ID F7XY37_MOREP Unreviewed; 1101 AA.
AC F7XY37;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 53.
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:AEI75013.1};
GN OrderedLocusNames=MEPCIT_387 {ECO:0000313|EMBL:AEI75013.1};
OS Moranella endobia (strain PCIT).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Moranella.
OX NCBI_TaxID=903503 {ECO:0000313|EMBL:AEI75013.1, ECO:0000313|Proteomes:UP000000504};
RN [1]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=PCIT;
RA McCutcheon J.P., von Dohlen C.D.;
RT "An interdependent metabolic patchwork in the nested three-way symbiosis of
RT mealybugs.";
RL Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AEI75013.1, ECO:0000313|Proteomes:UP000000504}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCIT {ECO:0000313|EMBL:AEI75013.1,
RC ECO:0000313|Proteomes:UP000000504};
RX PubMed=21835622; DOI=10.1016/j.cub.2011.06.051;
RA McCutcheon J.P., von Dohlen C.D.;
RT "An interdependent metabolic patchwork in the nested symbiosis of
RT mealybugs.";
RL Curr. Biol. 21:1366-1372(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; CP002243; AEI75013.1; -; Genomic_DNA.
DR RefSeq; WP_013975763.1; NC_015735.1.
DR AlphaFoldDB; F7XY37; -.
DR STRING; 903503.MEPCIT_387; -.
DR KEGG; men:MEPCIT_387; -.
DR eggNOG; COG1330; Bacteria.
DR HOGENOM; CLU_007513_0_0_6; -.
DR OrthoDB; 9762834at2; -.
DR Proteomes; UP000000504; 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 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; 2.
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:UP000000504}.
FT DOMAIN 799..1017
FT /note="RecC C-terminal"
FT /evidence="ECO:0000259|Pfam:PF17946"
SQ SEQUENCE 1101 AA; 126998 MW; C92A987C338150B2 CRC64;
MLTVYHSNQL DMLKTITAAL ITGRPLRDPF QPEVIIVQSN GIAQWIQLEL AANFGIAANL
EFPRPASFIW QMFTRILPNI PEESALAKSN ITWRLMALLP RLCQQPDCEV ISEYLRDDHD
HRKCFQFATR LAELFEQYMV YRPDWLENWQ RGKLIANVHE KTQRWQASVW RVLIDDTAQA
GKPLWHYANL YKRFIHTLVH STMRPPGLPD RVFICGISSL PPTYLKVFQA LGKHIDIHLL
FTNPCRYYWG DILDHAVLRR LLHRHRWQYP QPKKEQALFR RPAQAESLFN TIGEQQHIGN
PLLAAWGKQG RDHIYLLAQM EGIAEVDAFV EPAGNTLLSL LQRDILELEN HTVISSSLVG
QPLTQGNDQR PLRLDDRSLS LHVCHSTQRE VEVLHDSLLA MMVEDQTLRP REIIVMVADI
ERYTPAIQAV FGNDGNKQRY LPFAISDRRV RHIHPVLSAF FSILELPCKH VDANQVLALL
EVPALAARFA INEPGLRLLR QYMEESGICW GLDETLLSEL MYATGQHIRQ LAELLMQLRK
WRDLLAQPRS IAAWINYICE IINDFFMPDA DAEAALALLA NQCQQVLKCC LQVGYNQPVP
VTILQYELAA RLDQEQLSQQ FLTGTINFCT MMPMRSLAFR VICILGMNDS VYPRSIQPAW
FNLMAQQPRS GDRCQRDDDR YMFLEALFSA QQRLYISFIG RDIQDNTPRY PSVLVSELID
YIAHSFYLLG DEYVDAENRA KRVRSHLLQW HSRMPFAPEN FLPGSEHQSF AKEWLPAASA
KGKPIPDFIA PLKAQPYYTL ALDELLRFYH HPVRAWFVQR LALSVVHYKS LEQKTNEPFN
LNGFTRYQLN DQLVNALING ENIAQLFHQW RAAGLLPDGA FGELYLAKQY QEMMVLSEKV
RPWRLPETPR FQVSLTVNDI KLSGWLQRVQ VNGLLRWRPG TLSTRDGLLL WLEHLAYCAM
GGEGESRMFG VHGEWRFAPM NICQAKTFLL VMVTGYCQGM SSPLLLLPRS GGAWLSNSYD
AMTKSIDRNE RRQFQARNKL IQAWQGNYHV PGEGTDPYLQ LLIRQLEAKH IEAMILAAER
YLLPPVMFNI AHCEPTKRKK K
//
