ID A0A416ETJ2_9FIRM Unreviewed; 757 AA.
AC A0A416ETJ2;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 18.
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=DWZ56_01385 {ECO:0000313|EMBL:RHP36526.1};
OS Lachnotalea sp. AF33-28.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Lachnotalea.
OX NCBI_TaxID=2292046 {ECO:0000313|EMBL:RHP36526.1, ECO:0000313|Proteomes:UP000285302};
RN [1] {ECO:0000313|EMBL:RHP36526.1, ECO:0000313|Proteomes:UP000285302}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AF33-28 {ECO:0000313|EMBL:RHP36526.1,
RC ECO:0000313|Proteomes:UP000285302};
RA Zou Y., Xue W., Luo G.;
RT "A genome reference for cultivated species of the human gut microbiota.";
RL Submitted (AUG-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:RHP36526.1}.
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DR EMBL; QUEE01000001; RHP36526.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A416ETJ2; -.
DR OrthoDB; 9803432at2; -.
DR Proteomes; UP000285302; 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:RHP36526.1};
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:UP000285302}.
FT DOMAIN 331..518
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT BINDING 342..346
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01488"
SQ SEQUENCE 757 AA; 84784 MW; 2239BC6E9A014899 CRC64;
MEKVEGYVEH IVYRSEETGY TVMEISSSDE EYTLVGTLPF VSEGEYIEAR GEFSTHQMYG
EQLKVLEYEI KAPEDSVSIE RYLSSGAIKG IGPALAARIV GRFKDDTFRI IEEEPERLAE
IKGISENKAM EIASLVCEKR DMRSAMMFLQ NYGISLNLAA KIYNQYGAEV YSLIKQNPYR
MADDIPGVGF KIADEIAVKV GIHTDSDFRI RSGILYTLLQ GLSNGHVYLP EEELVRNTSS
LLGVELSSIE KYLMDLTIEK KLIVQKEPEG RIVYASKYYY MELNAAKMLH DLNIGYDVPD
IELQQRLSRI EAQSDIVLDT HQREAVAEAV KNGLLVITGG PGTGKTTTIT TIIRYLEQEN
MEILLAAPTG RAAKRMTEAT GYEARTIHRM LELTAVPDES PESGRFERNE QNPLEADAII
IDEMSMVDLN ILYALLKAVP VGTRLILVGD VDQLPSVGPG NVLKDIIESG CFHVVKLEKI
FRQATYSDII VNAHKINQGI PIDPAKRSND FLFIRRDDPN SIINATITLI KDKLPGYVHA
GMHEIQVMTP MRKGILGVER LNSILQEYLN PPADKKREKQ VGGTVFREGD KVMQVRNNYQ
IEWEVRSRYG IPSDRGKGVF NGDMGVVKEI NLFSEELTVE FDEHRLVTYS FKELEELELA
YAITVHKSQG SEYPAVILPL LSGPRMLMNR NLLYTGVTRA KSCVCIVGSV GAFQEMAANE
KEQKRYSGLD RRLKEVEQSG TDSVGGTFSG MGGLFGQ
//
