ID A0A1A7NRT9_9PAST Unreviewed; 1098 AA.
AC A0A1A7NRT9;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
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=QS62_09260 {ECO:0000313|EMBL:OBW92236.1};
OS Gallibacterium salpingitidis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Gallibacterium.
OX NCBI_TaxID=505341 {ECO:0000313|EMBL:OBW92236.1, ECO:0000313|Proteomes:UP000092649};
RN [1] {ECO:0000313|EMBL:OBW92236.1, ECO:0000313|Proteomes:UP000092649}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F150 {ECO:0000313|EMBL:OBW92236.1,
RC ECO:0000313|Proteomes:UP000092649};
RA Kudirkiene E., Bojesen A.M.;
RT "Pan-genome of Gallibacterium spp.";
RL Submitted (NOV-2014) 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:OBW92236.1}.
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DR EMBL; JTJL01000051; OBW92236.1; -; Genomic_DNA.
DR RefSeq; WP_066109221.1; NZ_JTJL01000051.1.
DR AlphaFoldDB; A0A1A7NRT9; -.
DR PATRIC; fig|505341.3.peg.1861; -.
DR OrthoDB; 9762834at2; -.
DR Proteomes; UP000092649; 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:UP000092649}.
FT DOMAIN 819..1032
FT /note="RecC C-terminal"
FT /evidence="ECO:0000259|Pfam:PF17946"
SQ SEQUENCE 1098 AA; 128380 MW; 5DA8D118D2097B5E CRC64;
MFTVYYANQL EYQKDLLIRL LEVQPLTDPF ASNIILVQSP GMAQWLQIQL ADHFGIAANF
TFPMPSTFIW QLYKESIPAA GEKNLFSKEN LVWRLMRIIP QTLDLPEFTS LRHYLGEQFT
TLKLFQLAEK IADLFDQYLV YRPDWIKQWE AREQQSLQQQ IAQQIAPRYQ AILPTIMQDL
SWQAILWQKL INDIQQDYQQ DMIWHRASLY QQYLDLLANG HKPKYLPKRV CVFGISALPP
MFLTVLHALS EHTDIHLFFN SPSRYYWGDI IDHRYLEKLK LKQLKQNSDE QQVVKTIYDE
SLTVGHPLLA SWGKLGRDFL YSLTQLEPHE IELYIEPTED SLLQQIQRSI LELTYAQNES
SQLHYQTGDT SLSFHACHSP MREVEVLHDN LLAMFAGDPN LTPKDIVVMV ADIDRYTPYI
QAVFSQYRFE DKRHIPFAIS DRKITESDVV IATFLQFLTF KESLFSVEMV LSLLDVACIR
QRFSIELEEL SQIREWAIQS GIRFGLYKQD AEDVPNYNAW QNGIERMLLG YALKNEQGVW
QDNVGFDYSE GLQGKIAGKL AHFIEALQEW YQQLQQPLDI EQWRQTLFTC IENFFEVTES
RTVVAILKQA VHQILDTALE SNYQETLDAE IISELLQAKL NEQENSVHFL MGQLNFCTLL
PMRAIPFKVI CLLGMNEGDF PRQLATNSFD VMQYQPQKGD RVRREDDSYL FLEALLSARE
KLYISYVGYS VVDNTEYQPS ILVSQLLDYL SENLTEPTQL AELKFSYPAT IFSVNNFLEP
HFSYAKEWAR VAELQMATKN IEPFVTELNQ SETDEVVKVI ALDDLIRFVV APQRYFFEQK
LGVFLNQNNE NVAESETFAL DNLAQYQLKE RLLQYDYASW NDEFEKAKRE GVLPRAGFAF
LQQAALEETC AALWNVVADY HTMPAESLKI EIHLDIDGEN VLLQGQIDQL YQEQYVGWRV
GRIREQEQIS LWLAHLLLQI AGEQQNSLFY GLESGKVTTL NFTPLEREDA LRQLEVYIRD
FLQSQQQISL VPTFRLEQFS KLFADENSDE ETLRYELSQL DKQNKQYQYW QRLLLQTPSL
DYQQIKASFI NWFEKMFA
//
