ID R5BM69_9FIRM Unreviewed; 714 AA.
AC R5BM69;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 36.
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=BN814_01439 {ECO:0000313|EMBL:CCX53872.1};
OS Veillonella sp. CAG:933.
OC Bacteria; Bacillota; Negativicutes; Veillonellales; Veillonellaceae;
OC Veillonella.
OX NCBI_TaxID=1262980 {ECO:0000313|EMBL:CCX53872.1, ECO:0000313|Proteomes:UP000018347};
RN [1] {ECO:0000313|EMBL:CCX53872.1, ECO:0000313|Proteomes:UP000018347}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGS:933 {ECO:0000313|Proteomes:UP000018347};
RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA Wang J., Brunak S., Ehrlich S.D.;
RT "Dependencies among metagenomic species, viruses, plasmids and units of
RT genetic variation.";
RL Submitted (NOV-2012) 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:CCX53872.1}.
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DR EMBL; CAWP010000045; CCX53872.1; -; Genomic_DNA.
DR AlphaFoldDB; R5BM69; -.
DR Proteomes; UP000018347; 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; 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; 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:CCX53872.1};
KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_01488};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_01488}.
FT DOMAIN 333..476
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT BINDING 344..348
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01488"
SQ SEQUENCE 714 AA; 79439 MW; 6F8590EBC6C004D7 CRC64;
METLRGIVQR LIYQNETNTY CVFLLEDYNE ERTVCTANLE APKEGDDLEL SGRYITHKKY
GRQFEAATLE RLKPDTLYGA KQYLINLGVK GLGEKSVDKI IAYFEEALLD ILRAEDPEAL
LEVPGLRKSV KEELYNALRG EGLLQEINRF LEKAGLSSRW SRTLYTTYGG AAIDVLRDNP
FRLMEVDGSI PFSMCDTLRN SLGIEPNDER RIEAAILYTL KNIGDNGHSC MPADELIGMV
FDMLGGFADE VAARLEELLD IGQIVATDYD GLLYIYSPNI YNAESDAAYL TQNLMADSDV
ITLDLESFIA GFEVKKGLQL GDAQKEAIAL ALQNKISLIT GGPGTGKTTI IQALVEAFQQ
TPQNRILLCA PTGRAAKRLT EATGYEATTI HRMLMPIQGS DSYEFTKNED DLLEADVIIV
DEASMLNVQL YYSLLAAIPE NAYVVIVGDV DQLPPIGAGF ILRDLLDSQI IPSVRLNTIF
RQKEGNRIVT NAHEINKGDM PELTSEGEFR FVEVHSVTDM MHRVVALYRE ALAECDDELD
VQIISPMRRG GAGSVAISKT VQAAVNPQVA TRSAVKINGQ TYRVGDKVIQ VLNNYELEVF
NGEIGVIFSI SKTEVCIRFM DKEVHVPMED MSSFMLAYAI TVHKSQGSEY GTVIIPFIPT
YHQMLQRNLL YTAVTRARNK VILVGTKSAV QRAVTTQSGT TRYTLFKERL QGLI
//
