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Database: UniProt
Entry: A0A1Q5L7K4_9ACTN
LinkDB: A0A1Q5L7K4_9ACTN
Original site: A0A1Q5L7K4_9ACTN 
ID   A0A1Q5L7K4_9ACTN        Unreviewed;       566 AA.
AC   A0A1Q5L7K4;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=DEAD/DEAH box helicase {ECO:0000313|EMBL:OKJ90313.1};
GN   ORFNames=AMK31_00710 {ECO:0000313|EMBL:OKJ90313.1};
OS   Streptomyces sp. TSRI0107.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1703942 {ECO:0000313|EMBL:OKJ90313.1, ECO:0000313|Proteomes:UP000185813};
RN   [1] {ECO:0000313|EMBL:OKJ90313.1, ECO:0000313|Proteomes:UP000185813}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TSRI0107 {ECO:0000313|EMBL:OKJ90313.1,
RC   ECO:0000313|Proteomes:UP000185813};
RX   PubMed=27999165; DOI=10.1128/mbio.02104-16;
RA   Yan X., Ge H., Huang T., Hindra, Yang D., Teng Q., Crnovcic I., Li X.,
RA   Rudolf J.D., Lohman J.R., Gansemans Y., Zhu X., Huang Y., Zhao L.X.,
RA   Jiang Y., Van Nieuwerburgh F., Rader C., Duan Y., Shen B.;
RT   "Strain Prioritization and Genome Mining for Enediyne Natural Products.";
RL   MBio 7:e02104-e02116(2016).
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:OKJ90313.1}.
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DR   EMBL; LIVZ01000001; OKJ90313.1; -; Genomic_DNA.
DR   RefSeq; WP_073938292.1; NZ_LIVZ01000001.1.
DR   AlphaFoldDB; A0A1Q5L7K4; -.
DR   STRING; 1703942.AMK31_00710; -.
DR   OrthoDB; 9805696at2; -.
DR   Proteomes; UP000185813; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0003724; F:RNA helicase activity; IEA:InterPro.
DR   CDD; cd00268; DEADc; 1.
DR   CDD; cd18787; SF2_C_DEAD; 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; IPR027417; P-loop_NTPase.
DR   InterPro; IPR014014; RNA_helicase_DEAD_Q_motif.
DR   PANTHER; PTHR47959:SF13; ATP-DEPENDENT RNA HELICASE RHLE; 1.
DR   PANTHER; PTHR47959; ATP-DEPENDENT RNA HELICASE RHLE-RELATED; 1.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
DR   PROSITE; PS51195; Q_MOTIF; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000313|EMBL:OKJ90313.1};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000185813}.
FT   DOMAIN          39..67
FT                   /note="DEAD-box RNA helicase Q"
FT                   /evidence="ECO:0000259|PROSITE:PS51195"
FT   DOMAIN          70..243
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          254..415
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          1..30
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          425..566
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           39..67
FT                   /note="Q motif"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00552"
FT   COMPBIAS        447..465
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        467..502
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   566 AA;  58845 MW;  908907A614953313 CRC64;
     MSRRPQKSNR RASSPPPSAS SPREFRLPEG TTPALPAVEE FAALDMPAGL LQTLTAQGVT
     TPFPIQAATL PNSLAGRDLL GRGRTGSGKT LAFGLALLAR TAGLRAEPKA PLALVLVPTR
     ELAQQVTDAL TPYATAVNVR LATVVGGLSI TKQAGALRRG TEVLVATPGR LNDLVERGDC
     VLDDVRITVL DEADQMTDMG FLPQITKLIQ RVRPDGQRML FSATLDRNID RLVQRFLTDP
     VVHSVDPSAG AVTTMEHHVL HVQDETDKKA VTTRIAARDG RVILFLDTKR SADRLAKRLL
     AVGVRAAALH GGRSQPQRNR TLEQFKNGQV TALVATNVAA RGIHVDDLDL VVNVDPPTDH
     KDYLHRGGRT ARAGGSGSVV TLVLPDQKRD VTRLMSDAGI RPRATRVASS DAELATITGA
     REPSGVAVTI EVPQQATTPK ASRPDGKPGG KPGRRSGRRR GNAEGAETAS RTATRKTAGA
     TPSGDSPSRS SGGTSATGGR GSARRTGSGG ATGAASAGTG GRGSDRRSGA RAANGTASGK
     AARGSARRKP ANGATGGATG TRGGTR
//
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