ID A0A0B7J5D1_PHOPO Unreviewed; 1205 AA. AC A0A0B7J5D1; DT 01-APR-2015, integrated into UniProtKB/TrEMBL. DT 01-APR-2015, sequence version 1. DT 27-MAY-2015, entry version 3. 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 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. OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Photobacterium. OX NCBI_TaxID=659 {ECO:0000313|EMBL:CEO38256.1}; RN [1] {ECO:0000313|EMBL:CEO38256.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ANT-220 {ECO:0000313|EMBL:CEO38256.1}; 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. Degrades ssDNA until it encounters a chi (crossover CC hotspot instigator) sequence from the 3' direction. Cuts DNA near CC or within the chi site, which attenuates 3'- but not 5'- CC exonuclease activity. The altered holoenzyme produces a long 3'- CC ssDNA overhang and facilitates RecA-binding to the ssDNA for CC homologous DNA recombination and repair. Holoenzyme degrades CC foreign DNA, contributing to antiviral protection. This subunit CC has DNA-dependent ATPase activity, exo- and endonuclease activity, CC 3'-5' helicase activity and loads RecA onto ssDNA. CC {ECO:0000256|HAMAP-Rule:MF_01485}. CC -!- CATALYTIC ACTIVITY: Exonucleolytic cleavage (in the presence of CC ATP) in either 5'- to 3'- or 3'- to 5'-direction to yield 5'- CC phosphooligonucleotides. {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}. CC -!- SIMILARITY: Contains 1 uvrD-like helicase ATP-binding domain. CC {ECO:0000256|HAMAP-Rule:MF_01485}. CC -!- SIMILARITY: Contains 1 uvrD-like helicase C-terminal domain. CC {ECO:0000256|HAMAP-Rule:MF_01485}. CC -!- SIMILARITY: Contains uvrD-like helicase ATP-binding domain. CC {ECO:0000256|SAAS:SAAS00048467}. CC -!- SIMILARITY: Contains uvrD-like helicase C-terminal domain. CC {ECO:0000256|SAAS:SAAS00048480}. 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 GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004003; F:ATP-dependent DNA helicase activity; IEA:InterPro. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0008854; F:exodeoxyribonuclease V activity; IEA:UniProtKB-EC. DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.300; -; 5. 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; IPR004586; RecB. DR InterPro; IPR011335; Restrct_endonuc-II-like. DR InterPro; IPR014016; UvrD-like_ATP-bd. DR PANTHER; PTHR11070; PTHR11070; 1. DR Pfam; PF00580; UvrD-helicase; 1. DR Pfam; PF13361; UvrD_C; 1. DR SUPFAM; SSF52540; SSF52540; 4. 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 Antiviral defense {ECO:0000256|HAMAP-Rule:MF_01485}; KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_01485, KW ECO:0000256|SAAS:SAAS00146071}; KW DNA damage {ECO:0000256|HAMAP-Rule:MF_01485, KW ECO:0000256|SAAS:SAAS00048487}; KW DNA repair {ECO:0000256|HAMAP-Rule:MF_01485, KW ECO:0000256|SAAS:SAAS00048304}; KW DNA-binding {ECO:0000256|HAMAP-Rule:MF_01485, KW ECO:0000256|SAAS:SAAS00048455}; KW Endonuclease {ECO:0000256|HAMAP-Rule:MF_01485}; KW Exonuclease {ECO:0000256|HAMAP-Rule:MF_01485, KW ECO:0000256|SAAS:SAAS00048355}; KW Helicase {ECO:0000256|HAMAP-Rule:MF_01485, KW ECO:0000256|SAAS:SAAS00146013}; KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_01485, KW ECO:0000256|SAAS:SAAS00146062}; 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:SAAS00048484}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01485, KW ECO:0000256|SAAS:SAAS00145996}. FT DOMAIN 9 456 UvrD-like helicase ATP-binding. FT {ECO:0000256|HAMAP-Rule:MF_01485}. FT DOMAIN 487 756 UvrD-like helicase C-terminal. FT {ECO:0000256|HAMAP-Rule:MF_01485}. FT NP_BIND 30 37 ATP. {ECO:0000256|HAMAP-Rule:MF_01485}. FT REGION 1 867 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 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 //