ID A0A0F0HNY7_9PSEU Unreviewed; 730 AA.
AC A0A0F0HNY7;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 30.
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=UK12_21600 {ECO:0000313|EMBL:KJK56631.1};
OS Saccharothrix sp. ST-888.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Saccharothrix.
OX NCBI_TaxID=1427391 {ECO:0000313|EMBL:KJK56631.1, ECO:0000313|Proteomes:UP000033409};
RN [1] {ECO:0000313|EMBL:KJK56631.1, ECO:0000313|Proteomes:UP000033409}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ST-888 {ECO:0000313|EMBL:KJK56631.1,
RC ECO:0000313|Proteomes:UP000033409};
RA Ju K.-S., Doroghazi J.R., Metcalf W.;
RL Submitted (FEB-2015) 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:KJK56631.1}.
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DR EMBL; JYJF01000071; KJK56631.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0F0HNY7; -.
DR PATRIC; fig|1427391.3.peg.6592; -.
DR OrthoDB; 9763659at2; -.
DR Proteomes; UP000033409; 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:RHEA.
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; 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 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:KJK56631.1};
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:UP000033409}.
FT DOMAIN 141..231
FT /note="RecD helicase-like helix-hairpin-helix"
FT /evidence="ECO:0000259|Pfam:PF14490"
FT DOMAIN 568..633
FT /note="RecD-like DNA helicase SH3"
FT /evidence="ECO:0000259|Pfam:PF18335"
FT DOMAIN 653..701
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13538"
FT BINDING 355..359
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01488"
SQ SEQUENCE 730 AA; 78816 MW; C1022C12C65F6E72 CRC64;
MAQVEGVLER ITYANEETGY TVARVDTGRG AHDLLTVVGA LLGAQPGESL RLFGRWGSHP
QYGKQFTVEN YTTVLPATVQ GIQRYLGSGL IKGIGPRFAE RIVERFGVDT LDVIEQEPER
LIEVPGLGPK RTKMIAAAWE EQKAIKEVMV FLQGVGVSTS LAVRIYKKYG DSSIGVVKNE
PYRLAADVWG IGFLTADRIA QAVGIPHDSP ERVKAGLQYA LSQSGDQGHC YLPEERLIAD
GVKLLQVDVG LVIDCLAELV AEEGVVREPV PGEAGEPITA VYLVPFHRAE ISLANQLVRL
LRSESDRMPV FGDVDWAAAL GWLAQRTGAE LAPEQRDSVR LALTEKVAVL TGGPGCGKSF
TVKSIVTLAL AKRAKVVLAA PTGRAAKRLS ELTGVEASTV HRLLELRPGG DAAYDRDRPL
DADLVVVDEA SMLDLILANK LVKAVAPGAH LLFVGDVDQL PSVGAGEVLR DMLSEGSPIP
SVRLTRIFRQ AQQSGVVTNA HRINEGLPPV TEGLADFFLF AEEDAERAAG LTVDVVARRI
PQKFGLDARR DVQVLAPMHR GPAGAGNLNT LLQAAVTPAR EGLPERRFGG RTFRVGDKVT
QIRNNYEKGQ NGVFNGTVGV VTSLSVEEQR LMVLTDEDEE VPYGFDELDE LAHAYAVTIH
RSQGSEYPAV VIPVTTSAWT MLQRNLLYTA VTRAKKLVVL VGSRRAIGQA VRAVSAGRRH
SALDHRLASG
//
