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Database: UniProt
Entry: A0A2S0MY16_9BURK
LinkDB: A0A2S0MY16_9BURK
Original site: A0A2S0MY16_9BURK 
ID   A0A2S0MY16_9BURK        Unreviewed;      1199 AA.
AC   A0A2S0MY16;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   24-JAN-2024, entry version 20.
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:AVO40782.1};
GN   ORFNames=C6571_05320 {ECO:0000313|EMBL:AVO40782.1};
OS   Simplicispira suum.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Simplicispira.
OX   NCBI_TaxID=2109915 {ECO:0000313|EMBL:AVO40782.1, ECO:0000313|Proteomes:UP000239326};
RN   [1] {ECO:0000313|EMBL:AVO40782.1, ECO:0000313|Proteomes:UP000239326}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SC1-8 {ECO:0000313|EMBL:AVO40782.1,
RC   ECO:0000313|Proteomes:UP000239326};
RA   Kim S.-J., Heo J., Kwon S.-W.;
RT   "Genome sequencing of Simplicispira sp.";
RL   Submitted (MAR-2018) 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; CP027669; AVO40782.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2S0MY16; -.
DR   KEGG; simp:C6571_05320; -.
DR   OrthoDB; 9762834at2; -.
DR   Proteomes; UP000239326; 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; 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}; DNA damage {ECO:0000256|HAMAP-Rule:MF_01486};
KW   DNA repair {ECO:0000256|HAMAP-Rule:MF_01486};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|HAMAP-
KW   Rule:MF_01486}; Exonuclease {ECO:0000256|HAMAP-Rule:MF_01486};
KW   Helicase {ECO:0000256|HAMAP-Rule:MF_01486};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, 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}.
FT   DOMAIN          847..1120
FT                   /note="RecC C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF17946"
SQ   SEQUENCE   1199 AA;  130800 MW;  58C8FC65A7E30266 CRC64;
     MPVAPSPRST PLAAGLIALQ GNRIETLADT VFAWLGRHPL GALETEVVLV QSNGVAEWFK
     MALAERSGVC AAAQVQLPAR FLWQSYRQVL GAAAVPTRSP VDRAALTWRL LQDLPSLATQ
     PGFEPVAAFL QGADAERLWQ LAGRLADLFD QYQVYRPDWL GDWAAGDDRL RAPGRGEIPV
     PPDQQWQPLL WRAALARLGD AERRSIRPQI HQQALAKLRD GTTLAEPLAR RVVLFGATHL
     PLPVLEMLAA IARHSQVLLA IPNPCRFHWA DAVDGRELLA ISRRRQPLRN GVDLAAVPLE
     SLHAHAHPLL AAWGRQGRDF VRQLDAFDEA ALAQEQATLP RLDLFVEGEA PDAPLLTQVQ
     NRIRDLVPLA EHPPVVLVPQ DRSIVFHSAH SALREVEVLH DQLLELLARP PGGAPLAPRD
     IVVMVPDIEK FAAAVRAVFG QVPRSDPRFI PWGIADLSAR ASHPLVGALD WLLRLPQQRC
     TLSELQGLLD IPAIAARLGL ASGDAEQLAH WMAGAGIRWG LDADQRSVLG LAACGAQNSV
     VFGLERMLLG YAAGTGSFDG IEAWNEIGGL AAELVGALAA LVARLKHWAQ QAAEPAAPLQ
     WAERFRALMA DFAEATDEAD RQTLQALEAA LGDWLRDCDD AEFSDAIPLD TARQAWQQAL
     DAPRLAQRFR AGGVTFCTLL PLRAIPFEVV CLLGMNDGDY PRRSPRSDFD LMALPGQARP
     GDRSRQGDDR QLMLEALLSA RRVLYVSWVG RSARDNSVQP PSVLVAQLRD YLVAGWGEGA
     VAERSTEHPL QAFSRRYFES DELQGGAGAA SWFTYAREWR VMHEVLPGSD AMPLPVLWEG
     QNVELESTTL SQLGRFIRHP ARAFLRERLA VVFDAPEEDV GDDESFSVAG LDSYQITSEL
     LDTLDAAWTA DANTLAEPLL GDAIARLGRA GRLPLAGLGQ RAQVQLMDEL LPLAEVWQAQ
     RAVWSAPAPR LRVLWSPENT PDLIASNVYP VSDRGQSYLK KPTTIALDDW IEPIWRAEDG
     RDALLTRTAS RVLAKAKAKT APHPRPEKLL GSWLQALAAA ASGQALHGVL VARDALLTWP
     PMDQTSAESN LAIVLALWQQ NLRGAAPLPL PLATTLAQVE GRAADAVYDG AGSNQGPSPE
     ASEPEWERFY PDFEALTADG QFEALAPLLH ACLADWVAKE VQVTLHPMAQ ADAEEESDA
//
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