ID A0A161IE53_9MICO Unreviewed; 1126 AA.
AC A0A161IE53;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
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:ANC31597.1};
GN ORFNames=I598_2054 {ECO:0000313|EMBL:ANC31597.1};
OS Isoptericola dokdonensis DS-3.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales;
OC Promicromonosporaceae; Isoptericola.
OX NCBI_TaxID=1300344 {ECO:0000313|EMBL:ANC31597.1, ECO:0000313|Proteomes:UP000076794};
RN [1] {ECO:0000313|EMBL:ANC31597.1, ECO:0000313|Proteomes:UP000076794}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DS-3 {ECO:0000313|EMBL:ANC31597.1,
RC ECO:0000313|Proteomes:UP000076794};
RA Kwon S.-K., Kim J.F.;
RT "Complete genome sequence of a soil Actinobacterium, Isoptericola
RT dokdonensis DS-3.";
RL Submitted (JAN-2016) 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; CP014209; ANC31597.1; -; Genomic_DNA.
DR RefSeq; WP_068202864.1; NZ_CP014209.1.
DR AlphaFoldDB; A0A161IE53; -.
DR STRING; 1300344.I598_2054; -.
DR KEGG; ido:I598_2054; -.
DR PATRIC; fig|1300344.3.peg.2063; -.
DR OrthoDB; 9762834at2; -.
DR Proteomes; UP000076794; 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; 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:UP000076794}.
FT DOMAIN 815..1044
FT /note="RecC C-terminal"
FT /evidence="ECO:0000259|Pfam:PF17946"
SQ SEQUENCE 1126 AA; 120423 MW; 009B47033E174E1E CRC64;
MLHIHRSERA DALVAPLAGV LATPPDDPFT PDVVAVPTRG VERWLAQRLS HLLGDGGTGA
GVCANVDFGS PTRLVASAVA AVTGVEPDDD PWRRERLVWP VLQVVDASLD EPWAAPLARY
VGGPDDVVRR SRRLALAQRA ADLFTAYSRQ RPSLPVAWRD GDLTDGAGAP VPPDLAWQPE
LWRRVRDLLA APSPAEVITD AVAVLERDPG VVDLPARLSV FGPTRLPQDE LRVLRALARH
RDVHLWLPHP SPALWNEVSA LPARPGDARR SGLPAVALHP LLTSTARDSV EMQLRLTGAF
DADEADVVET HHPAPAPPAT LLGALQTSLR TDTPDAADRA VLDPRDRSVQ VHACHGRSRQ
VEVLREALVG LFAADPTLEP RDVVVLCPDV EAFAPLITAT FGAVPDTAVA VHPGQRLRVS
LADRGAGATN PVLGVLSTLL RLADGRVTAS EVLDLAASPP VRRRFRLTDD DLDRWRGWAV
EVGVRWGEDG TRRERFGIDP RVRQGTWDAA LDRVLLGVAM AEEDARFVGP ALPLDDVGST
DVETAGRFAE LVARLSELLA ELAGVRPLGD WLDTLDRAVT LLTDPAPDDA WQTVQARRVL
VGVRTAGETH AGSRLALEDV RAVLADRLAG RPTRSGFRTG ALTVCSLEPM RAVPHRVVCL
LGMDDAVFPR SASPDGDDLL ARDACVGERD RRTEDRQIFL DALGAATEHL VVLHTGADER
TGAARPPAVP VAELLDALDR LAVTADGGAA REQVVVRHPL QAVGEPNFVP GALGTRGPFS
HDPAALAGAV AGRADRATPG LLVTEPLPVA PPGGDEVDLD DLVAVLEHPA RWFVTKSLGV
RLTQDADEVD DRLPLAADPL VGWGAGDRIL TATLAGADPQ QVFQAEWRRG QLPPRRLGHA
ALSNVMERVQ PVHATASNAM STGEPRAVDL SVTLPSGATV VGTVPGVHGE RVVRAEYSKL
APKHRLRSWV QVLALAAAHP GTAWETGTVG RAPVSAPRAA WSRIPAPDHA EAVRLLDDLV
RLRAEAARGP LPLPPEAAHA YAVTRDRGSV DVVAALREAA YTWGGGFEKQ DPFHVLCWGP
GAALDAFAGT PTDDDRRDLP GETTRFGALA RRVWDPLLER EEKGTS
//
