ID A0A117P082_9ACTN Unreviewed; 1108 AA.
AC A0A117P082;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=DNA 3'-5' helicase {ECO:0000256|ARBA:ARBA00034808};
DE EC=5.6.2.4 {ECO:0000256|ARBA:ARBA00034808};
GN ORFNames=AQI70_28465 {ECO:0000313|EMBL:KUM70688.1};
OS Streptomyces curacoi.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=146536 {ECO:0000313|EMBL:KUM70688.1, ECO:0000313|Proteomes:UP000054024};
RN [1] {ECO:0000313|EMBL:KUM70688.1, ECO:0000313|Proteomes:UP000054024}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 40107 {ECO:0000313|EMBL:KUM70688.1,
RC ECO:0000313|Proteomes:UP000054024};
RA Ruckert C., Winkler A., Kalinowski J., Kampfer P., Glaeser S.;
RT "Draft genome sequence of Streptomyces curacoi DSM 40107, type strain for
RT the species Streptomyces curacoi.";
RL Submitted (OCT-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:KUM70688.1}.
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DR EMBL; LMWJ01000023; KUM70688.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A117P082; -.
DR STRING; 146536.AQI70_28465; -.
DR Proteomes; UP000054024; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
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; IPR011335; Restrct_endonuc-II-like.
DR InterPro; IPR014016; UvrD-like_ATP-bd.
DR PANTHER; PTHR11070:SF59; 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; 1.
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:UP000054024}.
FT DOMAIN 1..294
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51198"
FT DOMAIN 294..666
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51217"
FT REGION 423..483
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 13..20
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ SEQUENCE 1108 AA; 119731 MW; 41E712234C0FBB32 CRC64;
MVDHAAGPLL VLAGPGTGKT TTLVESVAAR IARGGDPERI LVLTFSRKAA VELRDRMALR
IGAARAPQAT TFHSFCYALV RAHQDSDLFV EPLRLLSGPE QDVTVRELLA GQPDLERLGL
AHVRWPDELR ACLTTRGFAD EVRAVLARSR ELGLGPHALD AFARRLGRPD WRAAAAFLAE
YLDVLDLQGV LDYAELVHRA VLLARRPETA ERLAAQYDAV YVDEYQDTDP AQVRLLRALA
GGGRTLVAFG DPDQSIYAFR GADVNGILEF PQAFPRADGR PAPVEVLRTS RRSGAALLAA
TRLLTQRMPL TRLPAEKVRA HRELAPVREG GRVEVFTYPT PGTELDNIAD ILRRAHLEDG
VPWGEMAVLV RAGARMIPTV RRALTAAGVP LDIDGDDLPL RHEPAVAPLL TALRAVANAE
AAAREAPSGE AEAAAREAPS GEAEAAAREV PSEEEAQEVV PSEEAEAAGS EAVPDEPDPD
TCWLDTETAL TLLTSPLAGM DTADLRRLGR ALRDEERAAG NPLPPPSDEL LARALAEPER
LAVHDPTYAR GAQRLGALLR KARERLAGGG TAEEALWGLW EGTPWPARLE RTARRGGAAG
RNADRDLDAV CALFATAARA EERTGGRGAL NFLAEIEAED IAADTLTRRA VRPDAVRLMT
AHRSKGLEWR LVVVAGVQEG LWPDLRRRGS LLEADRIGRD GLAEPLTPGA LLAEERRLFY
VAATRARERL VVTAVKAPAD DGDQPSRFLT ELGVEPRDVT GRPRRPLSVA ALVAELRATT
VDPRASDALR EAAARRLARL AALTDEDGRP LVPSAHPYRW WGMFEPTESK VPLRDRDQPV
VLSGSALDQL ANTCALQWFL GREVKADAPA TAAQGFGNVV HVLADEVASG HTPADLAVLM
ERLDSVWNAL AFDAPWKSAQ EKDHARVALE RFLQWHVMDR AGRTPVASEH DFDVTLAAGE
FEVRIRGQMD RVEADGDGRA YVVDFKTGKQ APSAAEVARH PQLAVYQLAV REGAVDEAFH
GVRPEPGGAE LVQLRQGAAK RDGGETLPKV QGQAPLEGAE GEWVGDLLAT AAGKVLDERF
TPTAGQHCTH CAFRASCSAR SEGRHVVE
//
