ID A0A2S0MY16_9BURK Unreviewed; 1199 AA.
AC A0A2S0MY16;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 24-JAN-2024, entry version 20.
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:AVO40782.1};
GN ORFNames=C6571_05320 {ECO:0000313|EMBL:AVO40782.1};
OS Simplicispira suum.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Simplicispira.
OX NCBI_TaxID=2109915 {ECO:0000313|EMBL:AVO40782.1, ECO:0000313|Proteomes:UP000239326};
RN [1] {ECO:0000313|EMBL:AVO40782.1, ECO:0000313|Proteomes:UP000239326}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC1-8 {ECO:0000313|EMBL:AVO40782.1,
RC ECO:0000313|Proteomes:UP000239326};
RA Kim S.-J., Heo J., Kwon S.-W.;
RT "Genome sequencing of Simplicispira sp.";
RL Submitted (MAR-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}.
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DR EMBL; CP027669; AVO40782.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2S0MY16; -.
DR KEGG; simp:C6571_05320; -.
DR OrthoDB; 9762834at2; -.
DR Proteomes; UP000239326; 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}; DNA damage {ECO:0000256|HAMAP-Rule:MF_01486};
KW DNA repair {ECO:0000256|HAMAP-Rule:MF_01486};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|HAMAP-
KW Rule:MF_01486}; Exonuclease {ECO:0000256|HAMAP-Rule:MF_01486};
KW Helicase {ECO:0000256|HAMAP-Rule:MF_01486};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_01486};
KW Nuclease {ECO:0000256|ARBA:ARBA00022722, ECO:0000256|HAMAP-Rule:MF_01486};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_01486}.
FT DOMAIN 847..1120
FT /note="RecC C-terminal"
FT /evidence="ECO:0000259|Pfam:PF17946"
SQ SEQUENCE 1199 AA; 130800 MW; 58C8FC65A7E30266 CRC64;
MPVAPSPRST PLAAGLIALQ GNRIETLADT VFAWLGRHPL GALETEVVLV QSNGVAEWFK
MALAERSGVC AAAQVQLPAR FLWQSYRQVL GAAAVPTRSP VDRAALTWRL LQDLPSLATQ
PGFEPVAAFL QGADAERLWQ LAGRLADLFD QYQVYRPDWL GDWAAGDDRL RAPGRGEIPV
PPDQQWQPLL WRAALARLGD AERRSIRPQI HQQALAKLRD GTTLAEPLAR RVVLFGATHL
PLPVLEMLAA IARHSQVLLA IPNPCRFHWA DAVDGRELLA ISRRRQPLRN GVDLAAVPLE
SLHAHAHPLL AAWGRQGRDF VRQLDAFDEA ALAQEQATLP RLDLFVEGEA PDAPLLTQVQ
NRIRDLVPLA EHPPVVLVPQ DRSIVFHSAH SALREVEVLH DQLLELLARP PGGAPLAPRD
IVVMVPDIEK FAAAVRAVFG QVPRSDPRFI PWGIADLSAR ASHPLVGALD WLLRLPQQRC
TLSELQGLLD IPAIAARLGL ASGDAEQLAH WMAGAGIRWG LDADQRSVLG LAACGAQNSV
VFGLERMLLG YAAGTGSFDG IEAWNEIGGL AAELVGALAA LVARLKHWAQ QAAEPAAPLQ
WAERFRALMA DFAEATDEAD RQTLQALEAA LGDWLRDCDD AEFSDAIPLD TARQAWQQAL
DAPRLAQRFR AGGVTFCTLL PLRAIPFEVV CLLGMNDGDY PRRSPRSDFD LMALPGQARP
GDRSRQGDDR QLMLEALLSA RRVLYVSWVG RSARDNSVQP PSVLVAQLRD YLVAGWGEGA
VAERSTEHPL QAFSRRYFES DELQGGAGAA SWFTYAREWR VMHEVLPGSD AMPLPVLWEG
QNVELESTTL SQLGRFIRHP ARAFLRERLA VVFDAPEEDV GDDESFSVAG LDSYQITSEL
LDTLDAAWTA DANTLAEPLL GDAIARLGRA GRLPLAGLGQ RAQVQLMDEL LPLAEVWQAQ
RAVWSAPAPR LRVLWSPENT PDLIASNVYP VSDRGQSYLK KPTTIALDDW IEPIWRAEDG
RDALLTRTAS RVLAKAKAKT APHPRPEKLL GSWLQALAAA ASGQALHGVL VARDALLTWP
PMDQTSAESN LAIVLALWQQ NLRGAAPLPL PLATTLAQVE GRAADAVYDG AGSNQGPSPE
ASEPEWERFY PDFEALTADG QFEALAPLLH ACLADWVAKE VQVTLHPMAQ ADAEEESDA
//