ID A0A0U3DUA9_9BURK Unreviewed; 1192 AA.
AC A0A0U3DUA9;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
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=AT984_14570 {ECO:0000313|EMBL:ALT79892.1};
OS Paucibacter sp. KCTC 42545.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Sphaerotilaceae; Roseateles.
OX NCBI_TaxID=1768242 {ECO:0000313|EMBL:ALT79892.1, ECO:0000313|Proteomes:UP000056576};
RN [1] {ECO:0000313|EMBL:ALT79892.1, ECO:0000313|Proteomes:UP000056576}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KCTC 42545 {ECO:0000313|EMBL:ALT79892.1,
RC ECO:0000313|Proteomes:UP000056576};
RA Kim S.-G., Lee Y.-J.;
RT "Complete genome of Paucibacter sp. KCTC 42545.";
RL Submitted (DEC-2015) 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; CP013692; ALT79892.1; -; Genomic_DNA.
DR RefSeq; WP_058722343.1; NZ_CP013692.1.
DR AlphaFoldDB; A0A0U3DUA9; -.
DR STRING; 1768242.AT984_14570; -.
DR KEGG; pkt:AT984_14570; -.
DR OrthoDB; 9762834at2; -.
DR Proteomes; UP000056576; 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; 1.
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:UP000056576}.
FT DOMAIN 858..1118
FT /note="RecC C-terminal"
FT /evidence="ECO:0000259|Pfam:PF17946"
FT REGION 715..738
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1192 AA; 132066 MW; 7AAF872FAB0581ED CRC64;
MTDRPSAPAE LSSTSITPGL LVLHGNRAEL LGEAVFEWLR RQPLGPLEEE IFLVQSNGVA
EWLKMTLAQQ TGICAATRVE LPGRFLWRAY RQLLGRSAVP AESMLDKLPM TWRLMQLLPA
LQDQAGFEPL AGFLHLGGME RRLQLAQRLA DLFDQYQVYR SDWLDAWGQG HDVLIQQTGQ
DPHNSPSLPA DQRWQPLLWR ALQEPLSATE RAASRPQLHQ RFVAALQAGH APVTPMARRV
VLFGMTHVPM QTLQALAALS ETCQVLLAIP NPCRYHWADI IEGRELLKQS RRRQPLRKGL
DLAELGLEAM HQHAHPLLAS WGRQGRDFVR QLDAFDDALQ AQERFAQAKI DLFDEGEGAH
WLGQVQARIR DLVPLAEHEP VTLGSEDRSI VFHIAHGAQR EVEILQDQLL KRLAEGGLQP
RDIVVMVPDI DAFAPAIRSV FGQYGNSGRG GDKRFIPFDI ADLKDRGHNP LMIALEWLLR
LPQQRCRLSE VRDLLDVPGL AARFGLSAAD LPRLSQWMEG AGIRWGLNEA QRADLGLAAC
GEQNSWVFGL RRILLGYAVG DTTAQAEPFR GIAAYSEVGG LDAALAGCLA DLLGALQAWW
ELAATPVAPL EWAERGLWLM ETFFLAQDDQ ERQTLGALQA AMTQWLSACD TAEFAQSIEL
PVAREAWLSG IDLPTLNRRF KAGGVTFCTL MPMRAVPFEL VCLLGMNDGD YPRRSSRSDF
DLMGLPGQQR PGDRSGRDDD RQLILEALLS ARQQLYISWS GRSVRDNSEQ PPSVLVSQLR
DYLASGWGEA AVAARTVHHP LQPFSRSYFE VKTHAAQEQD LFTYAREWRQ AHAQAGGPGA
TGAMPLAGKV ELGSRELPLN LSALTAFLKN PVKSFFQQRL DVQFRDEEEA LEDDEAFGLG
GLEEWALLSE LSHEVLMSLE ALGVDAGDAN EALLSDLIQE QTRRVQAAGR LPLGEMGRRA
ERQLGQTLLP MLKAWVELQS LFPVKAAMAR LHFVAETETE AGAGSTVHLD DWLDGLQAAP
ALEQLVWLTL SPSRLCADEK CRTPRADHLL APWLRSLVAS ACGEPALGVL VGRDAQIHVN
PLPQEEAIEC LNALLQTWQQ GMEEPLPFAA KTALAFVADQ RDVALVFEGG GFGGVSGEGE
EACLARTYPD FAALSTDGRF EALARRLFEP MLQWMHRSVT LTLHSSENIF HD
//