ID A0A2P8HFW3_9BACI Unreviewed; 765 AA.
AC A0A2P8HFW3;
DT 23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT 23-MAY-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
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 ORFNames=B0H94_10798 {ECO:0000313|EMBL:PSL45093.1};
OS Salsuginibacillus halophilus.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Salsuginibacillus.
OX NCBI_TaxID=517424 {ECO:0000313|EMBL:PSL45093.1, ECO:0000313|Proteomes:UP000242310};
RN [1] {ECO:0000313|EMBL:PSL45093.1, ECO:0000313|Proteomes:UP000242310}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.07653 {ECO:0000313|EMBL:PSL45093.1,
RC ECO:0000313|Proteomes:UP000242310};
RA Whitman W.;
RT "Genomic Encyclopedia of Type Strains, Phase III (KMG-III): the genomes of
RT soil and plant-associated and newly described type strains.";
RL Submitted (MAR-2018) 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}.
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:PSL45093.1}.
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DR EMBL; PYAV01000007; PSL45093.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2P8HFW3; -.
DR OrthoDB; 9803432at2; -.
DR Proteomes; UP000242310; Unassembled WGS sequence.
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 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; 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 SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
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:PSL45093.1};
KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_01488};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_01488}; Reference proteome {ECO:0000313|Proteomes:UP000242310}.
FT DOMAIN 351..558
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT BINDING 362..366
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01488"
SQ SEQUENCE 765 AA; 85543 MW; 03CF7562C289ADD2 CRC64;
MQIFNPDANQ DMVQGTLVHT VYRSEETGYA VMHVKVVEAE PVVEKTRVTV VGLFPALELQ
ESYRFYGTHT EHPQYGEQFK AEQFERVLPT ENDAIVHYLS SDRFPGIGKK TAQAVVDVFG
SRTIQEILES PERLQEVPGL KAEKRELLVS QVAENQGMER VLLKLTQYGF GMNLAMKIYQ
VYAEETMATI EEDPYQLVWD IEGVGFHKAD RLGEVLGIAK TSPERMKAGL QFVMHELCLQ
GGHVYVPEEM LIDRAYTLLT TGGVVLEREK IMDAVVELAE ESRLVVDDGC AYLPSLYFAE
KGFVTHLLRL MNAADEEVEE AAFHEALGGA EEAFHMTYAP QQKEAIRTAV QSPVMILTGG
PGTGKTTVIQ AIVRVIAELE GLPAAPEPGG ETFPVLLAAP TGRAAKRMKE TTGLPAQTVH
KWLGYKGEMH EDENEGLERN ESHPLEGRLL IVDEFSMVDM WLANQLLRAV PEGMKVIFVG
DEDQLPSVGP GEVLGNLLTA DVLPAVSLST VYRQSEGSSI IDMAHAMKQG ELPKDWMEPK
DDRRFFSRAA EHIVEAVEQV CTNAKKRGYT AHEIQVLAPM YKGPAGIHAL NERLQQLFNP
PDEQRREVTF GEVVYRVGDV IMQLENDPES NVFNGDRGEI IAIFQAKEQA DRRMKIVLAF
DGNEVTYEKK DLRQITHAYC ASIHKSQGSE FPIVVAPVVM SYRRMLERNL IYTGITRAKD
FLILCGEKSA FEFAVQQDNR GSRNTRLVQL LKEAHNEEAK SAGYN
//
