ID R9H3P8_9SPHI Unreviewed; 1066 AA.
AC R9H3P8;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 31.
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=ADIARSV_1127 {ECO:0000313|EMBL:EOR95814.1};
OS Arcticibacter svalbardensis MN12-7.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Arcticibacter.
OX NCBI_TaxID=1150600 {ECO:0000313|EMBL:EOR95814.1, ECO:0000313|Proteomes:UP000014174};
RN [1] {ECO:0000313|EMBL:EOR95814.1, ECO:0000313|Proteomes:UP000014174}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MN12-7 {ECO:0000313|EMBL:EOR95814.1,
RC ECO:0000313|Proteomes:UP000014174};
RX PubMed=23846277;
RA Shivaji S., Ara S., Prasad S., Manasa B.P., Begum Z., Singh A.,
RA Kumar Pinnaka A.;
RT "Draft Genome Sequence of Arcticibacter svalbardensis Strain MN12-7T, a
RT Member of the Family Sphingobacteriaceae Isolated from an Arctic Soil
RT Sample.";
RL Genome Announc. 1:E00484-13(2013).
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:EOR95814.1}.
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DR EMBL; AQPN01000043; EOR95814.1; -; Genomic_DNA.
DR RefSeq; WP_016194371.1; NZ_AQPN01000043.1.
DR AlphaFoldDB; R9H3P8; -.
DR STRING; 1150600.ADIARSV_1127; -.
DR PATRIC; fig|1150600.3.peg.1109; -.
DR eggNOG; COG1330; Bacteria.
DR OrthoDB; 9762834at2; -.
DR Proteomes; UP000014174; 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:UP000014174}.
FT DOMAIN 781..991
FT /note="RecC C-terminal"
FT /evidence="ECO:0000259|Pfam:PF17946"
SQ SEQUENCE 1066 AA; 123257 MW; A736F8F6FFD16C2B CRC64;
MALHLQVSNS LAQLAKRLCV QLKHQEQGVF QPHIIVTQTD GMNNWLKLQF AEHMGIAANY
HFFKPSDIIN QIYYLLGGKG SGATLSADSI SWLLYALLED PVFIKRFPEV SDYYNYDGPD
KEVKRMGLAD KIADLFDQYQ IYRPEMIIKW NETDPNDRTI QDWQQYLWVK ARVIAEVQLP
DKTLICDYII ENLKRESAIE LLRAQMPAIH VFGLSITTGY HLTLFYEIAR YLDFSFHILN
PAPSVYWFED KSEKQLIWMK KKDFIDHSEE SLGNPLLTSW GRVIQNTFHL FFQNEEMLNV
YDEVEIEEPD ENSLLHKIQH DIFYNYSKAD RNLLVPEDLT DGSVTINSCF TAVREVEVLY
NYLVHLIDER RELLSPRDIV VMVSDIDAYA PYIKAVFSNA PYKFHYTIAD ENFTSTDTIS
NALHVLLSIN EQNFKAEEVL QILDSGYIRK RFGITDLQLI RNTVNKANIR FGMEGELADE
TIYVSWEYGI QRMMYGMCML GEEEYGSGTE SFYPLDSIEG AASYEIIRFC HFVEVLMDSI
RERKKNRTIA DWVVYMEHVL ENLVWDPEEG TVEDYELLLG QLEKYNLLTP LLMETISYEV
FSHKFLQSIS GATRAGSFVQ GGITFCSLIP MRSIPFKVVA LMGLNFDQFP RKETPVSFNL
LEKDKRRGDR NVKENDKHLF LETILSAEHY FYISYIGQSA KDNTVVPPSA LVDELIDYIE
SGTDGQAVIK EKLVIRHPLH SFSQKYQRGD GVLYTYLNEK IQTDRGLIDS AKEHQDQALD
QISPEVLVKF FKNPIKGYYN RVLGIYYNSD SVLLPETELF ELDKLQQWKL KQDLLHIDQH
EKSELKSRLV KTGNLPLKGM ADFTVDQMEQ NIMPARDLFN EVVQDEPLKG VPIELTIDSM
LIKGILQPVY GDKIVSVCWS KHEMKHLLDV SIRYILAQAS GLDLRVYFIS SNNQKVYEGI
SLSQEEAISR LKVLIGLFRL GHQQILAFYP DLEIDPIGLE LIDLGGYQSL VNDRFANSFL
PCNDIYGLKE YHNGYFKQEG IYEAFMNNAE LVLLPLIDLF PTYYAK
//
