ID S6HB85_9GAMM Unreviewed; 1146 AA.
AC S6HB85;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 37.
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=OFPII_26180 {ECO:0000313|EMBL:EPJ45603.1};
OS Osedax symbiont Rs1.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Oceanospirillaceae.
OX NCBI_TaxID=1330036 {ECO:0000313|EMBL:EPJ45603.1, ECO:0000313|Proteomes:UP000014822};
RN [1] {ECO:0000313|EMBL:EPJ45603.1, ECO:0000313|Proteomes:UP000014822}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Rs1 {ECO:0000313|Proteomes:UP000014822};
RA Yi H., Goffredi S.;
RT "Comparative genomics of two novel heterotrophic symbionts of deep-sea
RT Osedax worms: functional variation and environmental selection.";
RL Submitted (MAY-2013) 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:EPJ45603.1}.
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DR EMBL; ASZJ01000119; EPJ45603.1; -; Genomic_DNA.
DR AlphaFoldDB; S6HB85; -.
DR PATRIC; fig|1330036.3.peg.2508; -.
DR Proteomes; UP000014822; 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 CDD; cd22353; RecC_C-like; 1.
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}; Reference proteome {ECO:0000313|Proteomes:UP000014822}.
FT DOMAIN 870..1088
FT /note="RecC C-terminal"
FT /evidence="ECO:0000259|Pfam:PF17946"
SQ SEQUENCE 1146 AA; 129695 MW; B0DFA8FF09AC4966 CRC64;
MLKVYHSNSL DMLRDVLVEM ISREPIRDPF SAEQILVQSP GMAQWLKLEL AQRLKIAANI
DFPLPASFLW RTFSQLLVDV PERSAYSKES ISWILMRILP EYLPQLEFRA LAHYMADDKA
PIKLYQLCEK IADLFDQYLV YRPDWIAQWE QQNNAPAVDE QLWQPILWRA IVADTQRRNF
PHWHRANMFD AFIKAIESSF EENSTSAELP QRIFVFGISA LPENYLQALV ALGKRCDIHL
MVANPCRQFW SDIVDKRYLG KLARRNDQAD QAKIAQLSAY EQGNPLLASM GKLGRDYLYM
LGQLELPEVQ LFGADDNSSL LKSMQSDILS LRNRRSTTED QQAKTGSDQQ RLAITRNDDS
ISVHCCHSAM REVEVLQDQI LAMLEQDPAL EPRDIIVMMP DVSAYSPFVE AVFGQAKPRH
YLPFSISDRN AQQESPLIAN FLSLLTMIKS RYGASDVLEL LSLPALLRRF ELDEAKFDQL
RNWILESGIK WGLDADNRAE LALPSFAQNS WQFGLDRMFA GFALGEVNQT WQGIAPYSQI
EGLDAPILGQ LASFVEVLQR CKLAFSGSSN IVEWLAFFHQ LVDDLYLPDD SDLAAIEIIY
TCLEKLQTTI DEVDYQQSIP AEIVLDYLQQ SLTAQRSGQR FLSGQINFCT LMPMRAIPFK
VVCLLGMNDG DYPRSVPAMG FDLMAEHGRK GDRSRRDDDR YLFLEALLSA TAKLYVSYVG
RSIADNSSRA PSVLISELLE YAQQGYFLEP DEGSEGSQAA HDSLLAAANS SSSTKAEGFL
LSEAKGSLLV EAEGSDATGG QLVLKIQQQS AQLLQQLILE HPLTAYHRRY FEQHSRFFSY
AEQWLPIADT VPTQQGANFI QTLPASELES LALTSLVSFF RQPVRYFLQH KLQVNFVDDA
VMVEDEEPFA LAGLDNYILR DRLLQSALLE KDLLGFNDYL GASGLLPIGH AGSKLLSKNL
QDATELAEKV APLITGTKRR LSFDLEIDNL QLQGWIEPLY EIGVVKYSAA NSSGRSYICT
WVEHLAACAN GCDHATYFRA INQQFHFRAV ATEQAIDYLT ELLQLYRQGL QKPLSWLPDL
GWQLFNADDL TVFLRDVESN YNNFADPYIQ RVFPKWQNIS SGLMAVNQQI LAPLAEYLVI
DSEGDE
//
