RECD_HAEIN
ID RECD_HAEIN Reviewed; 640 AA.
AC P45158;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=RecBCD enzyme subunit RecD {ECO:0000255|HAMAP-Rule:MF_01487};
DE EC=3.1.11.5 {ECO:0000255|HAMAP-Rule:MF_01487};
DE AltName: Full=Exonuclease V subunit RecD {ECO:0000255|HAMAP-Rule:MF_01487};
DE Short=ExoV subunit RecD {ECO:0000255|HAMAP-Rule:MF_01487};
DE AltName: Full=Helicase/nuclease RecBCD subunit RecD {ECO:0000255|HAMAP-Rule:MF_01487};
GN Name=recD {ECO:0000255|HAMAP-Rule:MF_01487}; OrderedLocusNames=HI_1322;
OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=71421;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX PubMed=7542800; DOI=10.1126/science.7542800;
RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT Rd.";
RL Science 269:496-512(1995).
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:0000255|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:0000255|HAMAP-
CC Rule:MF_01487};
CC -!- SUBUNIT: Heterotrimer of RecB, RecC and RecD. All subunits contribute
CC to DNA-binding. {ECO:0000255|HAMAP-Rule:MF_01487}.
CC -!- SIMILARITY: Belongs to the RecD family. {ECO:0000255|HAMAP-
CC Rule:MF_01487}.
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DR EMBL; L42023; AAC22967.1; -; Genomic_DNA.
DR PIR; E64116; E64116.
DR RefSeq; NP_439473.1; NC_000907.1.
DR RefSeq; WP_005694450.1; NC_000907.1.
DR AlphaFoldDB; P45158; -.
DR SMR; P45158; -.
DR STRING; 71421.HI_1322; -.
DR EnsemblBacteria; AAC22967; AAC22967; HI_1322.
DR KEGG; hin:HI_1322; -.
DR PATRIC; fig|71421.8.peg.1374; -.
DR eggNOG; COG0507; Bacteria.
DR HOGENOM; CLU_007524_1_2_6; -.
DR OMA; MIDLEMM; -.
DR PhylomeDB; P45158; -.
DR BioCyc; HINF71421:G1GJ1-1347-MON; -.
DR Proteomes; UP000000579; Chromosome.
DR GO; GO:0009338; C:exodeoxyribonuclease V complex; IEA:InterPro.
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:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IEA:UniProtKB-UniRule.
DR Gene3D; 1.10.10.1020; -; 1.
DR Gene3D; 3.40.50.300; -; 3.
DR HAMAP; MF_01487; RecD; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR006344; RecD.
DR InterPro; IPR041851; RecD_N.
DR InterPro; IPR027785; UvrD-like_helicase_C.
DR Pfam; PF13538; UvrD_C_2; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR TIGRFAMs; TIGR01447; recD; 1.
PE 3: Inferred from homology;
KW ATP-binding; DNA damage; DNA repair; DNA-binding; Exonuclease; Helicase;
KW Hydrolase; Nuclease; Nucleotide-binding; Reference proteome.
FT CHAIN 1..640
FT /note="RecBCD enzyme subunit RecD"
FT /id="PRO_0000087116"
FT BINDING 194..201
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01487"
SQ SEQUENCE 640 AA; 72864 MW; C3C530AC398B5DA0 CRC64;
MLSVLHKLKE LRILSQGDYY FAKLIADKQC HTDYAEPVKN LAILLAALCS WRYTQGNTCS
QLDRYLEHNL FGLAYRTTEE DYLAEIHEKI GYLPVEDWQN ALCGHMAFTQ DPVNQIAPMA
FQFGALYFYR AWQDEYRIVQ YIKNTLKKYR TLAFSYDEIH QKLEKYFPEK QEKTDWQKVA
VATAIKSPFS IITGGPGTGK TTTVTRLLLV LQELFDCKLH IKLVAPTGKA ASRLEESIKN
ALGFMQEKMN VSHSLFNAIP QKASTLHSLL GVNAFNDYTR YNSHNPLQLD VLVVDETSMI
DLPMMAKLIN ALKPETRLIL LGDQAQLASV EAGAVLGELA QFVTQPYSHE QAAYLLATTG
YKVEGSDCSN PIRDCLCHLT ESRRFDKDSG IGKLSEFIQK GKADDSLELF DHYPQELHFN
SLNDEGDAVN QVVKSAVENY RTFLKMLDDL RKQKIDPNAK NEQGISYAEA IQVQFNSVRF
LTALRNNNLG VENLNKEIAL ALREQKLLWF RNEQDWYIGK PIMITENDHN VRLYNGDIGL
CLANGKVWFG NREVLTNRIP AHEPAFMMTI HKSQGSEFKH TVMVLPTEVN PVLSRELVFT
GVTRAKKELT VFADEKIWKT AIRQTVKRQS GLGKLLEDLN
