ID A0A1Y3WAS9_9FIRM Unreviewed; 736 AA.
AC A0A1Y3WAS9;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 24-JAN-2024, entry version 25.
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=B5G11_06020 {ECO:0000313|EMBL:OUN70344.1};
OS Drancourtella sp. An57.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC Drancourtella.
OX NCBI_TaxID=1965647 {ECO:0000313|EMBL:OUN70344.1, ECO:0000313|Proteomes:UP000196207};
RN [1] {ECO:0000313|Proteomes:UP000196207}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=An57 {ECO:0000313|Proteomes:UP000196207};
RA Medvecky M., Cejkova D., Polansky O., Karasova D., Kubasova T., Cizek A.,
RA Rychlik I.;
RT "Function of individual gut microbiota members based on whole genome
RT sequencing of pure cultures obtained from chicken caecum.";
RL Submitted (APR-2017) 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:OUN70344.1}.
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DR EMBL; NFHY01000006; OUN70344.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y3WAS9; -.
DR Proteomes; UP000196207; 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:SF6; DNA HELICASE B; 1.
DR PANTHER; PTHR43788; DNA2/NAM7 HELICASE FAMILY MEMBER; 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; 1.
DR SUPFAM; SSF47781; RuvA domain 2-like; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_01488};
KW 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|HAMAP-Rule:MF_01488};
KW Reference proteome {ECO:0000313|Proteomes:UP000196207}.
FT DOMAIN 331..480
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT BINDING 342..346
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01488"
SQ SEQUENCE 736 AA; 83797 MW; DA7656B6337A7BF4 CRC64;
MEKITGYIDH IIFRNEENGY TVFQFHNENG EVTCVGKFPY IGDGEFLELE GEYVMHPSYG
LQLQVTEHKV KEPEDRESIE RYLGSGAVKG IGPALAGKIV AKFGEDTFRI MEEEPERLAE
IKGISERKAR EICVQVEEKK DLRQAMIYLQ KYGISINLAV KIYQKYGLGI YSILEENPYR
LADDIEGVGF KTADEIAFRI GIHTDSDFRI QSGIFYTLLQ SVQEGHVYLE EKVLSAKAAQ
LLEVEITDIE KYLMDLAMEK KVVLKQDEEQ VRVYPAKYYY MEMNTARMLK ELNIRYEEDD
SLIRKRIEKL EKQNESTLDE RQREAVAEAV KNGIFILTGG PGTGKTTTIN AMIRYFLSEG
MDIRLAAPTG RAAKRMTETT GYEAQTIHRL LEVSGNPEET GKGGFGRNQE NPLETDVVII
DEMSMVDLPL MHALLSAVIP GTRLILVGDI NQLPSVGPGK VLKDLIDSEV FPVMMLTRIF
RQAQESDIVV NAHRINAGLE VRLDNKSRDF FFLKRQDADV IISVILTLIQ KKLPRYVDAK
MTDIQVLAPM KKGLLGVERL NRILQQYLNP PSPKKQEKEY GEKIFRVGDK VMQTKNNYQL
EWEIATKYGL VVDKGIGVFN GDIGIVTAIH TYDETVEVEF DEKRKVKYPF KLLDELELAY
AVTIHKSQGS EYPAVIIPLL SGPKQLYCRN LLYTAVTRAK KCVTLVGSDT VFQEMIRNVE
EQKRNTSLSE RIRELS
//