ID A0A149VY78_9PROT Unreviewed; 1134 AA.
AC A0A149VY78;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
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 ECO:0000313|EMBL:KXW58138.1};
GN ORFNames=FEMY_13140 {ECO:0000313|EMBL:KXW58138.1};
OS Ferrovum myxofaciens.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Ferrovales; Ferrovaceae;
OC Ferrovum.
OX NCBI_TaxID=416213 {ECO:0000313|EMBL:KXW58138.1, ECO:0000313|Proteomes:UP000075653};
RN [1] {ECO:0000313|EMBL:KXW58138.1, ECO:0000313|Proteomes:UP000075653}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Z-31 {ECO:0000313|EMBL:KXW58138.1,
RC ECO:0000313|Proteomes:UP000075653};
RA Poehlein A., Ullrich S.R., Schloemann M., Muehling M., Daniel R.;
RT "Genome sequence of the acidophilic iron oxidising Ferrovum strain Z-31.";
RL Submitted (JAN-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:KXW58138.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LRRD01000023; KXW58138.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A149VY78; -.
DR STRING; 1789004.FEMY_13140; -.
DR PATRIC; fig|1789004.3.peg.1334; -.
DR Proteomes; UP000075653; 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}; Reference proteome {ECO:0000313|Proteomes:UP000075653}.
FT DOMAIN 828..1065
FT /note="RecC C-terminal"
FT /evidence="ECO:0000259|Pfam:PF17946"
SQ SEQUENCE 1134 AA; 129351 MW; 38CD0AC83228550D CRC64;
MHPMSTHPPG LVVLHGNRLE LLQEAVVHWM RQHPLDPLTE EVILVNSIGA AEWVKASLAE
SLGICAATRA ELPGRFLWRL YRKILGRAMA ERSPLDRQAL IWRIMKLALQ NSLPAPLEAI
AHLLRVKDPE ARYGFASEVA DLFDQYQNYR SSWLADWIQG RDQLTTARGE RLPVPATQAW
QPALWRCLWQ ELSPTEQAFT LPVLHQQVLE GLHRNGKILG LPPRIVVFGI STLPHSTLQI
LDALAHHCQV LVALLNPCRF HWSDIVEGRE LWQAVQRRQP WRHHHDFSMT AFEDMHVHAH
PLLAAWGRQG RDFMRQLDAY DPSVPDTTDL PRVDLFDERI PRTLLEEVQC AIRDLLPLAE
HPLNAVAATD RSLIFHRAHS PLREVQVLQD QLLDLLTQAS PALQPRQIVV MVPALEDYVP
FIEAVFDRYE SGDPRFIPYE IALSRPRLST PLIHALKWLL ALDQHRITAS EVRSLLEVPA
LSQRFELDAN GVSKLSQWVE ASGIRWGLDD LHRTSLELGA CGDQNTWHFG LERLWLGYAN
GCSGPFDGIE PYPHLSGLEA TTLGSLARFI ETLKETWETL RTPAPPAVWV ERGRHLLNHW
FDATNELENL SLGLLHEALS DWLTLCQETG FADPIPLSLF RRSWFDTLEE PKESGRFLSG
GVTFCTLLPL RSLPFEVICL LGMNLEAFPR RSAARPHDLM QWPGMPRPGD RARQEDDRAL
MLDTLLAARR VLSISWCGRD PRDDSERPPS VLVAQLRDYL VRGWRPDESH GHSDLLAQQT
QDHPLQPFSR RYFEENQPLH TYAEEWRRIF DPELLKAPFP PLAPQDPPKT LSLKRLGRFL
RNPVRFYLES ILNTHFEETL TPPDEEIFET SGLARHEWID ALITPPFNPH ESQELETRLQ
RLCRAGQLPL AEMGQAVMTE LRNTVTPMLE TWGELQERYP HPCEKHPVHL SFGAYEIRDW
LEGLRGEGDG KPAAWLELHA SRVLEKNGKD LQLHKLLPVW LRHLVTSATG HVLDCHLVAQ
DTLLTLRAPA PEEAHGVLSS LIELWQEGHR RPLPMALKSA LTLVRSDDLG KAAQIYEGTD
HSPAEKDRYQ ERIYPTFACL NQTGEFESLA HCLGPPLWSW AKNAVLTPLG SFHE
//
