ID B1WAW5_XENTR Unreviewed; 678 AA.
AC B1WAW5;
DT 20-MAY-2008, integrated into UniProtKB/TrEMBL.
DT 20-MAY-2008, sequence version 1.
DT 27-MAR-2024, entry version 71.
DE RecName: Full=RNA helicase {ECO:0000256|ARBA:ARBA00012552};
DE EC=3.6.4.13 {ECO:0000256|ARBA:ARBA00012552};
GN Name=ddx4 {ECO:0000313|RefSeq:XP_012818309.1,
GN ECO:0000313|Xenbase:XB-GENE-1016809};
GN Synonyms=LOC549577 {ECO:0000313|EMBL:AAI61525.1}, vasa
GN {ECO:0000313|RefSeq:XP_012818309.1}, xvlg1
GN {ECO:0000313|RefSeq:XP_012818309.1};
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364 {ECO:0000313|EMBL:AAI61525.1};
RN [1] {ECO:0000313|EMBL:AAI61525.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Whole embryo {ECO:0000313|EMBL:AAI61525.1};
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|RefSeq:XP_012818309.1}
RP IDENTIFICATION.
RC STRAIN=Nigerian {ECO:0000313|RefSeq:XP_012818309.1};
RC TISSUE=Liver and blood {ECO:0000313|RefSeq:XP_012818309.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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:0000256|ARBA:ARBA00001556};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX4/VASA
CC subfamily. {ECO:0000256|ARBA:ARBA00010132}.
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DR EMBL; BC161525; AAI61525.1; -; mRNA.
DR RefSeq; XP_012818309.1; XM_012962855.3.
DR STRING; 8364.ENSXETP00000038054; -.
DR PaxDb; 8364-ENSXETP00000060512; -.
DR GeneID; 549577; -.
DR AGR; Xenbase:XB-GENE-1016809; -.
DR CTD; 54514; -.
DR Xenbase; XB-GENE-1016809; ddx4.
DR OMA; PRYGNNR; -.
DR OrthoDB; 5480645at2759; -.
DR Proteomes; UP000008143; Chromosome 1.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0003724; F:RNA helicase activity; IEA:InterPro.
DR CDD; cd18052; DEADc_DDX4; 1.
DR CDD; cd18787; SF2_C_DEAD; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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; IPR000629; RNA-helicase_DEAD-box_CS.
DR InterPro; IPR014014; RNA_helicase_DEAD_Q_motif.
DR PANTHER; PTHR47958; ATP-DEPENDENT RNA HELICASE DBP3; 1.
DR PANTHER; PTHR47958:SF11; RNA HELICASE; 1.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
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 ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU000492};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000256|RuleBase:RU000492};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU000492};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU000492};
KW Reference proteome {ECO:0000313|Proteomes:UP000008143}.
FT DOMAIN 252..280
FT /note="DEAD-box RNA helicase Q"
FT /evidence="ECO:0000259|PROSITE:PS51195"
FT DOMAIN 283..466
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 478..639
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..203
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 659..678
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 252..280
FT /note="Q motif"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00552"
FT COMPBIAS 10..52
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 85..99
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 180..203
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 678 AA; 75349 MW; 67523C421FF55178 CRC64;
MEENWDTEIS TEKPTYIPNF SSLETDNTDN YTAYSNNDIT NQNYQSERSF GNRGGYRSER
GGPTNFNRGS RIGRGRGFDS NRNDQYSDSS ERDGYNANED TQKPFRGRGG FRNENGQRRG
FGDRGGFRNE NGQQRNFDRG DWNNSGEGEE RPRGFGRGGF NNFDSDTGGR GHRGGRGGRG
GYKGRNEEVG VESGKNQEEG TEKEVKKVIY VPLPPSDSED DIFRHYQSGI NFDKYDEILV
DVTGKDVPPA ILTFEEANFC ETLSRNVTKA GYVKLTPVQK HSIPIILAGR DLMACAQTGS
GKTAAFLLPI LSHMMNEGIT ASQFLPLQEP QAIIIAPTRE LINQIYLDAR KFSYGTCVRP
VVVYGGIHPV HAMRDVERGC NILCATPGRL MDIIGREKIG LSKLKYLVLD EADRMLDMGF
APVMENLIGS PGMPAKEERQ TLMFSATYPA EIQRLASKFL KSDHLFVVVG LVGGACSDVE
QTILEIQEYR KRDKLVEILQ SSGNERTMIF VNTKKKADVI AGYLCQEHFP TTSIHGDREQ
CQREEAIRDF RSGKCPVIVC TAVAARGLDI ENVQHVINYD VPKEIDEYVH RIGRTGRCGN
VGKATSFFNV NEDHVVARPL VKILTDAHQE VPAWLEEIAF GGHGALNSLY AADSMGGEAG
EKYVSAPSSA QEEEASWD
//
