ID A0A031LX66_9GAMM Unreviewed; 1222 AA.
AC A0A031LX66;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, 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=CL42_01270 {ECO:0000313|EMBL:EZQ12370.1};
OS Acinetobacter sp. Ver3.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=466088 {ECO:0000313|EMBL:EZQ12370.1, ECO:0000313|Proteomes:UP000023816};
RN [1] {ECO:0000313|EMBL:EZQ12370.1, ECO:0000313|Proteomes:UP000023816}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ver3 {ECO:0000313|EMBL:EZQ12370.1,
RC ECO:0000313|Proteomes:UP000023816};
RA Kurth D.G., Ordonez O.F., Albarracin V.H., Revale S., Farias M.E.;
RT "Polyextremophylic features in the genome of Acinetobacter sp. Ver3
RT isolated from a high altitude andean lake.";
RL Submitted (MAR-2014) 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:EZQ12370.1}.
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DR EMBL; JFYL01000002; EZQ12370.1; -; Genomic_DNA.
DR RefSeq; WP_035264039.1; NZ_JFYL01000002.1.
DR AlphaFoldDB; A0A031LX66; -.
DR eggNOG; COG1330; Bacteria.
DR Proteomes; UP000023816; 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; 3.40.50.10930; -; 2.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR HAMAP; MF_01486; RecC; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR006697; RecC.
DR InterPro; IPR041500; RecC_C.
DR InterPro; IPR011335; Restrct_endonuc-II-like.
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 922..1133
FT /note="RecC C-terminal"
FT /evidence="ECO:0000259|Pfam:PF17946"
SQ SEQUENCE 1222 AA; 142875 MW; 6C94C94435FDE7E9 CRC64;
MGIHVIQSQR IEVLVQGIIT TQKRPTNNPF AVLQQQHFVV PSAAMQEWLT QRLSEHQGIS
ANTFFHQRIR GFQWYAYQQI LSDKDKVRKA NIPRLIMKWR IFQALKPFIQ RAHNQLEVEH
PLFPLITRIY DSAARIEQSN EQYRKKMSML YWVSDQVSKL FSNYMIYRAD CRRACEYDCR
CPENWIQVWG RNEALNIEQQ LQYLNDQDSS FKFSQAQQLE AWQRWLWLNI FHEDFVEMQS
IDHDFWGVLR DEQQQKIALK KLPQQLIVFT LLDLPPSQLQ FLRRLGQYID VLILHYNPSQ
EYWADSVDPN WKKKYDLKLK ERYIEKFQQK HQRKPADNEV EQFFENFSLS FNGLARESRH
PLLTRMGKQA RDHFSLLSNL SSGDEGQWID AFVDEAPQHL LSQLQSDILH LVEPQAQSYV
LDPADDSIHI HVCHSAVRQL EVLKDQLTRW LAQSTAEAPR RPSDILVLAP DLKQIEPLIR
SVFPQKNTAT GVYLPVKLAG ITQLDTVLAW RSVLGRIELI QSRFTIDDFA DWLNLAATQV
RYCLDINGTE RILSLLRQAG FRRGLDEQHL QKTLAEYDQD YRFSFKYALD RLALGVAVPV
HAMFQETLSS HVVDSGDFHL IATLIEIYKH FVERRDWLTM IEIENDQETS EHVEFWLNRL
ILEVNEFESA GVSSLEMIKE IIQKQIRMLT LANFYEEHDQ AILKNIRLPL SYILTEIQST
LESQLDYALP TGQITFSQIG LIRPIPYKLI VMMNLDGGKF PNRESHLPFD LMDLLKPMIG
DRSRLDDDQG AFLDALLLAK DNLWLFYNGF DVADGEVRDP SSSVQELLQH LAWIIKTSDQ
SSSNPLIDID GIQVHQNLST LYTVHPLQPF DPDGFQQQHQ RYEDEWYAVA SNLNRQDQRG
HREAWINTTL ELNQDIMVLD AEQWIKDICF PARLYLKTVG VSNLKDQDLP EVNEPLLLDG
LARYSIRDFL QQQPNVSKLQ TELLSDQLPV GKLQEVSLKM SLLEHQQLLK RQKYYIDEPT
KITQRVIAID DIHLQVTVPQ GDETSWVSVS TSSARAQRRA HVWLEYLFWL SYRDLPDHLA
TEMQRIQIFS DKTIMCTGVT TKQAKDMLSQ WIHAYKQAQI EPLVLPAALL MKLAVDGKAL
EWVTDEEGHQ QLNNFDKLLN EWNKSDAFLS YSLNDSEESH LHRDWQYILQ DLDAEHLLKQ
ACDQFAYVLY QPIYMYQSEA EI
//
