ID A0A3R9NGU2_9BACI Unreviewed; 805 AA.
AC A0A3R9NGU2;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 18.
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=EJF36_14365 {ECO:0000313|EMBL:RSK27970.1};
OS Bacillus sp. HMF5848.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=2495421 {ECO:0000313|EMBL:RSK27970.1, ECO:0000313|Proteomes:UP000274811};
RN [1] {ECO:0000313|EMBL:RSK27970.1, ECO:0000313|Proteomes:UP000274811}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HMF5848 {ECO:0000313|EMBL:RSK27970.1,
RC ECO:0000313|Proteomes:UP000274811};
RA Kang H., Kang J., Cha I., Kim H., Joh K.;
RT "Bacillus sp. HMF5848 Genome sequencing and assembly.";
RL Submitted (DEC-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:RSK27970.1}.
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DR EMBL; RWIV01000001; RSK27970.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3R9NGU2; -.
DR OrthoDB; 9803432at2; -.
DR Proteomes; UP000274811; 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; PF13604; AAA_30; 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; 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:RSK27970.1};
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:UP000274811}.
FT DOMAIN 158..249
FT /note="RecD helicase-like helix-hairpin-helix"
FT /evidence="ECO:0000259|Pfam:PF14490"
FT DOMAIN 593..656
FT /note="RecD-like DNA helicase SH3"
FT /evidence="ECO:0000259|Pfam:PF18335"
FT DOMAIN 681..728
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13538"
FT BINDING 369..373
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01488"
SQ SEQUENCE 805 AA; 91052 MW; F35739068086D535 CRC64;
MEEQGVLHFT EADRPYVKGS LIATIFHNEE NLFSVVRIQI DDTNTTYKEK DIVINGYFPR
LHDGEVYIFA GDLKDHPRFG LQFQAANFRK EKPQTKEGLV QYLSSDLFEG IGKKTAQSIV
KTLGDNAISK ILEDKEVLKQ VPNLSRDRAN KLYTTLSEHE GLEQIMIHLA KYGFGPQLSM
KIYQAYKDQT LQIIQDNPYQ LVEDVDGIGF SRADELGHQL GISGNHPDRI KAGCLYIIEN
ASMQEGHVYI LIENALSNIY DLLCKNNSES IEFKDISREM IHLHEEGKLV IEDQKVYLPS
LYYSEKGFVS NIKRVLDQTD FQDAFPESEF LLALGSLEER LNVQYAPSQK EAIETALMSP
MLILTGGPGT GKTTVIKGIV ELYAELHGLS LNHKDYKKEE GFPILLVAPT GRAAKRMSES
TGLPAHTIHR LLGWNGVDGF TYNEDQLLNG KLLIVDEFSM VDIWLANQLM KALPEQIQVV
FVGDEDQLPS VGPGQVLKDL LEAKVVPTVR LTDIYRQAEG SSIIDLAHDI KNGKVPRNLR
EQKQDRSFIN CSTSQVLDVV RKVAQNAKQK GFTAKDIQVL APMYRGAAGI DAINEALQEL
FNGKTETKRE INFGEKVFRT GDKVLQLVNL PEENVFNGDI GEIVSIFYAK ENQEKKDLVI
ISYDGNEVQY EKQDLGQITL AYCCSVHKAQ GSEFPIVILP IVKSYFRMLR RNLIYTAITR
SKKFLILCGE EEAFRRGIEF EDDTKRQTTL SEKLKITLNN HKQEAKLEQI PKPNSHDIKD
VLPELPCEDD MADISPYDFM EDNKS
//
