ID A0A3N0E471_9ACTN Unreviewed; 761 AA.
AC A0A3N0E471;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, 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=EFW17_18730 {ECO:0000313|EMBL:RNL82569.1};
OS Nocardiopsaceae bacterium YIM 96095.
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Nocardiopsaceae.
OX NCBI_TaxID=2487137 {ECO:0000313|EMBL:RNL82569.1, ECO:0000313|Proteomes:UP000269198};
RN [1] {ECO:0000313|EMBL:RNL82569.1, ECO:0000313|Proteomes:UP000269198}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YIM 96095 {ECO:0000313|EMBL:RNL82569.1,
RC ECO:0000313|Proteomes:UP000269198};
RA Tang S.-K., Chunyu W.-X., Feng Y.-Z.;
RT "The genome draft of YIM 96095.";
RL Submitted (NOV-2018) 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:RNL82569.1}.
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DR EMBL; RJMB01000022; RNL82569.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3N0E471; -.
DR OrthoDB; 9763659at2; -.
DR Proteomes; UP000269198; 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; 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, ECO:0000313|EMBL:RNL82569.1};
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:UP000269198}.
FT DOMAIN 371..562
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 382..386
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01488"
SQ SEQUENCE 761 AA; 82127 MW; 2CC958333EF14798 CRC64;
MGVSARLKGN RVATGRTGRA GPVGNGPRPT VLEGVLERIT YANEETGYTV ARIDDGRGGE
LTTAVGALLG AHPGESLRME GRWSSHPQYG RQFTVENYTT VLPATVQGVR RYLGSGLVKG
IGPRLAERIV GHFGAGALDV IEEDPQRLIE VPNLGPKRTR LIAEAWEEQK AIKEVMVFLQ
SIGVSTSLAV RIYKKYGDAA IGTVREEPYK LATDVWGIGF KTADTIAQSV GIPHDSAQRV
KAGIQFTLSE STSDGHCYLP EERLISEAVK ILQVDSGLVI DCLAELVEEE GVLTESVPGP
DGEPRTAVYL VPFHRAETSL ATQLRTLLNC DSDRMSVFSG VDWDTALGWL RSRTGTDLVE
EQQAAVRLAL TSRVAVLTGG PGCGKSFTVS SVITLAAAKR AKIVLAAPTG RAAKRLTELT
GHEASTVHRL LELKPGGDAS YDRDRPLDCD LLVVDEASML DLLLANKLAK AVPPGAHLLL
VGDVDQLPSV GAGQVLRDLL ATDDGGENAP IPNVRLTHIF RQAQQSGVVT NAHRVNSGKP
PLLDDMADFF LFPCDDAERA AEVTVDVVAN RAPRKFGLDP RRDIQVLTPM HRSPAGAGNL
NTLLQGALTP SREGVAERRF GGRVFRVGDK VTQIRNNYEK GANGVFNGTL GVLTGIDHDE
QQVTVRTDED EDIGYDFAEL DELVHAYAMT VHRSQGSEYP AVVIPVTTSA WMMLQRNLLY
TAITRAKRLV VLVGSRKAIA QAVRNATAGR RYTALAHRLV R
//
