ID   DDX25_BOVIN             Reviewed;         483 AA.
AC   Q2TBP1;
DT   03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   03-AUG-2022, entry version 92.
DE   RecName: Full=ATP-dependent RNA helicase DDX25;
DE            EC=3.6.4.13;
DE   AltName: Full=DEAD box protein 25;
GN   Name=DDX25;
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=Liver;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: ATP-dependent RNA helicase. Required for mRNA export and
CC       translation regulation during spermatid development (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   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9QY15}. Nucleus
CC       {ECO:0000250|UniProtKB:Q9QY15}. Note=Detected in both cytoplasm and
CC       nucleus of testicular cells. Also detected in chromatoid bodies of
CC       round spermatids. {ECO:0000250|UniProtKB:Q9QY15}.
CC   -!- PTM: Phosphorylated on threonine residues. The phosphorylated form is
CC       found in the cytoplasm but not in the nucleus (By similarity).
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the DEAD box helicase family. {ECO:0000305}.
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DR   EMBL; BC109867; AAI09868.1; -; mRNA.
DR   RefSeq; NP_001033606.1; NM_001038517.1.
DR   AlphaFoldDB; Q2TBP1; -.
DR   SMR; Q2TBP1; -.
DR   STRING; 9913.ENSBTAP00000005587; -.
DR   PaxDb; Q2TBP1; -.
DR   PRIDE; Q2TBP1; -.
DR   GeneID; 508962; -.
DR   KEGG; bta:508962; -.
DR   CTD; 29118; -.
DR   eggNOG; KOG0332; Eukaryota.
DR   InParanoid; Q2TBP1; -.
DR   OrthoDB; 608788at2759; -.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0033391; C:chromatoid body; ISS:UniProtKB.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; ISS:UniProtKB.
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; ISS:UniProtKB.
DR   GO; GO:0006406; P:mRNA export from nucleus; ISS:UniProtKB.
DR   GO; GO:0006417; P:regulation of translation; ISS:UniProtKB.
DR   GO; GO:0007286; P:spermatid development; 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; Cytoplasm; Developmental protein; Differentiation; Helicase;
KW   Hydrolase; mRNA transport; Nucleotide-binding; Nucleus; Phosphoprotein;
KW   Reference proteome; RNA-binding; Spermatogenesis; Translation regulation;
KW   Transport.
FT   CHAIN           1..483
FT                   /note="ATP-dependent RNA helicase DDX25"
FT                   /id="PRO_0000282328"
FT   DOMAIN          130..300
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          311..478
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   MOTIF           61..74
FT                   /note="Nuclear export signal"
FT                   /evidence="ECO:0000250"
FT   MOTIF           97..125
FT                   /note="Q motif"
FT   MOTIF           100..114
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000250"
FT   MOTIF           247..250
FT                   /note="DEAD box"
FT   BINDING         143..150
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ   SEQUENCE   483 AA;  54619 MW;  5751FBC0751EC6B7 CRC64;
     MASLLWGGDA GAAESERLNG HFSNLIHPQN HLLGIKSATI PNIDGSVNRI EEDDEDDVVD
     LAANSLLNKL IRQSLVESSH RVEVLQKDPS SPLYSVKTFE ELRLKEELLK GIYAMGFNRP
     SKIQEMALPM MLAHPPQNLI AQSQSGTGKT AAFVLAMLSR VNALKLFPQC LCLAPTYELA
     LQTGRVVERM GKFCVDVQVM YAIRGNRIPR GTDVTKQIVI GTPGTVLDWC FKRKLIDLTK
     IRVFVLDEAD VMIDTQGFED QSIRIQRALP SECQMLLFSA TFEDSVWQFA ERIIPDPNVI
     KLRKEELTLN NIRQYYVLCG NRKDKYQALC NIYGGITIGQ AIIFCQTRRN AKWLTVEMMQ
     DGHQVSLLSG ELTVDQRASI IQRFRDGKEK VLITTNVCAR GIDVKQVTIV VNFDLPVNQA
     EEPDYETYLH RIGRTGRFGK KGLAFNMIEV DKLPLLMKIQ DHFNSSIKQL DPEDMDEIEK
     IEY