ID   Q9RTI9_DEIRA            Unreviewed;       745 AA.
AC   Q9RTI9;
DT   01-MAY-2000, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2000, sequence version 1.
DT   27-MAR-2024, entry version 146.
DE   RecName: Full=DNA 3'-5' helicase {ECO:0000256|ARBA:ARBA00034808};
DE            EC=5.6.2.4 {ECO:0000256|ARBA:ARBA00034808};
GN   OrderedLocusNames=DR_1775 {ECO:0000313|EMBL:AAF11329.1};
OS   Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / CCUG
OS   27074 / LMG 4051 / NBRC 15346 / NCIMB 9279 / VKM B-1422 / R1).
OC   Bacteria; Deinococcota; Deinococci; Deinococcales; Deinococcaceae;
OC   Deinococcus.
OX   NCBI_TaxID=243230 {ECO:0000313|EMBL:AAF11329.1, ECO:0000313|Proteomes:UP000002524};
RN   [1] {ECO:0000313|EMBL:AAF11329.1, ECO:0000313|Proteomes:UP000002524}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 /
RC   NCIMB 9279 / R1 / VKM B-1422 {ECO:0000313|Proteomes:UP000002524};
RX   PubMed=10567266; DOI=10.1126/science.286.5444.1571;
RA   White O., Eisen J.A., Heidelberg J.F., Hickey E.K., Peterson J.D.,
RA   Dodson R.J., Haft D.H., Gwinn M.L., Nelson W.C., Richardson D.L.,
RA   Moffat K.S., Qin H., Jiang L., Pamphile W., Crosby M., Shen M.,
RA   Vamathevan J.J., Lam P., McDonald L., Utterback T., Zalewski C.,
RA   Makarova K.S., Aravind L., Daly M.J., Minton K.W., Fleischmann R.D.,
RA   Ketchum K.A., Nelson K.E., Salzberg S., Smith H.O., Venter J.C.,
RA   Fraser C.M.;
RT   "Genome sequence of the radioresistant bacterium Deinococcus radiodurans
RT   R1.";
RL   Science 286:1571-1577(1999).
RN   [2] {ECO:0007829|PDB:4C2T, ECO:0007829|PDB:4C2U}
RP   X-RAY CRYSTALLOGRAPHY (2.55 ANGSTROMS) OF 1-665 IN COMPLEX WITH ATP ANALOG.
RX   PubMed=24143224; DOI=10.1371/JOURNAL.PONE.0077364;
RA   Stelter M., Acajjaoui S., McSweeney S., Timmins J.;
RT   "Structural and mechanistic insight into DNA unwinding by Deinococcus
RT   radiodurans UvrD.";
RL   PLoS ONE 8:e77364-e77364(2013).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=5.6.2.4;
CC         Evidence={ECO:0000256|ARBA:ARBA00034618};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Couples ATP hydrolysis with the unwinding of duplex DNA by
CC         translocating in the 3'-5' direction.; EC=5.6.2.4;
CC         Evidence={ECO:0000256|ARBA:ARBA00034617};
CC   -!- SIMILARITY: Belongs to the helicase family. UvrD subfamily.
CC       {ECO:0000256|ARBA:ARBA00009922}.
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DR   EMBL; AE000513; AAF11329.1; -; Genomic_DNA.
DR   PIR; E75354; E75354.
DR   RefSeq; NP_295498.1; NC_001263.1.
DR   RefSeq; WP_010888410.1; NZ_JMLF01000027.1.
DR   PDB; 4C2T; X-ray; 4.00 A; A/B/C/D=1-745.
DR   PDB; 4C2U; X-ray; 2.55 A; A/D=1-665.
DR   PDB; 4C30; X-ray; 3.00 A; A/D/F/I=1-665.
DR   PDBsum; 4C2T; -.
DR   PDBsum; 4C2U; -.
DR   PDBsum; 4C30; -.
DR   AlphaFoldDB; Q9RTI9; -.
DR   SMR; Q9RTI9; -.
DR   DIP; DIP-48319N; -.
DR   IntAct; Q9RTI9; 1.
DR   STRING; 243230.DR_1775; -.
DR   PaxDb; 243230-DR_1775; -.
DR   EnsemblBacteria; AAF11329; AAF11329; DR_1775.
DR   GeneID; 69518015; -.
DR   KEGG; dra:DR_1775; -.
DR   PATRIC; fig|243230.17.peg.1987; -.
DR   eggNOG; COG0210; Bacteria.
DR   HOGENOM; CLU_004585_5_2_0; -.
DR   InParanoid; Q9RTI9; -.
DR   OrthoDB; 9810135at2; -.
DR   Proteomes; UP000002524; Chromosome I.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0033202; C:DNA helicase complex; IBA:GO_Central.
DR   GO; GO:0043138; F:3'-5' DNA helicase activity; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0000725; P:recombinational repair; IBA:GO_Central.
DR   CDD; cd17932; DEXQc_UvrD; 1.
DR   CDD; cd18807; SF1_C_UvrD; 1.
DR   Gene3D; 1.10.10.160; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   InterPro; IPR013986; DExx_box_DNA_helicase_dom_sf.
DR   InterPro; IPR014017; DNA_helicase_UvrD-like_C.
DR   InterPro; IPR000212; DNA_helicase_UvrD/REP.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR014016; UvrD-like_ATP-bd.
DR   PANTHER; PTHR11070:SF2; ATP-DEPENDENT DNA HELICASE SRS2; 1.
DR   PANTHER; PTHR11070; UVRD / RECB / PCRA DNA HELICASE FAMILY MEMBER; 1.
DR   Pfam; PF21196; PcrA_UvrD_tudor; 1.
DR   Pfam; PF00580; UvrD-helicase; 1.
DR   Pfam; PF13361; UvrD_C; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS51198; UVRD_HELICASE_ATP_BIND; 1.
DR   PROSITE; PS51217; UVRD_HELICASE_CTER; 1.
PE   1: Evidence at protein level;
KW   3D-structure {ECO:0007829|PDB:4C2T, ECO:0007829|PDB:4C2U};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU00560};
KW   Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000256|PROSITE-
KW   ProRule:PRU00560};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW   ProRule:PRU00560};
KW   Metal-binding {ECO:0007829|PDB:4C2T, ECO:0007829|PDB:4C2U};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU00560}; Reference proteome {ECO:0000313|Proteomes:UP000002524}.
FT   DOMAIN          11..293
FT                   /note="UvrD-like helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51198"
FT   DOMAIN          294..575
FT                   /note="UvrD-like helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51217"
FT   BINDING         32..39
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
FT   BINDING         39
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0007829|PDB:4C2U, ECO:0007829|PDB:4C30"
FT   BINDING         39
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0007829|PDB:4C2T"
FT   BINDING         227
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0007829|PDB:4C2T"
FT   BINDING         228
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0007829|PDB:4C2T"
FT   BINDING         397
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0007829|PDB:4C30"
SQ   SEQUENCE   745 AA;  82597 MW;  A4946F40E5FCD309 CRC64;
     MTSSAGPDLL QALNPTQAQA ADHFTGPALV IAGAGSGKTR TLIYRIAHLI GHYGVHPGEI
     LAVTFTNKAA AEMRERAGHL VPGAGDLWMS TFHSAGVRIL RTYGEHIGLR RGFVIYDDDD
     QLDIIKEVMG SIPGIGAETQ PRVIRGIIDR AKSNLWTPDD LDRSREPFIS GLPRDAAAEA
     YRRYEVRKKG QNAIDFGDLI TETVRLFKEV PGVLDKVQNK AKFIHVDEYQ DTNRAQYELT
     RLLASRDRNL LVVGDPDQSI YKFRGADIQN ILDFQKDYPD AKVYMLEHNY RSSARVLEAA
     NKLIENNTER LDKTLKPVKE AGQPVTFHRA TDHRAEGDYV ADWLTRLHGE GRAWSEMAIL
     YRTNAQSRVI EESLRRVQIP ARIVGGVGFY DRREIRDILA YARLALNPAD DVALRRIIGR
     PRRGIGDTAL QKLMEWARTH HTSVLTACAN AAEQNILDRG AHKATEFAGL MEAMSEAADN
     YEPAAFLRFV METSGYLDLL RQEGQEGQVR LENLEELVSA AEEWSQDEAN VGGSIADFLD
     DAALLSSVDD MRTKAENKGA PEDAVTLMTL HNAKGLEFPV VFIVGVEQGL LPSKGAIAEG
     PSGIEEERRL FYVGITRAME RLLMTAAQNR MQFGKTNAAE DSAFLEDIEG LFDTVDPYGQ
     PIEYRAKTWK QYRPTVPAAT TAVKNTSPLT AELAYRGGEQ VKHPKFGEGQ VLAVAGVGER
     QEVTVHFASA GTKKLMVKFA NLTKL
//