ID A8L2I8_FRASN Unreviewed; 1135 AA.
AC A8L2I8;
DT 04-DEC-2007, integrated into UniProtKB/TrEMBL.
DT 04-DEC-2007, sequence version 1.
DT 27-MAR-2024, entry version 96.
DE RecName: Full=DNA 3'-5' helicase {ECO:0000256|ARBA:ARBA00034808};
DE EC=5.6.2.4 {ECO:0000256|ARBA:ARBA00034808};
GN ORFNames=Franean1_0925 {ECO:0000313|EMBL:ABW10381.1};
OS Frankia sp. (strain EAN1pec).
OC Bacteria; Actinomycetota; Actinomycetes; Frankiales; Frankiaceae; Frankia.
OX NCBI_TaxID=298653 {ECO:0000313|EMBL:ABW10381.1};
RN [1] {ECO:0000313|EMBL:ABW10381.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=EAN1.pec {ECO:0000313|EMBL:ABW10381.1};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Hammon N.,
RA Israni S., Dalin E., Tice H., Pitluck S., Saunders E., Brettin T.,
RA Bruce D., Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L.,
RA Kyrpides N., Kim E., Rawnsley T., Niemann J., Benson D.R., Huang Y.,
RA Mastronunzio J., Bassi C.A., Tisa L.S., Richardson P.;
RT "Complete sequence of Frankia sp. EAN1pec.";
RL Submitted (AUG-2007) 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}.
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DR EMBL; CP000820; ABW10381.1; -; Genomic_DNA.
DR AlphaFoldDB; A8L2I8; -.
DR STRING; 298653.Franean1_0925; -.
DR KEGG; fre:Franean1_0925; -.
DR eggNOG; COG0210; Bacteria.
DR eggNOG; COG2887; Bacteria.
DR HOGENOM; CLU_004900_0_0_11; -.
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: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; 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 damage {ECO:0000256|ARBA:ARBA00022763};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
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}.
FT DOMAIN 1..297
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51198"
FT DOMAIN 308..655
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51217"
FT REGION 469..507
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1013..1082
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 21..28
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ SEQUENCE 1135 AA; 120587 MW; 375C4CA194CBDD07 CRC64;
MLDTAQTDVV GHAGGPLLVL AGPGTGKTTT LVEAVARRIE AGADPASLLV LTFSRRAARH
LRERFAVRLG AAAVGPAAWT FHAWCLGLLR AYGAATPLGG FRLLSGPEQD ARLRDLIEGS
RELGRPVWPD PLAGCLNTRG FAEEIRMLLT RAREIGVDPP ALARIARRVG RSDWAAVAEF
YSDYLDALGA EGALDYADLV HAAANLAAEP DVLAQLRQRY RAVFVDEYQD TDPAQERLLT
AVAGGGGDLV VFGDPDQSIY AFRGAEVRGL LDFPNRFPRA DGSPAPVAAL RRCRRMAPAP
LAASRRVAAS LPSAGLPVRH VRAHRDLVSA GAVGPGQVAA RTYPTAGAEA AAIAELLRRE
HLENGVDWDD MAVLVRSTAP LGLLRRVLTA AGVPVSVAGG ELPPAREPAA ALLLTALRCA
DDPAVQLTPE TARALLTSPL GGADPAGLRA LGRELRAHDA AARAAARAAA RGTAARGTTA
RDSTARDAVG PIALPEPRSA PEADGSVLGL PASSAELLRE AVADPERVLL AVPDELAAPV
RRLGRLLRTV RAELRRGAAP EDALWTLWTA SEWGPRLERA SAVGGPAGRS ADRDLDAVVA
LFDAVGRLGE RRGPGFGVSS VVEELTRQQI APETAQARAG RPATVRLLTA HRSKGLEWEV
VVVCGVQDGV WPDLRQRHTL LGAEQLDSPR NGGVRPPRTR EELLADERRL FYVALTRARR
RLVVTAVDGA DDDGEQPSRF LAELGVQVES VRARPPRPLT LVGLVAALRR LTVDPEASAA
MREAAGVRLA ALAAASDETG RALVPAAHPD RWWGLLDVTS SDVPVVAPDA PIRLSGSSLS
GLSSCGLRWF LEHEANAAEP ASPAQGFGKV VHALADEVTT GRTEARLEAL DARLDLVWRH
LEFDSRWRSE QERAAAREAL GRFLEWHAAQ RGREVVASEV RFSCDIEVAG RVVRLRGFID
RVELDDAGRV HVVDFKTGRT PPSRRDLATH AQLGSYQLAV REGALDPVLD EAARRHDPPA
PGEVPGAGDL SGAGAPSTAG ERPAPVPGGA ELVQLRRDAG GDNTGPRLPA EEPGPPEVQR
QDALPGGRAW IDDMVENAVR TVTTESFRPT PGEGCTMCSF RRCCPGRPEG EQVID
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