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Database: UniProt
Entry: U1GID2_9ACTN
LinkDB: U1GID2_9ACTN
Original site: U1GID2_9ACTN 
ID   U1GID2_9ACTN            Unreviewed;      1123 AA.
AC   U1GID2;
DT   13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2013, sequence version 1.
DT   11-DEC-2019, entry version 46.
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   ORFNames=H641_02207 {ECO:0000313|EMBL:ERF57900.1};
OS   Cutibacterium granulosum DSM 20700.
OC   Bacteria; Actinobacteria; Propionibacteriales; Propionibacteriaceae;
OC   Cutibacterium.
OX   NCBI_TaxID=1160719 {ECO:0000313|EMBL:ERF57900.1, ECO:0000313|Proteomes:UP000016307};
RN   [1] {ECO:0000313|EMBL:ERF57900.1, ECO:0000313|Proteomes:UP000016307}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 20700 {ECO:0000313|EMBL:ERF57900.1,
RC   ECO:0000313|Proteomes:UP000016307};
RX   PubMed=24053623; DOI=10.1186/1471-2164-14-640;
RA   Mak T.N., Schmid M., Brzuszkiewicz E., Zeng G., Meyer R., Sfanos K.S.,
RA   Brinkmann V., Meyer T.F., Bruggemann H.;
RT   "Comparative genomics reveals distinct host-interacting traits of three
RT   major human-associated propionibacteria.";
RL   BMC Genomics 14:640-640(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       contributes ATPase, 3'-5' helicase, exonuclease activity and loads RecA
CC       onto ssDNA. {ECO:0000256|HAMAP-Rule:MF_01485}.
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_01485};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01485};
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|HAMAP-Rule:MF_01485};
CC   -!- SUBUNIT: Heterotrimer of RecB, RecC and RecD. All subunits contribute
CC       to DNA-binding. Interacts with RecA. {ECO:0000256|HAMAP-Rule:MF_01485}.
CC   -!- DOMAIN: The C-terminal domain has nuclease activity and interacts with
CC       RecD. It interacts with RecA, facilitating its loading onto ssDNA.
CC       {ECO:0000256|HAMAP-Rule:MF_01485}.
CC   -!- DOMAIN: The N-terminal DNA-binding domain is a ssDNA-dependent ATPase
CC       and has ATP-dependent 3'-5' helicase function. This domain interacts
CC       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 EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:ERF57900.1}.
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DR   EMBL; AOSS01000059; ERF57900.1; -; Genomic_DNA.
DR   RefSeq; WP_021103461.1; NZ_AOSS01000059.1.
DR   EnsemblBacteria; ERF57900; ERF57900; H641_02207.
DR   EnsemblBacteria; OCT42394; OCT42394; L860_10450.
DR   PATRIC; fig|1160719.4.peg.419; -.
DR   OrthoDB; 137860at2; -.
DR   BioCyc; GCF_000463665:G1EH1-438-MONOMER; -.
DR   Proteomes; UP000016307; Unassembled WGS sequence.
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: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; 2.
DR   PANTHER; PTHR11070:SF23; PTHR11070:SF23; 2.
DR   Pfam; PF12705; PDDEXK_1; 1.
DR   Pfam; PF00580; UvrD-helicase; 2.
DR   Pfam; PF13361; UvrD_C; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   SUPFAM; SSF52980; SSF52980; 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};
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, ECO:0000256|SAAS:SAAS00553650};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_01485, 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, ECO:0000256|SAAS:SAAS01033141};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01485,
KW   ECO:0000256|SAAS:SAAS00145996};
KW   Reference proteome {ECO:0000313|Proteomes:UP000016307}.
FT   REGION          1..764
FT                   /note="DNA-binding and helicase activity, interacts with
FT                   RecC"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01485"
FT   REGION          801..1123
FT                   /note="Nuclease activity, interacts with RecD and RecA"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01485"
FT   ACT_SITE        1013
FT                   /note="For nuclease activity"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01485"
FT   METAL           867
FT                   /note="Magnesium; via tele nitrogen"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01485"
FT   METAL           999
FT                   /note="Magnesium"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01485"
FT   METAL           1013
FT                   /note="Magnesium"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01485"
SQ   SEQUENCE   1123 AA;  122416 MW;  1A341A3863A3602C CRC64;
     MTSPHEVKAF DISGEVPHGT TLLRASAGTG KTWSITAIVT RAILEGDVDI SQVLLVTFNR
     SAARQMRHRT YARLARTAEM LESGLPARDD LDHHLLAQRE RRDEFLSRAR SAIQRFSTAT
     IATTHEFCAQ MLTELGVLAD HDLRSSLLAD PTPLVDEVSA DLYLSRYSHV PRPPSSATIR
     SLARTVAAQY GTVELQRDSD SRRVEERLDI AEAVRTESSR RMRAGGLHTF DDLIEDLARS
     LGSTQRGRVA CATLADRFHL VMVDEFQDTD PLQWEILASA FHGRSDLWLI GDPKQSIYAF
     RGADIHAYLA ATRQVDHTYE LTTNWRSDQG IVDGVDQLFR HTHLGAEGIE FTTVSARHTH
     RRLQSTDPHG YDWSHPVQIR CITASDGSRL SSGRAEDLIA KDVGAQITAM LDGRSQWQPE
     KGQPSRPLQA GDIAVLVTAR RRGTKIQNEL RKIGQPAVFT GSTSVWSSPA ATDFLDLLSA
     LDDPDPTVIS RIAMSRLIGA APYDLARQDS QLRSALAMDI ANWALAWPNL GPWGVIESLL
     HRPGSLDSML TGPQAERYVT DLRQLAQETH VWACDQPTMP TPAQTCAWVE DQARYAPQET
     PRRLETDRNA VTIMTVHQAK GLEFPVVLLP DATLSWISKN GEGTRRKQRA SRTFMRDDGS
     PLVWFDGERR VLNLSDVNDP ARLEAWAQIR HDALAEELRK LYVALTRSQS AVRLWWAPVP
     GRIGDSGLQR LLALESAGSE APVFPEPVND AAVSPPWLSP RVGGASIEAV PVEVTEAPSR
     ELPVPPVGGT PATFTRSVDH QWKRTSYSGL TAGIHGATSS MADLVDASAG QDEPDEDALG
     TSPDVSPSTG DGLCAMPGGT SFGLVVHEIL EHVDTSVPDL SAEITNWTAR KLRAEPIDGV
     GATSLAAGLV DVMHTDLGEL APGQCLADFK PSDRLAELDF EMRLAPSSPM SNTVGALAQA
     LSDRSLVPEN DPLASYGRVL ATSPAASTVL SGYLTGSIDA VLRRPDGRFL VIDYKTNRAP
     RPAGQPLEPR AYDVTTMTSM MISSHYPLQA LLYSAALHRY LSHTMPGYDP ATCLGPVGYL
     FVRAMAGVAT PADASMPYGV FTWSVNPALV VAVSDILGGR HEH
//
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