DDX24_DICDI
ID DDX24_DICDI Reviewed; 940 AA.
AC Q54TD7;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=ATP-dependent RNA helicase ddx24;
DE EC=3.6.4.13;
DE AltName: Full=DEAD box protein 24;
GN Name=ddx24; ORFNames=DDB_G0281841;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
CC -!- FUNCTION: ATP-dependent RNA helicase. {ECO:0000305}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13;
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX24/MAK5
CC subfamily. {ECO:0000305}.
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DR EMBL; AAFI02000043; EAL66480.1; -; Genomic_DNA.
DR RefSeq; XP_640452.1; XM_635360.1.
DR AlphaFoldDB; Q54TD7; -.
DR SMR; Q54TD7; -.
DR STRING; 44689.DDB0234200; -.
DR PaxDb; Q54TD7; -.
DR PRIDE; Q54TD7; -.
DR EnsemblProtists; EAL66480; EAL66480; DDB_G0281841.
DR GeneID; 8623265; -.
DR KEGG; ddi:DDB_G0281841; -.
DR dictyBase; DDB_G0281841; ddx24.
DR eggNOG; KOG0347; Eukaryota.
DR HOGENOM; CLU_003041_13_1_1; -.
DR InParanoid; Q54TD7; -.
DR OMA; HYHVPRT; -.
DR PhylomeDB; Q54TD7; -.
DR PRO; PR:Q54TD7; -.
DR Proteomes; UP000002195; Chromosome 3.
DR GO; GO:0005730; C:nucleolus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR Gene3D; 3.40.50.300; -; 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 Pfam; PF00270; DEAD; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; SSF52540; 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; Coiled coil; Helicase; Hydrolase; Nucleotide-binding;
KW Reference proteome; RNA-binding.
FT CHAIN 1..940
FT /note="ATP-dependent RNA helicase ddx24"
FT /id="PRO_0000327813"
FT DOMAIN 326..607
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 650..797
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 50..243
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 364..398
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 517..556
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 42..66
FT /evidence="ECO:0000255"
FT MOTIF 294..322
FT /note="Q motif"
FT MOTIF 488..491
FT /note="DEAD box"
FT COMPBIAS 50..67
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 68..86
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 117..132
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 179..196
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 222..237
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 364..379
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 380..396
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 517..553
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 339..346
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 940 AA; 109176 MW; 17A5C2AF630C0B26 CRC64;
MAKKKFVENT NWKKIDTDNQ LIFEQGGFLG LEEIDPNDYF LTDKNVDKIE KQQKQKQKQE
QEQEQKPTNK LTTKSTTKST PVQNKNQKPV DKKRKSKKGN DDSDNEYSGY QDDSDQDDEY
SAAKKKPRII KPTETVDMGT ELLNSFVEGT VHNKKKQRKG IKVKQIIDDN DNDFEDEEEE
VKPQQKLQKQ KQQEQKQKQP QKQPQQPNKK NNKKELQKEE EEQMEEEKEE EEVQQEEEEE
KEIKKPIKEK KVKTQKQIEA AKKNINKLEK IKKRKEISEQ KTISKEEQDQ LDMSEWNSYN
LDPLILKGLR SLGFSKPTEI QSSVIPVAVS SGYDVIGAAQ TGSGKTLAFG IPMVQRILQH
LRKHGQNVEN KANKQQNDND DENEDVEEEE EEEEEEGRSK EYRKLFSLVI CPTRELAIQV
TNHIKSIISH TNLKVISIVG GMASQRQQRV LSKRPEIVVA TPGRLWELIT EGHQHLVELE
SLLCLGIDEA DRMVEQGHFA ELESILKTLP IHRTAMSKKE RLKKKETEEK RNKRRKVDKL
NDKGEMIKGD QDDMDDQIPD EEMEELEQEE QNHLTTTHKR QTFVFSATLV NIPGDGAPTS
QKKKYRKLTP IENLIEKVRF QRDYKLIDVT QKRLTAKNLL ETKIFCNLEE KDMYLYYFVE
RYPGRTLVFV NSIDCARRLI PIFNILEVPV FALHAQMQQK QRLKNLDRFR TLDNVVLIAT
DVAARGLDIP LVQHVIHYQV PRTTQLYIHR SGRTARSDQD GISVVLVTPK ERPLYIKLDS
SIEHDIGNFP TDIRYMEGVR DRIELAKEID KLSHQSLKDN REKSWFKKQA EEMDIELDGD
FFGENSDDEQ SEDTRIAEQK KQFKLKQLRA QLKHLLSRSL LPRGVSQSYI TASAIQELES
KSQSSAATDF SNKAKNVIGK KAKQLAIENH SKFLTKNKKK
