ID A0A4D6XS20_9GAMM Unreviewed; 1162 AA. AC A0A4D6XS20; DT 31-JUL-2019, integrated into UniProtKB/TrEMBL. DT 31-JUL-2019, sequence version 1. DT 18-SEP-2019, entry version 2. DE RecName: Full=RecBCD enzyme subunit RecB {ECO:0000256|HAMAP-Rule:MF_01485}; DE EC=3.1.11.5 {ECO:0000256|HAMAP-Rule:MF_01485}; DE AltName: Full=Exonuclease V subunit RecB {ECO:0000256|HAMAP-Rule:MF_01485}; DE Short=ExoV subunit RecB {ECO:0000256|HAMAP-Rule:MF_01485}; DE AltName: Full=Helicase/nuclease RecBCD subunit RecB {ECO:0000256|HAMAP-Rule:MF_01485}; GN Name=recB {ECO:0000256|HAMAP-Rule:MF_01485, GN ECO:0000313|EMBL:QCI17260.1}; GN ORFNames=D9V62_02300 {ECO:0000313|EMBL:QCI17260.1}; OS Buchnera aphidicola (Aphis helianthi). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; OC Erwiniaceae; Buchnera. OX NCBI_TaxID=2315802 {ECO:0000313|EMBL:QCI17260.1}; RN [1] {ECO:0000313|EMBL:QCI17260.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Ahe {ECO:0000313|EMBL:QCI17260.1}; RA Chong R.A.; RL Submitted (DEC-2018) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:QCI17260.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Ahe {ECO:0000313|EMBL:QCI17260.1}; RA Moran N.A.; RT "Genome evolution of the obligate endosymbiont Buchnera aphidicola."; RL Submitted (MAY-2019) 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 CC highly rapid and processive ATP-dependent bidirectional helicase CC activity. Unwinds dsDNA until it encounters a Chi (crossover CC hotspot instigator) sequence from the 3' direction. Cuts ssDNA a CC few nucleotides 3' to the Chi site. The properties and activities CC of the enzyme are changed at Chi. The Chi-altered holoenzyme CC produces a long 3'-ssDNA overhang and facilitates RecA-binding to CC the ssDNA for homologous DNA recombination and repair. Holoenzyme CC degrades any linearized DNA that is unable to undergo homologous CC recombination. In the holoenzyme this subunit contributes ATPase, CC 3'-5' helicase, exonuclease activity and loads RecA onto ssDNA. CC {ECO:0000256|HAMAP-Rule:MF_01485}. CC -!- CATALYTIC ACTIVITY: CC Reaction=Exonucleolytic cleavage (in the presence of ATP) in CC either 5'- to 3'- or 3'- to 5'-direction to yield 5'- CC phosphooligonucleotides.; EC=3.1.11.5; CC Evidence={ECO:0000256|HAMAP-Rule:MF_01485}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP- CC Rule:MF_01485}; CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|HAMAP- CC Rule:MF_01485}; CC -!- SUBUNIT: Heterotrimer of RecB, RecC and RecD. All subunits CC contribute to DNA-binding. Interacts with RecA. CC {ECO:0000256|HAMAP-Rule:MF_01485}. CC -!- DOMAIN: The C-terminal domain has nuclease activity and interacts CC with RecD. It interacts with RecA, facilitating its loading onto CC ssDNA. {ECO:0000256|HAMAP-Rule:MF_01485}. CC -!- DOMAIN: The N-terminal DNA-binding domain is a ssDNA-dependent CC ATPase and has ATP-dependent 3'-5' helicase function. This domain CC interacts with RecC. {ECO:0000256|HAMAP-Rule:MF_01485}. CC -!- SIMILARITY: Belongs to the helicase family. UvrD subfamily. CC {ECO:0000256|HAMAP-Rule:MF_01485, ECO:0000256|SAAS:SAAS00709641}. 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; CP034894; QCI17260.1; -; Genomic_DNA. DR Gene3D; 3.90.320.10; -; 1. DR HAMAP; MF_01485; RecB; 1. DR InterPro; IPR014017; DNA_helicase_UvrD-like_C. DR InterPro; IPR000212; DNA_helicase_UvrD/REP. DR InterPro; IPR011604; Exonuc_phg/RecB_C. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR038726; PDDEXK_AddAB-type. DR InterPro; IPR004586; RecB. DR InterPro; IPR011335; Restrct_endonuc-II-like. DR InterPro; IPR014016; UvrD-like_ATP-bd. DR InterPro; IPR034739; UvrD/AddA_N. DR PANTHER; PTHR11070; PTHR11070; 1. DR PANTHER; PTHR11070:SF23; PTHR11070:SF23; 1. DR Pfam; PF12705; PDDEXK_1; 1. DR Pfam; PF00580; UvrD-helicase; 1. DR Pfam; PF13361; UvrD_C; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF52980; SSF52980; 1. DR TIGRFAMs; TIGR00609; recB; 1. DR PROSITE; PS51198; UVRD_HELICASE_ATP_BIND; 1. DR PROSITE; PS51217; UVRD_HELICASE_CTER; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_01485, KW ECO:0000256|SAAS:SAAS00146071}; Coiled coil {ECO:0000256|SAM:Coils}; KW DNA damage {ECO:0000256|HAMAP-Rule:MF_01485, KW ECO:0000256|SAAS:SAAS01099294}; KW DNA repair {ECO:0000256|HAMAP-Rule:MF_01485, KW ECO:0000256|SAAS:SAAS01099287}; KW DNA-binding {ECO:0000256|HAMAP-Rule:MF_01485, KW ECO:0000256|SAAS:SAAS00745286}; KW Exonuclease {ECO:0000256|HAMAP-Rule:MF_01485, KW ECO:0000256|SAAS:SAAS01033115}; KW Helicase {ECO:0000256|HAMAP-Rule:MF_01485, KW ECO:0000256|SAAS:SAAS00553650}; KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_01485, KW ECO:0000256|SAAS:SAAS00146062, ECO:0000313|EMBL:QCI17260.1}; KW Magnesium {ECO:0000256|HAMAP-Rule:MF_01485}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_01485}; KW Nuclease {ECO:0000256|HAMAP-Rule:MF_01485, KW ECO:0000256|SAAS:SAAS01033141}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01485, KW ECO:0000256|SAAS:SAAS00145996}. FT DOMAIN 1 440 UvrD-like helicase ATP-binding. FT {ECO:0000259|PROSITE:PS51198}. FT DOMAIN 483 735 UvrD-like helicase C-terminal. FT {ECO:0000259|PROSITE:PS51217}. FT REGION 1 874 DNA-binding and helicase activity, FT interacts with RecC. {ECO:0000256|HAMAP- FT Rule:MF_01485}. FT REGION 887 1162 Nuclease activity, interacts with RecD FT and RecA. {ECO:0000256|HAMAP-Rule: FT MF_01485}. FT COILED 100 120 {ECO:0000256|SAM:Coils}. FT ACT_SITE 1066 1066 For nuclease activity. FT {ECO:0000256|HAMAP-Rule:MF_01485}. FT METAL 942 942 Magnesium; via tele nitrogen. FT {ECO:0000256|HAMAP-Rule:MF_01485}. FT METAL 1053 1053 Magnesium. {ECO:0000256|HAMAP-Rule: FT MF_01485}. FT METAL 1066 1066 Magnesium. {ECO:0000256|HAMAP-Rule: FT MF_01485}. SQ SEQUENCE 1162 AA; 139028 MW; 5F1FA975D3D63731 CRC64; MKKKLNIFNI PCNGIKLIEA SAGTGKTTSI VLMYLRLLLG IGSKKNNKPL LIQEILVVTF TNFAKEEIYK RIKKNIEQLY LYCITKNTNN SILKPFFKKI KNLEETIHLL EQAKKNINHM SIYTIHGFCK NILKLNFLNF HQKIIEDEKL LYLQATEDFW RSYFYEVPKK IINIILQDYK NPESLLSELK PIFNFRKVYF KKKFNKNQNL ITCHEENINI INIFKKKWLD YNPIILNIVK ELKPNKKIYN DFNISRWQKN ITKWAESETE DYQIPITLKY FLKDTIIKNI KSNQIPCHIF FQDIEKILKI KFSLKDIILF QAIKKITKFL NKEKQKKFLL GFNDLLDTLL KYIKKEKTLR KLIIEKYPIV FIDEFQDTDI QQYQIFNILY NKNNKQTGLF LIGDPKQSIY SFRGADIFSY LYAKSKIKKY YYLNNNWRSS KNICKAINYL FLRNKNPFLF KDIPFIKISS SFNNQNIQFK IKGRIQTAIS FFFKKKEKIY IKDYQEWISK QCANEICYWL ICAKKGEAIL INKDKERILK TNDIVILVRN KNEANIIQNS LEKVNIQSIY SSSNQNIFKT TDAFELLIIL QTILQPTNIK LLKQSIFTHI FYNILLQGKK QNKIKQSYFI IKKLYEYREI WKNVGIFYTI KTIVLDYQKY SNDLNKTQYY QKNINFLHIA ELLEKQSEYL YQDSSLIRWF ENKILEKQNI LEDEHIRYFK QSNAIKIITI HKSKGLEYPI VWIPFAATYK KSNVYLYHDK KTFKMFLDLN QNKETEKIAD EERLAEDLRF LYVAITRSIF HCSIGMGDII NKKHQKTNNN HKSALGYIIQ RGCYMNYNNL LNELSLLNAK SYIKVKYDTM NIKLPYTKQD VYLLSPPQYI IKKIQNCFQI TSFTKLKKEH VSLNKSQDNY NINNILDYKS IYKKQIIFEN FPRGEKTGIL MHYILNKINF IEKLNINFFY KVLKQYEFSE KWAPILMSWV NNIINVKLKN INVNLSMLKQ NQYIKEMKFF LPIQKTLNSI DFNHIIQSLD PISSLTSKIS FNPITGILTG SIDLVFIWNE RYYIIDYKSN YLGDNQNLYS LKNIKKEIIK NRYDLQYQIY TVALHQYLTK KLKKYKYKNN FGGVFYMFLR GINKINENNS IFYTIPDYLL IKKLINLFLI KN //