ID A0A1I0ZAG9_9CELL Unreviewed; 1170 AA.
AC A0A1I0ZAG9;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
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=SAMN05421867_11086 {ECO:0000313|EMBL:SFB22644.1};
OS Cellulomonas marina.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Cellulomonadaceae;
OC Cellulomonas.
OX NCBI_TaxID=988821 {ECO:0000313|EMBL:SFB22644.1, ECO:0000313|Proteomes:UP000199012};
RN [1] {ECO:0000313|EMBL:SFB22644.1, ECO:0000313|Proteomes:UP000199012}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 4.6945 {ECO:0000313|EMBL:SFB22644.1,
RC ECO:0000313|Proteomes:UP000199012};
RA de Groot N.N.;
RL Submitted (OCT-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}.
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DR EMBL; FOKA01000010; SFB22644.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I0ZAG9; -.
DR STRING; 988821.SAMN05421867_11086; -.
DR Proteomes; UP000199012; 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};
KW Helicase {ECO:0000256|HAMAP-Rule:MF_01486, ECO:0000313|EMBL:SFB22644.1};
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:UP000199012}.
FT DOMAIN 841..1079
FT /note="RecC C-terminal"
FT /evidence="ECO:0000259|Pfam:PF17946"
FT REGION 803..825
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1170 AA; 122928 MW; F4CDB1DDFC7B6DBD CRC64;
MHVAERFDVL VDALGAVLAD VPADPFVPDV VAVPTRGVER WVAQRLARRL GSDGEGGGDG
ICANVRFDPP RRLVADALAA VVGHPDGERD PWSRSALAWT VLAVLDERAE EPWLAPVVRH
LGTPDDDVRR GRRLPLAQHL ARLLVRYDEE RPAMVVAWAA GDDEDGTGAP LAPDLAWQAR
LWRAVRERLG VPAPAERLDD AVAALVADPG LVDLPARVSV LGATALPAQG LRVLGALAAH
REVHLWLPQP SLALWQRLAD LDLRPPLARA ALPRVARHRL LTATAGDAVE LGARVLAAGP
DHVELLPARP RPTTVLGALQ TRLAEDRRGG PVHVAAAEDR TVQVHACHGR ARQVEVLREV
LVGLLADDPT LEPRDVVVLC PDVEAFAPLV EAVLGPVATG EAAVDGPGGS SAVAADHPGR
TLRVRIADRA PARANPVLVV LATLLELAAS RVTASAVVDL AGQPPVRRRF DLDDADLDRV
RAWAVETGVR WGEDTGRRAR YGLGRVAQGT WSAALDRLAL GVAMAEEDGR YVEHALPVDD
VGSTDVDLVG RLTELVDRLS AVLASLDGTR PATAWCDALT DALALLTDVA PADRWQSVEA
ERVLADLRRT SADGGDPELR LPDVAAALEP RLRARPTRSG FRTGALTVCS LAPMRAVPHR
VVALLGMDDG AFPRGGGPDG DDVLARRPLV GERDRRQEDR QLFLDAVLSA TDHLVVVHAG
ADERTGARRP PAVPVGELLD ALDDAVASTD GRDARARVVR HPLQTVDERN FVDGALGRPG
PFSFDAVDLA AARRAREPRT AAAPFLPAPL GPAGADAAPT SGTATTATTA TTATVSSGVP
DVDLDDLVVV LEHPVRALVR GRLGVVPPRD EPPLEDRLPL ELDGLAMWDV GNRVLATVLA
GTGLDAAVAA ERRRGHVPPG ELGGTVMGTV RQRVQGVLDA AGDALAADPV ALDVALTLPP
HPGPDGQVVT GRRLTGTVDG VRGDVLVRVV LSRLAAKHRL RAWLGLLALT AALPGRTFSA
TTIGRGPGSG SANRAALLAA PAPDRAARLL ADLVVLHDAA RREVLPLPLA ASCAYARALT
GPAATADDAE AAARAELGTP EDAARGAGGF DLTDGYHVQV WGAGMSADDV LAPRPTPAEA
ARAPGHPTRF GALSVALWED LLAHEQVVPR
//
