ID A0A1A0EWE1_9GAMM Unreviewed; 1194 AA.
AC A0A1A0EWE1;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 34.
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=ADS46_06955 {ECO:0000313|EMBL:OAZ91570.1};
OS Halomonas sp. G11.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Halomonadaceae; Halomonas.
OX NCBI_TaxID=1684425 {ECO:0000313|EMBL:OAZ91570.1, ECO:0000313|Proteomes:UP000092250};
RN [1] {ECO:0000313|EMBL:OAZ91570.1, ECO:0000313|Proteomes:UP000092250}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=G11 {ECO:0000313|EMBL:OAZ91570.1,
RC ECO:0000313|Proteomes:UP000092250};
RA Naifar M., Chouchane H., Najjari A., El Hidri D., Mahjoubi M., Ghedira K.,
RA Soufi L., Salah A., Raddadi N., Sghaier H., Ouzari H.I.,
RA Eddine Masmoudi A.S., Cherif A.;
RT "Genomic basis for crude oil degradation, heavy metal resistance and high
RT salt tolerance of Halomonas hydrocarbonoclasticus G11 isolated from
RT Tunisian Chott El-Djerid salt lake.";
RL Submitted (FEB-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:OAZ91570.1}.
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DR EMBL; LYXG01000041; OAZ91570.1; -; Genomic_DNA.
DR RefSeq; WP_066321663.1; NZ_LYXG01000041.1.
DR AlphaFoldDB; A0A1A0EWE1; -.
DR OrthoDB; 9762834at2; -.
DR Proteomes; UP000092250; 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}.
FT DOMAIN 871..1116
FT /note="RecC C-terminal"
FT /evidence="ECO:0000259|Pfam:PF17946"
FT REGION 851..872
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1194 AA; 134543 MW; 515DB29A9491CCDE CRC64;
MPANSLLSPT SLTPGFMVVH GNRLEDLRGL AVEWMRLHPL GPLENETILV QSNGIGQWLK
LALAEDPDNG GAGIAAALDV MLPARFLWQA YRTVLTHVSN NEDAVPETSP FDKSRLVWRL
LRLLPTLAEQ DVFAPLAQFL EVDRDQRKHY QLAERLADLF DQYQVYRADW LDAWANGDDV
LITARGESRP LEDHQRWQPA LWRILRDDVA ATQGDAGLDS SRAQVHRRFL NATEQLDGQT
CPPGLPRRLI IFGISSLPQQ TLEALAALSR CCQVVLCVHN PCQFYWADII EHKDLLRASR
YRQRRKTGMP EALDVLGTGD ADDALHLHAQ PLLAAWGKQG RDYLRLLDEH DDTGDYQTLF
EQQALRIDMF EPFSGERGCL LSHLQDDIRE LRPVAETQTH WPALAPADDS LVFHIAHGPQ
REVEILHDQL LAAFSADPEL RPRDIIVMVP DIDRYAPHID AVFGQLQGDD PRFIPYTLSD
QASRHRLPLM IALEKLLRLP ELRLSVSDLL DLLDVPALRQ RFGLEERDLP VLERWMEGAG
IRWGLNAKQR QTLELPGGLS QNTWAFGLRR LLLGYTVGEG DAWQGIEPFD DIGGLEAGLA
GPLATLLEKL EATWETFRQP TDAASWVERL RTLLETFFLT DDAQESVMLT KLENGLQQIL
ESSREAQLED PLPLSMVREH WLAQIDEHSL SQRFLAGAVN FATLMPMRAI PFKRVCLLGM
NDGEYPRSQP PLDFDLMGSD YRPGDRSRRE DDRYLFLEAL LSARDQLYVS WVGRSQIDNT
PLPPSVLVGQ LRDHLAAGWH FEHGAPLLDA LTTEHPLQPF SRRYFEDSTE SFQLFTYIHE
WRGIHEWRDD QAPRAPRSQP EKLPPPENAP TSVSLGQLGG FLREPVRTFF NTRLGVYFEQ
EAIAELDAEP FALDGLQNWQ LQDRLIAAQR HAVDNGEPRL EALDAQLERF QGQGVLAMGA
FGERMRNALA EPMDDLFSAY QDALAQWPIA LPAPEPVRVE SADGIVLEDW LNELRQNEAG
DRCRLLLLSS SLISQGSGRG QYRWTHLLRP WVAHLAGNLS GPMTTQLLSK AGNITLDPIA
ADTARAHLDT QMTAWQAGLE APLPLAPQAA FAWLTKLGTP EIAEEKGRES DAYAAAEGAY
DGGRFQTGEV AQSAYLGHQW PRFERLFNEQ TQHGHRFATL TEALYAPLFY AVKG
//
