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Database: UniProt
Entry: D2B0M6_STRRD
LinkDB: D2B0M6_STRRD
Original site: D2B0M6_STRRD 
ID   D2B0M6_STRRD            Unreviewed;       697 AA.
AC   D2B0M6;
DT   09-FEB-2010, integrated into UniProtKB/TrEMBL.
DT   09-FEB-2010, sequence version 1.
DT   27-MAR-2024, entry version 71.
DE   RecName: Full=RNA helicase {ECO:0000256|ARBA:ARBA00012552};
DE            EC=3.6.4.13 {ECO:0000256|ARBA:ARBA00012552};
GN   OrderedLocusNames=Sros_8393 {ECO:0000313|EMBL:ACZ91038.1};
OS   Streptosporangium roseum (strain ATCC 12428 / DSM 43021 / JCM 3005 / NI
OS   9100).
OC   Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC   Streptosporangiaceae; Streptosporangium.
OX   NCBI_TaxID=479432 {ECO:0000313|EMBL:ACZ91038.1, ECO:0000313|Proteomes:UP000002029};
RN   [1] {ECO:0000313|EMBL:ACZ91038.1, ECO:0000313|Proteomes:UP000002029}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 12428 / DSM 43021 / JCM 3005 / NI 9100
RC   {ECO:0000313|Proteomes:UP000002029};
RX   PubMed=21304675; DOI=10.4056/sigs.631049;
RA   Nolan M., Sikorski J., Jando M., Lucas S., Lapidus A., Glavina Del Rio T.,
RA   Chen F., Tice H., Pitluck S., Cheng J.F., Chertkov O., Sims D., Meincke L.,
RA   Brettin T., Han C., Detter J.C., Bruce D., Goodwin L., Land M., Hauser L.,
RA   Chang Y.J., Jeffries C.D., Ivanova N., Mavromatis K., Mikhailova N.,
RA   Chen A., Palaniappan K., Chain P., Rohde M., Goker M., Bristow J.,
RA   Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of Streptosporangium roseum type strain (NI
RT   9100).";
RL   Stand. Genomic Sci. 2:29-37(2010).
CC   -!- SIMILARITY: Belongs to the DEAD box helicase family.
CC       {ECO:0000256|RuleBase:RU000492}.
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DR   EMBL; CP001814; ACZ91038.1; -; Genomic_DNA.
DR   AlphaFoldDB; D2B0M6; -.
DR   STRING; 479432.Sros_8393; -.
DR   KEGG; sro:Sros_8393; -.
DR   eggNOG; COG0513; Bacteria.
DR   HOGENOM; CLU_3429895_0_0_11; -.
DR   Proteomes; UP000002029; Chromosome.
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; IPR000629; RNA-helicase_DEAD-box_CS.
DR   InterPro; IPR014014; RNA_helicase_DEAD_Q_motif.
DR   PANTHER; PTHR47963:SF8; ATP-DEPENDENT RNA HELICASE DEAD; 1.
DR   PANTHER; PTHR47963; DEAD-BOX ATP-DEPENDENT RNA HELICASE 47, MITOCHONDRIAL; 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; PS00039; DEAD_ATP_HELICASE; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
DR   PROSITE; PS51195; Q_MOTIF; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU000492};
KW   Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000256|RuleBase:RU000492};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU000492};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU000492};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002029}.
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          272..418
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          443..697
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        443..479
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        487..527
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        551..579
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        599..635
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   697 AA;  77506 MW;  96CB3F6BFDD7A0BD CRC64;
     MTLRGLALPR GPGTGKNFFF SPWSRQDCLQ RRFRQAKLTT FRDLGVTPEI ADALETEGII
     TPFPIQEMAL PLALNGQDII GQARTGTGKT YAFGVAMLQR VGKPRKNRKK PRGLVVVPTR
     ELAVQVTEDL VTAAGKLGSR ILTVYGGRAY EPQVEALKQG VDVIVGTPGR LLDLVKQKHL
     DLGQIDVLVL DEADRMLDLG FLPDIERIIK LIPEKRQTML FSATLPGEIV ALSRRYLTRP
     THVRAENNDA EAEATPQTTQ FVWRAHRMDK IEIVGRLLQC DGRGLTMIFC ETKRACDMVV
     EQLKERGFAA AAVHGDLGQG QREQALRAFR NGKIDVLVAT DVAARGIDVD DVTHVVNYDC
     PQDEKAYVHR IGRTGRAGKT GVAVTFVEWE DLTRWKVINN ALSLDFAEPV ETYSTSPHVF
     SDLGIPEGTK GVLPHANRSR AGLAAEEVED LGETGRVRSR GPRRGREEER DERRERPART
     PRERRRTRGG RTGADATEPV ENVREETVAE AAPVEEPRRR RSRAGRAAEE TPVPVTEQEI
     QSPVVELTEV EVDVTSRKDD NRDDQPAETA PRRGRTRKAG LNPEVSLTEG TGVQSRREPV
     AEQADRPRRR REPVAEVPQW EDESVDGHWD DEPVAEAPAP RPQPEKIIPA SPFSVIFQSP
     DLATDDDEIA PSAASERAQS RRRPPSRGQQ RGPRRPS
//
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