DDX42_CHICK
ID DDX42_CHICK Reviewed; 944 AA.
AC Q5F485;
DT 06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=ATP-dependent RNA helicase DDX42;
DE EC=3.6.4.13 {ECO:0000250|UniProtKB:Q86XP3};
DE AltName: Full=DEAD box protein 42;
GN Name=DDX42; ORFNames=RCJMB04_2e15 {ECO:0000303|PubMed:15642098};
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=CB; TISSUE=Bursa of Fabricius;
RX PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA Hayashizaki Y., Buerstedde J.-M.;
RT "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT function analysis.";
RL Genome Biol. 6:R6.1-R6.9(2005).
CC -!- FUNCTION: ATP-dependent RNA helicase. Binds to partially double-
CC stranded RNAs (dsRNAs) in order to unwind RNA secondary structures.
CC Unwinding is promoted in the presence of single-strand binding
CC proteins. Mediates also RNA duplex formation thereby displacing the
CC single-strand RNA binding protein. ATP and ADP modulate its activity:
CC ATP binding and hydrolysis by DDX42 triggers RNA strand separation,
CC whereas the ADP-bound form of the protein triggers annealing of
CC complementary RNA strands. {ECO:0000250|UniProtKB:Q86XP3}.
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:Q86XP3};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q86XP3}. Nucleus
CC {ECO:0000250|UniProtKB:Q86XP3}.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX42 subfamily.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AJ851415; CAH65049.1; -; mRNA.
DR RefSeq; NP_001026097.1; NM_001030926.1.
DR AlphaFoldDB; Q5F485; -.
DR SMR; Q5F485; -.
DR STRING; 9031.ENSGALP00000000810; -.
DR PaxDb; Q5F485; -.
DR GeneID; 419959; -.
DR KEGG; gga:419959; -.
DR CTD; 11325; -.
DR VEuPathDB; HostDB:geneid_419959; -.
DR eggNOG; KOG0339; Eukaryota.
DR InParanoid; Q5F485; -.
DR OrthoDB; 245118at2759; -.
DR PhylomeDB; Q5F485; -.
DR PRO; PR:Q5F485; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; 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:0008104; P:protein localization; ISS:UniProtKB.
DR GO; GO:0042981; P:regulation of apoptotic process; 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 2: Evidence at transcript level;
KW ATP-binding; Coiled coil; Cytoplasm; Helicase; Hydrolase;
KW Nucleotide-binding; Nucleus; Reference proteome; RNA-binding.
FT CHAIN 1..944
FT /note="ATP-dependent RNA helicase DDX42"
FT /id="PRO_0000280061"
FT DOMAIN 284..459
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 487..632
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..119
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 131..155
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 182..203
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 642..682
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 723..753
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 794..944
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 120..157
FT /evidence="ECO:0000255"
FT MOTIF 253..281
FT /note="Q motif"
FT MOTIF 407..410
FT /note="DEAD box"
FT COMPBIAS 89..105
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 131..150
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 829..887
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 889..903
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 904..944
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 297..304
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 944 AA; 103054 MW; 0F4ACAC306DC7150 CRC64;
MNWNKGGPGT KRGFGFGGFA ITPGKKEEPK LSQQSHSAFG TAGSSAAFAK SGPPQLPSFY
KIGSKRANFD EENAYFEDEE EDNSNVDLPY IPAENSPTRQ QFNSKSADSD SDDDPLEAFM
AEVEDQAARD MKRLEDKDKE KKNAKGIRDD IEEEDDQEAY FRYMAENPTA GVVQEEEEDN
LEYDSDGNPI APSKKIIDPL PPIDHSEIEY PPFEKNFYDE HEEITSLTPQ QVVELRHKLN
LRVSGAAPPR PGSSFARFGF DEQLMHQIRK SEYTQPTPIQ CQGVPVAMSG RDMIGIAKTG
SGKTAAFIWP MLIHIMDQKE LEPGDGPIAV IVCPTRELCQ QIHSECKRFG KAYNLRSVAV
YGGGSMWEQA KALQEGAEIV VCTPGRLIDH VKKKATNLQR VTYLVFDEAD RMFDMGFEYQ
VRSIASHVRP DRQTLLFSAT FRKKIEKLAR DILIDPIRVV QGDIGEANED VTQIVEIFPS
GPSKWNWLTR RLVEFTSSGS VLLFVTKKAN AEELANNLKQ EDHNLGLLHG DMDQSERNKV
ISEFKKKGIP ILVATDVAAR GLDIPSIKTV INYDVARDID THTHRIGRTG RAGEKGVAYT
LLTPKDSNFA GDLVRNLEGA NQHVSKELLD LAMQNPWFRK SRFKGGKGKK PNIGGGGLGY
RERPGLGSES SDRGNNNSVM SNYEAYKPSS GAMGDRLTAM KAAFQSQYKS HFVAASLNNQ
KTGSSAAGAS GWTSAGSLNS VPTSSAQQNA ANPDSPIAAT AAAKGVPGFT STGTLSSVPT
FPSVGVQGYS NNSSANASAG NREGVGSAGS APRGGSSGGG GGGIVRERYS DNRNSRHNEV
PRRGEGGGRY NDVQHHGEGG GRYSDAYRHG EGRHGDSHRH AEGRHFTDTG GGNRNNVDGR
NISEGRSNES RNGENRKDAN SRDNKTDGFA VPEPPKRKKS RWDS
