DD21A_XENLA
ID DD21A_XENLA Reviewed; 759 AA.
AC Q9DF35; Q6GP16;
DT 04-MAR-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 2.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Nucleolar RNA helicase 2-A {ECO:0000305};
DE EC=3.6.4.13 {ECO:0000250|UniProtKB:Q9NR30};
DE AltName: Full=DEAD box protein 21-A;
DE AltName: Full=Gu-alpha-A;
DE AltName: Full=Nucleolar RNA helicase Gu-A {ECO:0000303|PubMed:12851405};
DE Short=xGu-1 {ECO:0000303|PubMed:12851405};
DE AltName: Full=Nucleolar RNA helicase II-A {ECO:0000303|PubMed:12851405};
DE AltName: Full=RH II/Gu-A {ECO:0000303|PubMed:12851405};
GN Name=ddx21-a;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Liver {ECO:0000312|EMBL:AAG22819.2};
RX PubMed=12851405; DOI=10.1074/jbc.m302258200;
RA Yang H., Zhou J., Ochs R.L., Henning D., Jin R., Valdez B.C.;
RT "Down-regulation of RNA helicase II/Gu results in the depletion of 18 and
RT 28 S rRNAs in Xenopus oocyte.";
RL J. Biol. Chem. 278:38847-38859(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 31-759.
RC TISSUE=Spleen {ECO:0000312|EMBL:AAH73332.1};
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: RNA helicase that acts as a sensor of the transcriptional
CC status of both RNA polymerase (Pol) I and II: promotes ribosomal RNA
CC (rRNA) processing and transcription from polymerase II (Pol II) (By
CC similarity). Binds various RNAs, such as rRNAs, snoRNAs, 7SK and, at
CC lower extent, mRNAs (By similarity). In the nucleolus, localizes to
CC rDNA locus, where it directly binds rRNAs and snoRNAs, and promotes
CC rRNA transcription, processing and modification (PubMed:12851405)
CC (Probable). Required for rRNA 2'-O-methylation, possibly by promoting
CC the recruitment of late-acting snoRNAs SNORD56 and SNORD58 with pre-
CC ribosomal complexes (By similarity). In the nucleoplasm, binds 7SK RNA
CC and is recruited to the promoters of Pol II-transcribed genes: acts by
CC facilitating the release of P-TEFb from inhibitory 7SK snRNP in a
CC manner that is dependent on its helicase activity, thereby promoting
CC transcription of its target genes (By similarity). Required to prevent
CC R-loop-associated DNA damage and transcription-associated genomic
CC instability (By similarity). {ECO:0000250|UniProtKB:Q9NR30,
CC ECO:0000305|PubMed:12851405}.
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:Q9NR30};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13066;
CC Evidence={ECO:0000250|UniProtKB:Q9NR30};
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:12851405}.
CC Nucleus, nucleoplasm {ECO:0000250|UniProtKB:Q9NR30}. Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:Q9JIK5}. Mitochondrion
CC {ECO:0000250|UniProtKB:Q9JIK5}.
CC -!- TISSUE SPECIFICITY: Widely expressed. Expressed at higher level in
CC stomach. Expressed at higher level compared to ddx21-b.
CC {ECO:0000269|PubMed:12851405}.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX21/DDX50
CC subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH73332.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF302423; AAG22819.2; -; mRNA.
DR EMBL; BC073332; AAH73332.1; ALT_INIT; mRNA.
DR RefSeq; NP_001082035.1; NM_001088566.1.
DR AlphaFoldDB; Q9DF35; -.
DR SMR; Q9DF35; -.
DR REBASE; 204842; Ppe194ORF77P.
DR DNASU; 398189; -.
DR GeneID; 398189; -.
DR KEGG; xla:398189; -.
DR CTD; 398189; -.
DR Xenbase; XB-GENE-17331446; ddx21.S.
DR OrthoDB; 1139373at2759; -.
DR Proteomes; UP000186698; Chromosome 7S.
DR Bgee; 398189; Expressed in lung and 19 other tissues.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; ISS:UniProtKB.
DR GO; GO:0097322; F:7SK snRNA binding; 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:0003724; F:RNA helicase activity; ISS:UniProtKB.
DR GO; GO:0019843; F:rRNA binding; ISS:UniProtKB.
DR GO; GO:0030515; F:snoRNA binding; ISS:UniProtKB.
DR GO; GO:0062176; P:R-loop disassembly; ISS:UniProtKB.
DR GO; GO:0006364; P:rRNA processing; IMP:UniProtKB.
DR GO; GO:0006366; P:transcription by RNA polymerase II; ISS:UniProtKB.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR012562; GUCT.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR035979; RBD_domain_sf.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF08152; GUCT; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF54928; SSF54928; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS51195; Q_MOTIF; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Cytoplasm; Helicase; Hydrolase; Mitochondrion;
KW Nucleotide-binding; Nucleus; Reference proteome; Repeat; RNA-binding;
KW rRNA processing; Transcription.
FT CHAIN 1..759
FT /note="Nucleolar RNA helicase 2-A"
FT /id="PRO_0000432388"
FT DOMAIN 210..389
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 422..566
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..154
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 709..759
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 179..207
FT /note="Q motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00552"
FT MOTIF 332..335
FT /note="DEAD box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT COMPBIAS 9..47
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 116..130
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 131..154
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 714..736
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 223..230
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT CONFLICT 50
FT /note="V -> I (in Ref. 2; AAH73332)"
FT /evidence="ECO:0000305"
FT CONFLICT 73
FT /note="S -> T (in Ref. 2; AAH73332)"
FT /evidence="ECO:0000305"
FT CONFLICT 128
FT /note="V -> I (in Ref. 2; AAH73332)"
FT /evidence="ECO:0000305"
FT CONFLICT 171
FT /note="D -> E (in Ref. 2; AAH73332)"
FT /evidence="ECO:0000305"
FT CONFLICT 631
FT /note="D -> V (in Ref. 2; AAH73332)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 759 AA; 84940 MW; F9278DC433C6785F CRC64;
MPVKVYAEEM EGESMKKKKL SETPLPKIKK RKMKNGDTED LDLEHMAESV NGEINNNNPT
PKLKKKKKPA PISDLSETAE ECDGEQPDPS TPTPKKVKKK KIKESKEDSD TQEEAEQSEP
QTNGVKSVKK SKKNITSDDN EPAPKKRKTD TTEITTAKEC EEKVLTKEEQ DINQEKIDGD
FSKFPLSKET IKNLQAKGVS YLFPIQSKTF HTAYSGKDVV VQARTGTGKT FSFAIPLVEK
LNEDQQPLAR GRAPRVIILT PTRELAIQIT NEIRSITKKL KVSCFYGGTP YQQQVFAIKD
GIDFLVGTPG RVRDLVQNYR LDLTTLKHVV LDEVDMMFDM GFSEQVEEIL SVRYKADPEE
NPQTLLFSAT CPDWMYNMAK KYMRKQFEKI DLIGHRSQKA ATTVEHLAIE CTRSQKAAVL
GDLVQVYSGS HGKTIIFCDS KLEAHTLATS CGSLKQSAKS LHGDLQQKER EVVLKGFRQG
TFEVLIATNV AARGLDIPEV DLVVLYSAPK EADAYVHRSG RTGRAGRTGV CISLYEPWER
HYLRNVERST GITFKRVGVP SLLNVAKSSS ADAIKSLDTV PADVIEHFKE YAQELIEQKG
ALTAIAAALA HISGATSIKQ RSLLNMEAGC DTITLKSSVP IHSLSYAWQS IKEQLGDDVD
SKIHRMCLLK DSMGVCFDVR SENLESMQER WTDTKQWQFT VATELPAIQE SERNFDGPRN
RGFGGRGRRP FDRRNNSRNS NRGGGGRGRN RNGGFRRGR
