ID DDX54_DICDI Reviewed; 1091 AA.
AC Q54CD8; Q23908;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 24-JAN-2024, entry version 114.
DE RecName: Full=ATP-dependent RNA helicase ddx54;
DE EC=3.6.4.13;
DE AltName: Full=ATP-dependent RNA helicase helA;
DE AltName: Full=DEAD box protein 54;
GN Name=helA; Synonyms=ddx54; ORFNames=DDB_G0292992;
OS Dictyostelium discoideum (Social amoeba).
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).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 277-374.
RC STRAIN=AX2;
RX PubMed=7695838; DOI=10.1515/bchm3.1994.375.11.759;
RA Mahal B., Nellen W.;
RT "Developmental regulation of DEAD box proteins and cloning of putative RNA
RT helicase genes from Dictyostelium discoideum.";
RL Biol. Chem. Hoppe-Seyler 375:759-763(1994).
CC -!- FUNCTION: ATP-binding RNA helicase which may be involved in the
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. DDX54/DBP10
CC subfamily. {ECO:0000305}.
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DR EMBL; AAFI02000199; EAL60848.1; -; Genomic_DNA.
DR EMBL; X81822; CAA57416.1; -; Genomic_DNA.
DR RefSeq; XP_629281.1; XM_629279.1.
DR AlphaFoldDB; Q54CD8; -.
DR SMR; Q54CD8; -.
DR STRING; 44689.Q54CD8; -.
DR PaxDb; 44689-DDB0215372; -.
DR EnsemblProtists; EAL60848; EAL60848; DDB_G0292992.
DR GeneID; 8629004; -.
DR KEGG; ddi:DDB_G0292992; -.
DR dictyBase; DDB_G0292992; helA.
DR eggNOG; KOG0337; Eukaryota.
DR HOGENOM; CLU_003041_5_2_1; -.
DR InParanoid; Q54CD8; -.
DR OMA; EDQFGMM; -.
DR PhylomeDB; Q54CD8; -.
DR PRO; PR:Q54CD8; -.
DR Proteomes; UP000002195; Chromosome 6.
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 GO; GO:0006364; P:rRNA processing; IBA:GO_Central.
DR CDD; cd17959; DEADc_DDX54; 1.
DR CDD; cd18787; SF2_C_DEAD; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR012541; DBP10_C.
DR InterPro; IPR033517; DDX54/DBP10_DEAD-box_helicase.
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; PTHR47959; ATP-DEPENDENT RNA HELICASE RHLE-RELATED; 1.
DR PANTHER; PTHR47959:SF8; RNA HELICASE; 1.
DR Pfam; PF08147; DBP10CT; 1.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR SMART; SM01123; DBP10CT; 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; Helicase; Hydrolase; Nucleotide-binding; Nucleus;
KW Reference proteome; Ribosome biogenesis; RNA-binding; rRNA processing.
FT CHAIN 1..1091
FT /note="ATP-dependent RNA helicase ddx54"
FT /id="PRO_0000327438"
FT DOMAIN 261..433
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 478..632
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..63
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 150..231
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 801..896
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 933..1091
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 230..258
FT /note="Q motif"
FT MOTIF 381..384
FT /note="DEAD box"
FT COMPBIAS 13..36
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 37..52
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 169..231
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 807..823
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 824..853
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 854..882
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 933..994
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1004..1056
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 274..281
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT CONFLICT 344..345
FT /note="FT -> LH (in Ref. 2; CAA57416)"
FT /evidence="ECO:0000305"
FT CONFLICT 350
FT /note="N -> Y (in Ref. 2; CAA57416)"
FT /evidence="ECO:0000305"
FT CONFLICT 355
FT /note="I -> L (in Ref. 2; CAA57416)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1091 AA; 125085 MW; 23F859D1A9D1D231 CRC64;
MVKPNNVKIK NKGNLKKSNE SQNDYMKGKK LETKSYQKAL LSKNSNNNND GAQAKRLKKK
EEFKKKLEKR QNTIVIKDKL KEPSTFLKED QSFFDQNIFN DQDDYKHQQM NRININENFE
TNLFGDMMNE FDGDLNEDLD LLDYNDEVID NSNFDNNGDQ FNSEDEEFYD DEKQAKKSNK
NKNADADNKK SKKSNKKEEI ESSEKFESFP MDENNEQEEE TTSKKKKKTG GFQSMDLTKN
LLKAILKKGF NVPTPIQRKS IPMILDGHDI VGMARTGSGK TGAFVIPMIQ KLGDHSTTVG
VRAVILSPTR ELAIQTFKVV KDFSQGTQLR TILIVGGDSM EDQFTDLARN PDIIIATPGR
LMHHLLETGM SLSKVQYIVF DEADRLFEMG FNEQLTEILS KLSENRQTLL FSATLPSLLV
DFVRAGLNNP KLINLDTDTK ISENLSLSFF TLRHEEKLGV LLFLLKDIIY KKPQLPTTET
TTTTTTNNES NQQQQKKSST IIFVSTKYHV EFIHILLERA GIASTYIHGY LDPVARKINL
AKFRSHQVGV MVVTDLAARG IDIPLLDNVI NFDFPPKEKI FIHRVGRVAR AGRSGIAYSL
VSPDEVPYMI DLHLYLGRKF LNKFQYEGQT INDPKYSFYG TIPQTIIDRE TEFVNVQRKE
CIELLSLTKT IHNAHKKYLS TRPGASHESN RRAKLMDKSK YHPMLSDHLN SNDQIRNDFI
QSLKSFRPPQ TVLELDARKN NVQVSIMKDK RKVHTNVIES QQKKLYLQQS ETNLGPENEE
FDYSKLDTRK RLLQLTENIT EEMLRSNKSN DNNDNNKDIK MNENDDENDD DDEEGENDDD
EEEENEKDED DEEDENKNKF NIKIESSDKN DNNKKKLKSR SSSRDPNFFI SATPENLIQE
RAMSISNRFT KDDEVNLVAD TDRKQKKSMV WDKRKGKFVS SQADADRKNS KKLVRNEAGK
LVEAKKSHKG YEEWKKKTHG RIQRVGEDEN SKYQPNQKEY LPQKWRGQGR EKEKKDNKAS
HAKGSHGLKG RPSELKDKNQ ISKNRSEKER KMRVNKTKGN PKGSKSKSGG GGGGKGSKFG
SGKSKGGKSR K
//
