ID A0A0J8BT31_STRVR Unreviewed; 751 AA.
AC A0A0J8BT31;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 40.
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=ACM01_37790 {ECO:0000313|EMBL:KMS68765.1};
OS Streptomyces viridochromogenes.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1938 {ECO:0000313|EMBL:KMS68765.1, ECO:0000313|Proteomes:UP000037432};
RN [1] {ECO:0000313|EMBL:KMS68765.1, ECO:0000313|Proteomes:UP000037432}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 3414 {ECO:0000313|EMBL:KMS68765.1,
RC ECO:0000313|Proteomes:UP000037432};
RA Ju K.-S., Doroghazi J.R., Metcalf W.W.;
RL Submitted (JUN-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:KMS68765.1}.
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DR EMBL; LFNT01000071; KMS68765.1; -; Genomic_DNA.
DR RefSeq; WP_048585959.1; NZ_LGUR01000173.1.
DR AlphaFoldDB; A0A0J8BT31; -.
DR PATRIC; fig|1938.3.peg.6472; -.
DR OrthoDB; 9763659at2; -.
DR Proteomes; UP000037432; 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:KMS68765.1};
KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_01488};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_01488}.
FT DOMAIN 365..562
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT BINDING 376..380
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01488"
SQ SEQUENCE 751 AA; 81019 MW; C44B682F38EA978E CRC64;
MSNQAGSSTG ERRLAVLEGV LERITYANEE NGYTVARVDT GRGGGDLLTV VGALLGAQVG
ESLRLEGRWG SHPQYGKQFT VENYTTVLPA TVQGIRRYLG SGLVKGIGPV FADRITQHFG
LDTLTIIEEE PKRLIEVPGL GPKRTKKIAD AWEEQKAIKE VMLFLQTVEV STSIAVRIYK
KYGDASISVV KNQPYRLAAD VWGIGFLTAD KIAQSVGIPH DSPERVKAGL QYALSQATDQ
GNCYLPEEQL IADAVKLLQV DTGLVIECLA ELAQVPEDGG DPGVVREKVP GPDGGSEPVT
AVYLVPFHRA ELSLSAQLLR LLRTDEDRMP GFHDVAWDKA LGWLRGRTGT DLAPEQEAAV
KLALTRKVAV LTGGPGCGKS FTVRSIVELA RAKKARVVLA APTGRAAKRL AELTGAEAST
VHRLLELKPG GDAAYDRERP LQADLVVVDE ASMLDLLLAN KLVKAVPPGA HLLFVGDVDQ
LPSVGAGEVL RDLLAEGSPI PAVRLTRVFR QAQQSGVVTN AHRINAGQHP VTDGMKDFFL
FVEDDTEAAG RLTVDVAARR IPAKFGLDPR RDVQVLAPMH RGPAGAGTLN GLLQQAVTPG
RPDLAEKRFG GRVFRVGDKV TQIRNNYEKG KNGVFNGTVG VVTSLDPVDQ RLTVLTDEDE
EVPYEFDELD ELAHAYAVTI HRSQGSEYPA VVIPVTTGAW MMLQRNLLYT AVTRAKRLVV
LVGSRKAIGQ AVRTVSAGRR CTALDYRLAG S
//
