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Database: UniProt
Entry: A0A3S9PMY8_STRLT
LinkDB: A0A3S9PMY8_STRLT
Original site: A0A3S9PMY8_STRLT 
ID   A0A3S9PMY8_STRLT        Unreviewed;       738 AA.
AC   A0A3S9PMY8;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   RecName: Full=ATP-dependent DNA helicase RecG {ECO:0000256|ARBA:ARBA00017846};
DE            EC=3.6.4.12 {ECO:0000256|ARBA:ARBA00012551};
GN   Name=recG {ECO:0000313|EMBL:AZQ73769.1};
GN   ORFNames=EKH77_23370 {ECO:0000313|EMBL:AZQ73769.1};
OS   Streptomyces luteoverticillatus (Streptoverticillium luteoverticillatus).
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=66425 {ECO:0000313|EMBL:AZQ73769.1, ECO:0000313|Proteomes:UP000267900};
RN   [1] {ECO:0000313|EMBL:AZQ73769.1, ECO:0000313|Proteomes:UP000267900}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 15060 {ECO:0000313|EMBL:AZQ73769.1,
RC   ECO:0000313|Proteomes:UP000267900};
RA   Feng Z., Chen G., Zhang J., Zhu H., Yu X., Zhang W., Zhang X.;
RT   "The whole draft genome of Streptomyce luteoverticillatus CGMCC 15060.";
RL   Submitted (DEC-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the helicase family. RecG subfamily.
CC       {ECO:0000256|ARBA:ARBA00007504}.
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DR   EMBL; CP034587; AZQ73769.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3S9PMY8; -.
DR   OrthoDB; 9804325at2; -.
DR   Proteomes; UP000267900; Chromosome.
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; IPR027417; P-loop_NTPase.
DR   InterPro; IPR047112; RecG/Mfd.
DR   InterPro; IPR045562; RecG_dom3_C.
DR   InterPro; IPR033454; RecG_wedge.
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; PF17191; RecG_wedge; 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:AZQ73769.1};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000267900}.
FT   DOMAIN          286..459
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          482..665
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          505..536
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        508..536
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   738 AA;  79996 MW;  B4EA7AF4B9218F32 CRC64;
     MPALDEPLKK TLGGTTAKVM AEHLDLHTVG DLLHHYPRRY AERGELTRLA DLPLDEHVTV
     VAQVLDARVH KFNQGRGQRL EVTVTDGGGR LQLVFFGRSI YHHQKELVPG RRGMFAGKVG
     TFRNIRQLSH PAYEMLGGDS DANTAKAWAD QLIPLYPACS KMESWKISNA VDVVLASMEA
     TGWEAVVDPL PPALREGRGL VPLPEALRKI HRPRAKTDIE DARARLKWDE AFVLQVALAR
     RRHADSQLPA VARKPAPGGL LDAFDAKLPF TLTDGQRKVS AEIFDDLATE HPMHRLLQGE
     VGSGKTMVAL RAMLAVVDAG GQAAMLAPTE VLAQQHHRSI TEMMGELAEG GMLGGAERGT
     KVVLLTGSMG TAARRQALLD LITGEAGVVV GTHALIEDKV QFHDLGLVVV DEQHRFGVEQ
     RDALRSKGKQ PPHLLVMTAT PIPRTVAMTV FGDLETSVLD QLPAGRSPIA THVVPAKDKP
     HFLARAWERV REEVAGGHQA YVVCPRIGDE EDAPKKKSAG SDESAESAED AAERRPPLAV
     LEVAEELSRG PLAGLRVEVL HGRMQPDAKD EVMRRFAAGE VDVLVATTVI EVGVNVPNST
     AMVIMDADRF GVSQLHQLRG RVGRGSAPGL CLLVSEMPEA SPARARLGAV AATLDGFELS
     RIDLEQRREG DVLGQAQSGV RSSLRMLTVI DDEEIIAAAR EEAAAVVAAD PELARLPELR
     TALDALLDKE REEFLDKG
//
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