DDX47_BOVIN
ID DDX47_BOVIN Reviewed; 457 AA.
AC Q29S22;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 04-APR-2006, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Probable ATP-dependent RNA helicase DDX47;
DE EC=3.6.4.13;
DE AltName: Full=DEAD box protein 47;
GN Name=DDX47;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Uterus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Involved in apoptosis. May have a role in rRNA processing and
CC mRNA splicing. Associates with pre-rRNA precursors (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: Interacts with AGO1 and AGO2. Interacts with GABARAP.
CC Interacts with NOL8; the interaction is RNA-dependent (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250}. Note=Localizes
CC in the nucleolar-organizing region during ribosome biogenesis.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX47/RRP3
CC subfamily. {ECO:0000305}.
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DR EMBL; BC113207; AAI13208.1; -; mRNA.
DR RefSeq; NP_001039850.1; NM_001046385.1.
DR AlphaFoldDB; Q29S22; -.
DR SMR; Q29S22; -.
DR STRING; 9913.ENSBTAP00000003058; -.
DR PaxDb; Q29S22; -.
DR PeptideAtlas; Q29S22; -.
DR PRIDE; Q29S22; -.
DR Ensembl; ENSBTAT00000003058; ENSBTAP00000003058; ENSBTAG00000019608.
DR GeneID; 534721; -.
DR KEGG; bta:534721; -.
DR CTD; 51202; -.
DR VEuPathDB; HostDB:ENSBTAG00000019608; -.
DR VGNC; VGNC:27970; DDX47.
DR eggNOG; KOG0330; Eukaryota.
DR GeneTree; ENSGT00940000155774; -.
DR HOGENOM; CLU_003041_1_1_1; -.
DR InParanoid; Q29S22; -.
DR OMA; YDIELYQ; -.
DR OrthoDB; 744428at2759; -.
DR TreeFam; TF105714; -.
DR Proteomes; UP000009136; Chromosome 5.
DR Bgee; ENSBTAG00000019608; Expressed in omasum and 104 other tissues.
DR ExpressionAtlas; Q29S22; baseline and differential.
DR GO; GO:0005730; C:nucleolus; ISS:UniProtKB.
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:0008625; P:extrinsic apoptotic signaling pathway via death domain receptors; ISS:UniProtKB.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0008380; P:RNA splicing; ISS:UniProtKB.
DR GO; GO:0006364; P:rRNA processing; ISS:UniProtKB.
DR CDD; cd17954; DEADc_DDX47; 1.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR044765; DDX47/Rrp3_DEADc.
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; Apoptosis; ATP-binding; Helicase; Hydrolase; mRNA processing;
KW mRNA splicing; Nucleotide-binding; Nucleus; Phosphoprotein;
KW Reference proteome; RNA-binding; rRNA processing.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9H0S4"
FT CHAIN 2..457
FT /note="Probable ATP-dependent RNA helicase DDX47"
FT /id="PRO_0000244563"
FT DOMAIN 57..228
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 239..399
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 415..457
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 26..54
FT /note="Q motif"
FT MOTIF 176..179
FT /note="DEAD box"
FT COMPBIAS 415..439
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 70..77
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q9H0S4"
FT MOD_RES 9
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H0S4"
FT MOD_RES 151
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9H0S4"
FT MOD_RES 426
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H0S4"
SQ SEQUENCE 457 AA; 50913 MW; 374C287B42FE8206 CRC64;
MAASVEHDSL ESMEAPQTAV EVEETKTFKD LGVTDVLCEA CDQLGWTKPT KIQIEAIPLA
LQGRDIIGLA ETGSGKTGAF ALPILNALLE TPQRLFALVL TPTRELAFQI SEQFEALGSS
IGVQCAVIVG GIDSMSQSLA LAKKPHIVIA TPGRLIDHLE NTKGFNLRAL KYLVMDEADR
ILNMDFETEV DKILKVIPRD RKTFLFSATM TKKVQKLQRA ALKNPVKCAV SSKYQTVEKL
QQYYLFIPSK FKDTYLVYIL NELAGNSFMI FCSTCNNTQR TALLLRNLGF TAIPLHGQMS
QSKRLGSLNK FKAKARSILL ATDVASRGLD IPHVDVVVNF DIPTHSKDYI HRVGRTARAG
RSGKAITFVT QYDVELFQRI EHLIGKKLPV FPTQDDEVMM LTERVTEAQR FARMELREHG
EKKKRSREDV GDNDDTEGAI GVRNKVAGGK MKKRKGR
