ID D6YBB0_THEBD Unreviewed; 746 AA.
AC D6YBB0;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 27-MAR-2024, entry version 67.
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=Tbis_1757 {ECO:0000313|EMBL:ADG88470.1};
OS Thermobispora bispora (strain ATCC 19993 / DSM 43833 / CBS 139.67 / JCM
OS 10125 / KCTC 9307 / NBRC 14880 / R51).
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Streptosporangiaceae; Thermobispora.
OX NCBI_TaxID=469371 {ECO:0000313|EMBL:ADG88470.1, ECO:0000313|Proteomes:UP000006640};
RN [1] {ECO:0000313|EMBL:ADG88470.1, ECO:0000313|Proteomes:UP000006640}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 19993 / DSM 43833 / CBS 139.67 / JCM 10125 / KCTC 9307 /
RC NBRC 14880 / R51 {ECO:0000313|Proteomes:UP000006640};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K., Ivanova N.,
RA Mikhailova N., Chertkov O., Brettin T., Detter J.C., Han C., Larimer F.,
RA Land M., Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T.,
RA Wu D., Jando M., Schneider S., Klenk H.-P., Eisen J.A.;
RT "The complete genome of Thermobispora bispora DSM 43833.";
RL Submitted (JAN-2010) 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; CP001874; ADG88470.1; -; Genomic_DNA.
DR AlphaFoldDB; D6YBB0; -.
DR STRING; 469371.Tbis_1757; -.
DR KEGG; tbi:Tbis_1757; -.
DR eggNOG; COG0507; Bacteria.
DR HOGENOM; CLU_007524_0_2_11; -.
DR Proteomes; UP000006640; Chromosome.
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:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006281; P:DNA repair; IEA:InterPro.
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; IPR003593; AAA+_ATPase.
DR InterPro; IPR006345; DNA_helicase_RecD-like.
DR InterPro; IPR003583; Hlx-hairpin-Hlx_DNA-bd_motif.
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 SMART; SM00382; AAA; 1.
DR SMART; SM00278; HhH1; 3.
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:ADG88470.1};
KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_01488, ECO:0000313|EMBL:ADG88470.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_01488}; Reference proteome {ECO:0000313|Proteomes:UP000006640}.
FT DOMAIN 105..119
FT /note="Helix-hairpin-helix DNA-binding motif class 1"
FT /evidence="ECO:0000259|SMART:SM00278"
FT DOMAIN 133..152
FT /note="Helix-hairpin-helix DNA-binding motif class 1"
FT /evidence="ECO:0000259|SMART:SM00278"
FT DOMAIN 197..216
FT /note="Helix-hairpin-helix DNA-binding motif class 1"
FT /evidence="ECO:0000259|SMART:SM00278"
FT DOMAIN 361..557
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT BINDING 372..376
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01488"
SQ SEQUENCE 746 AA; 81538 MW; 5F005BF372F775A4 CRC64;
MGVGLEGSER NKPNGVTLKG TLERITYVNE ETGYTIARLA TERSDKELLT VVGPLLGAQV
GESLLLTGRW TTHPRYGRQF EVWSYTTLLP ATIQGIQRYL GSGLIKGIGP KMAERIVNHF
GTDTLRVIEE EPERLTEVPG LGPKRMKMIA DAWEEQKIIK EVMVFLQGVG VSTSIAVRIF
KQYGEASINV VRNEPYRLAD EVWGIGFKTA DAIARSIGIP HDSPGRVKAG LRYTLSQAAD
NGHCYLPAPN LIAEAVKILD VPQDLAAKCL EELIAEEGVI REDIPAGENG ESAIPAIYLV
PFHRAEQSLA ATLRGLLTAD RDRLAAFANV DWDAAFDWLH ARTGGARLAP EQAEAVRLAL
TEKVAILTGG PGCGKSFTVR SIVMLARAKR AKVVLAAPTG RAAKRLAELT GHEATTVHRL
LQLRPGGDAS FDRDNPLDAD LVVVDEASML DLLLANKLAK AVPKGAHLLF VGDVDQLPSV
GAGEVLRDLL AAPEIPRVRL TRIFRQAQES GVVVNAHRVN SGKPPLVREF PDFFLFPAED
PEEIARLTVD VVARRIPARF GLDPRRDVQV LVPMHRGVAG AAALNVALQE ALTPYREGVP
ERRYGGRVFR VGDKVTQLRN NYDKGAAGVF NGTVGVVTDI SLEESTLTVR TDEDESVDYS
FDELDELAHA YAVSIHRSQG SEYPAVVIPL ATSAWMMLQR NLLYTAITRA KRLVVIVGSR
RAIWQAVRTK GAGRRYTGLT HRLRAR
//
