ID A0A239SQE6_9BURK Unreviewed; 1212 AA.
AC A0A239SQE6;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
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:SNU87691.1};
GN ORFNames=SAMEA4530655_03930 {ECO:0000313|EMBL:SNU87691.1};
OS Pandoraea sputorum.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Pandoraea.
OX NCBI_TaxID=93222 {ECO:0000313|EMBL:SNU87691.1, ECO:0000313|Proteomes:UP000215126};
RN [1] {ECO:0000313|EMBL:SNU87691.1, ECO:0000313|Proteomes:UP000215126}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC13161 {ECO:0000313|EMBL:SNU87691.1,
RC ECO:0000313|Proteomes:UP000215126};
RG Pathogen Informatics;
RL Submitted (JUN-2017) 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; LT906435; SNU87691.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A239SQE6; -.
DR STRING; 93222.NA29_23720; -.
DR Proteomes; UP000215126; Chromosome 1.
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}.
FT DOMAIN 897..1151
FT /note="RecC C-terminal"
FT /evidence="ECO:0000259|Pfam:PF17946"
SQ SEQUENCE 1212 AA; 133259 MW; C7578009D903DDDA CRC64;
MPGVPRSGDT AGYTRGADVG QACAPGMVSG HRPPAVTYDG VSFRICPMGF GAGHLLCLRT
VSLSRHARML HLFFSNRFTT LEAALLRDIA QAPDASPGAG NPFETETIVV PSVAVRRRLE
LDYADVFGVC ANVRLTYLAQ WLWDMAGKLL TVPESSPFAP DRLVWPLYQC LAQPWGESSP
RLAGYLAGAD DVMRFELADR LAHIYDQYLT YRPDWLERWQ SGEFISPGAS TTWGEVQRAD
EAWQSALWRQ VLAHLEIRER HPTLRAIDRI EQLTPETVPV GWPSRVCVFA LSSMPPLSMA
LLKAMSRLID VHLYVLNPCE SYWFDIVPPS RLSYLTQRDG KAHREVGHPL LAEWGRQTQS
HIDALYADLA PQAVEDRALF QPNPEPTLLA ALQNGILSLD DGRHGAPDGV AADGSVQVHV
CHSLARQIEV LHDRLLACFD EIPDLRPDDV LITVPDLGRA APLIDAVFGT ATPRIPYLVT
GLPPTRTNPV ARAFASILAL PQQRVAASSL VELARTEAVA QRYDLGGNVL DAIQNWLHSA
GARRGWRGDA LLRLDGTGQK SSDRTMTRAG ADIPPALERH TLGDAMMRLF LGYALPDDAM
PVDDWLPVGG IEGGRAELLG QLARLIDDLD MTAVSLQTER TGLAWRDQLL AMLELFFSDE
PRFADDVAEV RMAIEQIGTA IADGAPEVRV PVEVVARVLA DALDDPTRGG VPSGRVTFAA
IPSLRLLPYR VVCMIGMDDG VLPGRVRADE FDLMRALPQR GDRQRRDDER NLFLDLMLSA
QDRFLITYTG RSVRDNAPLP PSTVVDELLD FTGQLLAPAS QGFDLDEQRK ARETLVVLHP
LQPFSPAYFD GRKPSLYSYD VANGEAAQQL VGQLASPAPD AAELPFVHEP LPAIAQTHLT
LDDLLRFWRH PGRAWARDRL GLSLGDMLTE VEDEEPFVLD WSGRDALAAR LLPRLLRDDG
RDPQAQAAAI ERIANVSHEL PGGATGAVWR RRELGGLRAL ATQVRQAQAD GTQELLVTLP
LKPALPPSWT GSTDAIWHGD ATLCADCLLQ GRLAPVSRHG LVMYRYGSMR PSDLLAAWLA
HLALCAHLQQ PEHAGLEVAP RTLWYGEDET FALRPVDDAA ALLAQWVALY RLGQTRPLPF
FVRSAWKLAS TGKMTDTESA WSGSAFARGD ADDPYTKLIW RGVEDPLASP FDLLANTMFG
PMVQHLEIVE GA
//
