ID A0A5J6V8A6_9MICO Unreviewed; 1194 AA.
AC A0A5J6V8A6;
DT 11-DEC-2019, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2019, sequence version 1.
DT 18-JUN-2025, entry version 21.
DE RecName: Full=RecBCD enzyme subunit RecC {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=FY030_14845 {ECO:0000313|EMBL:QFG69807.1};
OS Ornithinimicrobium pratense.
OC Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
OC Ornithinimicrobiaceae; Ornithinimicrobium.
OX NCBI_TaxID=2593973 {ECO:0000313|EMBL:QFG69807.1, ECO:0000313|Proteomes:UP000326546};
RN [1] {ECO:0000313|EMBL:QFG69807.1, ECO:0000313|Proteomes:UP000326546}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=W204 {ECO:0000313|EMBL:QFG69807.1,
RC ECO:0000313|Proteomes:UP000326546};
RA Zhang W.;
RT "Serinicoccus pratensis sp. nov., isolated from meadow soil.";
RL Submitted (SEP-2019) 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 -!- SUBUNIT: Heterotrimer of RecB, RecC and RecD. All subunits contribute
CC to DNA-binding. {ECO:0000256|HAMAP-Rule:MF_01486}.
CC -!- MISCELLANEOUS: In the RecBCD complex, RecB has a slow 3'-5' helicase,
CC an exonuclease activity and loads RecA onto ssDNA, RecD has a fast 5'-
CC 3' helicase activity, while RecC stimulates the ATPase and processivity
CC of the RecB helicase and contributes to recognition of the Chi site.
CC {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; CP044427; QFG69807.1; -; Genomic_DNA.
DR RefSeq; WP_158062301.1; NZ_CP044427.1.
DR AlphaFoldDB; A0A5J6V8A6; -.
DR KEGG; serw:FY030_14845; -.
DR OrthoDB; 9762834at2; -.
DR Proteomes; UP000326546; 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 Gene3D; 1.10.486.10; PCRA, domain 4; 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 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; 2.
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};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000256|HAMAP-Rule:MF_01486};
KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_01486};
KW Nuclease {ECO:0000256|ARBA:ARBA00022722, 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:UP000326546}.
FT DOMAIN 869..1104
FT /note="RecC C-terminal"
FT /evidence="ECO:0000259|Pfam:PF17946"
FT REGION 634..658
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 636..653
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1194 AA; 127875 MW; 8C2D9DC5170DDE4A CRC64;
MTLFVHRGRS TDVLAHGLAE LLADPLEDPF AEEVVAVPTR GVERWLAQRL SHRLGAGDGD
DGVCAGVRFL TPHSLVAMVL GVERDDPWHP DQLAWPLLRV VDASLGEPWA ATLATHLGHG
LTGVERELRN GRRYAVARRL AGLFADYAAQ RPTMLADWRA GGAGDGHGGQ LDEDLAWQPE
LWRRVVDQVG GQTPDERAGR VVRLLREQGA GALGPLGGGR QGELVLPGRL SLFGHTRIAR
SEVEVVAALG EHLDVHLWLP QASPAAWDRL ASVAAQGPVA READDSALLV RHPLLASLGR
DSRELQRTLA IAGGQERVVD GAGELGVAGT GAGAGHGGPH SLLHLLQSDL AADHVPDETE
RAARQVPVTD RSVQVHACHG QSRQVEVLRD VLAQLLEDDP TLEPRDVLVM CPDIDAYAPL
VHAGFGLGEV VREEPAHPAH GLRVRLADRA PVQTNPLLGL ATRLLELAGG RVTASEVLDL
ARAAPVRHRF GLDDDDLERL GDWVKSTAVR WGLDAEHRAG YQLPHLTQNT WQVALDRLLV
GAAVDGEDTD HLGQTLALDD LDSGDLDLAG RLAELVDRLA HTVRGLRAAD TVVEWVRLLK
EGVFGLADTA YRDAWQLAQL ERELDRLETA ATRGGAAAGG GGAAAGGGAG RGGASQSAGR
GSAMSLSLSL SDVHALLGEQ AAGRATRANF RTGTLTVCTM VPMRSVPHRV VALVGLDDGV
FPRSTTPDGD DALARRPVTG ERDLRGEDRQ LLLDAVMSAG ETLVITYTGF DEHSGQERPP
AVPLGELLDA VRRTASPEGA DRVVTAHPLQ PFDVRNLGAV DEGRPALPPG DAPFSFDPAA
LAGARAAVEE RTGPEPVARH RLTPVDTEAD VDLGELIRFF DNPARAFLRS RLGLILPEVP
EIRGEGIPIE LDGLAAWAVG DRILSAVLGG RDPVATFDAE HWRGELPPFE LGTRVLDDIT
RNVQALCEAT WRTTGLGGLG QPLPREALDV DLTLPSGRRL VGTVPGMVGQ RALEVTYSTV
AAKQRLRSWI TSLALAAALG QEASSHVIGR YRWGRAKGYV LATHGPHEPQ AALDLLEQLV
DLRDRGLCEP LPLSPKTSLR WAQAWLSGPG DQAAATMDAE REWKTNDTFD SAFPKEQDDP
SVRYVHGDSV PLTAVLGVPD DDERWTPGVD SRLGQLALRV WAPVLRGAER LERV
//
