ID A0A430B251_9ENTE Unreviewed; 821 AA.
AC A0A430B251;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 16.
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=CBF29_03535 {ECO:0000313|EMBL:RSU14406.1};
OS Vagococcus elongatus.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae; Vagococcus.
OX NCBI_TaxID=180344 {ECO:0000313|EMBL:RSU14406.1, ECO:0000313|Proteomes:UP000287605};
RN [1] {ECO:0000313|EMBL:RSU14406.1, ECO:0000313|Proteomes:UP000287605}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCUG 51432 {ECO:0000313|EMBL:RSU14406.1,
RC ECO:0000313|Proteomes:UP000287605};
RA Gulvik C.A.;
RT "Vagococcus spp. assemblies.";
RL Submitted (MAY-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:RSU14406.1}.
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DR EMBL; NGKA01000003; RSU14406.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A430B251; -.
DR Proteomes; UP000287605; 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 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; 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; PF18335; SH3_13; 1.
DR Pfam; PF13538; UvrD_C_2; 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|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:UP000287605}.
FT DOMAIN 91..112
FT /note="Helix-hairpin-helix DNA-binding motif class 1"
FT /evidence="ECO:0000259|SMART:SM00278"
FT DOMAIN 126..145
FT /note="Helix-hairpin-helix DNA-binding motif class 1"
FT /evidence="ECO:0000259|SMART:SM00278"
FT DOMAIN 190..209
FT /note="Helix-hairpin-helix DNA-binding motif class 1"
FT /evidence="ECO:0000259|SMART:SM00278"
FT BINDING 358..362
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01488"
SQ SEQUENCE 821 AA; 92303 MW; CCBBAF4F93B3A3DD CRC64;
MIDKPYINGS VQAVFFQNPA NFYKVMLIAV EETNSRYEEP EIVVTGSFGD ILEGETYQFF
GDIVDHPRYG RQFQATTYKK VKPTTENGLV EYLSGEAFPG IGKKTAEKIV DMLGSDAIEV
IMNDPSRLSE IPGLTKKRQQ TLQEGIRENY GMEQMIVSLH EYGFGSQLAM TIYQLYKGET
LELIEEDPYR LIEDIEGVGF KRADALAERL GIAADAPVRL RAAIQFELLQ NSMSEGNTYM
EAEDLLREVI ETLESSRSVE ISPQMVADQI IQLTEENKIQ QEETKIFDNS LCFAEMGIGT
SIKRLLSRKK RIHYDDEKIT ELINLLEESN GMSYGPSQVE AMKEAICSPL FILTGGPGTG
KTTVVNGIVS LFAALNDLSL DINDYHDEVF PILLAAPTGR AAKRMNETTG LPASTIHRML
GLTGLEKNSM EEVQELEGGI LIVDEMSMVD TWLANTLLKS IPTNMQVIFV GDKDQLPSVG
PGQVLHDLLQ VNEIPSRELT EIYRQGNDSS IIPLAHSIKN GLLPRDFHEN QSDRSFFSCN
AYQVEGLIEQ IVKKAQIKGF TAQDIQILAP MYRGVAGIDN LNKMMQEVFN PNETGTRKEV
KWNDKVYRIG DKVLQLVNEP ELNVFNGDMG AITGIIYAKD NEDKVDKLVI SFDQTEVTYQ
RSEWNKITLS YCCSIHKSQG SEFKMVIMPM VQQYFRMLQR NLLYTGITRS QEKLILLGEL
GAFKRAVENE GTNRKTYLLK RISEAIGVVE GSLLSVTYDN EPLQKAEAAK PEFLIGEEDV
LADSEEKVSE SWILTLDKIE QRMISPMVGM DETLTPYDFQ T
//
