ID A0A0X3RYM6_9ACTN Unreviewed; 758 AA.
AC A0A0X3RYM6;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
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=ADL25_31640 {ECO:0000313|EMBL:KUJ36687.1};
OS Streptomyces sp. NRRL F-5122.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1609098 {ECO:0000313|EMBL:KUJ36687.1, ECO:0000313|Proteomes:UP000054048};
RN [1] {ECO:0000313|Proteomes:UP000054048}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL F-5122 {ECO:0000313|Proteomes:UP000054048};
RA Ju K.-S., Doroghazi J.R., Metcalf W.W.;
RL Submitted (OCT-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:KUJ36687.1}.
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DR EMBL; LMWH01000252; KUJ36687.1; -; Genomic_DNA.
DR RefSeq; WP_059131319.1; NZ_LMWH01000252.1.
DR AlphaFoldDB; A0A0X3RYM6; -.
DR OrthoDB; 9763659at2; -.
DR Proteomes; UP000054048; 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, ECO:0000313|EMBL:KUJ36687.1};
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:UP000054048}.
FT DOMAIN 368..565
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT BINDING 379..383
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01488"
SQ SEQUENCE 758 AA; 82010 MW; C3CD3B14D8E21590 CRC64;
MTQESSRAGQ AGAGERHLAV LEGVLERITY ANEENGYTVA RVDTGRGAGD LLTVVGALLG
AQVGESLRME GRWGSHPQYG KQFTVENYTT VLPATVQGIR RYLGSGLVKG IGPVFADRIT
QHFGLDTLQI IEEEPKRLIE VPGLGPKRTK KIADAWEEQK AIKEVMLFLQ SVEVSTSIAV
RIYKKYSDAS ISVVKNQPYR LASDVWGIGF LTADRIAQSV GIPHDSPERV KAGLQYALSQ
STDQGHCYLP EERLIADAVK LLQVDTGLVI ECLAELAAPP EDDSDPGVVR ERVPGPDGGD
PVTAVYLVPF HRAELSLSAQ LLRLLRTGED RMPAFGDVAW DKALGWLKGR TGAELAPEQE
EAVRLALTKK VAVLTGGPGC GKSFTVRSIV ELARAKRAKV VLAAPTGRAA KRLSELTGAE
ASTVHRLLEL KPGGDAAYDR DRPLDADLVV VDEASMLDLL LANKLVKAVP PGAHLLFVGD
VDQLPSVGAG EVLRDLLTDG SPVPAVRLTR VFRQAQQSGV VTNAHRINSG QHPLTDGLKD
FFLFVEDDTE EAGRLTVDVA ARRIPARFGL DPRRDVQVLA PMHRGPAGAG TLNGLLQQAV
TPARPDLPEK RFGGRVFRVG DKVTQIRNNY EKGKNGVFNG TVGVVTSLDP VDQRLTVLTD
EDEEVAYEFD ELDELAHAYA VTIHRSQGSE YPAVVIPVTT GAWMMLQRNL LYTAVTRAKK
LVVLVGSRKA IGQAVRTVSA GRRCTALDFR LSPRPVEG
//
