ID F4H557_CELFA Unreviewed; 1138 AA.
AC F4H557;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 60.
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 OrderedLocusNames=Celf_2538 {ECO:0000313|EMBL:AEE46663.1};
OS Cellulomonas fimi (strain ATCC 484 / DSM 20113 / JCM 1341 / NBRC 15513 /
OS NCIMB 8980 / NCTC 7547).
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Cellulomonadaceae;
OC Cellulomonas.
OX NCBI_TaxID=590998 {ECO:0000313|EMBL:AEE46663.1, ECO:0000313|Proteomes:UP000008460};
RN [1] {ECO:0000313|EMBL:AEE46663.1, ECO:0000313|Proteomes:UP000008460}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 484 / DSM 20113 / JCM 1341 / NBRC 15513 / NCIMB 8980 /
RC NCTC 7547 {ECO:0000313|Proteomes:UP000008460};
RG US DOE Joint Genome Institute;
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Chertkov O., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA Kyrpides N., Ivanova N., Ovchinnikova G., Pagani I., Mead D., Brumm P.,
RA Woyke T.;
RT "Complete sequence of Cellulomonas fimi ATCC 484.";
RL Submitted (APR-2011) 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}.
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DR EMBL; CP002666; AEE46663.1; -; Genomic_DNA.
DR AlphaFoldDB; F4H557; -.
DR STRING; 590998.Celf_2538; -.
DR KEGG; cfi:Celf_2538; -.
DR eggNOG; COG1330; Bacteria.
DR HOGENOM; CLU_007513_1_0_11; -.
DR Proteomes; UP000008460; Chromosome.
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}; Reference proteome {ECO:0000313|Proteomes:UP000008460}.
FT DOMAIN 826..1046
FT /note="RecC C-terminal"
FT /evidence="ECO:0000259|Pfam:PF17946"
SQ SEQUENCE 1138 AA; 121206 MW; 6DC90D42342C5BC8 CRC64;
MTAVRDTTDG TDAGAMHVHV AERADVLVEE LARVLAEAPA DPFTPDVVLV PTRGVERWVA
QRLSHRLGQA GGGDGVCANV RFSSPARAVA DVLAAVVGAA PEDDPWAPEQ LAWHVLGVLD
DHADDPLLAA PVHHLGARDD AMRQGRRFGL AQHVAHLLAA YDVQRPTVVR AWADGRDEDG
AGAPLPADLA WQAHLWRLVR ARAAVPSPAQ RIDEAVAMLA SAPDTVSLPA RLSVLGATRL
PDAHVRVLDA LARHRDVHLW LPHPSLRLWE RVGAASPPAG RRRDLPPVAE HPLLASMAGD
AVELQIRLRA VDAQVILHAA ADPPATALGH LQRRLRADAA PTEAAAQRPV VDVGDRSVQV
HACHGRSRQV EVMREAVLGL LADDPSLEPR DVVVMCPDVE AFAPLVSAAF GAGSTGGTQW
EHPGRSLRVR VADRAPARAN PLLAFISTLL DLAASRVTAS AVVDLAGLAP VRHRFRLDDA
DLDRIRAWAL ESGVRWGEDV ARRDRFRLGS VPQGTWSGAL DRLLLGVAMA EEDQRYVGAV
LPVDDVGSTD VDLVGRLAEL LDRLTAVLHA LDGTRPATAW LDTLTAALDL LTDVAPADRW
QQVEALRVLG EVRTSAAQHD RDLRLPDVVA VLEPHLRGRP TRAGFRTGAL TVCSLEPMRA
VPHRVVVLLG LDDGAFPRGH GRDGDDLLAR EPLVGERDRR AEDRRLFLDA VTSATDHLLV
VHSGADERTG ATRPAAVPVG ELLDALDDAV VFPDGLPARE HVVVHHPLQT VDERNFVGGA
LGRPGPFSFD ALDLAAARAG RAVRAGRRPF LVEPLPPVEP LDDVGDVADV LTHPVRAFVR
RRLRAMPPGD APQLDDRLPL QLDGLERWEI GDRLLDAALT GADLTTAVAA ERRRGHVPPG
SLGTATLDDV ARSVVPVLDA VRTLRVQPGR TLDVALTLPD GRPVTGTVGP CHGDTLVRAV
YSRLAAKHRL RAWVLLLAAA VAEPGALARA VTVGRGPGGG ARIAELQAPA PELAASLLGQ
LAAVADQALC EPLPLPLAAS CAYGSARWDG QPVHDALAAA RKELGTLDEA RRGAGGFDVV
EPSHALVWGE GFSLDTIAGT ATPVDLARWP EDVTRFGALA RTVWDALLDH ETVAMVVA
//
