ID A0A1I1X8J1_9FIRM Unreviewed; 716 AA.
AC A0A1I1X8J1;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 27.
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=SAMN05216245_101117 {ECO:0000313|EMBL:SFE03736.1};
OS Succiniclasticum ruminis DSM 9236.
OC Bacteria; Bacillota; Negativicutes; Acidaminococcales; Acidaminococcaceae;
OC Succiniclasticum.
OX NCBI_TaxID=1123323 {ECO:0000313|EMBL:SFE03736.1, ECO:0000313|Proteomes:UP000198896};
RN [1] {ECO:0000313|EMBL:SFE03736.1, ECO:0000313|Proteomes:UP000198896}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 9236 {ECO:0000313|EMBL:SFE03736.1,
RC ECO:0000313|Proteomes:UP000198896};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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}.
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DR EMBL; FONL01000001; SFE03736.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I1X8J1; -.
DR STRING; 1123323.SAMN05216245_101117; -.
DR OrthoDB; 9803432at2; -.
DR Proteomes; UP000198896; 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:SF6; DNA HELICASE B; 1.
DR PANTHER; PTHR43788; DNA2/NAM7 HELICASE FAMILY MEMBER; 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; 3.
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|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:UP000198896}.
FT DOMAIN 82..103
FT /note="Helix-hairpin-helix DNA-binding motif class 1"
FT /evidence="ECO:0000259|SMART:SM00278"
FT DOMAIN 117..136
FT /note="Helix-hairpin-helix DNA-binding motif class 1"
FT /evidence="ECO:0000259|SMART:SM00278"
FT DOMAIN 181..200
FT /note="Helix-hairpin-helix DNA-binding motif class 1"
FT /evidence="ECO:0000259|SMART:SM00278"
FT DOMAIN 333..473
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT BINDING 344..348
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01488"
SQ SEQUENCE 716 AA; 78591 MW; 7B8A2733F5485738 CRC64;
METIEGTVEN IIFQSDDRQF CVFRTKCTSL GLVTTVYKGP APFMGEMIRA RGEWTQHARF
GRQFSVTGYQ SLKPGSAEGM ERFLASGAVK GIGKAMASRI VAHFGKDTLD ILGKAPERLA
EVSGIGAKKA KSIGEAYNMI SDLRELMLFL EENGVSGNYA AKLQLAYGDT AITRIKANPY
SLITDIDGIG FKTADRIALS LGFEPASEER VRAGIGYALT LAASGGHTCI PEEELLRYAS
QVLQIDFTDV ETVFRKMIAN DQLRTEDWGG QRFVYPEYLY RAETGTARML RALRDHPDSL
GKVNVEKIIG DWEAEAGIEL AEAQKDAIRS SLKFGVFALT GGPGTGKTTI IKGILSVLKR
AGCTVLLAAP TGRAARRLEM AAGDKAQTVH RLLEYTVTGE FGKNADDLLE TQAVIVDEAS
MLDIYLFYHL LEALPLGCRL ILVGDVDQLP SVGPGSVLKD IIRCGKMPVV RLQEVFRQAE
VSPIVRNAHR INRGLLPECA ADSDFSMTEF ADEEMAAAYI TDLYAAATKS GGWQSLQILS
PMHKGPCGVQ NLNSLLQDRV NPPSARKEEI RQPGGATLRL GDKVMQIRNN YEKDVYNGDI
GQIADISGKA VKVWYPERPD GEYVTYGDGE TDELQLAYAM SVHKSQGSEY SRVVLALVPG
HYIMLQRNLL YTAVTRAREK VELVGTKTAL QTAVANDRTR RRYSLLKERL QESGDL
//