ID C0ZQ87_RHOE4 Unreviewed; 1093 AA.
AC C0ZQ87;
DT 26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 26-MAY-2009, sequence version 1.
DT 27-MAR-2024, entry version 78.
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:BAH31565.1};
GN OrderedLocusNames=RER_08570 {ECO:0000313|EMBL:BAH31565.1};
OS Rhodococcus erythropolis (strain PR4 / NBRC 100887).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Rhodococcus; Rhodococcus erythropolis group.
OX NCBI_TaxID=234621 {ECO:0000313|EMBL:BAH31565.1, ECO:0000313|Proteomes:UP000002204};
RN [1] {ECO:0000313|Proteomes:UP000002204}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PR4 / NBRC 100887 {ECO:0000313|Proteomes:UP000002204};
RA Takarada H., Sekine M., Hosoyama A., Yamada R., Fujisawa T., Omata S.,
RA Shimizu A., Tsukatani N., Tanikawa S., Fujita N., Harayama S.;
RT "Comparison of the complete genome sequences of Rhodococcus erythropolis
RT PR4 and Rhodococcus opacus B4.";
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:BAH31565.1, ECO:0000313|Proteomes:UP000002204}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PR4 / NBRC 100887 {ECO:0000313|Proteomes:UP000002204};
RX PubMed=16423019; DOI=10.1111/j.1462-2920.2005.00899.x;
RA Sekine M., Tanikawa S., Omata S., Saito M., Fujisawa T., Tsukatani N.,
RA Tajima T., Sekigawa T., Kosugi H., Matsuo Y., Nishiko R., Imamura K.,
RA Ito M., Narita H., Tago S., Fujita N., Harayama S.;
RT "Sequence analysis of three plasmids harboured in Rhodococcus erythropolis
RT strain PR4.";
RL Environ. Microbiol. 8:334-346(2006).
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; AP008957; BAH31565.1; -; Genomic_DNA.
DR RefSeq; WP_020906251.1; NC_012490.1.
DR AlphaFoldDB; C0ZQ87; -.
DR KEGG; rer:RER_08570; -.
DR PATRIC; fig|234621.6.peg.1311; -.
DR eggNOG; COG1330; Bacteria.
DR HOGENOM; CLU_007513_1_0_11; -.
DR Proteomes; UP000002204; 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}.
FT DOMAIN 787..1013
FT /note="RecC C-terminal"
FT /evidence="ECO:0000259|Pfam:PF17946"
SQ SEQUENCE 1093 AA; 118476 MW; 24032FF58090C41E CRC64;
MLKLYRAERS DTLVSALATL LRTPLSDPFA RETVAVPAKG VERWLNQRLS SQLGTSGPSA
VDGISANIAF PSPARLVAES VAAVSGITAD DDPWSPTRLV WTVLDVIDES LGEPWCGVLA
KHLEGHREGR RFASATHVTE LFRSYAAQRP QMLIDWAAGR LTDGHGLALS EDFEWQARLW
CIVADKIDVP GPAERLGQVS RALVEDPALV DLPERLSVFG PTRLPVDQRM ILSALSANRD
VHIWLPHPSP ALWTKMSSRI PPRSESTIRR SEDGSALISA NPLLSSLARD VRELQISLGA
AEFESVHLPE PAGPKSLLAT VKADVIADRA PSVAAEPDGT VQVHACHGPA RQVEVLRECL
LRLFEDDPTL QPRDVLVMCP DVETYAPLVR AAFGQGVHGH PGHLLRVRLA DRGLRQTNPV
LAVLGSLLEL ADGRATASEV LDLAAADPVR TRFSWGEDEL ERLREWTTEA GARWGIGSRQ
RATFGLDAFP QNTFNTAMDR ILLGVSADES ENAWLDLALP LDDVDGTDID LTGRFAEFVD
RLAVSLRDLA GPHSPAEWLR VLMRALDLLT DTAPADSWQS AGAHRELVAA VEFGGETMLR
LADVRAMLSR SLAGRPTRAN FRTGELTVCT MVPMRSVPHR VVVLIGLDDE VFPRTGGVDG
DDILSRHPVV GERDLRSEDR QLLLDAVMSA GEHLILLYTG ADPVTGVVRP PAIPLSGLLD
VLSATVGPEA INGVLTRHPL QSFDNRNFSP DQPFSFDTAA LAGARAAAGT PIELPTVLSA
ELLEVHPKEV NLADLVNFLV HPARGFLRQR LGVRVPELDD DIADSLATEL DPLSTWALGD
RMLLSRLAGR SSADFRAAEW RRGTLPPYNL GASVLGNVEW VVDQLAGLAL PHLEGDSEAV
DVDIDLGDGH RLTGTVTGVH GNSVVRASYS SLAPKHRMTA WINLLALKAH GRPGALDAVS
IGRGRGKIAA ARSVLDAPGN AAEILQQLVD LRERGLQRPL PMWAATSAEY ARRRFGGESV
DDATNGADTQ WTGQYGEMID PSNAYVFGEA RTLAELAADP PSDDEFVWAE EPTRFGVLAR
RLWDPLLTNE RAE
//
