DDX27_DICDI
ID DDX27_DICDI Reviewed; 783 AA.
AC Q54TJ4;
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 ddx27;
DE EC=3.6.4.13;
DE AltName: Full=DEAD box protein 27;
GN Name=ddx27; ORFNames=DDB_G0281711;
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-dependent RNA helicase. Component of the
CC nucleolar ribosomal RNA (rRNA) processing machinery that may be
CC involved in ribosome biogenesis. {ECO:0000250|UniProtKB:Q96GQ7}.
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
CC {ECO:0000250|UniProtKB:Q96GQ7}. Chromosome
CC {ECO:0000250|UniProtKB:Q96GQ7}.
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 -!- DOMAIN: The C-terminal domain regulates nucleolar localization.
CC {ECO:0000250|UniProtKB:Q96GQ7}.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX27/DRS1
CC subfamily. {ECO:0000305}.
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DR EMBL; AAFI02000042; EAL66617.1; -; Genomic_DNA.
DR RefSeq; XP_640597.1; XM_635505.1.
DR AlphaFoldDB; Q54TJ4; -.
DR SMR; Q54TJ4; -.
DR STRING; 44689.DDB0234201; -.
DR PaxDb; Q54TJ4; -.
DR EnsemblProtists; EAL66617; EAL66617; DDB_G0281711.
DR GeneID; 8623207; -.
DR KEGG; ddi:DDB_G0281711; -.
DR dictyBase; DDB_G0281711; ddx27.
DR eggNOG; KOG0338; Eukaryota.
DR HOGENOM; CLU_003041_3_3_1; -.
DR InParanoid; Q54TJ4; -.
DR OMA; AAHTDIR; -.
DR PhylomeDB; Q54TJ4; -.
DR PRO; PR:Q54TJ4; -.
DR Proteomes; UP000002195; Chromosome 3.
DR GO; GO:0005694; C:chromosome; ISS:UniProtKB.
DR GO; GO:0005730; C:nucleolus; ISS:UniProtKB.
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:UniProtKB.
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 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; 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; Chromosome; Coiled coil; Helicase; Hydrolase;
KW Nucleotide-binding; Nucleus; Reference proteome; Ribosome biogenesis;
KW RNA-binding; rRNA processing.
FT CHAIN 1..783
FT /note="Probable ATP-dependent RNA helicase ddx27"
FT /id="PRO_0000327434"
FT DOMAIN 221..395
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 406..570
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 56..173
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 665..783
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 72..180
FT /evidence="ECO:0000255"
FT MOTIF 190..218
FT /note="Q motif"
FT MOTIF 343..346
FT /note="DEAD box"
FT COMPBIAS 1..18
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 73..111
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 128..148
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 156..172
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 684..740
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 761..783
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 234..241
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 783 AA; 89631 MW; E77962D2A4E71AF0 CRC64;
MLVDNQTSTT TNLVGTKRKS PENDFIMTID IAGDDDFVDD DENDDDEDLK EDFFFEESDK
PQLPWDFAPT IEKMKQQTHK KTDGQTSLED KINQRKTVKK LKADDDKSVT TKTTNNNKSK
KSNNNDNDDD DEEVNEEEEE EEEEEDNENE KEINKKQQQQ QQQSNKQTTD KIKVLQSNRK
LKKIVEEELP TFEELHLSRP LLKAVQKLGF SQPTPIQAKA IPLALNGKDI LASASTGSGK
TAAFLLPVLE RLLFRDSEYR AIRVLILLPT RELALQCQSV MENLAQFSNI TSCLIVGGLS
NKAQEVELRK SPDVVIATPG RLIDHLLNAH GIGLDDLEIL ILDEADRLLD MGFKDEINKI
VESCPTNRQT MLFSATLNDE VKTLAKLSLQ QPIRVQVDAL MQVTSTLEQE FVKIKPQHLS
DRPAILLSLC TRVFNQGGTI IFCRSKKEVH RLRIIFGLSD LKAAELHGNL SQEQRFDSLQ
QFRDGQVNYL LASDVASRGL DIIGVKTVIN YNMPNNMANY IHRVGRTARA GMDGKSCSFI
TDNDRKLLKD IVTKARNKAK SRSVSQDNVN FWRNRIEELT EDIKSIVREE MKEADLRKAE
KTLDKAEKII SNADANVETP KVWYKTKQEE DKSKELWKIE NNIVNPGKKL KAPIDVTGVN
NVPSIKKLKQ KKDPYYGLSR KQRRHRQFKE EFEREQQEER KRKGGDDGDD NEEIDSGKMF
ERSQRAQKSS GKETKRIESL RRNYMAGGAL TDQEKQRVDN KKSKKNKRMI VNKKEKKQRL
SKK
