DDX55_DICDI
ID DDX55_DICDI Reviewed; 663 AA.
AC Q54EC2;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Probable ATP-dependent RNA helicase ddx55;
DE EC=3.6.4.13;
DE AltName: Full=DEAD box protein 55;
GN Name=ddx55; ORFNames=DDB_G0291588;
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. DDX55/SPB4
CC subfamily. {ECO:0000305}.
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DR EMBL; AAFI02000177; EAL61778.1; -; Genomic_DNA.
DR RefSeq; XP_635318.1; XM_630226.1.
DR AlphaFoldDB; Q54EC2; -.
DR SMR; Q54EC2; -.
DR STRING; 44689.DDB0234215; -.
DR PaxDb; Q54EC2; -.
DR PRIDE; Q54EC2; -.
DR EnsemblProtists; EAL61778; EAL61778; DDB_G0291588.
DR GeneID; 8628262; -.
DR KEGG; ddi:DDB_G0291588; -.
DR dictyBase; DDB_G0291588; ddx55.
DR eggNOG; KOG0345; Eukaryota.
DR HOGENOM; CLU_003041_26_4_1; -.
DR InParanoid; Q54EC2; -.
DR OMA; IQFEDHM; -.
DR PhylomeDB; Q54EC2; -.
DR PRO; PR:Q54EC2; -.
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; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR025313; DUF4217.
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; 2.
DR Pfam; PF13959; DUF4217; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM01178; DUF4217; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; SSF52540; 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; Coiled coil; Helicase; Hydrolase; Nucleotide-binding; Nucleus;
KW Reference proteome; Ribosome biogenesis; RNA-binding; rRNA processing.
FT CHAIN 1..663
FT /note="Probable ATP-dependent RNA helicase ddx55"
FT /id="PRO_0000327416"
FT DOMAIN 41..266
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 297..457
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 556..663
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 531..658
FT /evidence="ECO:0000255"
FT MOTIF 10..38
FT /note="Q motif"
FT MOTIF 214..217
FT /note="DEAD box"
FT COMPBIAS 556..581
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 594..623
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 646..663
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 54..61
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 663 AA; 76590 MW; FE9051DCFA4B4683 CRC64;
MTSKVDTGGW NKLENKLSDS TLNTINRLGF KSMSPVQSAV IPLFMSNKDV LVEACTGSGK
TLAFVIPIIE KILKRETNLK KTDIASIIIS PTRELAIQIQ QVLLEFLNDL NRIDDQNDLE
NIKTLEDELL EEQEEEENEK EEEEIEKKKK KKKIEISSLL LIGGTDIYQD LVNYKNYGGN
ILIGTPGRTD EFLTRVVRND QQFKFKEFEM LILDEADRLL DMGFHLPINS ILLKLPKQRR
TGLFSATQTS EVKELARTGM RNPFKVSVSV KHIETHEDQS IPTTLDNRYM IVPVEERLNQ
LVHFLLNHID KNKIIIYFLT CSTVDYFFKI LQSVKVLSGK PFFSLHGKAP HSQRIKVFDS
FSQATNGCLL STDLAARGLD IPNVDWVLQY DSPQDPKAFV HRIGRTARMG RDGNALIFLS
PEEDSYIEFL KIKKVPLVEM VKAENVTNVL PEIKKISFND REIMEKGVIA MVSHVRGYKE
HLCPYIFVFH RLNIGLLATG FGLLYLPRMP EIRDKTLIAE WTSGYTKDQI LKIAYKEKKK
EKQRLEKVNK IKLKKEKDAK ERQDAINEKK RKLEQQEADK LLQKQQPKQS SIEIQLKKQE
EKKKQEQESI NEILHETQAF KKARKSKQQK KDKSSRFSDL MGSDTEQNNN EDEEDEEEED
EDN
