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Database: UniProt
Entry: Q9DF35
LinkDB: Q9DF35
Original site: Q9DF35 
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   16-OCT-2019, entry version 94.
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;
OC   Amphibia; Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus;
OC   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
RT   and 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
CC       transcriptional status of both RNA polymerase (Pol) I and II:
CC       promotes ribosomal RNA (rRNA) processing and transcription from
CC       polymerase II (Pol II) (By similarity). Binds various RNAs, such
CC       as rRNAs, snoRNAs, 7SK and, at lower extent, mRNAs (By
CC       similarity). In the nucleolus, localizes to rDNA locus, where it
CC       directly binds rRNAs and snoRNAs, and promotes rRNA transcription,
CC       processing and modification (PubMed:12851405) (Probable). Required
CC       for rRNA 2'-O-methylation, possibly by promoting the recruitment
CC       of late-acting snoRNAs SNORD56 and SNORD58 with pre-ribosomal
CC       complexes (By similarity). In the nucleoplasm, binds 7SK RNA and
CC       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
CC       promoting transcription of its target genes (By similarity).
CC       {ECO:0000250|UniProtKB:Q9NR30, 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   -!- SUBCELLULAR LOCATION: Nucleus, nucleolus
CC       {ECO:0000269|PubMed:12851405}. Nucleus, nucleoplasm
CC       {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};
DR   EMBL; AF302423; AAG22819.2; -; mRNA.
DR   EMBL; BC073332; AAH73332.1; ALT_INIT; mRNA.
DR   RefSeq; NP_001082035.1; NM_001088566.1.
DR   SMR; Q9DF35; -.
DR   REBASE; 204842; Ppe194ORF77P.
DR   GeneID; 398189; -.
DR   KEGG; xla:398189; -.
DR   CTD; 398189; -.
DR   Xenbase; XB-GENE-17331446; ddx21.
DR   KO; K16911; -.
DR   OrthoDB; 1139373at2759; -.
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; IEA:UniProtKB-SubCell.
DR   GO; GO:0097322; F:7SK snRNA binding; ISS:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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:0006364; P:rRNA processing; IMP:UniProtKB.
DR   GO; GO:0006366; P:transcription by RNA polymerase II; ISS:UniProtKB.
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   InterPro; IPR014014; RNA_helicase_DEAD_Q_motif.
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; Repeat; RNA-binding; rRNA processing;
KW   Transcription.
FT   CHAIN         1    759       Nucleolar RNA helicase 2-A.
FT                                /FTId=PRO_0000432388.
FT   DOMAIN      210    389       Helicase ATP-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00541}.
FT   DOMAIN      422    566       Helicase C-terminal.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00542}.
FT   NP_BIND     223    230       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00541}.
FT   MOTIF       179    207       Q motif. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00552}.
FT   MOTIF       332    335       DEAD box. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00541}.
FT   COMPBIAS     16    148       Lys-rich. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00012}.
FT   COMPBIAS    719    759       Arg-rich. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00002}.
FT   CONFLICT     50     50       V -> I (in Ref. 2; AAH73332).
FT                                {ECO:0000305}.
FT   CONFLICT     73     73       S -> T (in Ref. 2; AAH73332).
FT                                {ECO:0000305}.
FT   CONFLICT    128    128       V -> I (in Ref. 2; AAH73332).
FT                                {ECO:0000305}.
FT   CONFLICT    171    171       D -> E (in Ref. 2; AAH73332).
FT                                {ECO:0000305}.
FT   CONFLICT    631    631       D -> V (in Ref. 2; AAH73332).
FT                                {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
//
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