DDX1_XENTR
ID DDX1_XENTR Reviewed; 740 AA.
AC Q5XH91;
DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=ATP-dependent RNA helicase DDX1;
DE EC=3.6.4.13;
DE AltName: Full=DEAD box protein 1;
GN Name=ddx1; ORFNames=TEgg029l11.1;
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Egg;
RG Sanger Xenopus tropicalis EST/cDNA project;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Acts as an ATP-dependent RNA helicase, able to unwind both
CC RNA-RNA and RNA-DNA duplexes. Possesses 5' single-stranded RNA overhang
CC nuclease activity. Acts as a positive regulator of transcription. May
CC be involved in 3'-end cleavage and polyadenylation of pre-mRNAs. Binds
CC DNA and RNA. Component of the tRNA-splicing ligase complex required to
CC facilitate the enzymatic turnover of catalytic subunit rtcb. Binds (via
CC helicase ATP-binding domain) on both short and long poly(I:C) dsRNA (By
CC similarity). {ECO:0000250|UniProtKB:Q91VR5,
CC ECO:0000250|UniProtKB:Q92499}.
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: Nucleus {ECO:0000250|UniProtKB:Q92499}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q92499}. Cytoplasmic granule
CC {ECO:0000250|UniProtKB:Q92499}. Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:Q91VR5}. Mitochondrion
CC {ECO:0000250|UniProtKB:Q91VR5}.
CC -!- DOMAIN: The helicase domain is involved in the stimulation of RELA
CC transcriptional activity. {ECO:0000250|UniProtKB:Q92499}.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX1 subfamily.
CC {ECO:0000305}.
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DR EMBL; CR855610; CAJ81838.1; -; mRNA.
DR EMBL; BC084181; AAH84181.1; -; mRNA.
DR RefSeq; NP_001011133.1; NM_001011133.2.
DR AlphaFoldDB; Q5XH91; -.
DR SMR; Q5XH91; -.
DR STRING; 8364.ENSXETP00000010295; -.
DR PaxDb; Q5XH91; -.
DR PRIDE; Q5XH91; -.
DR DNASU; 496549; -.
DR GeneID; 496549; -.
DR KEGG; xtr:496549; -.
DR CTD; 1653; -.
DR Xenbase; XB-GENE-969096; ddx1.
DR eggNOG; KOG0349; Eukaryota.
DR HOGENOM; CLU_016321_0_0_1; -.
DR InParanoid; Q5XH91; -.
DR OMA; EYCIRAI; -.
DR OrthoDB; 973872at2759; -.
DR PhylomeDB; Q5XH91; -.
DR TreeFam; TF106114; -.
DR Proteomes; UP000008143; Chromosome 5.
DR Proteomes; UP000790000; Unplaced.
DR Bgee; ENSXETG00000017825; Expressed in ovary and 14 other tissues.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0072669; C:tRNA-splicing ligase complex; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003682; F:chromatin binding; ISS:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0033677; F:DNA/RNA helicase activity; ISS:UniProtKB.
DR GO; GO:0004527; F:exonuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0004518; F:nuclease activity; ISS:UniProtKB.
DR GO; GO:0008143; F:poly(A) binding; ISS:UniProtKB.
DR GO; GO:0003724; F:RNA helicase activity; ISS:UniProtKB.
DR GO; GO:0003712; F:transcription coregulator activity; ISS:UniProtKB.
DR GO; GO:0032508; P:DNA duplex unwinding; ISS:UniProtKB.
DR GO; GO:0006302; P:double-strand break repair; ISS:UniProtKB.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0006388; P:tRNA splicing, via endonucleolytic cleavage and ligation; ISS:UniProtKB.
DR Gene3D; 2.60.120.920; -; 1.
DR Gene3D; 3.40.50.300; -; 3.
DR InterPro; IPR001870; B30.2/SPRY.
DR InterPro; IPR043136; B30.2/SPRY_sf.
DR InterPro; IPR013320; ConA-like_dom_sf.
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 InterPro; IPR003877; SPRY_dom.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF00622; SPRY; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00449; SPRY; 1.
DR SUPFAM; SSF49899; SSF49899; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR PROSITE; PS50188; B302_SPRY; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 2.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS51195; Q_MOTIF; 1.
PE 2: Evidence at transcript level;
KW Activator; ATP-binding; Cytoplasm; DNA-binding; Exonuclease; Helicase;
KW Hydrolase; Mitochondrion; mRNA processing; Nuclease; Nucleotide-binding;
KW Nucleus; Reference proteome; RNA-binding; Transcription;
KW Transcription regulation; tRNA processing.
FT CHAIN 1..740
FT /note="ATP-dependent RNA helicase DDX1"
FT /id="PRO_0000312361"
FT DOMAIN 2..428
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 70..247
FT /note="B30.2/SPRY"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00548"
FT DOMAIN 493..681
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..448
FT /note="Interaction with dsRNA"
FT /evidence="ECO:0000250|UniProtKB:Q91VR5"
FT MOTIF 370..373
FT /note="DEAD box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT BINDING 46..53
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 740 AA; 82213 MW; 11E3ED4CDE84A434 CRC64;
MAAFSEMGVM AEIAQAVEEM DWLLPTDIQA ESIPLILGGG DVLMAAETGS GKTGAFSIPV
IQIVYETLKD QQEGKKGKTS VKTGSTVLNK WQMNPYDRGS SFAIGSDGLC CQSREIKEWH
GCRSTRGVNK GKYYYEVSCH DQGLCRVGWS TLQASLDLGT DKFGFGFGGT GKKSHNKQFD
NYGEEFTMHD TIGCYIDIDN GTVKYSKNGK DLGLAFQIPA HLKNQAVFAS CVLKNAELKF
NFGEEDFKFP PKDGFVALSK APDGHVVKSQ NTGSAQVSQA KNLPNAPKAL IIEPSRELAE
QTLNNVKQFK KYVDSPKLRE LLIIGGVAAK EQLTLLENGV DIVVGTPGRI DDLISTGKLN
LSQVRFLVLD EADGLLSQGY SDFINRIHGQ IPQVTSDGKR LQVIVCSATL HSFDVKKLSE
KIMHFPTWVD LKGEDSVPET VHHVVVPVNP KKDKQWERLG KNHIRTDGVH DKDNTRPGGN
SAEMWSEAIK VLKGEYTVRA IKEHKMDQAI IFCRTKLDCD NMEQYFIQQG GGPDKKGHQF
SCVCLHSDRK PQERKHNLER FKKCEVRFLI CTDVAARGID IHGVPYVINV TLPDEKQNYV
HRIGRVGRAE RMGLAISLVA AEKEKVWYHV CSSRGKGCHN TRLKEDGGCT IWYNETQLLS
EIEEHLTCTI SQVEPDIKVP LDEFDGKVVY GQRRATGGGL YKGHVDILAP TVQELAALEK
EAQTSFLHLG YLSNQLFRTF
