ID C1D6T7_LARHH Unreviewed; 1159 AA.
AC C1D6T7;
DT 26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 26-MAY-2009, sequence version 1.
DT 27-MAR-2024, entry version 69.
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:ACO74194.1};
GN OrderedLocusNames=LHK_01203 {ECO:0000313|EMBL:ACO74194.1};
OS Laribacter hongkongensis (strain HLHK9).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales;
OC Aquaspirillaceae; Laribacter.
OX NCBI_TaxID=557598 {ECO:0000313|EMBL:ACO74194.1, ECO:0000313|Proteomes:UP000002010};
RN [1] {ECO:0000313|EMBL:ACO74194.1, ECO:0000313|Proteomes:UP000002010}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HLHK9 {ECO:0000313|EMBL:ACO74194.1,
RC ECO:0000313|Proteomes:UP000002010};
RX PubMed=19283063; DOI=10.1371/journal.pgen.1000416;
RA Woo P.C., Lau S.K., Tse H., Teng J.L., Curreem S.O., Tsang A.K., Fan R.Y.,
RA Wong G.K., Huang Y., Loman N.J., Snyder L.A., Cai J.J., Huang J.D., Mak W.,
RA Pallen M.J., Lok S., Yuen K.Y.;
RT "The complete genome and proteome of Laribacter hongkongensis reveal
RT potential mechanisms for adaptations to different temperatures and
RT habitats.";
RL PLoS Genet. 5:E1000416-E1000416(2009).
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; CP001154; ACO74194.1; -; Genomic_DNA.
DR RefSeq; WP_012696681.1; NC_012559.1.
DR AlphaFoldDB; C1D6T7; -.
DR STRING; 557598.LHK_01203; -.
DR KEGG; lhk:LHK_01203; -.
DR eggNOG; COG1330; Bacteria.
DR HOGENOM; CLU_007513_1_0_4; -.
DR Proteomes; UP000002010; 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; 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:UP000002010}.
FT DOMAIN 851..1097
FT /note="RecC C-terminal"
FT /evidence="ECO:0000259|Pfam:PF17946"
SQ SEQUENCE 1159 AA; 128488 MW; FA55798CC1AC6389 CRC64;
MTALTGFTIL HANRAEMLRD VILAWLARDP LSSPLDDEVF LVQSQGMAQW LKHALAESPA
GIAAALDFQL PQGFLWRCYR AVLGEDSVPA QSPFDKAPLS WRLYRELPAW LHEPVFAPLA
RFVEADADPR RLYQLAHQLA DLYDQYQSYR ADWLTGWENG HDDITRHGRP APLPEGERWQ
AELWRRLAGQ LASARHTHRA AVHQRFVAAL REGTPPPGSL PERVVVFGLS ALPQQTLEAL
DAISRHSHVL MAVNNPCRYY WGDIVEGREW LRRQAEQRHR RRSGMPAALD DSTLHLHAHP
LLASWGRQGR DFIALLADYD RWQSAAATHA QDIDLFDEAV PAGTLPLLQQ VQQAVLELEP
LPAEPHRLPL PDHSIAFHVA HSPLREVEIL HDQLLAMFDD PELALKPRDV MVMVPDISSY
APFIRAVFGK LPPDHPRFIP FALSDQSAVS TEPLLRALQQ LLDLPALRLT VSEVLELLDV
AAMRRRFRLR ETDLPLLTRW IEGSGIRWGL SAAQRAELGM PDDFDQNSWH FGLDRMLLGY
ACGAGASWQG MAPYDEVGGM DAALAGQLAD LLSTLAHWRQ CLQEPATPAG WQARIAALAE
ACLDIKDEHD LLLYAGIADT LDNWVATLDG NGLADTRLPL EVVRDVLLGQ LADTSVSMRF
LGGAVNFGTL MPMRAIPFKV ICLLGLNDGD YPRSQNRADF DLMAQDYRPG DRSRRDDDRY
LLLEALLSAR RRFYLSWVGK SPRDNRPRPP SVLVEQLRDY LAAGWQAAPL GTEPATTGLL
AALTTEHPLQ PFSPRYFSRA PDARPQPDQP PLFTYDSDWR AIHDATDPPA EPAAALPLPL
PDWDGRTDAV TLARFLRQPA ATFLHGRLKV RFGELDELAE DEPFALDPLA THQLKSRLLE
AVRDVPEAET GRHWQAAATR LTEEGGLPFG AAGAQLLQAC HAPVMALRQN WHRLDDLTDL
PPLTLPPLLL PLAGDQTATL LAHCDGLQAV AADSPPLRRR VMRTGRLADS AGRGADTRWI
PRLHTLVGFW PAHLALQAAG LAIPTLIVGE TVTLQLAPLP ADEARHCLQV LAGYWRQAHG
EPLPLPCKTA GVWLQQQDAS AARQAYEGGY HSTGERAESP ALARLFPAFE DLDLARLDAL
ATDLYAPLLA SVTVPESAA
//
