ID A0A3N7AA67_9BACT Unreviewed; 1060 AA.
AC A0A3N7AA67;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 18-JUN-2025, entry version 23.
DE RecName: Full=RecBCD enzyme subunit RecC {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=DBR32_06780 {ECO:0000313|EMBL:RQO31650.1};
OS Taibaiella sp. KBW10.
OC Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia; Chitinophagales;
OC Chitinophagaceae; Taibaiella.
OX NCBI_TaxID=2153357 {ECO:0000313|EMBL:RQO31650.1, ECO:0000313|Proteomes:UP000279469};
RN [1] {ECO:0000313|EMBL:RQO31650.1, ECO:0000313|Proteomes:UP000279469}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KBW10 {ECO:0000313|EMBL:RQO31650.1,
RC ECO:0000313|Proteomes:UP000279469};
RA Lee F., Williams K.B., Levin M., Wolfe B.E.;
RT "The microbiome of the planarian worm Dugesia japonica mediates outcomes of
RT regeneration via indole production.";
RL Submitted (APR-2018) 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 -!- SUBUNIT: Heterotrimer of RecB, RecC and RecD. All subunits contribute
CC to DNA-binding. {ECO:0000256|HAMAP-Rule:MF_01486}.
CC -!- MISCELLANEOUS: In the RecBCD complex, RecB has a slow 3'-5' helicase,
CC an exonuclease activity and loads RecA onto ssDNA, RecD has a fast 5'-
CC 3' helicase activity, while RecC stimulates the ATPase and processivity
CC of the RecB helicase and contributes to recognition of the Chi site.
CC {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:RQO31650.1}.
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DR EMBL; QAJI01000003; RQO31650.1; -; Genomic_DNA.
DR RefSeq; WP_124635529.1; NZ_QAJI01000003.1.
DR AlphaFoldDB; A0A3N7AA67; -.
DR OrthoDB; 9762834at2; -.
DR Proteomes; UP000279469; 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 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};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000256|HAMAP-Rule:MF_01486};
KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_01486};
KW Nuclease {ECO:0000256|ARBA:ARBA00022722, 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:UP000279469}.
FT DOMAIN 787..996
FT /note="RecC C-terminal"
FT /evidence="ECO:0000259|Pfam:PF17946"
SQ SEQUENCE 1060 AA; 123214 MW; CD09C6475863B09B CRC64;
MALEIYISNH IRSLSAAMID DFKHHGAPVL QPYYIITQTI GMNNWLVVNT ANQLGIAANM
KFLKPADILW EVYGLLGGQS YYKINRQNID WLIYAVLSSA AFRNRFPKQA AYYIEEGVEQ
DVKKWEFAAK IADLFDQYQI YRNHIMQQWN TQAIEDIDPV MQWQAFIWQA IKSKSGEAFP
DITAIHHFIL AELKHPVQQE RIRQAMPVLY LFGLSILTPF HLHIFYELSR VIDFKCYLVN
PAPDHYWFED EQEQQIFLKQ FKGKNVAHLN VGNALLTSWG KVLQNTYRLL FRSDEFINAV
NELPITQPAQ GSLLQQVQYD IFYNKTENIQ FTEAQLRDKT ISITAHYSIP REVEVLYNYL
LDAVIQQTYG AITERDIVVM VSDINAYAPY IRAVFDNAPH KFSYSIIDES IANGDTVISA
LILLLQVNEY NFTAELVLQL LESEHIRRRF GIYKMEYIRK IVLAANIRFG IDNDYQEGID
DTYLVSWKYG LQKLMFGMCF DESQWYVAGR DVYTTDIADN IEDMHQITAL SSFVQALEET
LKRRKVNKNL SDWKTYVDDL IMGFVIEEEQ EKDEQYWDLI TRFKQNEIID AYLDDTKISY
EVFSKRLLNA ISGEQQSLNF MNRGITFCSP LPFRSIPFKI IALLGLNFDA FPRKESYVDF
DLMIQKPMLG DRNIRNNDKH LFLESVLSAE SALYLSYIGR SIKDNKPLPP SVLIDELLDY
IQIGYRATGA GKLRDLLIQQ HPLHSFSKVY NQADRALIPN YLIQEAKPFP ITFKATEAQV
MMQEQVFSLK DLLQFFTKPT QYYYNKVLQV YINDTIAQVA AHENFTLDSL QRWAVRQALI
EGKIHGDEAE RLKALYANAI LPLRNVAPTF IAEQDEAITQ IYQQYQDFLK DTAPQSITVM
YTCDQYVFTG IIDNILDGNL IDYALKASKR SLKNKVQLFL KYLLAKATEQ VAAAFLITLD
GILALKPCTK LVAQETLEVF LRFFIKHHKA MILFPMDLYE EKLHADNYLT KLEESIQQNR
YYDNYIIHAL PFIDEAAQKE YFTDFKDLLD QYILPAFDHA
//
