ID F0Z9N9_DICPU Unreviewed; 593 AA.
AC F0Z9N9;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE RecName: Full=RNA helicase {ECO:0000256|ARBA:ARBA00012552};
DE EC=3.6.4.13 {ECO:0000256|ARBA:ARBA00012552};
GN ORFNames=DICPUDRAFT_27074 {ECO:0000313|EMBL:EGC39333.1};
OS Dictyostelium purpureum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=5786 {ECO:0000313|EMBL:EGC39333.1, ECO:0000313|Proteomes:UP000001064};
RN [1] {ECO:0000313|Proteomes:UP000001064}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=QSDP1 {ECO:0000313|Proteomes:UP000001064};
RX PubMed=21356102; DOI=10.1186/gb-2011-12-2-r20;
RG US DOE Joint Genome Institute (JGI-PGF);
RA Sucgang R., Kuo A., Tian X., Salerno W., Parikh A., Feasley C.L., Dalin E.,
RA Tu H., Huang E., Barry K., Lindquist E., Shapiro H., Bruce D., Schmutz J.,
RA Salamov A., Fey P., Gaudet P., Anjard C., Babu M.M., Basu S.,
RA Bushmanova Y., van der Wel H., Katoh-Kurasawa M., Dinh C., Coutinho P.M.,
RA Saito T., Elias M., Schaap P., Kay R.R., Henrissat B., Eichinger L.,
RA Rivero F., Putnam N.H., West C.M., Loomis W.F., Chisholm R.L., Shaulsky G.,
RA Strassmann J.E., Queller D.C., Kuspa A., Grigoriev I.V.;
RT "Comparative genomics of the social amoebae Dictyostelium discoideum and
RT Dictyostelium purpureum.";
RL Genome Biol. 12:R20.1-R20.23(2011).
CC -!- SIMILARITY: Belongs to the DEAD box helicase family.
CC {ECO:0000256|RuleBase:RU000492}.
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DR EMBL; GL870959; EGC39333.1; -; Genomic_DNA.
DR RefSeq; XP_003284121.1; XM_003284073.1.
DR AlphaFoldDB; F0Z9N9; -.
DR STRING; 5786.F0Z9N9; -.
DR EnsemblProtists; EGC39333; EGC39333; DICPUDRAFT_27074.
DR GeneID; 10510026; -.
DR KEGG; dpp:DICPUDRAFT_27074; -.
DR eggNOG; KOG0331; Eukaryota.
DR InParanoid; F0Z9N9; -.
DR OMA; PKQDFRN; -.
DR OrthoDB; 5477821at2759; -.
DR Proteomes; UP000001064; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:1990904; C:ribonucleoprotein complex; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0003724; F:RNA helicase activity; IBA:GO_Central.
DR GO; GO:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; IEA:UniProtKB-KW.
DR CDD; cd17966; DEADc_DDX5_DDX17; 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; PTHR47958; ATP-DEPENDENT RNA HELICASE DBP3; 1.
DR PANTHER; PTHR47958:SF150; RNA HELICASE; 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; 2.
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:UP000001064}.
FT DOMAIN 219..247
FT /note="DEAD-box RNA helicase Q"
FT /evidence="ECO:0000259|PROSITE:PS51195"
FT DOMAIN 250..425
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 450..593
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..133
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 219..247
FT /note="Q motif"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00552"
FT COMPBIAS 1..38
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 51..67
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 68..94
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 95..133
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 593 AA; 65825 MW; 3F701D16F74DA603 CRC64;
MSYSNSNNRG DSSSSGFSDS RGGGGDYKPS SSSSGGGYRR YDDNRGGSGD SRDYKSSYNS
GRSGGDRNSS YNKDRTYNKD NRDYKKDSGS KDYKSRDYNG NSGGGNRDYR NNSNGYNNSG
SSNNNSNGYN KGSIGYAQNN SGYVGKNSYG YNNSNNTKND QFGSALTDLK WDLSKLQRFE
KNFYHENEEL TRTSDEEIEE FRESCMMTVK GRDIPKPIIH FNQAPFPNYL MKEIMAAGFP
NPTPIQSQAW PIALKGRDII GLAKTGSGKT LAFLLPSIVH INAQPTLKPG DGPIVLVLAP
TRELALQIQE QARKFGGTSQ ISNVCVYGGA SKHSQVMMLK KGVEIVIATP GRLIDILTSG
DTNLRRVTYL VLDEADRMLD MGFEPQIRKI LSQIRPDRQT LMFSATWPKE VQSLANDFLS
DHIQVHIGSS ELTANHNVNQ IVEVCSEYEK KERLFKFLEA NVSKDDKVII FAETRKGVDE
LHRSLQSAGF KSIGIHGNKS QPERDFVLSQ FKNGIFPIMI ATDLASRGLD VKDIKFVVNY
DFPNTIETYV HRIGRTARAG ATGTSISFLT RENARLANDL IKVLSEAKQI YSS
//
