ID A0A4Q8U822_9ALTE Unreviewed; 1103 AA.
AC A0A4Q8U822;
DT 31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT 31-JUL-2019, sequence version 1.
DT 18-JUN-2025, entry version 22.
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:TAP37370.1};
GN ORFNames=EYS00_16665 {ECO:0000313|EMBL:TAP37370.1};
OS Alteromonas sp. KUL49.
OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC Alteromonadales; Alteromonadaceae; Alteromonas/Salinimonas group;
OC Alteromonas.
OX NCBI_TaxID=2480798 {ECO:0000313|EMBL:TAP37370.1, ECO:0000313|Proteomes:UP000293649};
RN [1] {ECO:0000313|EMBL:TAP37370.1, ECO:0000313|Proteomes:UP000293649}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KUL49 {ECO:0000313|EMBL:TAP37370.1,
RC ECO:0000313|Proteomes:UP000293649};
RA Ohnishi K., Kobayashi S., He C.;
RT "Draft geome sequence of Ulvan-utilizing strain KUL49.";
RL Submitted (FEB-2019) 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:TAP37370.1}.
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DR EMBL; SIHN01000010; TAP37370.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A4Q8U822; -.
DR OrthoDB; 9762834at2; -.
DR Proteomes; UP000293649; 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; 3.40.50.10930; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 1.10.486.10; PCRA, domain 4; 1.
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:TAP37370.1};
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:UP000293649}.
FT DOMAIN 808..1023
FT /note="RecC C-terminal"
FT /evidence="ECO:0000259|Pfam:PF17946"
SQ SEQUENCE 1103 AA; 124438 MW; B0279B3C159F7D5F CRC64;
MFIRDVFELL ALYPSNKIEH LSFLLATLLE QQQSSIFESQ TILVESPGMQ HWVNMELAKH
HGVAMNLDFP LPVRFMWNAA RAILGEDTIP RQSPYRREIL TWRIDELIQR SDIQNKPEFS
EVNAYWQTIE NSQERGVQRL QFSTAMADVY EQYLMYRPEW LLAWEAGESL SVQNSMEPWQ
GELWRELVSQ NPLHPAGLLK SALSSLQQGT VPEGLPSSVI VFAINTMAPQ FVQLLDALST
HIDIHIFHLN PSVNYWGDAK SRGEQARVLR EQGIEKWMSE AQSHPLLGNL GKQGRELFNL
LTELNTFEVS AFDIPPLDEE HTSNTLLQRI QIDILHGELS DAPVNADDSL TIVSAHSALR
EVQLLHDHLL HWLSQDPDRS PSDILVMCPA IENYAPFVDS IFQRVGTFAP TREVPRLPCS
IADRSPLDAN PIVSAFISLL SLPDSRFGVV DIVDYLQLPA VQRKFEFTQD DVAQMTVWLH
KAHVHWGLDA HHKALMSETE DTSIQDTYTW WWGLKRLLLG MAATDSETLV NGLLTVPDVE
GQNTLVLGKL IDLVSALQQQ ARLLNQNRTA SEWHRCLVDL LNTCFDADVK EQSTWDMLTN
VCADLELRCE EAGYTSELQL SQVRMLLLNR FSSPDAGNHF MTGQVTVCSM LPMRSIPFKK
VCILGLNDGE FPRQSTPMGL DLMAQSSRKI GDRSRRLEDR YLFLEALISA RDSIYLSYQG
NDVRNNNERQ TSLVLGELLD VLINGYGLLK STLVTQAPLH PFSEGNFTRP IPSYEAGWLR
LTESMRHQMG TSESLDEIET VVLNDVYQVS DIANAFNDPL SYFGRNVLGV YLTQPHIELD
SSEPFDVNSL VRYQVVDALI DDVVGPVQHN ASFDAIELAT MRGDIPQTPA TEVTTGVWKE
ATTALHEAIG DLPQELTQVS WQGEQFQIQG VGWLADDSTI NLCPTAISDK RGFAFYLSQL
CFCASGIQQP LDVFFPVWEK GEYNIKVARY APVEPQIAKD MLSIVEELFS QLHRCPTPIY
LSLITELVKK AGKNDVFEYL DTAQAYADLA NWQTQSNQSA NIANDNPYLS WLLPSGISME
HINHAPIFTL LSHVASIKKV VKL
//
