ID A0A0A1MWT4_9BACI Unreviewed; 778 AA.
AC A0A0A1MWT4;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 27-MAR-2024, entry version 32.
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 ECO:0000313|EMBL:CEI83852.1};
GN ORFNames=BN997_03774 {ECO:0000313|EMBL:CEI83852.1};
OS Oceanobacillus oncorhynchi.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Oceanobacillus.
OX NCBI_TaxID=545501 {ECO:0000313|EMBL:CEI83852.1, ECO:0000313|Proteomes:UP000040453};
RN [1] {ECO:0000313|EMBL:CEI83852.1, ECO:0000313|Proteomes:UP000040453}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Oc5 {ECO:0000313|EMBL:CEI83852.1,
RC ECO:0000313|Proteomes:UP000040453};
RA Urmite Genomes Urmite Genomes;
RL Submitted (NOV-2014) 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; CDGG01000001; CEI83852.1; -; Genomic_DNA.
DR RefSeq; WP_042534325.1; NZ_JAUDBP010000007.1.
DR AlphaFoldDB; A0A0A1MWT4; -.
DR STRING; 545501.BN997_03774; -.
DR OrthoDB; 9803432at2; -.
DR Proteomes; UP000040453; 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: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; 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; 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; PF18335; SH3_13; 1.
DR Pfam; PF13538; UvrD_C_2; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
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:CEI83852.1};
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:UP000040453}.
FT DOMAIN 155..245
FT /note="RecD helicase-like helix-hairpin-helix"
FT /evidence="ECO:0000259|Pfam:PF14490"
FT DOMAIN 585..655
FT /note="RecD-like DNA helicase SH3"
FT /evidence="ECO:0000259|Pfam:PF18335"
FT DOMAIN 672..720
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13538"
FT REGION 759..778
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 361..365
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01488"
SQ SEQUENCE 778 AA; 87767 MW; E20F166DA1928744 CRC64;
MGNQIETKEA LPFVTGSVIN TIFRNEAEHF SIVRIKITKT NLDYQDKEII VKGYFDQLQD
QTAYCFYGVM EKHPRYGSQL KVQSYETILP TTKDGLVQYL SSDLFYGVGK KSALKIVEKL
GENAVSKIMD DPSVLDGVSG VSKETGKKLA ERLRENQGFE RVAVKLSEYG IGLKMAQVIY
QTYRDEALEV LKKDPYQYVF DIEGFGFKMA DQIASGQGIS HTHESRIGAG VIYILQQSIQ
AGHVYLPFEK CMQEVIYLLH LPNPDQGSVS DVIMQLNTEK KVIVIDERVY LPSLYYAEDN
FTASLKKILT KPIEDEVPLA ELLKITGEIE EEESLSYGKE QFDAIVQAIH SKIMILTGGP
GTGKTTVITG IIQAFAQIHE LSLNLSDYQK KDNFPFILTA PTGRAAKRMS ESTGLPAVTI
HRLLGWNGMG SFEKDEHEPL SGKLLIVDEF SMVDTWLANH LFKAIPDTMQ IILVGDEDQL
PSVGPGQVLT DLMKSEVLPV ISLTDVYRQK EGSKIIQLAH QIKNTDCDKN SLENARDFSF
ISCHDYQMTD VLTSIIDKAQ KKGIDSSSIQ VLSPMYRSQA GIHAINEALQ QLINPPGEKK
REIAFQDVVY RVGDRVIQLI NQPEDGIYNG DIGEIVAMFK PEENAENEEQ IVIAFEDKEV
VFIRKDYNNF THAFCISIHK SQGSEFPIVI LPVVYSHHRM LRKNLLYTAI TRGKESLIIC
GEKEAFIKGV QTEDTNRRYT SLQEMLHIQL ANQKAEKKEY ETVEDIPEEE LSPYDFMD
//
