ID A0A368U6X4_9GAMM Unreviewed; 1217 AA.
AC A0A368U6X4;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 18.
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:RCV92704.1};
GN ORFNames=DU506_06695 {ECO:0000313|EMBL:RCV92704.1};
OS Halomonas rituensis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Halomonadaceae; Halomonas.
OX NCBI_TaxID=2282306 {ECO:0000313|EMBL:RCV92704.1, ECO:0000313|Proteomes:UP000253204};
RN [1] {ECO:0000313|EMBL:RCV92704.1, ECO:0000313|Proteomes:UP000253204}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TQ8S {ECO:0000313|EMBL:RCV92704.1,
RC ECO:0000313|Proteomes:UP000253204};
RA Lu H., Xing P., Wu Q.;
RT "Halomonas rutogse sp. nov., isolated from Lake TangqianCo on Tibetan
RT Plateau.";
RL Submitted (JUL-2018) 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:RCV92704.1}.
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DR EMBL; QPIJ01000010; RCV92704.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A368U6X4; -.
DR OrthoDB; 9762834at2; -.
DR Proteomes; UP000253204; 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}.
FT DOMAIN 890..1131
FT /note="RecC C-terminal"
FT /evidence="ECO:0000259|Pfam:PF17946"
SQ SEQUENCE 1217 AA; 136828 MW; AD40DE4645231F9C CRC64;
MLSTATALTP GFMVIHGNRM EDLRGLAVEW MQRHPLGPLE NETILVQSNG IGQWLKLALA
EDAAQGGAGI AAALDISLPA RFLWQAYRSV LNAHESASEA EAVPTTSPFD KSRLVWRLLR
LLPELVEREE FAPLRQFLEG DNDLRKHHQL AERLADLFDQ YQVYRADWLE AWAEGQDTLL
GAHGEPKSLD DAQRWQPALW RAVCESVADD IGQGGISSSR AQVHRRFLDA TQAFSATHSP
PGLPRRVIVF GISSLPQQTL EALAAIARFS QVLLCVHNPC QYYWADIIEH KELLRATSRR
QRRKSGMPER LDVLGAGDGE ADLHLHAQPL LAAWGKQGRD YLRLLDEHDD AGAYQGLFEH
QALRIDLFEP FVDESDKPRL LHQLQDDIRE LRPLAETREH WPNADPRQDA SIVFHITHGP
QREVEILHDQ LLAAFSGDPE LRPRDIIVMV PDIDQYAPHI RAVFGCLERD DPRYIPFTLS
DQGSRHRLPL LIALETLLRL PELRLSVSEL LDLLEVPALR ARFGIQESDL PTLARWIQGA
GIRWGLHSGQ RHNLDLPEGM EQNTWAFGLR RLLLGYTVGN AGSGAWQGIE PFDDIGGLEA
ALAGALAGLL ETLEDWWKKL QSPSDAQQWA QRLRGLLDAC FRAEDARDSL MLTQLEDALQ
RFQESTEEAG LVDELPLAIV REHWLEQIDE HSLSQRFMAG AVNFATLMPM RAIPFKRVCL
LGMNDGDYPR SHPPLDFDLM NVDYRPGDRS RREDDRYLFL EALLSARDQF YLSWVGRSIV
DNADKPPSVL VGQLRDHLKA GWRDSQAGEN AGETLLAALT TEHPLQPFSR VYFPSPAQHA
ACNIAAQRLV TYAHEWREVH DDSVAPSALP DEPSQDAEAE GPLAAFEQDN PLTLSQLGNF
LRDPTKAFFT TRLKVYLEQQ DILSLDQEPF TLNGLENWQL QDTLIQAQRH AIDNGQPREQ
ALHDTLERLQ GQGVLAMGAF AERMRQQLAD PMAALFEDYA NALEEWPNAM EEPQPVYYSH
PGSPALEDWL DAMRTDSHGN RCRLLLLSSS LIKKKTYHWH HLLRPWVSHL AGNLESPMTT
QLLSKAGNVT LAPLETEAAR RHLESLITTW QAGMRMPLPL APATAFAWLA KEGTPDSDAQ
SDAWRAAAKA YEGDDFASGE VARNPYLAHR WQRFSALTEA NRHPESPSGY DFLECGFANL
TQRLLAPVYQ AVKGGGK
//
