ID A0A0N0T351_9ACTN Unreviewed; 1192 AA.
AC A0A0N0T351;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=DNA 3'-5' helicase {ECO:0000256|ARBA:ARBA00034808};
DE EC=5.6.2.4 {ECO:0000256|ARBA:ARBA00034808};
GN ORFNames=ADL01_19715 {ECO:0000313|EMBL:KOV71748.1};
OS Streptomyces sp. NRRL WC-3618.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1519490 {ECO:0000313|EMBL:KOV71748.1, ECO:0000313|Proteomes:UP000037738};
RN [1] {ECO:0000313|EMBL:KOV71748.1, ECO:0000313|Proteomes:UP000037738}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL WC-3618 {ECO:0000313|EMBL:KOV71748.1,
RC ECO:0000313|Proteomes:UP000037738};
RA Noorani M.;
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
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=5.6.2.4;
CC Evidence={ECO:0000256|ARBA:ARBA00034618};
CC -!- SIMILARITY: Belongs to the helicase family. UvrD subfamily.
CC {ECO:0000256|ARBA:ARBA00009922}.
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:KOV71748.1}.
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DR EMBL; LGDW01000213; KOV71748.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0N0T351; -.
DR PATRIC; fig|1519490.3.peg.4306; -.
DR Proteomes; UP000037738; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0003678; F:DNA helicase activity; IEA:InterPro.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-UniRule.
DR CDD; cd17932; DEXQc_UvrD; 1.
DR Gene3D; 1.10.10.160; -; 1.
DR Gene3D; 3.90.320.10; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 3.
DR InterPro; IPR013986; DExx_box_DNA_helicase_dom_sf.
DR InterPro; IPR014017; DNA_helicase_UvrD-like_C.
DR InterPro; IPR000212; DNA_helicase_UvrD/REP.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR011604; PDDEXK-like_dom_sf.
DR InterPro; IPR038726; PDDEXK_AddAB-type.
DR InterPro; IPR014016; UvrD-like_ATP-bd.
DR PANTHER; PTHR11070:SF55; DNA HELICASE; 1.
DR PANTHER; PTHR11070; UVRD / RECB / PCRA DNA HELICASE FAMILY MEMBER; 1.
DR Pfam; PF12705; PDDEXK_1; 1.
DR Pfam; PF00580; UvrD-helicase; 1.
DR Pfam; PF13361; UvrD_C; 2.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS51198; UVRD_HELICASE_ATP_BIND; 1.
DR PROSITE; PS51217; UVRD_HELICASE_CTER; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00560}; DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW Exonuclease {ECO:0000256|ARBA:ARBA00022839};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000256|PROSITE-
KW ProRule:PRU00560};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW ProRule:PRU00560}; Nuclease {ECO:0000256|ARBA:ARBA00022722};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00560}; Reference proteome {ECO:0000313|Proteomes:UP000037738}.
FT DOMAIN 27..353
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51198"
FT DOMAIN 354..673
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51217"
FT REGION 842..953
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 842..857
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 863..880
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 926..953
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 48..55
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ SEQUENCE 1192 AA; 129738 MW; 1CAADD1DF18F59B4 CRC64;
MSVAAASLCD VPASISDPEQ LKELLGIPFT PEQTACITAP PAPQVIVAGA GSGKTTVMAA
RVVWLVGTGQ VAPEQVLGLT FTNKAAGELA ERVRKALVKA GVTDPDVIDP DNPPGEPVIS
TYHSFAGRLL TDHGLRIGLE PTARLLADAT RYQLAARVLR EAPGPYPSLT RSFPDLVSDL
LTLDAELSEH LVRPEELRAY DAELLSALEG TKLTNADLRK VPETAAARRE LAELVTRYRA
AKRERDLLDF GDQIALSATL ARIPEVGRVL RDEFRVVLLD EYQDTSVAQR ILLAGLFGDG
TGHPVTAVGD PCQAIYGWRG ASVANLDDFP EHFAHADGGS AARQSLSENR RSGGRLLDLA
NDLAEPLRAM HAGVEALRPA PGAERDGQVR CALLPTHAEE IDWLADSIAH LVRTGKAPGE
IAVLCRTATD FAEIQGALVA RDVPVEVVGL SGLLHLPEVA DLVSVCEVLQ DPGANASLVR
LLTGPRWRIG PRDLALLGRR ARFLVSHARV GDPDDPDRRL AEAVEGVDPS EVISLADALD
TFLETSMRGE GDDDGLPFSP DARVRFARLA TELRDLRRSL ADPLMDVLHR VLAVTGLEVE
LSASPHALAA RRRETLSNFL DIAASFAAHE SEASLLAFLG FLRTAAQYEK GLDNALPGGE
NTVKVLTAHK SKGLEWDVVA VPGLVTGTFP SAQGREKWTS QAKVLPHGLR GDTDTLPDIE
AWDSRGMKAF QEAMKNHQHT EELRLGYVTF TRPRSLLLGS GHWWGPSQKK PRGPSDFLRA
LHDHCTAGHG EIEVWADEPA QDEENPALHA TTADQLWPLP LDDAAFRRRR AAAETVLAHL
ETLSSHDEGR PAAAPDPDTY DDPDWPPPPD DEPPYEDDEP FDDAYLAHGH PDQDAPFPAA
DDTDWDAWTT DRPEPPAPTS PHARVPHTGR GHDRPPTVPH ARRHPAEADL TPEEARAVAS
WDRDLDALAG ELLRARESVT DVPLPLSMTA SQLMLLAADP DALAQELARP MPRPPQPAAR
RGIRFHAWVE ARFEALRLPM LEHDELPGSD AEIADERDLE TLKDAFENTA YAHRTPYRVE
APFQLDIAGR VVRGRIDAVY KEGDGADVTY EIIDWKTHRA PTADPLQLAV YRLAWAEQQG
VPLEAVEAAF LYVRTGETVR PDDLPDRAAL ERLLLDEPAA FELPDEDVSA GR
//
