ID Q47P31_THEFY Unreviewed; 736 AA.
AC Q47P31;
DT 13-SEP-2005, integrated into UniProtKB/TrEMBL.
DT 13-SEP-2005, sequence version 1.
DT 27-MAR-2024, entry version 121.
DE RecName: Full=ATP-dependent RecD-like DNA helicase {ECO:0000256|HAMAP-Rule:MF_01488};
DE EC=3.6.4.12 {ECO:0000256|HAMAP-Rule:MF_01488};
GN Name=recD2 {ECO:0000256|HAMAP-Rule:MF_01488};
GN OrderedLocusNames=Tfu_1753 {ECO:0000313|EMBL:AAZ55788.1};
OS Thermobifida fusca (strain YX).
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Nocardiopsaceae; Thermobifida.
OX NCBI_TaxID=269800 {ECO:0000313|EMBL:AAZ55788.1};
RN [1] {ECO:0000313|EMBL:AAZ55788.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=YX {ECO:0000313|EMBL:AAZ55788.1};
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 -!- FUNCTION: DNA-dependent ATPase and ATP-dependent 5'-3' DNA helicase.
CC Has no activity on blunt DNA or DNA with 3'-overhangs, requires at
CC least 10 bases of 5'-ssDNA for helicase activity. {ECO:0000256|HAMAP-
CC Rule:MF_01488}.
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=3.6.4.12;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01488};
CC -!- SIMILARITY: Belongs to the RecD family. RecD-like subfamily.
CC {ECO:0000256|HAMAP-Rule:MF_01488}.
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DR EMBL; CP000088; AAZ55788.1; -; Genomic_DNA.
DR AlphaFoldDB; Q47P31; -.
DR STRING; 269800.Tfu_1753; -.
DR KEGG; tfu:Tfu_1753; -.
DR eggNOG; COG0507; Bacteria.
DR HOGENOM; CLU_007524_0_2_11; -.
DR OrthoDB; 9763659at2; -.
DR GO; GO:0043139; F:5'-3' DNA helicase activity; 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-UniRule.
DR CDD; cd17933; DEXSc_RecD-like; 1.
DR CDD; cd18809; SF1_C_RecD; 1.
DR Gene3D; 1.10.10.2220; -; 1.
DR Gene3D; 2.30.30.940; -; 1.
DR Gene3D; 1.10.150.20; 5' to 3' exonuclease, C-terminal subdomain; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR HAMAP; MF_01488; RecD_like; 1.
DR InterPro; IPR006345; DNA_helicase_RecD-like.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR029493; RecD-like_HHH.
DR InterPro; IPR041451; RecD-like_SH13.
DR InterPro; IPR010994; RuvA_2-like.
DR InterPro; IPR027785; UvrD-like_helicase_C.
DR NCBIfam; TIGR01448; recD_rel; 1.
DR PANTHER; PTHR43788; DNA2/NAM7 HELICASE FAMILY MEMBER; 1.
DR PANTHER; PTHR43788:SF6; RECBCD ENZYME SUBUNIT RECD; 1.
DR Pfam; PF13245; AAA_19; 1.
DR Pfam; PF14490; HHH_4; 1.
DR Pfam; PF14520; HHH_5; 1.
DR Pfam; PF18335; SH3_13; 1.
DR Pfam; PF13538; UvrD_C_2; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF47781; RuvA domain 2-like; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_01488}; DNA-binding {ECO:0000256|HAMAP-Rule:MF_01488};
KW Helicase {ECO:0000256|HAMAP-Rule:MF_01488, ECO:0000313|EMBL:AAZ55788.1};
KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_01488, ECO:0000313|EMBL:AAZ55788.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_01488}.
FT DOMAIN 148..238
FT /note="RecD helicase-like helix-hairpin-helix"
FT /evidence="ECO:0000259|Pfam:PF14490"
FT DOMAIN 575..640
FT /note="RecD-like DNA helicase SH3"
FT /evidence="ECO:0000259|Pfam:PF18335"
FT DOMAIN 660..708
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13538"
FT BINDING 362..366
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01488"
SQ SEQUENCE 736 AA; 80291 MW; D925E92D9BEE8EBB CRC64;
MASGEPFRPA VLEGVLERIT YVNEETGYTV ARVDTGRGSD LVTVVGALLG AHPGESLRME
GRWTSHPQYG RQFQVENYTT VLPATVQGIR RYLGSGLVKG IGPRLAEHIV NHFGAAALDV
IENSPERLLE VPKLGPKRTK IITEAWEEQK AIKEVMVFLQ TVKVSTSLAV RIYKQYGDDA
IRVVREEPYS LAADVWGIGF KTADSIAQAV GIPHDSPQRV KAGIQFTLSE FTNDGHCYLP
EDTLINEAVK ILQVDSALVI DCLAELVAEE RVVREKVPDR DGESVTAIYL LPFYRAETAL
ANQVRALLHT EHDRLASFAT VDWDRALAWL RSQTGAELAP AQEKAVKLAL TNKVAVLTGG
PGCGKSFTVA SIIKLAAAKR AKIMLAAPTG RAAKRLTELT GYDASTVHRL LELKPGGEAA
YDRDNPLDCD LLVVDEASML DLLLANKLVK AVPPGAHLLL VGDVDQLPSV GAGQVLRDLL
ADGSPVPSVR LTHVFRQAAQ SGVVTNAHRI NTGKPLLLEG MTDFYLFPCE DTEAAAELTV
DVVARRIPRR FGLDPRRDIQ VLTPMHRGPA GAGNLNMLLQ EALTPARPGV AERRVGSRVF
RVGDKVVQIR NNYDKGANGV FNGTLGTVTA IDLDDQTLTV LTDENEEVGY EFTELDELTH
AYALTVHRSQ GSEYPCVVVP VTTSAWMMLQ RNLLYTAVTR AKKLVVLVGS RRAIAQAIRN
ASSGRRHTAL DYRLQR
//
