEWRAAQTDA NPGDAAAALN
GNLNGNLHGT TNTQPSNPVN DPIQLEPLQS ATGTPVITLG QLGRFLQKPV GAFFRERLQV
NLDVERSELP DEELFGLGGL DLYQLLDHEL QHVSTDLTPH NMPSYTQRVV QRLRQAGAMP
LAGVGELEAH KLSLKLEAML GAALQERQAY PQPAPRVLID LAHPQVHLQD ALSGVLSRHG
PAWMLLSLRA NALADLKGKP PKALPAKLID VWLISLASAA MGQPLVCVVV GANAVLRVPP
PEPQEARAQL QVLLDTWTEG MRWPLPVPPV LALQWLKDPD NLNALHDLYE GSSHVRAERN
KDPALARTYP TLSDVLDSGH FERIAQAVYA PLRDWAAHIV VEALPEDSAQ DEQEELS
//
