DX39B_CHICK
ID DX39B_CHICK Reviewed; 428 AA.
AC Q5ZHZ0;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 80.
DE RecName: Full=Spliceosome RNA helicase DDX39B;
DE EC=3.6.4.13;
DE AltName: Full=56 kDa U2AF65-associated protein;
DE AltName: Full=DEAD box protein UAP56;
GN Name=DDX39B; Synonyms=BAT1, UAP56; ORFNames=RCJMB04_32b9;
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: Involved in nuclear export of spliced and unspliced mRNA.
CC Assembling component of the TREX complex which is thought to couple
CC mRNA transcription, processing and nuclear export, and specifically
CC associates with spliced mRNA and not with unspliced pre-mRNA. TREX is
CC recruited to spliced mRNAs by a transcription-independent mechanism,
CC binds to mRNA upstream of the exon-junction complex (EJC) and is
CC recruited in a splicing- and cap-dependent manner to a region near the
CC 5' end of the mRNA where it functions in mRNA export to the cytoplasm
CC via the TAP/NFX1 pathway. May undergo several rounds of ATP hydrolysis
CC during assembly of TREX to drive subsequent loading of components such
CC as ALYREF/THOC and CHTOP onto mRNA. Also associates with pre-mRNA
CC independent of ALYREF/THOC4 and the THO complex. Involved in the
CC nuclear export of intronless mRNA; the ATP-bound form is proposed to
CC recruit export adapter ALYREF/THOC4 to intronless mRNA; its ATPase
CC activity is cooperatively stimulated by RNA and ALYREF/THOC4 and ATP
CC hydrolysis is thought to trigger the dissociation from RNA to allow the
CC association of ALYREF/THOC4 and the NXF1-NXT1 heterodimer. Involved in
CC transcription elongation and genome stability (By similarity).
CC {ECO:0000250}.
CC -!- FUNCTION: Splice factor that is required for the first ATP-dependent
CC step in spliceosome assembly and for the interaction of U2 snRNP with
CC the branchpoint. Has both RNA-stimulated ATP binding/hydrolysis
CC activity and ATP-dependent RNA unwinding activity. Even with the
CC stimulation of RNA, the ATPase activity is weak. Can only hydrolyze ATP
CC but not other NTPs. The RNA stimulation of ATPase activity does not
CC have a strong preference for the sequence and length of the RNA.
CC However, ssRNA stimulates the ATPase activity much more strongly than
CC dsRNA. Can unwind 5' or 3' overhangs or blunt end RNA duplexes in
CC vitro. The ATPase and helicase activities are not influenced by U2AF2;
CC the effect of ALYREF/THOC4 is reported conflictingly (By similarity).
CC {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: Homodimer, and heterodimer with DDX39A. Component of the
CC transcription/export (TREX) complex at least composed of ALYREF/THOC4,
CC DDX39B, SARNP/CIP29, CHTOP and the THO subcomplex; TREX seems to have
CC dynamic structure involving ATP-dependent remodeling; in the complex
CC bridges ALYREF/THOC4 and the THO complex, and, in a ATP-dependent
CC manner, ALYREF/THOC4 and SARNP/CIP29. Component of the spliceosome (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Nucleus speckle
CC {ECO:0000250}.
CC -!- DOMAIN: The helicase C-terminal domain mediates interaction with
CC ALYREF/THOC4. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DECD subfamily.
CC {ECO:0000305}.
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DR EMBL; AJ720994; CAG32653.1; -; mRNA.
DR AlphaFoldDB; Q5ZHZ0; -.
DR SMR; Q5ZHZ0; -.
DR VEuPathDB; HostDB:geneid_416704; -.
DR InParanoid; Q5ZHZ0; -.
DR PhylomeDB; Q5ZHZ0; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR GO; GO:0005681; C:spliceosomal complex; IEA:UniProtKB-KW.
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; IBA:GO_Central.
DR GO; GO:0003724; F:RNA helicase activity; IBA:GO_Central.
DR GO; GO:0006406; P:mRNA export from nucleus; IBA:GO_Central.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IBA:GO_Central.
DR GO; GO:2000002; P:negative regulation of DNA damage checkpoint; ISS:UniProtKB.
DR GO; GO:0032786; P:positive regulation of DNA-templated transcription, elongation; 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; 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; 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; Helicase; Hydrolase; mRNA processing; mRNA splicing;
KW mRNA transport; Nucleotide-binding; Nucleus; Reference proteome;
KW RNA-binding; Spliceosome; Transport.
FT CHAIN 1..428
FT /note="Spliceosome RNA helicase DDX39B"
FT /id="PRO_0000055078"
FT DOMAIN 76..249
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 261..422
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..35
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 45..73
FT /note="Q motif"
FT MOTIF 196..199
FT /note="DECD box"
FT COMPBIAS 1..22
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 89..96
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 428 AA; 49003 MW; 07A42B0D8325A5AD CRC64;
MAENDVDNEL LDYEEDEVEN AAGGDGSEAP PKKDVKGSYV SIHSSGFRDF LLKPELLRAI
VDCGFEHPSE VQHECIPQAI LGMDVLCQAK SGMGKTAVFV LATLQQLEPV TGQVSVLVMC
HTRELAFQIS KEYERFSKYM PSVKVAVFFG GLAVKKDEEV LKKNCPHIVV GTPGRILALA
RNKSLNLKHI KHFILDECDK MLEQLDMRRD VQEIFRMTPH EKQVMMFSAT LSKEIRPVCR
KFMQDPMEIF VDDETKLTLH GLQQYYVKLK DNEKNRKLFD LLDVLEFNQV VIFVKSVQRC
IALAQLLVEQ NFPAIAIHRG MPQEERLSRY QQFKDFQRRI LVATNLFGRG MDIERVNIAF
NYDMPEDSDT YLHRVARAGR FGTKGLAITF VSDENDAKIL NDVQDRFEVN ISELPDEIDI
SSYIEQTR
