ID A0A1A1YNX0_9MYCO Unreviewed; 1083 AA.
AC A0A1A1YNX0;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
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=A5724_20520 {ECO:0000313|EMBL:OBF33010.1};
OS Mycobacterium sp. ACS1612.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=1834117 {ECO:0000313|EMBL:OBF33010.1, ECO:0000313|Proteomes:UP000092025};
RN [1] {ECO:0000313|Proteomes:UP000092025}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ACS1612 {ECO:0000313|Proteomes:UP000092025};
RA Sutton G., Brinkac L., Sanka R., Adams M., Lau E., Kiyimba A., Mayanja H.,
RA Musoke P., Ssengooba W., Joloba M.;
RL Submitted (JUN-2016) 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:OBF33010.1}.
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DR EMBL; LZHZ01000037; OBF33010.1; -; Genomic_DNA.
DR RefSeq; WP_067804471.1; NZ_LZHZ01000037.1.
DR AlphaFoldDB; A0A1A1YNX0; -.
DR STRING; 1834117.A5724_20520; -.
DR OrthoDB; 9762834at2; -.
DR Proteomes; UP000092025; 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}; Reference proteome {ECO:0000313|Proteomes:UP000092025}.
FT DOMAIN 792..1018
FT /note="RecC C-terminal"
FT /evidence="ECO:0000259|Pfam:PF17946"
SQ SEQUENCE 1083 AA; 120561 MW; D4C5BC70F52B71AD CRC64;
MGLHLHRAER TDLLADGLGL LLSTPLADPF TEELIIVPAK GIERWLSQRL SHVLGRGAGQ
DGVCAGIAFR NPRSLIAEIT GTVDDDPWAP DAMVWPLLDV IDASCTEAWC KPLATHLGHF
EAGEEKELRQ GRRYAVARRL AGLFASYGRQ RPQLLIDWEQ RTTGDIDPDL AWQPPLWRAL
LDKVDADPPH VRHAETLARL QQSPLDLPER LSLFGHTRLP STEVELLTAL TTHHDLHLWL
PHPSDDLWQR LTDQHGPIPR RDDTSHRQVD HPLLATLGRD LRELQRSLPA APQTDEYLGS
ASHPDTLLGW LQSDIAANTV RADGRTLRAG DRSVQVHSCH GPARQIDVLR EVLLGLLADD
LTLEPRDILV MCPDIESYAP LINADFGLGD VVHGAHPAHR LRVRLADRSL IQTNPLLGVA
SQLLTLAGSR VTASEVLNLA QTAPVRARFG FTDDDLESIT RWVRQANIRW GFDKEHRKPF
GVDFVHNTWR FGIDRVLAGV ALSDDSHAWI ATTLPLDDVS SNRVELAGQL AEYVHRLQHT
VDSLNGARPL QDWLAALADG ITSLTKVDDN DAWQTSQMQR EFADVLETAG PRKDTIMRLP
DIRALLERHL AGRPTRANFR TGTLTVCTMV PMRSVPHRVV CLVGLDDGVF PRLGIVDGDD
VLARDPMTGE RDIRSEDRQL LLDAIGAATE NLVITYTGSN EFSGQDRPPA VPLAELLDTL
DLTTGERIRD RIVVKHPLQP FDIRNVIPGK LIPGEPFTFD PTVQRAAIAS TGHRTEQPPF
ISGPLPPTPL DDVVLEDLIG FYRDPVKGFF RALDYTLPWD VDGVEDAMPV DINALEEWTV
GDRMLHDMLR GMSPQDARQA EWCRGTLPPG QLGWRKAQEI TKQAAQLAQR ALRYRNTEPR
AYDVDVDLGA GRRLTGTVSP VFGDRLVSVT YSKLDGKHLL ASWIPLLALY AHDSARDWQA
ICIGRAKKRD MLRTEGIGRP EVDAAVLLRD LVAVYDSGRR EPIPLPIKTS YAWAAARHCG
DSPEGEARYR WKSGDRYPGE DAEPAHVRAW GERADLSILI DKGFGDYAER VWLPMLRAGR
PAE
//
