ID A0A3N0CBA7_9ACTN Unreviewed; 1083 AA.
AC A0A3N0CBA7;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 22.
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:RNL60599.1};
GN ORFNames=EFK50_20000 {ECO:0000313|EMBL:RNL60599.1};
OS Nocardioides marmoriginsengisoli.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Nocardioidaceae; Nocardioides.
OX NCBI_TaxID=661483 {ECO:0000313|EMBL:RNL60599.1, ECO:0000313|Proteomes:UP000267128};
RN [1] {ECO:0000313|EMBL:RNL60599.1, ECO:0000313|Proteomes:UP000267128}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Gsoil 097 {ECO:0000313|EMBL:RNL60599.1,
RC ECO:0000313|Proteomes:UP000267128};
RA Li F.;
RL Submitted (NOV-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 -!- 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}.
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:RNL60599.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; RJSE01000009; RNL60599.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3N0CBA7; -.
DR OrthoDB; 9762834at2; -.
DR Proteomes; UP000267128; 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}; 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:UP000267128}.
FT DOMAIN 789..1010
FT /note="RecC C-terminal"
FT /evidence="ECO:0000259|Pfam:PF17946"
SQ SEQUENCE 1083 AA; 117418 MW; 433F03D8D033C6D4 CRC64;
MTFLVHRAER ADLLAEGLAD LLRTPLPDPF ARELVIVPAR GVERWLSQRL SHRVGNGGGR
GDGVCAGVDF RSPGSLIAEV LGTRDEDPWS PEALMWPLLR VIDDALGEPW AKVLAEHLGH
DVPGEEGDLR RGRRLAVARR LARLFASYAV QRPAMLADWE AGGCGDGGGG DLPDDLAWQP
ELWRRSVAAI DLPSPVVRHA EVVADLRARR LTLDLPARIS LFGHTRLSST EAELLAALGT
DREVHLWLPH PSAPLWEALR SQPLTGWRRD DDSHLQVGHP LLAAMGRDIR ETESALLTAG
AVEAPAPPVL PRPATVLGHL QGDIAADRAP TPCEHQDASV QVHACHGPAR QVEVLREVIL
GLLAEDPTLE PRDILVMCPD IDEYAPLISG AFGLGDAVAG SHPGHQLRVM LADRSAQQTN
PLLAVLSQLV DLADGRAEAS RVLDLLAAEP VRRRFGFSES DLETMTSWVA ESGIRWAWDV
EGRQRYGLAD FPQNTWRFGL DRILTGVALS DDSGLWLGPT LPLDDVSTTD ISLAGRFAEA
IDRLAALTAE LGGEHDVTHW MDVLAGGVEQ LAQVPRDDEW QVAQVRRELA GLGVAAGDRL
SLRLADIRAL LGSQLAGRPT RANFRTGTLT VCTMTPMRSV PHRVVCLLGL DDGVFPRGGS
LDGDDVLARL PRVGERDVRS QDRQLFLDAI MAATDTLVIT YTGFSESSGL ERPPSVPLRE
FLDVVEPTSP AFEVRRHRSQ AFHPEYLDAA NGPAFSFDPD AARAARSAAG TRTPVAALAS
VVAAPAPAAD IDLAELISVI GNPVRGFLRF RLGVDLPREE DEVSDSLPVE LGGLARWQVG
DRMLAEMIAG RDPADAMQAE WRRGTMPPGR FGWRQTAQLA AAAAPITEMF AASTQGIAAK
AYDVDVDLGD GRRLLGTVPD LYDSRLVRAT FSRLGARHRL DTWISLVALS ASVRGDWVAR
MIGRSAAGDD PVRATYGVVV EPAAVLADLV AFYDLALQRV LPYAAETSRL AARSATSSRP
GWMVQRELGD QWRKDNAGIE MSTAWGHRPS WDEVTAEPGT SGRPLFDELA DRVWKHALTA
EVE
//
