DDX51_DICDI
ID DDX51_DICDI Reviewed; 563 AA.
AC Q54BD6;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Probable ATP-dependent RNA helicase ddx51;
DE EC=3.6.4.13;
DE AltName: Full=DEAD box protein 51;
GN Name=ddx51; ORFNames=DDB_G0293740;
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: Probable ATP-binding RNA helicase which may be involved in
CC ribosome biogenesis. {ECO:0000250}.
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 -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250}.
CC -!- DOMAIN: The Q motif is unique to and characteristic of the DEAD box
CC family of RNA helicases and controls ATP binding and hydrolysis.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX51/DBP6
CC subfamily. {ECO:0000305}.
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DR EMBL; AAFI02000218; EAL60682.1; -; Genomic_DNA.
DR RefSeq; XP_629093.1; XM_629091.1.
DR AlphaFoldDB; Q54BD6; -.
DR SMR; Q54BD6; -.
DR STRING; 44689.DDB0234210; -.
DR PaxDb; Q54BD6; -.
DR EnsemblProtists; EAL60682; EAL60682; DDB_G0293740.
DR GeneID; 8629386; -.
DR KEGG; ddi:DDB_G0293740; -.
DR dictyBase; DDB_G0293740; ddx51.
DR eggNOG; KOG0350; Eukaryota.
DR HOGENOM; CLU_003041_15_3_1; -.
DR InParanoid; Q54BD6; -.
DR OMA; TEQYCVT; -.
DR PhylomeDB; Q54BD6; -.
DR PRO; PR:Q54BD6; -.
DR Proteomes; UP000002195; Chromosome 6.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; 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 GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-KW.
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; IPR000629; RNA-helicase_DEAD-box_CS.
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; 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; Helicase; Hydrolase; Nucleotide-binding; Nucleus;
KW Reference proteome; Ribosome biogenesis; RNA-binding; rRNA processing.
FT CHAIN 1..563
FT /note="Probable ATP-dependent RNA helicase ddx51"
FT /id="PRO_0000327415"
FT DOMAIN 48..276
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 308..482
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 493..537
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 15..43
FT /note="Q motif"
FT MOTIF 179..182
FT /note="DEAD box"
FT COMPBIAS 507..536
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 61..68
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 563 AA; 64642 MW; 7856633C3EAD037E CRC64;
MTTINYNENI NNNNNTLESF GIEEWLINNL KEQSIINLFP VQQEIVPFIN RTEGHDICVC
APTGSGKTLA YAIPLVQKIV KRVVRRVRVA VIVPTHDLVI QVEKTFQSII KGTDLVVLSL
GVKPFHIEQK LLIKNHSYGE HALYESLVDI IVSTPGRIVD HINETLGFTL KYLNYLVIDE
ADRLLRQSFQ DWLEIVIDST NQHSDLNQQQ EEQLIKYNSK GDIELFEKSI SLKDNNNQMN
HLCWSEFKLV KLLLSATMTY NPSKISLLQL NAPLFFTTSK TKEIKYSMPS TLKECYIISN
GDQKPLVLLN IIYESLLKNN ANGENKKKII CFTKSVDITH RLNTLLKLIG QVDKLKFTCE
EYSSSLSTVE RADLLSRFKL NQIDILICSD IMSRGMDIQD IDVVINYNTP PNITLYVHRV
GRTARAGNFG VSYTIVDKSE IKYYISMMKK AERSQTLHCL KWKPNVYEKF QSSYKLGLNQ
MRLIYSKRKI NDIGDNGDDN NDNNNEDGNE IDGSVENIEN NNNNNNNNNK NNNNNNFEKD
YEVKLKHSLL EISKKKAKIN FNI
