ID A0A376BM93_9NEIS Unreviewed; 1111 AA.
AC A0A376BM93;
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:SSY70755.1};
GN ORFNames=NCTC10283_00866 {ECO:0000313|EMBL:SSY70755.1};
OS Alysiella crassa.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Alysiella.
OX NCBI_TaxID=153491 {ECO:0000313|EMBL:SSY70755.1, ECO:0000313|Proteomes:UP000254209};
RN [1] {ECO:0000313|EMBL:SSY70755.1, ECO:0000313|Proteomes:UP000254209}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC10283 {ECO:0000313|EMBL:SSY70755.1,
RC ECO:0000313|Proteomes:UP000254209};
RG Pathogen Informatics;
RA Doyle S.;
RL Submitted (JUN-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; UFSO01000002; SSY70755.1; -; Genomic_DNA.
DR RefSeq; WP_034294150.1; NZ_UFSO01000002.1.
DR AlphaFoldDB; A0A376BM93; -.
DR STRING; 1120980.GCA_000745955_01877; -.
DR OrthoDB; 9762834at2; -.
DR Proteomes; UP000254209; 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; 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:UP000254209}.
FT DOMAIN 798..1026
FT /note="RecC C-terminal"
FT /evidence="ECO:0000259|Pfam:PF17946"
SQ SEQUENCE 1111 AA; 125814 MW; CAB8C11FC382F0AB CRC64;
MLHLYQSNRL EDLADMLATL HQVAPLQSPL APEQIVVQSQ GMRRFINQFL AKKQGIAANI
QFSLPAGLSF RLMRETMPDT PELNPFDTEV MRWRLLALFQ SPEFQGADFQ AAREVLHSYL
DNGEYAAYQL AGQLADVFDQ YLVYRPHWIE TWHAGQLVDG VSDEQIWQAQ LWRYLDDGRQ
SAPHRVELWH NLMKHLDNPP EWLPERFFVF GIATLAPMYL ELLIRLAKTR EVHIFALNPS
ELYWGQVIEP AKILNQSEEP DLSLQGHPLL ASLGKQGRDF FDALSEAQIG IDVNSYDTAA
FSGCLLHELQ KNLQTQTLPE DSDYLQNHDL TTETVLKHLQ TKDRSIQIHS AHSPLRELQI
LKDQILVLLE QNKDWQPHDI AILTPHIEPY APYIHAVFGQ QTGSGQALPY SLSDVKLSRR
QPLLYALEQT LSLLNSRFEV DKLLPLLDSE TVLQRFDLTR EDLLLLHDTI AKLNIHWGAD
SAQRAKFGDS QRLFTWQQGL ERLILGWLLP ESKQNKGLWQ NISAWHTRPD HLDVLSKFTA
LVRTLAQTQR EWQAATHVSG WAERIRRLMA NVFAPSDDDR EAIYQLEQSL ARWVAESELA
DFAQSLTQDT AIAHIQRFLN SADETHFLRG GITFCGMVPM RSLPFKMIAL IGLNDGDFPR
NTKAASFDLI AKHPKKGDRA RRDDDRYLFL EAVLSARQVL YLSFIGKDIR SDEPRTPSTL
LNELVDCVAE MVGVSSKDLL DNWLTQHPLQ AFSPKYFSGS LHSSRTDYAA ALNAEKIAVA
DFFRQPETDF TEHASYLIEQ KDFIQFWRNP VRSYLRNTLN WQAPNAGMEW DAAEPFAPVQ
TRLLSDAYVS ARRHNRQFDD VAAELTAQSL LPAGELGALA QGDFAAQAAA LDGKLLYSKA
LPERSGVLPS VSGCLNYRLN HDYEVGQVIY AGQFLNEFNE HGNLSAADKI ELLLQHVIFC
AATPEHDRQP ESRQTHFIQL PNVLTLPPLA QDLAQEILSL WISVYQQGHA APQPFFPRVQ
LAAANKLFTP KKGQDGLDYD GAIAAAANIY HNGYKGFAQE DYPEVKLVFG RNPDSEPPYR
SDLFMNLTEN LFAGLAGCLK ALAGENETDV G
//
