ID A0A0B7J5D1_PHOPO Unreviewed; 1205 AA. AC A0A0B7J5D1; DT 01-APR-2015, integrated into UniProtKB/TrEMBL. DT 01-APR-2015, sequence version 1. DT 05-DEC-2018, entry version 24. 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:CEO38256.1}; GN ORFNames=PPBDW_I20269 {ECO:0000313|EMBL:CEO38256.1}; OS Photobacterium phosphoreum ANT-2200. OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Photobacterium. OX NCBI_TaxID=1454202 {ECO:0000313|EMBL:CEO38256.1, ECO:0000313|Proteomes:UP000019762}; RN [1] {ECO:0000313|EMBL:CEO38256.1, ECO:0000313|Proteomes:UP000019762} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ANT220 {ECO:0000313|Proteomes:UP000019762}; RA Genoscope - CEA; RL Submitted (DEC-2014) 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 -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CEO38256.1}. 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; CCAR020000004; CEO38256.1; -; Genomic_DNA. DR RefSeq; WP_054262090.1; NZ_LN794352.1. DR EnsemblBacteria; CEO38256; CEO38256; PPBDW_I20269. DR Proteomes; UP000019762; Unassembled WGS sequence. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0004003; F:ATP-dependent DNA helicase activity; IEA:UniProtKB-UniRule. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule. DR GO; GO:0008854; F:exodeoxyribonuclease V activity; IEA:UniProtKB-EC. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IEA:UniProtKB-UniRule. 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:SAAS01099289}; KW Complete proteome {ECO:0000313|Proteomes:UP000019762}; 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, ECO:0000313|EMBL:CEO38256.1}; KW Helicase {ECO:0000256|HAMAP-Rule:MF_01485, KW ECO:0000256|SAAS:SAAS00938801}; KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_01485, KW ECO:0000256|SAAS:SAAS01033118, ECO:0000313|EMBL:CEO38256.1}; 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:SAAS01099286}. FT DOMAIN 9 456 UvrD-like helicase ATP-binding. FT {ECO:0000259|PROSITE:PS51198}. FT DOMAIN 487 756 UvrD-like helicase C-terminal. FT {ECO:0000259|PROSITE:PS51217}. FT REGION 1 864 DNA-binding and helicase activity, FT interacts with RecC. {ECO:0000256|HAMAP- FT Rule:MF_01485}. FT REGION 914 1205 Nuclease activity, interacts with RecD FT and RecA. {ECO:0000256|HAMAP-Rule: FT MF_01485}. FT ACT_SITE 1107 1107 For nuclease activity. FT {ECO:0000256|HAMAP-Rule:MF_01485}. FT METAL 980 980 Magnesium; via tele nitrogen. FT {ECO:0000256|HAMAP-Rule:MF_01485}. FT METAL 1094 1094 Magnesium. {ECO:0000256|HAMAP-Rule: FT MF_01485}. FT METAL 1107 1107 Magnesium. {ECO:0000256|HAMAP-Rule: FT MF_01485}. SQ SEQUENCE 1205 AA; 135182 MW; 645E2B41FB7141EB CRC64; MATEVLTTEV LTNILQPMTF PLHGTRLIEA SAGTGKTFTI ASLYLRLLLG HGNDNNRHQQ QLTVDQILVV TFTEAATAEL RDRIRARIHD ARLAFSRGVS HDPVIAPLLN EHQDHKLAAT ILLQAERQMD EAAIYTIHGF CQRMLTQNAF ESGSRFNNEF VTDESQLKKL VVADYWRSNF YHLPPALAHE VREIWSSPTA LLKEIGNSLT GAPVRLSVAA MTESLAQLHQ QNIVRIDEVK ALWRAHQADL EALIASSGIN KRSYTKKSLP NWLEQVSGWA AQPTVGYELP DNLIRFHQQT LIEKTAKGDA PEHAVFSAIA ELLDNPANLR EPLLAHAIEH CRQLLADAKA RKGWLSFDDL LTQLGAAIDN DVDELLAGKI RAQYPVAMID EFQDTDPLQY GIFSDVYRHH PECGLFMIGD PKQAIYAFRG ADIFTYIQAR RQVSDHYTLA TNWRSTANMI AAVNGVFQQP DSPFIYDQDI EFLAVDHSPK AAQRSWWLEG EAQHALTFWL QESADGKPIT KGNYQATMAA ATAAQIQHIL TQSQQQQAYF LDGEQQHAIA AGDIAVLVRT GTEGRLVREV LSKQGIASVY LSNRDSVFST SEAADIQRLL QAVLTPEDDR ILRAALASGL FARTAIELDQ LNNDENEWEI AVNSFKQYRQ QWLKRGVMPM LRSVMAKNQI AERLLAEDGG ERKLTDLLHI GELLQQASQT LDSDYALLRW LAEHVAEPDG NADDQVMRLE SERNLVQIVT IHKSKGLEYD LVFMPFVCSY REVDSKGEVK YHDEVDNITV LDIAKQAAAI EKADQERLAE DLRLIYVALT RAVYGCYVGM APIRNGRSTK EPTGLHRSAM GHLVQNGQAG GVAALELALA KLSEAQIAIT VTAPPQLLDS QWQPQDEVTE ALVKRPFAAS LERNWWMTSY SNLVKQGHQT AHDSSLDLPG FDIDSVQNAT EEVDDSELEL EPQYSIYTFP RGARPGTFLH TVFEEIDFTA AVDCDETVAK LTELLQLENY ELAWLPVLQQ LIRDVLTCPL DGDMLRLADK TASQRLTEME FLLPIEILQA VTLNKVIAKH DPLSAKAGEL GFATVSGMLK GFIDLVFEHQ GKYYVLDWKS NYLGDDPQVY RGEQLQTAMR EHRYDLQYQI YALALQRFLR SRIPNYSYET HFGGVYYLFL RGVQAGSDSG IFYARPSEIL LDELDLVMNG ALPHA //