DDX25_XENLA
ID DDX25_XENLA Reviewed; 483 AA.
AC Q9DGP9;
DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=ATP-dependent RNA helicase DDX25;
DE EC=3.6.4.13;
DE AltName: Full=DEAD box protein 25;
DE AltName: Full=RNA helicase DEADSouth;
DE AltName: Full=Xcat3;
GN Name=deadsouth {ECO:0000312|EMBL:AAF99574.1};
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAF99574.1}
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RC TISSUE=Oocyte {ECO:0000269|PubMed:10906480};
RX PubMed=10906480; DOI=10.1016/s0925-4773(00)00357-9;
RA MacArthur H.C., Houston D.W., Bubunenko M., Mosquera L., King M.L.;
RT "DEADSouth is a germ plasm specific DEAD-box RNA helicase in Xenopus
RT related to eIF4A.";
RL Mech. Dev. 95:291-295(2000).
RN [2] {ECO:0000305}
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=11784096; DOI=10.1006/dbio.2001.0488;
RA Kloc M., Dougherty M.T., Bilinski S., Chan A.P., Brey E., King M.L.,
RA Patrick C.W. Jr., Etkin L.D.;
RT "Three-dimensional ultrastructural analysis of RNA distribution within
RT germinal granules of Xenopus.";
RL Dev. Biol. 241:79-93(2002).
CC -!- FUNCTION: ATP-dependent RNA helicase. {ECO:0000250|UniProtKB:Q9QY15}.
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:0000269|PubMed:10906480,
CC ECO:0000269|PubMed:11784096}. Nucleus {ECO:0000250|UniProtKB:Q9QY15}.
CC Note=Also detected in chromatoid bodies of round spermatids.
CC {ECO:0000250|UniProtKB:Q9QY15}.
CC -!- TISSUE SPECIFICITY: An mRNA component of germ plasm. Localizes to the
CC granulo-fibrillar material (GFM) of the mitochondrial cloud in stage I
CC oocytes. Associated, at a low level, with the periphery of mature
CC germinal granules in later stage oocytes. Localizes to the vegetal
CC cortex in stage II oocytes and segregates with germ plasm during early
CC embryogenesis. In adults, expression is restricted to the ovary and, at
CC a lower level, to spermatogonia, spermatocytes and spermatids of the
CC testis. {ECO:0000269|PubMed:10906480, ECO:0000269|PubMed:11784096}.
CC -!- DEVELOPMENTAL STAGE: Expressed at a constant level throughout oogenesis
CC and in the egg. Levels decrease during gastrulation and are not
CC detectable by the end of gastrulation. {ECO:0000269|PubMed:10906480}.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. {ECO:0000255}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF190623; AAF99574.1; -; mRNA.
DR RefSeq; NP_001082017.1; NM_001088548.1.
DR AlphaFoldDB; Q9DGP9; -.
DR SMR; Q9DGP9; -.
DR MaxQB; Q9DGP9; -.
DR GeneID; 398180; -.
DR KEGG; xla:398180; -.
DR CTD; 398180; -.
DR Xenbase; XB-GENE-958142; ddx25.L.
DR OMA; DFKNLCM; -.
DR OrthoDB; 608788at2759; -.
DR Proteomes; UP000186698; Chromosome 7L.
DR Bgee; 398180; Expressed in egg cell and 7 other tissues.
DR GO; GO:0033391; C:chromatoid body; ISS:UniProtKB.
DR GO; GO:0032019; C:mitochondrial cloud; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0045495; C:pole plasm; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; ISS:UniProtKB.
DR GO; GO:0003723; F:RNA binding; ISS:UniProtKB.
DR GO; GO:0003724; F:RNA helicase activity; 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; Helicase; Hydrolase; Nucleotide-binding; Nucleus;
KW Reference proteome; RNA-binding.
FT CHAIN 1..483
FT /note="ATP-dependent RNA helicase DDX25"
FT /id="PRO_0000253934"
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 97..125
FT /note="Q motif"
FT /evidence="ECO:0000255"
FT MOTIF 247..250
FT /note="DEAD box"
FT /evidence="ECO:0000255"
FT BINDING 143..150
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 483 AA; 54545 MW; EBE1ECBAE9C049D8 CRC64;
MAAKFLPRFW RSGSQAELLD FQNNNVVAEG KLDFEHGTLK GKSGRYGDDE EDVRRGHIED
LANHSLLNKL LRRTLVDSPH NVEVLQRDPT SPLFSVKSFE ELHLKNELLR GIYAMGFNRP
SKIQENALPM MLADPPQNLI AQSQSGTGKT AAFVLAMLSR VDANKKYPQC ICLSPTFELA
LQTGKVVEEM GKFCAGIEVI YALRGNRPGK GSRLEAQIVI GTPGTVLDWC FKLRLITVEN
ISVFVLDEAD VMINVQGHSD HSVRVKRSMP KSCQMLLFSA TFEDSVWAFA ERIVPDPNII
KLKKEELTLK NIQQFYDQCE NKEQKYSALC NLYGVITIAQ AIVFCQTRKI ASWLSQKLSD
DGHQVALLSG ELPVYDRADM IQRFREGREK VLVTTNVCAR GIDVEQVSIV VNFDLPVNVD
GSVDFETYLH RIGRTGRFGK KGIAVSLIEN FFVYMLKEIE DHFNTKITKL NSMDMDEMGK
IWK
