ID Q47LQ9_THEFY Unreviewed; 754 AA.
AC Q47LQ9;
DT 13-SEP-2005, integrated into UniProtKB/TrEMBL.
DT 13-SEP-2005, sequence version 1.
DT 27-MAR-2024, entry version 130.
DE RecName: Full=ATP-dependent DNA helicase {ECO:0000256|RuleBase:RU364053};
DE EC=5.6.2.4 {ECO:0000256|RuleBase:RU364053};
GN OrderedLocusNames=Tfu_2580 {ECO:0000313|EMBL:AAZ56613.1};
OS Thermobifida fusca (strain YX).
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Nocardiopsaceae; Thermobifida.
OX NCBI_TaxID=269800 {ECO:0000313|EMBL:AAZ56613.1};
RN [1] {ECO:0000313|EMBL:AAZ56613.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=YX {ECO:0000313|EMBL:AAZ56613.1};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Di Bartolo G., Chain P., Schmutz J.,
RA Larimer F., Land M., Lykidis A., Richardson P.;
RT "Complete sequence of Thermobifida fusca YX.";
RL Submitted (JUL-2005) 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 ECO:0000256|RuleBase:RU364053};
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, ECO:0000256|RuleBase:RU364053}.
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DR EMBL; CP000088; AAZ56613.1; -; Genomic_DNA.
DR AlphaFoldDB; Q47LQ9; -.
DR STRING; 269800.Tfu_2580; -.
DR KEGG; tfu:Tfu_2580; -.
DR eggNOG; COG0210; Bacteria.
DR HOGENOM; CLU_004585_5_2_11; -.
DR OrthoDB; 5240387at2; -.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
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:UniProtKB-KW.
DR GO; GO:0003678; F:DNA helicase activity; IEA:InterPro.
DR GO; GO:0006268; P:DNA unwinding involved in DNA replication; IEA:InterPro.
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; IPR005751; ATP-dep_DNA_helicase_PcrA.
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 NCBIfam; TIGR01073; pcrA; 1.
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 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00560}; DNA-binding {ECO:0000256|RuleBase:RU364053};
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 Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00560}.
FT DOMAIN 9..295
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51198"
FT DOMAIN 296..591
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51217"
FT BINDING 30..37
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ SEQUENCE 754 AA; 84043 MW; 8EE61CF43472AC8A CRC64;
MSSQEQLLEG LNELQRAAVL HHGSPLLIIA GAGSGKTRVL THRIAYLLAE RGVRPSEVLA
ITFTNKAAAE MKERVERLLG ERTASAMWVM TFHSACVRIL RREAARLGYP SSFTIYDSAD
SQRLMQLVCR ELDLDPKRFP PKSFSAQVSS LKNELVDYDT FAGRAETVQE RALAEAYQLY
QQRLYEAGAM DFDDLIMVTV HLLQMFPEVA EHYRRRFRHL LVDEYQDTNH AQYALIRELV
GDGDPATPGP ELCVVGDADQ SIYAFRGATI RNILEFERDY PQATTILLEQ NYRSTQTILS
AANAVIAHNT ERRPKNLWSA QGEGEPIVGY VADDERDEAT FVVQEIDALT DAGTCTPGDV
AVFYRTNAQS RVLEEVFVRT GMPYRIVGGV RFYERKEIRD ILAYLRVLAN PEDSVSLRRI
LNVPKRGIGE RAEQVIEQFA AQERITFAQA LRRADEAPGI ATRSLKAIKE FVALLEELEE
LAATRSPAET IEAVLERTGY LEELVNSKDI QDESRVENLE EFVGVAREFE SSFDAALAAE
GADGETGRDG AEPTLVDFLE QVSLIADTDQ LPDEDDQGGA VTLMTLHSAK GLEFPVVFLT
GLEDGVFPHL RALGDRSALE EERRLVYVGI TRAQERLYLT RAATRSSWGA AAYNPPSRFL
DEIPAELVTW RRAESTTEAL RRSVSPARTS RPTRKAERPV LALRPGDKVN HDSFGLGTVL
SVDGTGDRTR ARVDFGAGVG QKDLMVKFAP LEKL
//