DDX56_DICDI
ID DDX56_DICDI Reviewed; 685 AA.
AC Q54VF1;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Probable ATP-dependent RNA helicase ddx56;
DE EC=3.6.4.13;
DE AltName: Full=DEAD box protein 56;
GN Name=ddx56; ORFNames=DDB_G0280407;
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: May play a role in later stages of the processing of the pre-
CC ribosomal particles leading to mature 60S ribosomal subunits.
CC {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 -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX56/DBP9
CC subfamily. {ECO:0000305}.
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DR EMBL; AAFI02000036; EAL67182.1; -; Genomic_DNA.
DR RefSeq; XP_641158.1; XM_636066.1.
DR AlphaFoldDB; Q54VF1; -.
DR SMR; Q54VF1; -.
DR STRING; 44689.DDB0234216; -.
DR PaxDb; Q54VF1; -.
DR EnsemblProtists; EAL67182; EAL67182; DDB_G0280407.
DR GeneID; 8622538; -.
DR KEGG; ddi:DDB_G0280407; -.
DR dictyBase; DDB_G0280407; ddx56.
DR eggNOG; KOG0346; Eukaryota.
DR HOGENOM; CLU_003041_17_1_1; -.
DR InParanoid; Q54VF1; -.
DR OMA; GYEKDFK; -.
DR PhylomeDB; Q54VF1; -.
DR PRO; PR:Q54VF1; -.
DR Proteomes; UP000002195; Chromosome 3.
DR GO; GO:0005730; C:nucleolus; ISS:dictyBase.
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; ISS:dictyBase.
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; 2.
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 Phosphoprotein; Reference proteome; Ribosome biogenesis; RNA-binding;
KW rRNA processing.
FT CHAIN 1..685
FT /note="Probable ATP-dependent RNA helicase ddx56"
FT /id="PRO_0000327823"
FT DOMAIN 54..232
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 351..504
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 332..423
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 593..617
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 23..51
FT /note="Q motif"
FT MOTIF 180..183
FT /note="DEAD box"
FT COMPBIAS 343..406
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 407..423
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 67..74
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 685 AA; 78501 MW; 1A67959B9BCC942C CRC64;
MNLNKNNNSV EDSVSSDLID LECTFESMGL DNRILRALKK MGFQNPSLVQ SKSIPLSLQG
KDILAKARTG SGKTAAYSIP IIQKVLMAKE KSNIKGVKAV VLVPTRELCE QVKNHFNQVS
YYCQQLVSVV QLGNDKTLDE QKGLLRDIPD VIVSTPTRLV QHLENKTIQL QSTLDILVID
EADLVLNYGH QNDINIIKSF LPKVCQCFLM SATLTKEVEE LKKLVLHTPA VLKLEEDKAI
QTNLSEYSIK CAEVDKFLLV FSLLRLRLMQ GKILFFVNDT NNCYKLKLFF ERFHIKCAVL
NSELPINSRH DIILQFNKGL FDYLIATDES FKSDSNKKEE QELEDNENED DDDDDDEMTD
VKKEDDEENE DEEENDEENE EDEENEEDEE DEENEEDDDE EENEEDDDKK NKNKKINNSK
GDKEYGVARG IDFRNVDIVV NFDFPRTIKN YIHRIGRTAR GTNKGIALSF VTYHNEELLK
KVSKTRGDAG YNLKPFEFKM NAIEGFRYRV EDVLRTIGIR AIKEAKKTEL KQELLNNEKL
KSHFSENPQD LLALKHDTTL IKKQVPLHLR VVPEYLLPTQ FKNHADQKLE IIPSRPQSGH
HGTTGRSLGV NKKLEQKKRK KDILKTLSIK KNTTLTGEEL AQARSKSLIK RLKIKEGNIS
ADGSYKTVKV QKKGANNNRR KLIVD