DDX20_DANRE
ID DDX20_DANRE Reviewed; 761 AA.
AC P0C218;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Probable ATP-dependent RNA helicase DDX20;
DE EC=3.6.1.15 {ECO:0000250|UniProtKB:Q9UHI6};
DE EC=3.6.4.13 {ECO:0000250|UniProtKB:Q9UHI6};
DE AltName: Full=DEAD box protein 20;
GN Name=ddx20;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
CC -!- FUNCTION: The SMN complex catalyzes the assembly of small nuclear
CC ribonucleoproteins (snRNPs), the building blocks of the spliceosome,
CC and thereby plays an important role in the splicing of cellular pre-
CC mRNAs. Most spliceosomal snRNPs contain a common set of Sm proteins
CC SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG that assemble in
CC a heptameric protein ring on the Sm site of the small nuclear RNA to
CC form the core snRNP (Sm core). In the cytosol, the Sm proteins SNRPD1,
CC SNRPD2, SNRPE, SNRPF and SNRPG are trapped in an inactive 6S pICln-Sm
CC complex by the chaperone CLNS1A that controls the assembly of the core
CC snRNP. To assemble core snRNPs, the SMN complex accepts the trapped 5Sm
CC proteins from CLNS1A forming an intermediate. Binding of snRNA inside
CC 5Sm triggers eviction of the SMN complex, thereby allowing binding of
CC SNRPD3 and SNRPB to complete assembly of the core snRNP. May also play
CC a role in the metabolism of small nucleolar ribonucleoprotein (snoRNPs)
CC (By similarity). {ECO:0000250|UniProtKB:Q9UHI6}.
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 Evidence={ECO:0000250|UniProtKB:Q9UHI6};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13066;
CC Evidence={ECO:0000250|UniProtKB:Q9UHI6};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside 5'-
CC diphosphate + H(+) + phosphate; Xref=Rhea:RHEA:23680,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:57930, ChEBI:CHEBI:61557; EC=3.6.1.15;
CC Evidence={ECO:0000250|UniProtKB:Q9UHI6};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23681;
CC Evidence={ECO:0000250|UniProtKB:Q9UHI6};
CC -!- SUBUNIT: Part of the core SMN complex. {ECO:0000250|UniProtKB:Q9UHI6}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9UHI6}. Nucleus
CC {ECO:0000250|UniProtKB:Q9UHI6}.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX20 subfamily.
CC {ECO:0000305}.
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DR EMBL; BX664742; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; P0C218; -.
DR SMR; P0C218; -.
DR STRING; 7955.ENSDARP00000118603; -.
DR PaxDb; P0C218; -.
DR ZFIN; ZDB-GENE-030131-202; ddx20.
DR eggNOG; KOG4284; Eukaryota.
DR InParanoid; P0C218; -.
DR Reactome; R-DRE-191859; snRNP Assembly.
DR PRO; PR:P0C218; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0032797; C:SMN complex; ISS:UniProtKB.
DR GO; GO:0034719; C:SMN-Sm protein complex; 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:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0003724; F:RNA helicase activity; IBA:GO_Central.
DR GO; GO:0000387; P:spliceosomal snRNP assembly; 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; 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; Cytoplasm; DNA-binding; Helicase; Hydrolase; mRNA processing;
KW mRNA splicing; Nucleotide-binding; Nucleus; Reference proteome.
FT CHAIN 1..761
FT /note="Probable ATP-dependent RNA helicase DDX20"
FT /id="PRO_0000259533"
FT DOMAIN 57..231
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 266..415
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 428..525
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 570..720
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 26..54
FT /note="Q motif"
FT MOTIF 175..178
FT /note="DEAD box"
FT COMPBIAS 428..452
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 453..469
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 494..518
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 584..637
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 647..681
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 684..702
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 48
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 53
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 70..77
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT BINDING 73..78
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 761 AA; 85002 MW; 88042E764886AB78 CRC64;
MAASVKAAHE LQSRTRTDDV LISGGVEFSS LLLSKPVLEG LSASGFQRPS PIQLKAIPLG
RCGLDLIVQA KSGTGKTCVF TTIALDSLIL ENATTQVLVL APTREIAVQI HAVVMAIGSA
MEGLECHVFI GGRPISQDKQ HLKKCHIAIG SPGRIKQLIE MGALMVSSIR LFVLDEADKL
LEDDSSSSFQ EQINWIYSSL PANKQMLALS ATYPESLAQQ LSRYMREPTF VRLNPTDPGL
LGLKQYYKIV PSHSLPHKVF EEKVQSLLEL FSKIPFNQAL VFSNLHTRAQ HLADILSSKG
LPAVCISGGL SQDQRLEAMW KLKQYQCRVL ISTDLTSRGI DAEKVNLVIN LDVPQDWETY
MHRIGRAGRF GTLGVAVTYC CHGEEENKMM AIAQKCSLDL MHLPDPIPPG IMEEACDHDV
IIETLSKPKI PDNFKPEKKK KAKSEQMKSK PSRESHISVV ITESVTGDKS CSRAETKTKN
HSPKPGRQKQ MAPAANLQHD STITQKQQNN TLPKIPPLSS FKSHTGKRMT FDDALVDYET
FIREGPGRSV EIIHQYDGFY RSQDKVNGLH DAHDEDEASE SYVLEESQSH QDLPPAQEVS
ELSSEQKTSS ESSSESEMEV ESESSSSVPS KSTLEALPDN KVSLVRNHSE LAKSTLPSTR
VPQQATRSKQ KPCQPQSQDT AHHHNLPHKH RTASKSSRRP TGPKRRTRET DETEEEEAGQ
DYWSSYRAWA EYYNSYYHHS PYNWMTAFYM NSVYIKEMMK H
