ID A0A1H2RXD2_9FIRM Unreviewed; 755 AA.
AC A0A1H2RXD2;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
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=SAMN05216391_103162 {ECO:0000313|EMBL:SDW24131.1};
OS Lachnospiraceae bacterium KHCPX20.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae.
OX NCBI_TaxID=1855375 {ECO:0000313|EMBL:SDW24131.1, ECO:0000313|Proteomes:UP000199590};
RN [1] {ECO:0000313|EMBL:SDW24131.1, ECO:0000313|Proteomes:UP000199590}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KHCPX20 {ECO:0000313|EMBL:SDW24131.1,
RC ECO:0000313|Proteomes:UP000199590};
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; FNOC01000003; SDW24131.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H2RXD2; -.
DR STRING; 1855375.SAMN05216391_103162; -.
DR Proteomes; UP000199590; 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:UP000199590}.
FT DOMAIN 337..510
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT BINDING 348..352
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01488"
SQ SEQUENCE 755 AA; 85156 MW; F2C29A2FD11571C6 CRC64;
MSELTGYVDH IIYRNAANAY TVLVLIPEEE PEEESLRDEG EVSVTGIFPS ISEGENIRLT
GEYRMHESFG MQFAMRSYEV VAPKDEESIR RYLGSGAIKG VGAVLAKRIV ETFGRDTFKI
IEIQPERLAE VRGISEKKAR EIAAQMLQKR DQREVMLQLS KLGVTTNMAV KIYQHYGQAS
MDAIRENPYR LADEVDGIGF HTADEIATKM GFNSNSEFRI QSGILFVLEQ ASMNGNTYLP
TEELTLQAAQ LLAVEPQMLE AAYESLVMNR KLKILKDHVY SMVMYRMEER VAGMLLNLNE
RFLTDPSALT TQISDIEKEE GMVLDARQRE AVEGAADHGV FVLTGGPGTG KTTTIKAIIR
YFEREGLTIR LAAPTGRAAK RMSEACGQEA QTIHRLLEVN GSVIATESDE DGKVRPGTFQ
RNEDNPLEAD VVIIDEMSMV DISLMYALLR AIAEGTRLVL VGDVDQLPSV GPGNVLRDII
ESNAFRVITL TNVFRQDEAG DIVLNAHRIH RGETVVLDNK SKDFFFLKRY DSDHILKVVM
LLVQEKLPKY VNASPYDIQI LTPTRKGLLG VENLNPILQK YLNPPDEHKA EHSFGTMLIR
EGDKVMQTKN DYQMEWQILG KYGITIEKGT GIFNGDIGIV EEVNDFNSTL RIRFDDGHMV
DYPYKQIDQL ELAYAMTIHK SQGSEYPAVV MPLLSGPRML YNRNLLYTAV TRAKNCVVIV
GDENVFYKME QNNQQQRRYS GLEDRLREQS MLLEA
//
