ID D3D6C1_9ACTN Unreviewed; 1148 AA.
AC D3D6C1;
DT 23-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 23-MAR-2010, sequence version 1.
DT 24-JAN-2024, entry version 72.
DE RecName: Full=DNA 3'-5' helicase {ECO:0000256|ARBA:ARBA00034808};
DE EC=5.6.2.4 {ECO:0000256|ARBA:ARBA00034808};
GN ORFNames=FrEUN1fDRAFT_5343 {ECO:0000313|EMBL:EFC81514.1};
OS Parafrankia sp. EUN1f.
OC Bacteria; Actinomycetota; Actinomycetes; Frankiales; Frankiaceae;
OC Parafrankia.
OX NCBI_TaxID=102897 {ECO:0000313|EMBL:EFC81514.1, ECO:0000313|Proteomes:UP000004777};
RN [1] {ECO:0000313|EMBL:EFC81514.1, ECO:0000313|Proteomes:UP000004777}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EUN1f {ECO:0000313|EMBL:EFC81514.1,
RC ECO:0000313|Proteomes:UP000004777};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Tice H., Bruce D., Goodwin L.,
RA Pitluck S., Larimer F., Land M.L., Hauser L., Beauchemin N., Sen A.,
RA Fernandez M., Tisa L.;
RT "The draft genome of Frankia sp. EUN1f.";
RL Submitted (JAN-2010) 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:EFC81514.1}.
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DR EMBL; ADGX01000103; EFC81514.1; -; Genomic_DNA.
DR AlphaFoldDB; D3D6C1; -.
DR Proteomes; UP000004777; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003678; F:DNA helicase activity; IEA:InterPro.
DR GO; GO:0004527; F:exonuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
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; IPR011335; Restrct_endonuc-II-like.
DR InterPro; IPR014016; UvrD-like_ATP-bd.
DR PANTHER; PTHR11070:SF59; 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; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF52980; Restriction endonuclease-like; 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-binding {ECO:0000256|ARBA:ARBA00023125};
KW Helicase {ECO:0000256|PROSITE-ProRule:PRU00560,
KW ECO:0000313|EMBL:EFC81514.1};
KW Hydrolase {ECO:0000256|PROSITE-ProRule:PRU00560};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00560}.
FT DOMAIN 5..302
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51198"
FT DOMAIN 313..655
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51217"
FT REGION 470..516
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1013..1061
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1024..1038
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 26..33
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ SEQUENCE 1148 AA; 121272 MW; 9C974224D5FB9B11 CRC64;
MVSPIVLDAA QAEVVGHAGG PLLVLAGPGT GKTTTLVEAV ARRVEAGADP ASLLVLTFSR
RAARHLRERL AVRLGAGAVG PAAWTFHAWC LALLRVYGAD TASGGPRLLS GPEQDARLRD
LLEGSRELGR PAWPDALAGA LGTRGFAEEV RMLMARAREV GVDPPALARI ARRVGRADWK
AVAEFYGDYL DALGAEGAID YADLVHSAAN LTAQQPVLAS LRQRYQAVFV DEYQDTDPAQ
ERLLAAVAGG GGDLVVFGDP DQAIYAFRGA QVRGLLDFPA RFPSRDGSPA PVTALRRCRR
MAPAPLAASR RVAARLPSAG LPVRYVRAHR DLVPADSAAG PGQVSVRTYP TAGAEAEAVA
DLLRREHLEN GVGWADMAVL VRSTAGLGVL RRVLTASGVP VSVGGGELPV AREPAAELLL
TALRCADDPS RHLTPETARA LLTSPLGGAD PAGLRALGRE LRALDAATTV SPAQDDALAR
DAAADDAPAQ EDVPSPDGGD EHAGAARMPG TPASSSELLR AAVADPQRML LMVPDELAAP
VHRLGQLLRT VRAELRRGGA PEDALWTLWS ASGWGPRLER ASAAGGAAGR SADRDLDAVV
ALFDAVERLG ERRGPGFGVA SVVSELTHQQ IAPDTETRAG RPATVRLLTA HRSKGLEWQV
VVVCGVQDGV WPDLRQRHSL LGAEQLDAPH RGGGGVRPPR TRDELLADER RLFYVALTRA
RRRLVVTAVD GADDDGEQPS RFLDELGVQV EKVRSRSVRP LTLVGLVAAL RRLTVDPDAS
AAMRSAAAVR LAALAAARDG AGRTLVPAAH PNRWWGLVDV TSSSVPVVAP DGPIALSGSS
LSGLATCGLR WFLEHEAQAA EPASAAQGFG KVVHALADEV SSGRTPARMD ALDARLDLVW
RQLEFDSRWR SEQERSAARE ALRRFLDWHA ARRREVVASE VRFACDIEVA GRVVRLRGFI
DRVELDDDGR VHVVDFKTGR AAPSRRDLQT HAQLGSYQLA VREGALDRVL DEAAAGSRAA
PDPGSATDSG SATGLGSGSD PGSVPDPGSA AGSRPPAVPG GAELVHLRRD AGGESLGPRL
PDEQPAPPEV QAQEALPTDG RVWIDDLVED AVRTITSESF RPTPGDACTM CSFRRSCPAR
PEGEQVID
//