ID A0A158J8S4_9BURK Unreviewed; 1133 AA.
AC A0A158J8S4;
DT 27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT 27-SEP-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 ORFNames=AWB68_03601 {ECO:0000313|EMBL:SAL65268.1};
OS Caballeronia choica.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Caballeronia.
OX NCBI_TaxID=326476 {ECO:0000313|EMBL:SAL65268.1, ECO:0000313|Proteomes:UP000054770};
RN [1] {ECO:0000313|Proteomes:UP000054770}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Peeters C.;
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}.
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; FCON02000037; SAL65268.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A158J8S4; -.
DR OrthoDB; 9762834at2; -.
DR Proteomes; UP000054770; 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}.
FT DOMAIN 824..1071
FT /note="RecC C-terminal"
FT /evidence="ECO:0000259|Pfam:PF17946"
SQ SEQUENCE 1133 AA; 125054 MW; 793D79707ED59064 CRC64;
MLELFYSNRH ETLSQALFDD LAAFSMGSGD PFASQPVIVA SAAVRRRLEL DMAERFGICA
NVEFGYLAQW LWAQIGRVMT VPVHSPFAPD RLAWRCFRLL SGPSSGDSAR LRSYLDAADD
SMRYELARRI ATVFDHYLTY RPEWLTQWQQ GGSILATPGA GELDLRGPRL PGASEIQRED
ERWQAALWRA LLADLAAGAD QAGYDPTPPA YRFLAESVKL DLDAVMRAEW PERISVFALP
TMPPLHIALL RELSRWIDVR IYAINPCQEF WFDIVSVARV EQLEMKGELD YQEVGNPLLA
EWGRQTQAQL HMLQELTESA ASREASHFER NPAPSWLARV QNAILELGDP ADDSDDATEP
GIEVHVCHSL SRQLEALHDR LLGWFDSIEG LEPSDVLVAF PDLAAAGPLI DGVFGTAPAG
VANERRRIPY RITGLPPSQA NPVARVLLDW LALPERSVGA PDLIEWLRVD AIAARYGIDA
AALETAQAWL AAAGARRGLT PPEVSAEHVP SARHTFSDAL TRLFLGYALP DGGAPVDEWL
PVEGANGSDA ELLGRLTRFI DDIDAFAERV AIPRTPRAWG ELMQDALERF FDPGLAFSDS
IADVRGTLDA LIVAMREGAG DAEVAAAVLR TAFTDALDDP ARGGVPWGGV TFSSLTSLRG
LPYRVICLLG MDDGMLPSLA RADEFDLMAK FGKLGDRQRR DDERNLFLDL LLAARDRLLI
AYTGRSIRDN AALPPAALID ELLDYLAEAS AGAHASPGEL ADARARFVFE HPLQPFAPEY
FEPGAPLFTY EPERAELART LALGRPEAPV TFFAEPLPPE DETEPVAFDD FVRFWRHPAR
ALLRDRLGIA LFDAESELDD TEPFELDFSG RDALAERVLP ALLDMTEDGE TAARERARRV
ARASPEMPGG ATGGVWQSQE LHALHQLANR VRVATEEGTT RLPFTLDIAP RWPDTAGVAL
FGAHDDRLSG DAAKPLQLHG TLNLLTPQGQ VIYRYDAPRA RDYLSAWLAH LAYCAALPDG
PRRTVWHGRG AQSSNFELTP VDDPGRHLAM LAALYRAGRR MPLRFFPKSA WLKMTEGDSK
AEDAWLSERK RSESDDAALR IAFRGADLSL DETFAALAKL VFEPLIQHLR SDA
//
