DDX46_DANRE
ID DDX46_DANRE Reviewed; 1018 AA.
AC Q4TVV3;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Probable ATP-dependent RNA helicase DDX46;
DE EC=3.6.4.13;
DE AltName: Full=DEAD box protein 46;
GN Name=ddx46;
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 [MRNA].
RA Amsterdam A., Hopkins N.;
RT "The Danio rerio ddx46 gene.";
RL Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Plays an essential role in splicing, either prior to, or
CC during A complex formation. {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 -!- SUBUNIT: Integral component of the 17S U2 snRNP. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000250}. Nucleus, Cajal
CC body {ECO:0000250}. Note=Present in Cajal bodies (CBs) and nuclear
CC speckles. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX46/PRP5
CC subfamily. {ECO:0000305}.
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DR EMBL; DQ054379; AAY46301.1; -; mRNA.
DR RefSeq; NP_001019988.1; NM_001024817.1.
DR AlphaFoldDB; Q4TVV3; -.
DR SMR; Q4TVV3; -.
DR STRING; 7955.ENSDARP00000129124; -.
DR PaxDb; Q4TVV3; -.
DR GeneID; 321948; -.
DR KEGG; dre:321948; -.
DR CTD; 9879; -.
DR ZFIN; ZDB-GENE-030131-667; ddx46.
DR eggNOG; KOG0334; Eukaryota.
DR InParanoid; Q4TVV3; -.
DR Reactome; R-DRE-72163; mRNA Splicing - Major Pathway.
DR PRO; PR:Q4TVV3; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
DR GO; GO:0015030; C:Cajal body; IEA:UniProtKB-SubCell.
DR GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; 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:0007420; P:brain development; IMP:ZFIN.
DR GO; GO:0060216; P:definitive hemopoiesis; IMP:ZFIN.
DR GO; GO:0048546; P:digestive tract morphogenesis; IMP:ZFIN.
DR GO; GO:0031017; P:exocrine pancreas development; IMP:ZFIN.
DR GO; GO:0072576; P:liver morphogenesis; IMP:ZFIN.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IMP:ZFIN.
DR GO; GO:0045648; P:positive regulation of erythrocyte differentiation; IMP:ZFIN.
DR GO; GO:1902038; P:positive regulation of hematopoietic stem cell differentiation; IMP:ZFIN.
DR GO; GO:0045621; P:positive regulation of lymphocyte differentiation; IMP:ZFIN.
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 2: Evidence at transcript level;
KW ATP-binding; Coiled coil; Helicase; Hydrolase; mRNA processing;
KW mRNA splicing; Nucleotide-binding; Nucleus; Reference proteome;
KW RNA-binding.
FT CHAIN 1..1018
FT /note="Probable ATP-dependent RNA helicase DDX46"
FT /id="PRO_0000055125"
FT DOMAIN 371..549
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 560..721
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..200
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 900..927
FT /evidence="ECO:0000255"
FT MOTIF 340..368
FT /note="Q motif"
FT MOTIF 497..500
FT /note="DEAD box"
FT COMPBIAS 24..43
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 44..86
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 87..112
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 123..172
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 173..200
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 384..391
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 1018 AA; 115140 MW; A4A7F8B1AF8C2F5C CRC64;
MGRESRHYRK RSSSRGRSGS LSKSRSPDSK RSKKDDRTAS RTHSRRERSR SRERRRSRER
KRQRRSSRDR RRSRSRERRR SKSRSRGRSK EKPENGDQTA DKKKIKEEKE EEKPEDQDFD
QNTLEEEMRK RKERVEKWRE EQRKTAMENI GEIKKELEEM KQGKKWSLED DDEEQDKAAE
AEESERMEEE EVGEEVDPLD AYMEEVKEEV KKFNMGTMKG ANDKKGGMSV TKVVTVVKTK
KMPHATKKKG ELMENDQDAM EYSSEEEEVD LQTALTGFQT KQRKVLEPVD HQKIQYEPFR
KNFYVEVPEL ARMSPEEVSE YRLELEGISV KGKGCPKPIK TWVQCGISMK VLNALKKHNY
EKPTPIQAQA IPAIMSGRDL IGIAKTGSGK TIAFLLPMFR HILDQRPVGE AEGPLAVIMT
PTRELALQIT KECKKFSKSL ALRVVCVYGG TGISEQIAEL KRGAEIIVCT PGRMIDMLGA
NNGRVTNLRR VTYVVIDEAD RMFDMGFEPQ VMRIVDNVRP DRQTVMFSAT FPRTMEALAR
RILSKPVEVQ VGGRSVVCSD VEQHVIVIEE EKKFLKLLEI LGHYQEKGSV IIFVDKQEHA
DGLLKDLMKA SYPCMSLHGG IDQYDRDSII NDFKNGACRL LVATSVAARG LDVKQLILVV
NYSCPNHYED YVHRAGRTGR AGNKGYAYTF ITEGQARYSG DILKALELSG SSVPAELEQL
WTNFKEQQKA EGKIIKSSSG FSGKGFKFDE TEHALANERK KLQKWALGLH DSDDEDTALD
IDEQIESMFN SKKRVKDFSA PGSVSAGSAG GVSGSVSAVS GLGSLSTPSA GNIQKLEIAK
KLALRIQAQK NLGAEAQDVM QQATNAILRG GTIIAPSVSA KTIAEQQAEK INAKLNYTPV
EKLEEERQAA EAAETVKRYE EELEINDFPQ TARWKVTSKE ALQRIGEYSE AAITIRGTYF
PPGKEPKEGE RKIYLAIESA NELAVQKAKA EITRLIKEEL IRLQNSYQPT SKGRYKVL
