DD19A_BOVIN
ID DD19A_BOVIN Reviewed; 478 AA.
AC Q3ZBV2;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=ATP-dependent RNA helicase DDX19A;
DE EC=3.6.4.13 {ECO:0000250|UniProtKB:Q9UMR2};
DE AltName: Full=DEAD box protein 19A;
GN Name=DDX19A;
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=Crossbred X Angus; TISSUE=Ileum;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: ATP-dependent RNA helicase involved in mRNA export from the
CC nucleus. Rather than unwinding RNA duplexes, DDX19 functions as a
CC remodeler of ribonucleoprotein particles, whereby proteins bound to
CC nuclear mRNA are dissociated and replaced by cytoplasmic mRNA binding
CC proteins. {ECO:0000250|UniProtKB:Q9UMR2}.
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:Q9UMR2};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9UMR2}.
CC Nucleus, nucleoplasm {ECO:0000250|UniProtKB:Q9UMR2}. Note=Associates
CC with the nuclear pore complex cytoplasmic fibrils.
CC {ECO:0000250|UniProtKB:Q9UMR2}.
CC -!- DOMAIN: The N-terminal extension helix acts as an autoinhibitory
CC domain, preventing ATP hydrolysis, unless the N-terminus of the protein
CC is displaced by RNA binding, allowing cleft closure to bring key side
CC chains into position for catalysis. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX19/DBP5
CC subfamily. {ECO:0000305}.
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DR EMBL; BC103093; AAI03094.1; -; mRNA.
DR RefSeq; NP_001029743.1; NM_001034571.2.
DR AlphaFoldDB; Q3ZBV2; -.
DR SMR; Q3ZBV2; -.
DR STRING; 9913.ENSBTAP00000004645; -.
DR PaxDb; Q3ZBV2; -.
DR PeptideAtlas; Q3ZBV2; -.
DR PRIDE; Q3ZBV2; -.
DR Ensembl; ENSBTAT00000004645; ENSBTAP00000004645; ENSBTAG00000003570.
DR GeneID; 529929; -.
DR KEGG; bta:529929; -.
DR CTD; 55308; -.
DR VEuPathDB; HostDB:ENSBTAG00000003570; -.
DR VGNC; VGNC:52191; DDX19A.
DR eggNOG; KOG0332; Eukaryota.
DR GeneTree; ENSGT00940000154417; -.
DR HOGENOM; CLU_003041_1_0_1; -.
DR InParanoid; Q3ZBV2; -.
DR OMA; MDIPQVN; -.
DR OrthoDB; 608788at2759; -.
DR TreeFam; TF314957; -.
DR Proteomes; UP000009136; Chromosome 18.
DR Bgee; ENSBTAG00000003570; Expressed in milk and 105 other tissues.
DR ExpressionAtlas; Q3ZBV2; baseline and differential.
DR GO; GO:0010494; C:cytoplasmic stress granule; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; IEA:UniProtKB-SubCell.
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; IBA:GO_Central.
DR GO; GO:0003724; F:RNA helicase activity; IBA:GO_Central.
DR GO; GO:0016973; P:poly(A)+ mRNA export from nucleus; IBA:GO_Central.
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 Acetylation; ATP-binding; Cytoplasm; Helicase; Hydrolase; Isopeptide bond;
KW Nucleotide-binding; Nucleus; Reference proteome; RNA-binding;
KW Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9NUU7"
FT CHAIN 2..478
FT /note="ATP-dependent RNA helicase DDX19A"
FT /id="PRO_0000282323"
FT DOMAIN 124..294
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 305..473
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 2..299
FT /note="N-terminal lobe"
FT /evidence="ECO:0000250"
FT REGION 31..55
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 54..67
FT /note="N-terminal helix"
FT /evidence="ECO:0000250"
FT REGION 300..478
FT /note="C-terminal lobe"
FT /evidence="ECO:0000250"
FT MOTIF 91..119
FT /note="Q motif"
FT MOTIF 241..244
FT /note="DEAD box"
FT BINDING 118
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 137..144
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT BINDING 428
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 431
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q9NUU7"
FT CROSSLNK 26
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9NUU7"
FT CROSSLNK 26
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9NUU7"
SQ SEQUENCE 478 AA; 53986 MW; 62FC172EC387521C CRC64;
MATDSWALAV DEQEAAVKSM SNLQIKEEKV KPDTNGVIKT NATPEKTDEE EKEDRAAQSL
LNKLIRSNLV DNTNQVEVLQ RDPNSPLYSV KSFEELRLKP QLLQGVYAMG FNRPSKIQEN
ALPMMLAEPP QNLIAQSQSG TGKTAAFVLA MLSRVEPAER YPQCLCLSPT YELALQTGKV
IEQMGKFHPE LKLAYAVRGN KLERGQKISE HIVIGTPGTV LDWCSKLKFI DPKKIKVFVL
DEADVMIATQ GHQDQSIRIQ RMLPRNCQML LFSATFEDSV WKFAQKVVPD PNIIKLKREE
ETLDTIKQYY VLCNSRDEKF QALCNIYGAI TIAQAMIFCH TRKTASWLAA ELSKEGHQVA
LLSGEMVVEQ RAAVIERFRE GKEKVLVTTN VCARGIDVEQ VSVVINFDLP VDKDGNPDNE
TYLHRIGRTG RFGKRGLAVN MVDSKHSMNI LNRIQEHFNK KIERLDTDDL DEIEKIAN
