ID A0A4Q0MB51_9SPHI Unreviewed; 1064 AA.
AC A0A4Q0MB51;
DT 31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT 31-JUL-2019, sequence version 1.
DT 18-JUN-2025, entry version 17.
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 ECO:0000313|EMBL:RXF70049.1};
GN ORFNames=EKH83_09165 {ECO:0000313|EMBL:RXF70049.1};
OS Arcticibacter tournemirensis.
OC Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
OC Sphingobacteriales; Sphingobacteriaceae; Arcticibacter.
OX NCBI_TaxID=699437 {ECO:0000313|EMBL:RXF70049.1, ECO:0000313|Proteomes:UP000290848};
RN [1] {ECO:0000313|EMBL:RXF70049.1, ECO:0000313|Proteomes:UP000290848}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R1 {ECO:0000313|EMBL:RXF70049.1,
RC ECO:0000313|Proteomes:UP000290848};
RA He J.;
RT "The Draft Genome Sequence of the Soil Bacterium Pedobacter tournemirensis
RT R1.";
RL Submitted (DEC-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:RXF70049.1}.
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DR EMBL; RXOC01000005; RXF70049.1; -; Genomic_DNA.
DR RefSeq; WP_128769122.1; NZ_RXOC01000005.1.
DR AlphaFoldDB; A0A4Q0MB51; -.
DR Proteomes; UP000290848; 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};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000256|HAMAP-Rule:MF_01486};
KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_01486, ECO:0000313|EMBL:RXF70049.1};
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:UP000290848}.
FT DOMAIN 778..989
FT /note="RecC C-terminal"
FT /evidence="ECO:0000259|Pfam:PF17946"
SQ SEQUENCE 1064 AA; 121825 MW; 0CFB7FAB65280054 CRC64;
MALYLQVSNS LSQLAKKLCS DLQAQGNQVF QPYYIVTQTE GMNNWLKLQL ADSMGIAANY
RFLRPNDIVF KIYQLLGGRY SQSLSPENLS WVFYKLLNDK EFKERFGNIA AYFGEGSDKE
VKRLALAEKV ADLLDQYQIY RPEMVQEWNR ASIADVKDDE WQKFLWIRAK ELTKDRLPDR
TLMGQFILQA LQQGDRIDDL QRGMPAVHIF GLSVITSYHL QLFSELSRHI DFSFHILNPA
PSEYWFEDRS EKQMLFLKKK GLVNADEPVP GNPLLTSWGR LIQNTFSLFF QNDALINAYD
EVGIEEPGDK TLLQCIQQDI FYNRNNADRR LISPDHIRDG SVTINACYTA AREVEALYNY
LVHLIDKHGE VLSARDIVVM VSDIDAYAPY IRAVFNNAPY SFHYTIADES FAANDSLSNA
LQSVLRMNRQ TFKAEEVLQL LDSGYIRKRF AISDLNLIRK AVDRANIRFG MEGDKDDDTI
YVSWKYGIER IIYGICMSGD EEFKDEDGTG FYPLELTEGH ASAELIRFCH FVQVLMDSVK
ERERSRSVSE WVGYVESVLY DLVSEPGEDA GEDYDILLKQ LENYNALNEL ITENISYEVF
SHNFLQSISS ATRSSSFATG GVTFCSLIPM RSIPFRVVAL LGLNFDKFPR KENPSNFNLM
EREKRKGDRN IKENDKHLFL ETILSARDYL YISYIGQSTK DNTVLPPSAL VDELVDYIEA
GVAAEEHVPI VIRQPLHSFS RKYNLADDRL YNYLNYKQGN GETDVQGERK DPPAFDPEVV
SLDALVNFFK NPVKGYYNDV LGIYFNNDEV LLSDTELFEL DGLSKWSLKQ DLLLLPPEDI
EILKDKLVKK GVLPLKNMAD IALRDVEAEV SAIRGLFNEC TGGMPGRSLQ VEVNVGDVLL
KGRVNRIFGD RMICISWSRK ETKYLLEAYL RYLAVRASGT LVDLYFISAK EGRVFEASAI
TSADALSRLE ELLDLYKQGH KDMLAFFPDF EIEPPKLADL DEAVFQSIAE KKLNSYPFPC
TDAYVMREAV NGFYKREGVF EEYKMAAEML LLPLAEIFPG YYQN
//