ID A0A1X1Q726_9FIRM Unreviewed; 721 AA.
AC A0A1X1Q726;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
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=D081_1124 {ECO:0000313|EMBL:ORU00601.1};
OS Anaerovibrio sp. JC8.
OC Bacteria; Bacillota; Negativicutes; Selenomonadales; Selenomonadaceae;
OC Anaerovibrio.
OX NCBI_TaxID=1240085 {ECO:0000313|EMBL:ORU00601.1, ECO:0000313|Proteomes:UP000192538};
RN [1] {ECO:0000313|EMBL:ORU00601.1, ECO:0000313|Proteomes:UP000192538}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JC8 {ECO:0000313|EMBL:ORU00601.1,
RC ECO:0000313|Proteomes:UP000192538};
RA Evans P.N., Cheung J.L., Rosewarne C.P., Morrison M.;
RT "Genomic and phenotypic data suggests Anaerovibrio species JC8 from the
RT bovine rumen reduces fumarate and sulphite to decrease the inhibitory
RT effect of hydrogen.";
RL Submitted (OCT-2012) 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:ORU00601.1}.
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DR EMBL; ANBM01000004; ORU00601.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1X1Q726; -.
DR STRING; 1240085.D081_1124; -.
DR OrthoDB; 9803432at2; -.
DR Proteomes; UP000192538; 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; PF13604; AAA_30; 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; 2.
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|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:ORU00601.1};
KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_01488};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_01488}.
FT DOMAIN 118..137
FT /note="Helix-hairpin-helix DNA-binding motif class 1"
FT /evidence="ECO:0000259|SMART:SM00278"
FT DOMAIN 182..201
FT /note="Helix-hairpin-helix DNA-binding motif class 1"
FT /evidence="ECO:0000259|SMART:SM00278"
FT DOMAIN 334..453
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT BINDING 345..349
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01488"
SQ SEQUENCE 721 AA; 79300 MW; EDD5B694F2382928 CRC64;
MEELQGSVEN IIFASSDGRF SVFRLRPDGQ RGMVTVTVQM EPPLQGQQLE LKGTWVEHPR
FGQQFKAEHM MVAAPTSLEG IERFLASGAI DGVGPVNAKR IVAHFGGAAL EVIEKAPNRL
KEVSGIGAKT AEKIHKSYME KAELRQIMIW LEQHNVSGIY AGKIYGQYGS FAIEVMESNP
YRLVREIDGV GFATADAIAA GIGMQADDAL RISAALEFQL QRISLSGHCC VPENMLVDEV
ERVRGIGRNS IWEVLKQDLA TGVLNQEVVG DTILVYPEYL YQAEVETAET LLFLQERAKP
INVGNSMKLV EKWEKFTGIE LAQKQKEAIQ GVLEHGIFVL TGGPGTGKTT VIRGMIDMLE
SQGMEIILGA PTGRAAKRLS EATGRTASTI HRMLEAQGGD SSDGSMFGRD IDDQLEADAI
ILDEVSMMDI VLMRHFLEAV PAGCHVILVG DVDQLPAVGP GSVLKDILRS GVIASVCLTE
VFRQSEASSI VMNAHAINAG RVPRFNNAPN SDFEFIELNN PEAVEYQIVS LCRDLLPKQG
YAPYEDIQVL SPMHRQACGV ENLNKRLQAA LNPPASYKSE YVSSTRNFRL GDKVMQTKNN
YDKGVFNGDI GFIVEMDEDS ITVQFSDDLS AVYQKSELGE LQLAYCMSVH KSQGSEYPVV
ILPLVPGHRI MLQRNLLYTA ITRARKKVIL IGTKAALNTA VANDKTRRRY TLLAERLARS
L
//
