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Database: UniProt
Entry: D9WEU1_9ACTN
LinkDB: D9WEU1_9ACTN
Original site: D9WEU1_9ACTN 
ID   D9WEU1_9ACTN            Unreviewed;       823 AA.
AC   D9WEU1;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   27-MAR-2024, entry version 65.
DE   RecName: Full=ATP-dependent DNA helicase {ECO:0000256|RuleBase:RU364053};
DE            EC=5.6.2.4 {ECO:0000256|RuleBase:RU364053};
GN   ORFNames=SSOG_05020 {ECO:0000313|EMBL:EFL25306.1};
OS   Streptomyces himastatinicus ATCC 53653.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces; Streptomyces violaceusniger group.
OX   NCBI_TaxID=457427 {ECO:0000313|EMBL:EFL25306.1, ECO:0000313|Proteomes:UP000003963};
RN   [1] {ECO:0000313|EMBL:EFL25306.1, ECO:0000313|Proteomes:UP000003963}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 53653 {ECO:0000313|EMBL:EFL25306.1,
RC   ECO:0000313|Proteomes:UP000003963};
RG   The Broad Institute Genome Sequencing Platform;
RG   Broad Institute Microbial Sequencing Center;
RA   Fischbach M., Godfrey P., Ward D., Young S., Zeng Q., Koehrsen M.,
RA   Alvarado L., Berlin A.M., Bochicchio J., Borenstein D., Chapman S.B.,
RA   Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA   Gujja S., Heilman E.R., Heiman D.I., Hepburn T.A., Howarth C., Jen D.,
RA   Larson L., Lewis B., Mehta T., Park D., Pearson M., Richards J.,
RA   Roberts A., Saif S., Shea T.D., Shenoy N., Sisk P., Stolte C., Sykes S.N.,
RA   Thomson T., Walk T., White J., Yandava C., Straight P., Clardy J., Hung D.,
RA   Kolter R., Mekalanos J., Walker S., Walsh C.T., Wieland-Brown L.C.,
RA   Haas B., Nusbaum C., Birren B.;
RT   "Annotation of Streptomyces hygroscopicus strain ATCC 53653.";
RL   Submitted (FEB-2009) 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         ECO:0000256|RuleBase:RU364053};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Couples ATP hydrolysis with the unwinding of duplex DNA by
CC         translocating in the 3'-5' direction.; EC=5.6.2.4;
CC         Evidence={ECO:0000256|ARBA:ARBA00034617};
CC   -!- SIMILARITY: Belongs to the helicase family. UvrD subfamily.
CC       {ECO:0000256|ARBA:ARBA00009922, ECO:0000256|RuleBase:RU364053}.
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DR   EMBL; GG657754; EFL25306.1; -; Genomic_DNA.
DR   AlphaFoldDB; D9WEU1; -.
DR   STRING; 457427.SSOG_05020; -.
DR   HOGENOM; CLU_004585_3_1_11; -.
DR   Proteomes; UP000003963; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
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   GO; GO:0006268; P:DNA unwinding involved in DNA replication; IEA:InterPro.
DR   CDD; cd17932; DEXQc_UvrD; 1.
DR   CDD; cd18807; SF1_C_UvrD; 1.
DR   Gene3D; 1.10.10.160; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   InterPro; IPR005751; ATP-dep_DNA_helicase_PcrA.
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; IPR014016; UvrD-like_ATP-bd.
DR   NCBIfam; TIGR01073; pcrA; 1.
DR   PANTHER; PTHR11070:SF2; ATP-DEPENDENT DNA HELICASE SRS2; 1.
DR   PANTHER; PTHR11070; UVRD / RECB / PCRA DNA HELICASE FAMILY MEMBER; 1.
DR   Pfam; PF21196; PcrA_UvrD_tudor; 1.
DR   Pfam; PF00580; UvrD-helicase; 1.
DR   Pfam; PF13361; UvrD_C; 1.
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-binding {ECO:0000256|RuleBase:RU364053};
KW   Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000256|PROSITE-
KW   ProRule:PRU00560};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW   ProRule:PRU00560};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU00560}.
FT   DOMAIN          72..357
FT                   /note="UvrD-like helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51198"
FT   DOMAIN          358..641
FT                   /note="UvrD-like helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51217"
FT   REGION          1..58
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          723..762
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        723..759
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         93..100
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ   SEQUENCE   823 AA;  90309 MW;  4604D15ED5C2052C CRC64;
     MASLGPPEEE PPPPEDSAHP GHSGGSDGSG GEEVPHHLFT GAFDAPVPSG TREPYYRDGA
     ARPAVDPAAL LEGLNEQQRA AVEHTGSPLL IVAGAGSGKT RVLTHRIAYL LGTRHVHPGQ
     ILAITFTNKA AGEMKERVEE LVGPRANAMW VMTFHSACVR ILRRESKKLG FTSSFSIYDA
     ADSKRLMALV CRDLDLDPKK FPPKSFSAKI SNLKNELIDE ETFAGQAADG FEKTLAEAYA
     MYQSRLREAN ALDFDDIIMT TVNLLQAFPD VAEHYRRRFR HVMVDEYQDT NHAQYTLVRE
     LVGTDTDEVA AGELCVVGDA DQSIYAFRGA TIRNILQFEE DYPDARTILL EQNYRSTQTI
     LSAANAVIER NENRRPKNLW TEAGTGATIT GYVADTEHDE AQFVADEIDR LTDAGDARAG
     DVAVFYRTNA QSRVFEEIFI RVGLPYKVVG GVRFYERKEV RDVLAYLRVL ANPEDAVPLR
     RIMNVPKRGI GDRAEAMIDA LASREKITFP QALRRVDEAY GMAARSANAV KRFNTLMEEL
     RTIVESGAGP ATVLEAVLER TGYLAELQAS TDPQDETRIE NLQELASVAL EFEQDRGEEN
     PGTLAEFLEQ VALVADSDQI PDEDEEGTGV ITLMTLHTAK GLEFPVVFLS GMEDGVFPHM
     RALGQTKELE EERRLAYVGI TRARERLYLS RSTMRSAWGT PSYNPPSRFL EEIPDQYVQW
     RRTGPATPSA SMGAMTSGGG AGLSSSRSRS GTSASGASGF ATRRAKDRPV VSLAIGDRVT
     HDSFGLGTVV AVKGTGDNAE ATIDFGGEKP KRLLLRYAPV EKL
//
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