ID L1L8I1_9ACTN Unreviewed; 1231 AA.
AC L1L8I1;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE RecName: Full=DNA 3'-5' helicase {ECO:0000256|ARBA:ARBA00034808};
DE EC=5.6.2.4 {ECO:0000256|ARBA:ARBA00034808};
GN ORFNames=STRIP9103_06568 {ECO:0000313|EMBL:EKX69321.1};
OS Streptomyces ipomoeae 91-03.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=698759 {ECO:0000313|EMBL:EKX69321.1, ECO:0000313|Proteomes:UP000010411};
RN [1] {ECO:0000313|EMBL:EKX69321.1, ECO:0000313|Proteomes:UP000010411}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=91-03 {ECO:0000313|EMBL:EKX69321.1,
RC ECO:0000313|Proteomes:UP000010411};
RA Huguet-Tapia J.C., Durkin A.S., Pettis G.S., Badger J.H.;
RL Submitted (NOV-2012) 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:EKX69321.1}.
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DR EMBL; AEJC01000012; EKX69321.1; -; Genomic_DNA.
DR RefSeq; WP_009293542.1; NZ_AEJC01000012.1.
DR AlphaFoldDB; L1L8I1; -.
DR PATRIC; fig|698759.3.peg.150; -.
DR Proteomes; UP000010411; Unassembled WGS sequence.
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-KW.
DR GO; GO:0003678; F:DNA helicase activity; IEA:InterPro.
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; IPR011335; Restrct_endonuc-II-like.
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 SUPFAM; SSF52980; Restriction endonuclease-like; 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 DNA-binding {ECO:0000256|ARBA:ARBA00023125};
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:UP000010411}.
FT DOMAIN 17..343
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51198"
FT DOMAIN 344..664
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51217"
FT REGION 838..978
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1201..1231
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 838..858
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 859..908
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 909..930
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 38..45
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ SEQUENCE 1231 AA; 134051 MW; D11A2E0CE3FCC106 CRC64;
MSARISDPEQ LKELLGIPFT PEQTACIIAP PAPQVIVAGA GSGKTTVMAA RVVWLVGTGQ
VAPEQVLGLT FTNKAAGELA ERVRKALVKA GITDPDVIDP DNPPGEPVIS TYHAFAGRLL
TDHGLRVGLE PTSRLLADAT RYQLAARVLR EAPGPYPALT RSFPDLVSDL LALDSELAEH
LVRPEELRAY DAELLRDLES AKLTNADLRK VPEAAAARRE LAELVGRYRT VKRERDLLDF
GDQIALSARL AQLPEVGRIL RDEFRVVLLD EYQDTSVAQR VLLAGLFGGG TGHPVTAVGD
PCQAIYGWRG ASVANLDDFP EHFAHADGSP ATRQALSENR RSGGRLLDLA NGLAEPLRAM
HAGVEALRPA PGAERDGVVR CALLPTHAEE LDWIADSIAH LVRTGKEPGE IAVLCRTATD
FAEIQGALVA RDIPVEVVGL SGLLHLPEVA DLVAVCEVLQ DPGANASLVR LLTGPRWRIG
PRDLALLGRR ARLLVSHARV GADDDPDRRL AAAVEGVDPS EVISLADALD TFLELPLEAE
AEDDGLPFSP DARVRFARLA TELRDLRRSL ADPLMDVLHR VLAVTGLEVE LSASPHALAA
RRRETLSNFL DIAAAFAANS EGEATLLAFL GFLRTAAQYE KGLDNALPGG ENTVKVLTAH
KSKGLEWDVV AVPGLVTGTF PSTQGREKWT AQGRVLPHEL RGDADTLPDV EAWDSRGLKT
FQEAMKDHQH TEELRLGYVT FTRPRSLLLG SGHWWGPSQK RPRGPSDFLK ALYDHCAAGY
GEIEAWADEP EEGAENPALR ETAADHAWPL PLDDTALARR RAAAETVLAH LERVASHEDT
HPGAAHDLDP HSYDDPEWPP PPDDEEALYG DDDFPEDIPY EDDDFHEEDD FSADLSQDIP
EEDTSDWDSW TEDRPAHSVR PPHARVPHPG HDEGTPVGPH PGHQENAPTG PRSGHDGRTP
VVPHARRHPA ASDLTPEEAR TIASWDRDLD ALTGELLRAR AKVTDVPLPM SLTASQLVRL
AADPDGFAQE LARPMPRPPQ PAARRGTRFH AWVEARFEEL RLPMLEPEDL PGSEAEIADE
RDLEALKAAF ERTPYAHRTP YRVEAPFQLG IAGRVVRGRI DAVYRDSDGD GTTTYEIVDW
KTSRNRTADP LQLALYRLAW AEQQGVPLES VKAAFLYVRT GDVVHPEDLP GRSALERLLL
EEPGADGLES DPVGPQPLTD EPPDEHVGAG L
//
