GenomeNet

Database: UniProt
Entry: Q5ZHZ0
LinkDB: Q5ZHZ0
Original site: Q5ZHZ0 
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   11-DEC-2019, entry version 72.
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}.
DR   EMBL; AJ720994; CAG32653.1; -; mRNA.
DR   SMR; Q5ZHZ0; -.
DR   PRIDE; Q5ZHZ0; -.
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:0000346; C:transcription export complex; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR   GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR   GO; GO:0000398; P:mRNA splicing, via spliceosome; IBA:GO_Central.
DR   GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
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   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   NP_BIND         89..96
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   MOTIF           45..73
FT                   /note="Q motif"
FT   MOTIF           196..199
FT                   /note="DECD box"
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
//
DBGET integrated database retrieval system