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Database: UniProt
Entry: A0A069JYI6_9ACTN
LinkDB: A0A069JYI6_9ACTN
Original site: A0A069JYI6_9ACTN 
ID   A0A069JYI6_9ACTN        Unreviewed;       762 AA.
AC   A0A069JYI6;
DT   01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   SubName: Full=ATP-dependent DNA helicase RecG {ECO:0000313|EMBL:KDQ69741.1};
GN   ORFNames=DT87_21885 {ECO:0000313|EMBL:KDQ69741.1};
OS   Streptomyces sp. NTK 937.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1487711 {ECO:0000313|EMBL:KDQ69741.1, ECO:0000313|Proteomes:UP000027475};
RN   [1] {ECO:0000313|EMBL:KDQ69741.1, ECO:0000313|Proteomes:UP000027475}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NTK 937 {ECO:0000313|EMBL:KDQ69741.1,
RC   ECO:0000313|Proteomes:UP000027475};
RA   Olano C., Cano-Prieto C., Losada A., Mendez C., Salas J.A.;
RT   "Draft genome sequence of marine actinomycete Streptomyces sp. NTK 937,
RT   producer of the benzoxazol antibiotic caboxamycin.";
RL   Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the helicase family. RecG subfamily.
CC       {ECO:0000256|ARBA:ARBA00007504}.
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:KDQ69741.1}.
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DR   EMBL; JJOB01000001; KDQ69741.1; -; Genomic_DNA.
DR   RefSeq; WP_037879738.1; NZ_JJOB01000001.1.
DR   AlphaFoldDB; A0A069JYI6; -.
DR   OrthoDB; 9804325at2; -.
DR   Proteomes; UP000027475; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR   CDD; cd17992; DEXHc_RecG; 1.
DR   CDD; cd04488; RecG_wedge_OBF; 1.
DR   Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR004365; NA-bd_OB_tRNA.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR047112; RecG/Mfd.
DR   InterPro; IPR045562; RecG_dom3_C.
DR   PANTHER; PTHR47964; ATP-DEPENDENT DNA HELICASE HOMOLOG RECG, CHLOROPLASTIC; 1.
DR   PANTHER; PTHR47964:SF1; ATP-DEPENDENT DNA HELICASE HOMOLOG RECG, CHLOROPLASTIC; 1.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF19833; RecG_dom3_C; 1.
DR   Pfam; PF01336; tRNA_anti-codon; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW   Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000313|EMBL:KDQ69741.1};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}.
FT   DOMAIN          287..478
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          501..689
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          532..555
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   762 AA;  82888 MW;  50895AC75AB1D689 CRC64;
     MERVSAFDEP LKKLLGGPTA KVMADHLDLH TVGDLLHHYP RRYEERGRLT ALTDLPLDEH
     VTVVAQVADA RVMTFNGGRG RRLEVTLTDG SGRLQLVFFG HGVHKPHKEL LPGRRAMFAG
     KVSVFNRKLQ LAHPTYQLLD VRDEDEATEA ADAFAGQLLP IYPACKQLDS WRIAKAVDTV
     LPGAGEAVDP LPASLRDGRG FVSLPEALLK IHRPHTKADV AAARERLKWD EAFVLQVALA
     RRRHSDTELP ATARRPVPGG LLDAFDAGLP FTLTDGQRTV TDEIFRDLAT EHPMHRLLQG
     EVGSGKTLVA LRAMLRVVDA GGQTALLAPT EVLAQQHHRS ITEMMGELAE NWGLWREAPL
     DEGRRPGDGR ALGGSHRGTK VVLLTGSMGT AARRQALLDL VTGEAGIVIG THALIEDKVK
     FHDLGLVVVD EQHRFGVEQR DALRSKGKQQ PHLLVMTATP IPRTVAMTVF GDLETSVLDQ
     LPAGRSPIAS HVVPAKDKPH FLDRAWERVR EEAEGGHQAY VVCPRIGDDT DEAAEKKGKK
     RDDAAADAAA DAADDAEKRP PLAVLDIAAQ LARGPLAGLR VEVLHGRMPP DEKDDVMRRF
     AAGRVDVLVA TTVIEVGVNV PNATAMVIMD ADRFGVSQLH QLRGRVGRGS APGLCLLVSE
     AHEASPARAR LSAVAATLDG FELSRIDLEQ RREGDVLGQA QSGVRSSLRV LSVIDDEEVI
     AAAREEAVRI VADDPALERL PELRTALDAL LDKDREEYLD KG
//
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