ID A0A0Q8AHT0_9PSED Unreviewed; 1150 AA.
AC A0A0Q8AHT0;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 33.
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=ASD60_07780 {ECO:0000313|EMBL:KQZ82369.1};
OS Pseudomonas sp. Root562.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1736561 {ECO:0000313|EMBL:KQZ82369.1, ECO:0000313|Proteomes:UP000051426};
RN [1] {ECO:0000313|EMBL:KQZ82369.1, ECO:0000313|Proteomes:UP000051426}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root562 {ECO:0000313|EMBL:KQZ82369.1,
RC ECO:0000313|Proteomes:UP000051426};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQZ82369.1, ECO:0000313|Proteomes:UP000051426}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root562 {ECO:0000313|EMBL:KQZ82369.1,
RC ECO:0000313|Proteomes:UP000051426};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) 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:KQZ82369.1}.
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DR EMBL; LMGK01000021; KQZ82369.1; -; Genomic_DNA.
DR RefSeq; WP_056854905.1; NZ_LMGK01000021.1.
DR AlphaFoldDB; A0A0Q8AHT0; -.
DR OrthoDB; 9762834at2; -.
DR Proteomes; UP000051426; 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 839..1077
FT /note="RecC C-terminal"
FT /evidence="ECO:0000259|Pfam:PF17946"
SQ SEQUENCE 1150 AA; 130032 MW; A014052E26E09CCA CRC64;
MPDATSLSAG FMVVHGNRLD ELRSLVVSWM RRYPLAPLEN EIALVQSNGI AQWLKLALAE
DAEDDDMGGC GIAAAIDVQL PGSFMWQLYR MVLGRDEIPA KSLLDKSPLT WRLMRLLPQL
INEPHFEPLQ RFLTNDNDLR KRYQLAERLA DLFDQYQVYR ADWLEDWAEG RHQLRNARGE
PKPLTAANYW QAQLWRALLL DVGEEGMAQS RAGVHQRFVE RINSLDVAPP GLPSRVIVFG
ISSLPAQALE ALAGLARFSQ VLLCVHNPCR HHWADIVADK DLLRHQYKRQ ARKSGMPVVL
DSQTLHQHAH PLLAAWGKQG RDYINLLDSY DDPNSYRSAF RDGRIDLFSD SQPLNMLNQL
QDDILELRPL NETRERWPAV DLDADQSIRF HIAHSAQREV EILHDQLLAR FSADPQLRPR
DVIVMVPDID SYAPHIRAVF GQLERQDPRF IPFTLADQGQ RGRDPLLIAI EHLLKLPDSR
FPVSEILDLL DVPALRARFG VEERDLPTLH RWIEGAGIRW GMNAEQRAGL GLPQALEQNS
WRFGLRRMLL GYAVGSASAC EGIEPYDEIG GLDAALIGPL VALLDALEIA HRELTQPASP
QQWSLRLQAL VSLFFQASNE HDDYVLTQLE ELREAWLENC EAVGLQDDLP LTVVREAWLA
GLDQGRLSQR FLAGAVNFCT LMPMRAIPFK LVCLLGMNDG DYPRAQPPLD FDLMGSDYRP
GDRSRREDDR YLLLEALLSA RDQLYISWVG RSIRDNSERP ASVLIGQLRD HLASGWRLAQ
DSEDLLEAIT QEHPLQPFSA RYFHEGDELF SYASEWQVLH KFAEQSADIE RLDAHLQDEP
LSLGQLQDFL RNPVRHFFSQ RLKVFFESAQ VPLADEEPFV LDALQRYSLS DSLLEAGLAD
LENSDQALEV QARRLQNGGL LPMAGFGQCL QRELIEPLPD LLQRYQQLLT LWPTRLTSAL
PVNLELHALR IEGWLSGLHQ RTDGGLLSIT TIPNSIGAIK SRKWHRLIRP WVNHLVACAS
GLSMTTALVA SDDSLLLAPM DAEPARRILG DLLLAWQSGM RQPLPVAVKT AFAWLGQSDP
VKAEAAARKA YEGDGVNTDG ERRESVALVR QFADYDALVA DETFTDWCDA LYRPLLEAPW
RSLSTEEGRS
//
