ID A0A0M8W5V1_9NOCA Unreviewed; 720 AA.
AC A0A0M8W5V1;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 34.
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=ADL03_37165 {ECO:0000313|EMBL:KOV79369.1};
OS Nocardia sp. NRRL S-836.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Nocardia.
OX NCBI_TaxID=1519492 {ECO:0000313|EMBL:KOV79369.1, ECO:0000313|Proteomes:UP000037746};
RN [1] {ECO:0000313|Proteomes:UP000037746}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL S-836 {ECO:0000313|Proteomes:UP000037746};
RA Ju K.-S., Doroghazi J.R., Metcalf W.W.;
RL Submitted (JUL-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:KOV79369.1}.
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DR EMBL; LGDY01000134; KOV79369.1; -; Genomic_DNA.
DR RefSeq; WP_053738281.1; NZ_LGDY01000134.1.
DR AlphaFoldDB; A0A0M8W5V1; -.
DR STRING; 1519492.ADL03_37165; -.
DR PATRIC; fig|1519492.3.peg.7936; -.
DR OrthoDB; 9763659at2; -.
DR Proteomes; UP000037746; 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; 2.
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:KOV79369.1};
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:UP000037746}.
FT DOMAIN 334..531
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT BINDING 345..349
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01488"
SQ SEQUENCE 720 AA; 78653 MW; D174A9CDD1FB44BD CRC64;
MNVLEAVLER ITYANEDNGY TVAKVDTGRG DLVTVVGALL GAQPGESIRM RGHWGSHPQY
GKQFHVDDYT TVLPATIQGI RRYLGSGLIK GIGPVLADKI VTHFGTDALD VIEHTPERLV
EVPKLGPKRT KLIADAWEEQ KAIKEVMVFL QGVGVSTSLA VRIYKQYADK AIDVVREEPY
RLASDVWGIG FKTADVIAKA VGIPHDSPQR VKAGLQFTLS EATTDGNCYL PEQALIAEAI
KILQVDTGLV IDCLAELVEE EGVVREELPD DEIAIYLVPF HRAEISMAAQ LKRLLHTDTD
RMPSFRDVDW DKAFAWLGTE LEQHQAEAVK LALTQKVAVL TGGPGCGKSF TVRSIVRLAL
AKRAKIVLAA PTGRAAKRLS ELTGHEARTV HRLLELKPGG DAAYDRDHPL DADLVVVDEA
SMLDLLLANK LVKAVPPGAH LLLVGDVDQL PSVGAGEVLR DVLAQGSPVP NVRLTHIFRQ
AQESGVVTNA HRINSGDYPV VQGLPDFFLF ATDEAEEAAT TTVDVVANRI PRRFGLDPRK
DVQVLAPMHR GPAGAGSLNT VLQEALTPSR ENLPEKRFGG RVFRVGDKVT QIRNNYDKGR
NGVFNGTLGV VTALDPVEQK LTIRTDEDED VDYEFSELDE LSHAYAMTIH RSQGSEYPCV
VIPITTSAWM MLQRNLLYTA VTRAKKLVVL VGSKRAIGQA VRTVGAGRRH TALAHRLRTG
//
