ID A0A143ZVE6_9FIRM Unreviewed; 749 AA.
AC A0A143ZVE6;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-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_1 {ECO:0000313|EMBL:CZT56811.1};
GN Synonyms=recD2 {ECO:0000256|HAMAP-Rule:MF_01488};
GN ORFNames=BN3661_01591 {ECO:0000313|EMBL:CZT56811.1};
OS Eubacteriaceae bacterium CHKCI005.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Eubacteriaceae.
OX NCBI_TaxID=1780381 {ECO:0000313|EMBL:CZT56811.1, ECO:0000313|Proteomes:UP000199521};
RN [1] {ECO:0000313|EMBL:CZT56811.1, ECO:0000313|Proteomes:UP000199521}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CHKC5 {ECO:0000313|EMBL:CZT56811.1};
RA Oliw E.H.;
RL Submitted (JAN-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; FJVJ01000023; CZT56811.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A143ZVE6; -.
DR STRING; 1780381.BN3661_01591; -.
DR Proteomes; UP000199521; 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; 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 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:CZT56811.1};
KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_01488, ECO:0000313|EMBL:CZT56811.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_01488}; Reference proteome {ECO:0000313|Proteomes:UP000199521}.
FT DOMAIN 350..489
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT BINDING 361..365
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01488"
SQ SEQUENCE 749 AA; 84550 MW; A16575D6E09C50A5 CRC64;
MSYTGVYDRT IFYNPSNKYC VISVKTSDQS IPQQARSAYT HRDHLIRFTA VGYELPQTDK
VSMILDGEWQ NGKYGQQLQV TQCEEIVPQT RDGVKGYLSS RLIKGVGERT AELIVDRFGA
DALKVLEKEP ERLLEIKGIT PAKLEEIQSS YTESRCLRDL MILLSPFNVT PAAATRIYEH
FGSRSVDILR DNPFELCQVS GFGFKRVDAI VRKGDCPLNS PMRIHGAIYA ALDTQRNENG
HLFLDSEELL KAAFRLLNDR IPQPQLRVKP EEIAQVLENM VLKGEVVSNK GRIYQISCFT
QEDETARKIA EMLSVKPEKV NIETALESIR KNLGIVLSQR QSEAVYMAFR SNLSIITGSP
GTGKTTVLRA IIEVYQSLYP DKKIMLGAPT GRASRRMAES TGRNDAKTLH SLLGLLGENG
YVRDKNQEPL DASLIIVDES SMIDMWLARQ FFQRVRLGTK VILVGDVDQL QSVGAGDVFR
ELIGCGRIPV TILNEIFRQK KDSLIAYNAK SINEDSTNLY YGDDFVFIKC KTQEEAADII
CRTFCEQVEK FGIEHVQILS PFRSEGMTAV EQLNQVIREL VNPADEDIPD LKIGSRYFRE
NDKVMQTKNN GKASNGDIGF IRKIAPDDKN EMKVTIEFAE DRVVEYGLED MANIELAYAT
TIHKAMGSEY DIVILPIIRS HAIMLKRNLV YTAITRAKRR VFLVGQKGML FMAIHKNDTG
QRNTLLGERI GKYLNAFTMA EQRNLKKVS
//
