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Database: UniProt
Entry: Q5R7D1
LinkDB: Q5R7D1
Original site: Q5R7D1 
ID   DDX42_PONAB             Reviewed;         942 AA.
AC   Q5R7D1;
DT   06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   31-JUL-2019, entry version 82.
DE   RecName: Full=ATP-dependent RNA helicase DDX42;
DE            EC=3.6.4.13;
DE   AltName: Full=DEAD box protein 42;
GN   Name=DDX42;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: ATP-dependent RNA helicase. Binds to partially double-
CC       stranded RNAs (dsRNAs) in order to unwind RNA secondary
CC       structures. Unwinding is promoted in the presence of single-strand
CC       binding proteins. Mediates also RNA duplex formation thereby
CC       displacing the single-strand RNA binding protein. ATP and ADP
CC       modulate its activity: ATP binding and hydrolysis by DDX42
CC       triggers RNA strand separation, whereas the ADP-bound form of the
CC       protein triggers annealing of complementary RNA strands. Involved
CC       in the survival of cells by interacting with TP53BP2 and thereby
CC       counteracting the apoptosis-stimulating activity of TP53BP2.
CC       Relocalizes TP53BP2 to the cytoplasm (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: Component of splicing factor SF3B complex which is
CC       composed of at least eight subunits; SF3B1, SF3B2, SF3B3, SF3B4,
CC       SF3B5, SF3B6, PHF5A/SF3B14B, and DDX42/SF3B125. Interacts (via the
CC       C-terminus) with TP53BP2; the interaction is not inhibitied by
CC       TP53BP2 ubiquitination and is independent of p53/TP53 (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus speckle
CC       {ECO:0000250}. Nucleus, Cajal body {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX42
CC       subfamily. {ECO:0000305}.
DR   EMBL; CR860187; CAH92329.1; -; mRNA.
DR   RefSeq; NP_001126368.1; NM_001132896.1.
DR   SMR; Q5R7D1; -.
DR   STRING; 9601.ENSPPYP00000009583; -.
DR   GeneID; 100173349; -.
DR   KEGG; pon:100173349; -.
DR   CTD; 11325; -.
DR   eggNOG; KOG0334; Eukaryota.
DR   eggNOG; ENOG410XSQV; LUCA.
DR   InParanoid; Q5R7D1; -.
DR   KO; K12835; -.
DR   OrthoDB; 245118at2759; -.
DR   Proteomes; UP000001595; Unplaced.
DR   GO; GO:0015030; C:Cajal body; IEA:UniProtKB-SubCell.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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   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   Acetylation; ATP-binding; Coiled coil; Complete proteome; Cytoplasm;
KW   Helicase; Hydrolase; Isopeptide bond; Methylation; Nucleotide-binding;
KW   Nucleus; Phosphoprotein; Reference proteome; RNA-binding;
KW   Ubl conjugation.
FT   CHAIN         1    942       ATP-dependent RNA helicase DDX42.
FT                                /FTId=PRO_0000280060.
FT   DOMAIN      284    459       Helicase ATP-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00541}.
FT   DOMAIN      487    632       Helicase C-terminal.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00542}.
FT   NP_BIND     297    304       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00541}.
FT   REGION      738    833       Necessary for interaction with TP53BP2.
FT                                {ECO:0000250}.
FT   COILED      116    157       {ECO:0000255}.
FT   MOTIF       253    281       Q motif.
FT   MOTIF       407    410       DEAD box.
FT   COMPBIAS     43     46       Poly-Ser.
FT   COMPBIAS    175    178       Poly-Glu.
FT   COMPBIAS    654    659       Poly-Gly.
FT   COMPBIAS    762    883       Gly-rich.
FT   COMPBIAS    819    871       His-rich.
FT   MOD_RES       5      5       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:Q86XP3}.
FT   MOD_RES      12     12       Omega-N-methylarginine.
FT                                {ECO:0000250|UniProtKB:Q86XP3}.
FT   MOD_RES      58     58       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q86XP3}.
FT   MOD_RES      96     96       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q86XP3}.
FT   MOD_RES     104    104       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q86XP3}.
FT   MOD_RES     109    109       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q86XP3}.
FT   MOD_RES     111    111       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q86XP3}.
FT   MOD_RES     185    185       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q86XP3}.
FT   MOD_RES     754    754       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q86XP3}.
FT   CROSSLNK    899    899       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000250|UniProtKB:Q86XP3}.
SQ   SEQUENCE   942 AA;  103498 MW;  47492B68C09042AF CRC64;
     MNWNKGGPGT KRGFGFGGFA ISAGKKEEPK LPQQSHSAFG ATSSSSGFGK SAPPQLPSFY
     KIGSKRANFD EENAYFEDEE EDSSNVDLPY IPAENSPTRQ QFHSKPIDSD SDDDPLEAFM
     AEVEDQAARD MKRLEEKDKE RKNVKGIRDD IEEEDDQETY FRYMAENPTA GVVQEEEEDN
     LEYDSDGNPI APTKKIIDPL PPIDHSEIDY PPFEKNFYNE HEEITNLTPQ QLIDLRHKLN
     LRVSGAAPPR PGSSFAHFGF DEQLMHQIRK SEYTQPTPIQ CQGVPVALSG RDMIGIAKTG
     SGKTAAFIWP MLIHIMDQKE LEPGDGPIAV IVCPTRELCQ QIHAEGKRFG KAYNLRSVAV
     YGGGSMWEQA KALQEGAEIV VCTPGRLIDH VKKKATNLQR VSYLVFDEAD RMFDMGFEYQ
     VRSIASHVRP DRQTLLFSAT FRKKIEKLAR DILIDPIRVV QGDIGEANED VTQIVEILHS
     GPSKWNWLTR RLVEFTSSGS VLLFVTKKAN AEELANNLKQ EGHNLGLLHG DMDQSERNKV
     ISDFKKKDIP VLVATDVAAR GLDIPSIKTV INYDVARDID THTHRIGRTG RAGEKGVAYT
     LLTPKDSNFA GDLVRNLEGA NQHVSKELLD LAMQNAWFRK SRFKGGKGKK LNIGGGGLGY
     RERPGLGSEN MDRGNNNVMS NYEAYKPSTG AMGDRLTAMK AAFQSQYKSH FVAASLSNQK
     AGSSAAGASG WTSAGSLNSV PTNSAQQGHN SPDSPITSAT KGIPGFGNIG NISGAPVTYP
     SAGAQGVNNT ASGNNSREGT GGSNGKRERY TENRGSSRHS HGETGNRHSD SPRHGDGGRH
     GDGYRHPESS SRHTDGHRHG ENRHGGSAGR HGENRGANDG RNGESRKEAC NRESKMEPKM
     EPKMEPKVDS NKMDKVDSKT DKTADGFAVP EPPKRKKSRW DS
//
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