ID A0A0L6U2E3_9FIRM Unreviewed; 737 AA.
AC A0A0L6U2E3;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 28.
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=AKG39_06195 {ECO:0000313|EMBL:KNZ42512.1};
OS Acetobacterium bakii.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Eubacteriaceae;
OC Acetobacterium.
OX NCBI_TaxID=52689 {ECO:0000313|EMBL:KNZ42512.1, ECO:0000313|Proteomes:UP000036873};
RN [1] {ECO:0000313|Proteomes:UP000036873}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 8239 {ECO:0000313|Proteomes:UP000036873};
RA Song Y., Hwang S., Cho B.-K.;
RT "Draft genome sequence of Acetobacterium bakii DSM 8293, a potential
RT psychrophilic chemical producer through syngas fermentation.";
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:KNZ42512.1}.
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DR EMBL; LGYO01000012; KNZ42512.1; -; Genomic_DNA.
DR RefSeq; WP_050739508.1; NZ_UOGO01000001.1.
DR AlphaFoldDB; A0A0L6U2E3; -.
DR STRING; 52689.AKG39_06195; -.
DR PATRIC; fig|52689.4.peg.335; -.
DR OrthoDB; 9803432at2; -.
DR Proteomes; UP000036873; 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 GO; GO:0006281; P:DNA repair; IEA:InterPro.
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; IPR003583; Hlx-hairpin-Hlx_DNA-bd_motif.
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; 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; PF14520; HHH_5; 1.
DR Pfam; PF18335; SH3_13; 1.
DR Pfam; PF13538; UvrD_C_2; 1.
DR SMART; SM00382; AAA; 1.
DR SMART; SM00278; HhH1; 4.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR SUPFAM; SSF47781; RuvA domain 2-like; 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}; Reference proteome {ECO:0000313|Proteomes:UP000036873}.
FT DOMAIN 81..102
FT /note="Helix-hairpin-helix DNA-binding motif class 1"
FT /evidence="ECO:0000259|SMART:SM00278"
FT DOMAIN 116..135
FT /note="Helix-hairpin-helix DNA-binding motif class 1"
FT /evidence="ECO:0000259|SMART:SM00278"
FT DOMAIN 180..199
FT /note="Helix-hairpin-helix DNA-binding motif class 1"
FT /evidence="ECO:0000259|SMART:SM00278"
FT DOMAIN 332..478
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT DOMAIN 471..490
FT /note="Helix-hairpin-helix DNA-binding motif class 1"
FT /evidence="ECO:0000259|SMART:SM00278"
FT BINDING 343..347
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01488"
SQ SEQUENCE 737 AA; 82693 MW; 8E0ECA25E4E765F2 CRC64;
METIKGAVEH IVFRNSSNGY TVAHFDIEGD MVTVVGNFEE LNLGEYLKMT GFWIEHKNYG
DQFSMESYAM EIPTSTEGIT RYLASGILPG IGEKTAKAIV KHFGEDTLDI LDNNPDRLSE
IKGIGKKTLA GIKEVYTEQR EVRHIMIQIQ DYGISANWAM KLYKTYKADT ISVLLNNPYQ
MIDDIRGIGF KIADQIAEQL GFETTSPGRI LAGINYSLSE CYNRGNTFMT EAELVDTSSR
ILGVDADEIV YQLGELILMG GIIQETVRDQ IVYYPRNLYE AEDNTALAMA RISKGIYEIP
NMDIEAKIKK YEKDMSITLD DKQREAIIAA MDHGVIIITG GPGTGKTTII NGIVRIFEEM
GLKTVLAAPT GRAAKRITET TGHEAKTIHR LLEYEFSQNE DFPSFSKDEG NPLEVDAIIV
DESSMIDILL MDSLLTAIQP GTRLIMVGDA DQLPSVGPGN VLKDVIESDV VKVLGLERIY
RQSAESMISV NAFEINHGHM PDINNESDFL FLNKNDGDKL LKDILELVTY RIPNAKGFKS
IQDIQVISPM KKGKVGVVNL NKELQGVLNP PSDSRAQREF GMVIYREGDK VMQIKNNYRM
KWEDVNGFEE GEGIYNGDIG ILETINEREK SFTIIFNDGK RVVYDFDQMD EITHAYAMTV
HKSQGSEFPV VIMPIVGGPP LFLNRKLLYT AVTRAKKLLI LMGSNYVFRQ MIKSGDSQER
QTALKERIID YINNPMI
//
