ID A0A401IQV6_9LACO Unreviewed; 836 AA.
AC A0A401IQV6;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 20.
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=recD {ECO:0000313|EMBL:GBG93929.1};
GN Synonyms=recD2 {ECO:0000256|HAMAP-Rule:MF_01488};
GN ORFNames=LFYK43_03880 {ECO:0000313|EMBL:GBG93929.1};
OS Ligilactobacillus salitolerans.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Ligilactobacillus.
OX NCBI_TaxID=1808352 {ECO:0000313|EMBL:GBG93929.1, ECO:0000313|Proteomes:UP000286848};
RN [1] {ECO:0000313|Proteomes:UP000286848}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YK43 {ECO:0000313|Proteomes:UP000286848};
RA Tohno M., Tanizawa Y.;
RT "Draft genome sequences of Lactobacillus sp. YK43.";
RL Submitted (APR-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:GBG93929.1}.
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DR EMBL; BFFP01000004; GBG93929.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A401IQV6; -.
DR OrthoDB; 9803432at2; -.
DR Proteomes; UP000286848; 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};
KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_01488};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_01488}.
FT DOMAIN 162..251
FT /note="RecD helicase-like helix-hairpin-helix"
FT /evidence="ECO:0000259|Pfam:PF14490"
FT DOMAIN 590..661
FT /note="RecD-like DNA helicase SH3"
FT /evidence="ECO:0000259|Pfam:PF18335"
FT DOMAIN 678..726
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13538"
FT BINDING 372..376
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01488"
SQ SEQUENCE 836 AA; 93297 MW; 3E604499D3A9AA1B CRC64;
MVQQNLELLD DRQMQGEFYL VGRVAQIFFQ SSTNFYKVLL VTVKENNFNW AEKTITVTGS
FAEIREETLY RFSGQVVHHP KYGQQFQAAN YQTEMPTSKA GLVTYLSSSQ FPGIGQKTAE
RIVDILGDDA LNILLKDPSQ ISKLGLKEQQ QEVLKTNLQA DQGMEQIIVG LNSLGFSSNM
AARIYGFFQE DTLKTLHEDP YQLSIHINGI GFYRADQIAR QLGFAADAPG RLRGAIFQVL
YEFSASEGNT YIPGKILLQQ TQQLLQAGQN QKITVDQIAD ELIKLVNARK LALEDHNFYL
KKYFYGEWEI ATELERIISS NEDEDTTEEP EKLATDLAKI EQRMGIEYDE TQKEAIIQAL
STQVFLLTGG PGTGKTTIIN GIVALYAYEN DIDLEDKHLP ILLAAPTGRA AKRMSEMTGL
PASTIHRLLG INGHDDELPD EIDELDGTLL IIDETSMVDT DLMKILLKSI PAGMQVIFVG
DRHQLPSVGP GQVFADMLQS NVLPKKELTK IYRQGEFSTI VSLAHAINAG QLPANFAEQQ
GDRSFIPCST AQVPQVIAQV IKVALRKGNS EEKIQVLAPM YRGPAGIDNL NQLLQNIMNP
KTNTHQKEIE VNGQIFRIGD RVLQLVNDPE KNIYNGDIGK IVAIDIGEQK EKAADSITVA
FEQTEVEIGK KDWNNLTLAY CLSIHKSQGG EFPIVILPMV KQFSRMFARN LLYTAVTRAK
SKLILVGDLD AFRQSVLKVS HNRLTSLKER LVNTLGQQES DKQDETVPNN QLATPEKLQF
EQKTNEKAAA GVQNSDPDAV QADFKNSYRL TLSLIANQKI DPMIGMNGIS PRDFMH
//
