ID A0A1I0P3F0_9FIRM Unreviewed; 746 AA.
AC A0A1I0P3F0;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
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=SAMN05421659_104126 {ECO:0000313|EMBL:SEW08741.1};
OS [Clostridium] fimetarium.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae.
OX NCBI_TaxID=99656 {ECO:0000313|EMBL:SEW08741.1, ECO:0000313|Proteomes:UP000199701};
RN [1] {ECO:0000313|EMBL:SEW08741.1, ECO:0000313|Proteomes:UP000199701}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 9179 {ECO:0000313|EMBL:SEW08741.1,
RC ECO:0000313|Proteomes:UP000199701};
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; FOJI01000004; SEW08741.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I0P3F0; -.
DR STRING; 99656.SAMN05421659_104126; -.
DR OrthoDB; 9803432at2; -.
DR Proteomes; UP000199701; 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};
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:UP000199701}.
FT DOMAIN 336..487
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT BINDING 347..351
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01488"
SQ SEQUENCE 746 AA; 83876 MW; 7EA21AD3FE92D53E CRC64;
MEHNNENSIE GFVDSIVFRN EDNGYTVFNI ICNGSEVTCV GVLSYINEGE FIAATGEYVM
HPIYLQQFKI TSYEIRVPED IQSVKRYLGS GAIKGIGEKL AESIIKKFGE DTFRIIEDEP
ERLAEIKGIS VKKAMEIADQ LVEKKDMRKA MMFLQEYGIN MNLANKIYTQ YGNDIYRIIK
ENPYKLADDI NGIGFKIADE IAQRVGVKSD SDFRIRSGIM YELLLATTNG HVYLPMKELI
NSTRQLLLID MVNIDKFIMD LSIDKKIIVK QVKDQQVVYA SSYYYTELSV AGMLVNLDIK
YSDDDLEVEK SIGSIEKSNE MILDGVQRQA VKDAILNGLM VITGGPGTGK TTTINTIIKY
FEIEGMDIRL AAPTGRAAKR MSETTGYEAQ TIHRMLELSG NAGDNTAAMN FERNELNPLE
TDVIIIDEMS MVDINLMNSL LKAIAVGTRL ILVGDVDQLP SVGPGNVLKD IIQSGCVNVV
MLTKIFRQAA TSEIIINAHK INNGEEVILN KYSKDFLFIK RDNPESITGA ICTLIRDKLP
DYVNAKISDI QILTPMKKGA VGVEKLNKIL QEFLNPAAKE KTEKEYGDTV FKVGDKVMQV
KNNYQLEWEK RSKYGIPTDG GTGIFNGDIG IIETINLFSE QMIVKFDDEK YVEYSFKQLE
ELELAYAVTI HKSQGSEYPA VIIPMFSGPK MLMTRNLLYT AVTRAKTCVC IVGSQNFFQE
MIRNVSEQMR YSTLAERIKE MQSIAD
//
