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Database: UniProt
Entry: G4CRW5_9NEIS
LinkDB: G4CRW5_9NEIS
Original site: G4CRW5_9NEIS 
ID   G4CRW5_9NEIS            Unreviewed;       576 AA.
AC   G4CRW5;
DT   14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT   14-DEC-2011, sequence version 1.
DT   24-JAN-2024, entry version 47.
DE   RecName: Full=RecBCD enzyme subunit RecD {ECO:0000256|HAMAP-Rule:MF_01487};
DE            EC=3.1.11.5 {ECO:0000256|HAMAP-Rule:MF_01487};
DE   AltName: Full=Exonuclease V subunit RecD {ECO:0000256|HAMAP-Rule:MF_01487};
DE            Short=ExoV subunit RecD {ECO:0000256|HAMAP-Rule:MF_01487};
DE   AltName: Full=Helicase/nuclease RecBCD subunit RecD {ECO:0000256|HAMAP-Rule:MF_01487};
GN   Name=recD {ECO:0000256|HAMAP-Rule:MF_01487,
GN   ECO:0000313|EMBL:EGZ44879.1};
GN   ORFNames=HMPREF9370_1825 {ECO:0000313|EMBL:EGZ44879.1};
OS   Neisseria wadsworthii 9715.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Neisseria.
OX   NCBI_TaxID=1030841 {ECO:0000313|EMBL:EGZ44879.1, ECO:0000313|Proteomes:UP000005336};
RN   [1] {ECO:0000313|EMBL:EGZ44879.1, ECO:0000313|Proteomes:UP000005336}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=9715 {ECO:0000313|EMBL:EGZ44879.1,
RC   ECO:0000313|Proteomes:UP000005336};
RA   Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., Zhang L.,
RA   Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., Korchina V.,
RA   Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., Nguyen N., Okwuonu G.,
RA   Ongeri F., Pham C., Simmons D., Wilczek-Boney K., Hale W., Jakkamsetti A.,
RA   Pham P., Ruth R., San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C.,
RA   Zhu D., Lee S., Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S.,
RA   Hirani K., Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S.,
RA   Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L.,
RA   Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P.,
RA   Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K.,
RA   Petrosino J., Highlander S., Gibbs R.;
RL   Submitted (JUN-2011) 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 has
CC       ssDNA-dependent ATPase and 5'-3' helicase activity. When added to pre-
CC       assembled RecBC greatly stimulates nuclease activity and augments
CC       holoenzyme processivity. Negatively regulates the RecA-loading ability
CC       of RecBCD. {ECO:0000256|HAMAP-Rule:MF_01487}.
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_01487};
CC   -!- SUBUNIT: Heterotrimer of RecB, RecC and RecD. All subunits contribute
CC       to DNA-binding. {ECO:0000256|HAMAP-Rule:MF_01487}.
CC   -!- SIMILARITY: Belongs to the RecD family. {ECO:0000256|HAMAP-
CC       Rule:MF_01487}.
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:EGZ44879.1}.
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DR   EMBL; AGAZ01000063; EGZ44879.1; -; Genomic_DNA.
DR   RefSeq; WP_009116966.1; NZ_JH165159.1.
DR   AlphaFoldDB; G4CRW5; -.
DR   STRING; 1030841.HMPREF9370_1825; -.
DR   PATRIC; fig|1030841.3.peg.1816; -.
DR   HOGENOM; CLU_007524_1_1_4; -.
DR   OrthoDB; 9803432at2; -.
DR   Proteomes; UP000005336; Unassembled WGS sequence.
DR   GO; GO:0009338; C:exodeoxyribonuclease V complex; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
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   CDD; cd18809; SF1_C_RecD; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   HAMAP; MF_01487; RecD; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR006344; RecD.
DR   InterPro; IPR027785; UvrD-like_helicase_C.
DR   NCBIfam; TIGR01447; recD; 1.
DR   PANTHER; PTHR43788:SF6; DNA HELICASE B; 1.
DR   PANTHER; PTHR43788; DNA2/NAM7 HELICASE FAMILY MEMBER; 1.
DR   Pfam; PF13245; AAA_19; 1.
DR   Pfam; PF13538; UvrD_C_2; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_01487};
KW   DNA damage {ECO:0000256|HAMAP-Rule:MF_01487};
KW   DNA repair {ECO:0000256|HAMAP-Rule:MF_01487};
KW   DNA-binding {ECO:0000256|HAMAP-Rule:MF_01487};
KW   Exonuclease {ECO:0000256|HAMAP-Rule:MF_01487};
KW   Helicase {ECO:0000256|HAMAP-Rule:MF_01487};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_01487, ECO:0000313|EMBL:EGZ44879.1};
KW   Nuclease {ECO:0000256|HAMAP-Rule:MF_01487};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01487}.
FT   DOMAIN          136..296
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   BINDING         144..151
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01487"
SQ   SEQUENCE   576 AA;  62836 MW;  4CC1E34ABD9C74C4 CRC64;
     MDSLVLDGFA AEAAVSLLER VAPEVGGVVS PFVDKLFAAL AEGHSFIWLD KHDIAALKQA
     RPVVGGDAGS PLILRGNKLF LGKMWQLEQD LARQILRIAA VKPEPVDWLN ASHHLADWFS
     EPGSRDQKAA AALALLQNFM VISGGPGTGK TTTVAKLLAL LCVNAGKLPR IALVAPTGKA
     AAHMAKALHR ALGQFNAGAA IKAHLEHLEG QTVHRLLKFK PPYMQPAYHA DNPLPLDMIV
     VDEASMLDTA LLLQLLSAVP DGCRVIILGD ENQLPSVGAG AVLAALARQT VLTETTAQEL
     TDLLPEQPFA VSDRPDPLAA NIARLTISHR FGEYSGIGCL ARAVVQGNVE DALAQFERFP
     NEIRIHDMNI DGQLETLYRL QQNYWQAVAQ NDVKAAFGHQ ADCMVLAAWR NNAEHFNQAY
     QAYLKKIGII KQEEYWFAGQ MLMVSRNDYT LDLFNGDIGL VLRDDASDTG ALAAYFPDGD
     EFRKIALSRL PECETAFAMT VHKSQGSEYK EVWLLPPMGY DLAKTAGAGL NRALLYTAIT
     RARERFVFLG KTEAFKAACL QEETRRSAVR EMLAEG
//
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