ID D7N8L4_9FIRM Unreviewed; 728 AA.
AC D7N8L4;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 27-MAR-2024, entry version 51.
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=HMPREF0629_00409 {ECO:0000313|EMBL:EFI41783.1};
OS Peptoniphilus sp. oral taxon 386 str. F0131.
OC Bacteria; Bacillota; Tissierellia; Tissierellales; Peptoniphilaceae;
OC Peptoniphilus.
OX NCBI_TaxID=575609 {ECO:0000313|EMBL:EFI41783.1, ECO:0000313|Proteomes:UP000004712};
RN [1] {ECO:0000313|EMBL:EFI41783.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0131 {ECO:0000313|EMBL:EFI41783.1};
RG The Broad Institute Genome Sequencing Platform;
RA Ward D., Feldgarden M., Earl A., Young S.K., Zeng Q., Koehrsen M.,
RA Alvarado L., Berlin A., Bochicchio J., Borenstein D., Chapman S.B.,
RA Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA Gujja S., Heilman E., Heiman D., Hepburn T., Howarth C., Jen D., Larson L.,
RA Mehta T., Park D., Pearson M., Roberts A., Saif S., Shea T., Shenoy N.,
RA Sisk P., Stolte C., Sykes S., Thomson T., Walk T., White J., Yandava C.,
RA Izard J., Baranova O.V., Blanton J.M., Tanner A.C., Dewhirst F.E., Haas B.,
RA Nusbaum C., Birren B.;
RT "The Genome Sequence of Peptoniphilus sp. oral taxon 386 strain F0131.";
RL Submitted (FEB-2010) 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; GL349422; EFI41783.1; -; Genomic_DNA.
DR RefSeq; WP_009221722.1; NZ_GL349422.1.
DR AlphaFoldDB; D7N8L4; -.
DR STRING; 575609.HMPREF0629_00409; -.
DR eggNOG; COG0507; Bacteria.
DR HOGENOM; CLU_007524_0_2_9; -.
DR Proteomes; UP000004712; Miscellaneous, Scaffold supercont1.1.
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 GO; GO:0006281; P:DNA repair; IEA:InterPro.
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; IPR003583; Hlx-hairpin-Hlx_DNA-bd_motif.
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; PF13604; AAA_30; 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 SMART; SM00278; HhH1; 2.
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:EFI41783.1};
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:UP000004712}.
FT DOMAIN 116..135
FT /note="Helix-hairpin-helix DNA-binding motif class 1"
FT /evidence="ECO:0000259|SMART:SM00278"
FT DOMAIN 180..199
FT /note="Helix-hairpin-helix DNA-binding motif class 1"
FT /evidence="ECO:0000259|SMART:SM00278"
FT DOMAIN 331..475
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 728 AA; 82689 MW; 697392B50ED0932F CRC64;
MIEIKGVVEK IIYRNEDNGY TVARFSTEEE SITINGSCAE IKTSMEYELK GDFIFHKKYG
EQFKFESIEE ILPQSENGII NYLSSGIIPF IGEKTAKNIV DKFKTETLKI LEEDTERLLE
VDGIGPRKLD KIKSALLENR GLRRLTLFLN KHELGTTLAV KIYKEYGERA IQIIKENPYK
LAEDISGVGF KKADKIAMSI GEFRGSSFRN RAALKYILSL ATLEGHSFLP KDILIKRTHK
LVGDNIEQLE NELLNLSLDD RFFIEQSDGE ICCYYAPYLR AENYISGKIK ELVSGKFEYD
TNIDEILKKI EERNEIKFAT NQVIAVREAV EKGVLIITGG PGTGKTTTLK AIIEIFESMG
KSVKLAAPTG RAAKRMKEAT NRDASTIHRL LEIRVPDDDR INYGYEEEVE LDCDVLIVDE
VSMVDLGLMN TLLHSIKKGT RLILVGDKDQ LPSVGAGNVL SDLIESKRVS VVNLNEIFRQ
KEQSSIIKNA HLINNGILPE ISNSGDFYMI SEQNEKKSLE VIKELVSRRL PQYYGVNSNK
IQVLAPMKKG NVGIYSLNKT LQEVLNPKGD EIIFGDNVFR VGDKVMQTKN NYNLEYKIES
EFYLEEGEGV FNGDIGYVVE IDIENKSLVV LYDDVKKVKY EYSDLDELIL SYACTIHKSQ
GSEFDIVIIP LHFAPYILLT RNLIYTAITR AKKLVVLVGE YKYLDIMVKN NRISKRYSNL
CKKLMKDD
//
