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Database: UniProt
Entry: A0A1G9EEP4_9ACTN
LinkDB: A0A1G9EEP4_9ACTN
Original site: A0A1G9EEP4_9ACTN 
ID   A0A1G9EEP4_9ACTN        Unreviewed;       830 AA.
AC   A0A1G9EEP4;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   RecName: Full=ATP-dependent DNA helicase {ECO:0000256|RuleBase:RU364053};
DE            EC=5.6.2.4 {ECO:0000256|RuleBase:RU364053};
GN   ORFNames=SAMN05421806_111123 {ECO:0000313|EMBL:SDK74612.1};
OS   Streptomyces indicus.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=417292 {ECO:0000313|EMBL:SDK74612.1, ECO:0000313|Proteomes:UP000199155};
RN   [1] {ECO:0000313|EMBL:SDK74612.1, ECO:0000313|Proteomes:UP000199155}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 4.5727 {ECO:0000313|EMBL:SDK74612.1,
RC   ECO:0000313|Proteomes:UP000199155};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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; FNFF01000011; SDK74612.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G9EEP4; -.
DR   STRING; 417292.SAMN05421806_111123; -.
DR   OrthoDB; 4812256at2; -.
DR   Proteomes; UP000199155; 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}; Reference proteome {ECO:0000313|Proteomes:UP000199155}.
FT   DOMAIN          71..365
FT                   /note="UvrD-like helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51198"
FT   DOMAIN          366..649
FT                   /note="UvrD-like helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51217"
FT   REGION          14..37
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        14..29
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         92..99
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ   SEQUENCE   830 AA;  91154 MW;  938628F2FDA55916 CRC64;
     MSSLFDDSFL AELQSKDGAR DHSAPPPPED EGPEEIPADL FAGKFDAPVQ RDAYYRDGAP
     RPVLDGAALL DGLNENQRAA VTHSGSPLLI VAGAGSGKTR VLTHRIAYLL AERNVHPGQI
     LAITFTNKAA GEMKERVEEL VGPRAGAMWV MTFHSACVRI LRRESKKLGF TSSFSIYDAA
     DSKRLMALVC RDLDLDPKRF PPKAFSAKIS NLKNELIDEE DFASQAADGF EKTLAQAYAM
     YQARLREANA LDFDDLIMTT VNLLRAFPDV AEHYRRRFRH VMVDEYQDTN HAQYALVREL
     VGTGAHPEDV PPSEHDLPPA ELCVVGDADQ SIYAFRGATI RNILDFEEDY PDATTILLEQ
     NYRSTQTILS AANAVIERNE SRRPKNLWTN AGNGAQITGY VADTEHDEAQ FVADEIDRLT
     DAGDAKAGDV AVFYRTNAQS RVFEEVFIRV GLPYKVVGGV RFYERKEVRD VLAYLRVLAN
     PEDSVPLRRI LNVPKRGIGE RAEAMIDALS LREKITFPQA LVRVDEAYGM AARSTNAVKR
     FNTLMEELRT IVESGAGPAT VLEAVLERTG YLAELQASTD PQDETRIENL QELAAVALEF
     EQEAEDGETG TLADFLERVA LVADSDQIPD EDEDGSGVIT LMTLHTAKGL EFPVVFLTGM
     EDGVFPHMRA LGQTKELEEE RRLAYVGITR ARERLYLTRS TLRSAWGQPS YNPPSRFLEE
     IPAQHLEWKR TGAKLGAPVG KGPAASVATS LSSSMNARAS RGGPSGFATG RAGDKPVVSL
     AVGDRVTHDQ FGLGTVVGVE GAGDKARATI DFGDAKPKVL LLRYAPVEKL
//
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