ID C0N788_9GAMM Unreviewed; 1069 AA.
AC C0N788;
DT 05-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 05-MAY-2009, sequence version 1.
DT 27-MAR-2024, entry version 50.
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:EEF79324.1};
GN ORFNames=MDMS009_1911 {ECO:0000313|EMBL:EEF79324.1};
OS Methylophaga thiooxydans DMS010.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales;
OC Piscirickettsiaceae; Methylophaga.
OX NCBI_TaxID=637616 {ECO:0000313|EMBL:EEF79324.1, ECO:0000313|Proteomes:UP000004679};
RN [1] {ECO:0000313|EMBL:EEF79324.1, ECO:0000313|Proteomes:UP000004679}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DMS010 {ECO:0000313|EMBL:EEF79324.1,
RC ECO:0000313|Proteomes:UP000004679};
RX PubMed=21478352; DOI=10.1128/JB.00388-11;
RA Boden R., Ferriera S., Johnson J., Kelly D.P., Murrell J.C., Schafer H.;
RT "Draft genome sequence of the chemolithoheterotrophic, halophilic
RT methylotroph Methylophaga thiooxydans DMS010.";
RL J. Bacteriol. 193:3154-3155(2011).
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; GG657899; EEF79324.1; -; Genomic_DNA.
DR RefSeq; WP_008291410.1; NZ_GG657899.1.
DR AlphaFoldDB; C0N788; -.
DR HOGENOM; CLU_007513_0_0_6; -.
DR OrthoDB; 9762834at2; -.
DR Proteomes; UP000004679; 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 CDD; cd22353; RecC_C-like; 1.
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:UP000004679}.
FT DOMAIN 783..1004
FT /note="RecC C-terminal"
FT /evidence="ECO:0000259|Pfam:PF17946"
SQ SEQUENCE 1069 AA; 122490 MW; 287B9B5BBA5E9150 CRC64;
MLKIVYSNDT GQLAAWLADH LLSEPLPPLQ PETIIVQSNE LSRWLSLRLA KTHQIAANLE
FPFPSAYIWQ LFRQLWPDVP LQSPYAKEPM AWRLFELLPQ AASLDGFEAV AAYLGGDDDD
LKRYELAEKI ADTFDQYLMY RPDWVQQWEQ GQATSWQGKL WQMLTADDPQ PMHRARLLQQ
LHDLLSHSDV VPPGLPNRIS IFGISALPPV YLEIVNLLAR YVDITLYYLS PSEHYWGDII
DPKKQQRQQL LLDFNEDEIE PGHPLLASLG KQGQAFFRQL QETQHLDDSC FVEPVGETML
SQLKRDIFEM ATDQPSVAVK DDTSISIQVC HSPMREMEIL HDQLLAMFEQ NPTLTPTDIV
VMTPDIDVYA PWIEAVFATA DKSRFIPFSI ADSSGQQESL LITTFYSFLQ LPQSRFDVES
ILAMLECPAV QRRFGLDDAA LNWIREWCQQ TRTRWGLDAN DKAALDLPDT ESNTWRAGLD
RLLLGYAMPL NEPDQPWRLF DGQLAMDGIS GERAHIVAAL CDFIDALDAW RQRLARQNTI
ADWQKQLNQC LDAFFNTEGL EETQFETEIT AIRTQLERLS SGAKQADFEQ TIGADLILSW
LQSHLQPVDN AHRFLGHGIT FCGMVPMRSI PFDVVCLVGM NDEVFPRRQP SVSFDLLAHD
HREGDRSRRD DDRYLFLEAL LSAQQTFYMS YVGASVVDNS EIPPSVLVSD LQDLLAERFE
TETTATILEQ IITKHPLQAF SRRYFDGNND QLFSFNASHC PTQEMLEQAN WFETPLPEAD
DSWRQVTRDQ LIRFFAHPTK FILRERLGIR LELDEEALES REPFALDGLE SWQLRQWIVD
ESLSQHSDEG LKPVVQATGM LPQGRLGDAW FEKESQTVDD FIEKLRPVLP EQGWITLAID
LNIDGFQING QLPQFSQQGL LRYRLAKKKG KDLIAAWIDH LILNILKPEG VTLQTHLILQ
DAEYVFLPVT GPTQILANLL KLYWQGCHLP LKFFDQASLA FAATYFGKKP EQKFKKAHDK
WSASGDFAGE GDDNYYRRLY SQPPLDDEFA ELAIQVYEPL QQHLQEGKL
//
