ID A0A0K9H8F4_9BACI Unreviewed; 796 AA.
AC A0A0K9H8F4;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 34.
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=AC623_13605 {ECO:0000313|EMBL:KMY54842.1};
OS Bacillus sp. FJAT-27231.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=1679168 {ECO:0000313|EMBL:KMY54842.1, ECO:0000313|Proteomes:UP000037077};
RN [1] {ECO:0000313|Proteomes:UP000037077}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FJAT-27231 {ECO:0000313|Proteomes:UP000037077};
RA Liu B., Wang J., Zhu Y., Liu G., Chen Q., Chen Z., Che J., Ge C., Shi H.,
RA Pan Z., Liu X.;
RT "Genome sequencing project for genomic taxonomy and phylogenomics of
RT Bacillus-like bacteria.";
RL Submitted (JUL-2015) 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:KMY54842.1}.
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DR EMBL; LFZU01000001; KMY54842.1; -; Genomic_DNA.
DR RefSeq; WP_049663343.1; NZ_LFZU01000001.1.
DR AlphaFoldDB; A0A0K9H8F4; -.
DR STRING; 1679168.AC623_13605; -.
DR PATRIC; fig|1679168.3.peg.2913; -.
DR OrthoDB; 9803432at2; -.
DR Proteomes; UP000037077; 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; 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};
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:UP000037077}.
FT DOMAIN 157..248
FT /note="RecD helicase-like helix-hairpin-helix"
FT /evidence="ECO:0000259|Pfam:PF14490"
FT DOMAIN 592..660
FT /note="RecD-like DNA helicase SH3"
FT /evidence="ECO:0000259|Pfam:PF18335"
FT DOMAIN 680..728
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13538"
FT BINDING 368..372
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01488"
SQ SEQUENCE 796 AA; 89159 MW; 55510C91C9E06321 CRC64;
MEQESMDLFA NGEKYVKGRH LVTIFHNEEN FYSVIRVRVT ETNDACEDKE VVVTGYFPQI
HEHEVYIFYG VFKEHPKFGR QFQARHAQKE IPQTKQGIVA YLSSDLFKGI GKKTAEAIVE
TLGEGAISQI LNHPSALEEV PRLPADKAQT IYETLLEHQG LEQIMIALSQ YGFGPQLSMK
IYQAYQQQAI EIIQKNPYQL VEDIEGIGFG RADELGAQIG IHGEHPDRIK AGILFTIEQQ
CMQEGHCYLE AEPLLKEVKI LLEKSGRESV SFEAIAKQLI ALEGAGKVMG EEDRVFLPSL
YFSEKGLVTN IERLLKQTEY EDQFPESEFL LALGDLEDRT GVQYAPSQKE AIQKALMSPM
MLLTGGPGTG KTTVIKGIVE LYAELHGCSL DPKSYGKDEP FPIKLAAPTG RAAKRMAEST
GLPAVTIHRL LGFSGQETME DEEGREVSGR LLIVDEVSMV DIWLAHQLFK SLPDDMQVVL
VGDEDQLPSV GPGQVLKDLL ASGVIPTVKL TDIYRQEEGS SIIEMAHEIK NGLVPSNLTK
QQKDRSFISC HVQQMPDVVE QVVKSAIRKG FTAKDIQVLA PMYKGPAGID RLNEILQEIL
NANPDGSRKQ IDFGDVHYRI GDKVLQLVNQ PEQNIFNGDI GEVVSIFFAK ENTEKQDMVI
VSYEGNEVTY TRQELNQITH AFCCSIHKSQ GSEFPIVILP VVKSYYRMLR RNLLYTAITR
SKQFLILCGE EEAFRMGIER NDDLMRKTSL KEKLVEALKA GQSEEEASSP ISLTEDTIMT
IDPMIGMGNI TPYDFL
//
