ID F6FX98_ISOV2 Unreviewed; 1137 AA.
AC F6FX98;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 27-MAR-2024, entry version 57.
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 OrderedLocusNames=Isova_0815 {ECO:0000313|EMBL:AEG43601.1};
OS Isoptericola variabilis (strain 225).
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales;
OC Promicromonosporaceae; Isoptericola.
OX NCBI_TaxID=743718 {ECO:0000313|Proteomes:UP000009236};
RN [1] {ECO:0000313|EMBL:AEG43601.1, ECO:0000313|Proteomes:UP000009236}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=225 {ECO:0000313|Proteomes:UP000009236};
RG US DOE Joint Genome Institute;
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Mikhailova N., Zeytun A., Han C., Tapia R., Land M., Hauser L.,
RA Kyrpides N., Ivanova N., Pagani I., Siebers A., Allgaier M., Thelen M.,
RA Hugenholtz P., Gladden J., Woyke T.;
RT "Complete sequence of Isoptericola variabilis 225.";
RL Submitted (MAY-2011) 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}.
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DR EMBL; CP002810; AEG43601.1; -; Genomic_DNA.
DR RefSeq; WP_013837993.1; NC_015588.1.
DR AlphaFoldDB; F6FX98; -.
DR STRING; 743718.Isova_0815; -.
DR KEGG; iva:Isova_0815; -.
DR eggNOG; COG1330; Bacteria.
DR HOGENOM; CLU_007513_1_0_11; -.
DR Proteomes; UP000009236; 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; 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:UP000009236}.
FT DOMAIN 828..1057
FT /note="RecC C-terminal"
FT /evidence="ECO:0000259|Pfam:PF17946"
SQ SEQUENCE 1137 AA; 122540 MW; A58D523DA7512C46 CRC64;
MLHVHRSERA DALVAPLAAV LAPPPSDPFT PDVVAVPTRG VERWLAQRLA HHLGTGPDGE
AGVCANVEFA SPARLVADVV ARLGGHDAES DPWQAERLTW TVLEVLDDAV GEAWAAPLAR
YLGADDVAEG TAGDARRGRR LGVARRLARL FTSYAAQRPD MVAAWAGESA AGTPDVPTDV
PTDVPTDLAW QVELWRRVRE RVGEPGPAER LAGVVRAVVE RPDEVDLPER VSVFGPTRLP
EDQLRVLHAL GAHRDVHLWL PHPSPALWDR VAAAGPAAAR RREQVVHARH PVLASMARDA
TELQVRLARL AVGGEAHAHA HHPAPEPPST LLGELQRRLR ADDAASPPAE LDPADRSVEV
HACHGLARQV EVLRDVLAGL LADDPTLEPR DVVVMCPDVE AVAPLVAATF GLADGDGDAA
GAAHPGQALR VRVADRSPRQ VNPVLMLLAT LLDLADGRVT ASEVLDLAAS EPVRRRFRLS
DDDLARVRDW AVEAGVHWGE DASRRARFGL PAVRQGTWDT ALDRILLGAA MAEEDHRYVS
SALPLDDVDS TDVDLAGRLA ELLDRLRTVL ADLDGARPRD AWLDALDRAI TLLADAAPTE
EWQLSQARRV LADVRVAAAG HDGVLLRLPD VRALLADRLQ GRPTRAGFRT GALTVCSLEP
MRAVPHRVVC LLGLDDGAFP RGGAEDGDDV LLRDPCVGER DRRSEDRQLF LDAVSAASER
LVVLYSGADE RTGAPRPPAV PVGELLDALD AAARRRDGRP AREHVLVRHP LQPVDERNFA
AGALGRPGPF SFDAHAFAAA VAGRGERVDR VPFLREPLPP AEPEGPGAQV DLDDLVAALE
HPVRWFLRRR LQVSLAGEAD DVDDRLPLEL EPLGQWPLGE RLLGALLDGV EPNRALNVEW
RRGEVPPKEL GRATLLAVQE KVLPVAQAAH RYAGEPASGV DVTAELPGGA VVTGTVPGVR
GDVVLRSTFS KLGPKHRLRA WVQLLALVAA RPETPWRAVT IGRAPVRAPR AAVSTLRTPT
RAEALRHLGE LVALRDAAAR EPLPLPVACA CAYATSRDGG AEEVQALEAA SLEWSQGFER
TDDHHVLCWG AGATLREVAG VPSAAERAWW PEERTRLGVL ARRVWQPLLA HEETVTL
//
