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Database: UniProt
Entry: A0A0N1GRF2_9ACTN
LinkDB: A0A0N1GRF2_9ACTN
Original site: A0A0N1GRF2_9ACTN 
ID   A0A0N1GRF2_9ACTN        Unreviewed;      1197 AA.
AC   A0A0N1GRF2;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   27-MAR-2024, entry version 41.
DE   RecName: Full=DNA 3'-5' helicase {ECO:0000256|ARBA:ARBA00034808};
DE            EC=5.6.2.4 {ECO:0000256|ARBA:ARBA00034808};
GN   ORFNames=OV320_7337 {ECO:0000313|EMBL:KPI25862.1};
OS   Actinobacteria bacterium OV320.
OC   Bacteria; Actinomycetota; Actinomycetes.
OX   NCBI_TaxID=1592329 {ECO:0000313|EMBL:KPI25862.1, ECO:0000313|Proteomes:UP000037870};
RN   [1] {ECO:0000313|EMBL:KPI25862.1, ECO:0000313|Proteomes:UP000037870}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OV320 {ECO:0000313|EMBL:KPI25862.1,
RC   ECO:0000313|Proteomes:UP000037870};
RA   Brown S.D., Utturkar S.M., Klingeman D.M., Pelletier D.;
RT   "Draft genome sequences for four actinobacteria strains OK006 OK074 OV450
RT   and OV320.";
RL   Submitted (AUG-2015) to the EMBL/GenBank/DDBJ databases.
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   -!- SIMILARITY: Belongs to the helicase family. UvrD subfamily.
CC       {ECO:0000256|ARBA:ARBA00009922}.
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:KPI25862.1}.
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DR   EMBL; LJCX01000029; KPI25862.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0N1GRF2; -.
DR   PATRIC; fig|1592329.3.peg.6712; -.
DR   Proteomes; UP000037870; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0003678; F:DNA helicase activity; IEA:InterPro.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-UniRule.
DR   CDD; cd17932; DEXQc_UvrD; 1.
DR   Gene3D; 1.10.10.160; -; 1.
DR   Gene3D; 3.90.320.10; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 3.
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; IPR011604; PDDEXK-like_dom_sf.
DR   InterPro; IPR038726; PDDEXK_AddAB-type.
DR   InterPro; IPR014016; UvrD-like_ATP-bd.
DR   PANTHER; PTHR11070:SF55; DNA HELICASE; 1.
DR   PANTHER; PTHR11070; UVRD / RECB / PCRA DNA HELICASE FAMILY MEMBER; 1.
DR   Pfam; PF12705; PDDEXK_1; 1.
DR   Pfam; PF00580; UvrD-helicase; 1.
DR   Pfam; PF13361; UvrD_C; 2.
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   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU00560}; DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW   DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW   Exonuclease {ECO:0000256|ARBA:ARBA00022839};
KW   Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000256|PROSITE-
KW   ProRule:PRU00560};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW   ProRule:PRU00560}; Nuclease {ECO:0000256|ARBA:ARBA00022722};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU00560}; Reference proteome {ECO:0000313|Proteomes:UP000037870}.
FT   DOMAIN          17..343
FT                   /note="UvrD-like helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51198"
FT   DOMAIN          344..666
FT                   /note="UvrD-like helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51217"
FT   REGION          835..947
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1164..1197
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        856..891
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         38..45
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ   SEQUENCE   1197 AA;  129624 MW;  AAA7E73C77AC9F60 CRC64;
     MPARISDPEQ LKELLGIPFT PEQTACITAP PAPQVIVAGA GSGKTTVMAA RVVWLVGTGQ
     VAPEQVLGLT FTNKAAGELA ERVRKALVKA GVTDPDLIDP DNPPGEPVIS TYHSFAGRLL
     TDHGLRIGLE PTSRLLADAT RYQLAARVLR EAPGPYPSLT RSFADLISDL LALDAELAEH
     LVRPEDLRAW DAALLNGLEG AGLTNADLRK VPEAAAARRE LAELVLRYRT AKRERDLLDF
     GDQIALAARL SQVPEVGPIL REEFRVVLLD EYQDTSVAQR ILLAGLFGGG TGHPVTAVGD
     PCQAIYGWRG ASVANLDDFP EHFAHTDGSR ARRQSLSENR RSGGRLLDLA NGLAEPLRAM
     HAGVEALRPA PGAERDGLVR CALLNTHAEE MDWIADSIAH LVRTGKAPGE IAVLCRTATD
     FAEIQGALVA RDIPVEVVGL SGLLHLPEVA DLVAVCEVLQ DPGANASLVR LLTGPRWRIG
     PRDLALLGRR ARLLVTHARG GGDDDPDRRL AEAVEGVDPS EVISLADALD TFLETPLYGD
     GGAGYDDGLP FSPDARVRFA RLATELRDLR RSLADPLMDV LHRVLAVTGL EVELSASPQA
     LAARRRETLS NFLDVAASFA ASESQASLLA FLGFLRTAAQ YEKGLDNALP GGENTVKVLT
     AHKSKGLEWD VVAVPGLVTG TFPSGQGREK WTAQAKVLPH ELRGDAATLP DLDSWDARGM
     KAFHEAMKDH QHTEELRLGY VTFTRPRSLL LGSGHWWGPT QKKPRGPSDF LQELYRHCAA
     GHGEIEAWAD EPEEGTENPV LHRPTADQVW PLPLDDDSLA RRRAAAETVL AHLEDLASHQ
     DGNPGATHDP DTYDDPDWPP PPDEDELSYG SEYDEPEYGD PEYDEPEYGG PGYDDPEYGS
     DSSYDESGPF EDAPLENTPL AVPHQATAPE LPVTRPRRRP SLTPEEARAV ASWDRDLDAL
     AGELLRARRS VTDVTLPTTL TASQVLRLAA DPDGLAQELA RPMPRPPQPA ARRGTRFHAW
     VEARFEELTL PLLEPHELPG EDAEIADERD LEALKEAFES TEYAHRTPYR VEAPFQLALA
     GRVVRGRIDA VYKEGDGDTA TYDIVDWKTH RARTADPLQL ALYRLAWAEQ QGVPVESVTA
     AFLYVRSGDV VRPEGLPDRA ALERLLTGED GAGDGRGGPA AQVNPAQGPG EDVGAGR
//
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