DDX1_XENLA
ID DDX1_XENLA Reviewed; 740 AA.
AC A2VD92;
DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-2007, sequence version 1.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=ATP-dependent RNA helicase DDX1;
DE EC=3.6.4.13;
DE AltName: Full=DEAD box protein 1;
GN Name=ddx1;
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]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Intestine;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (DEC-2006) 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 (By
CC similarity). Binds (via helicase ATP-binding domain) on both short and
CC long poly(I:C) dsRNA (By 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; BC129617; AAI29618.1; -; mRNA.
DR RefSeq; NP_001091352.1; NM_001097883.1.
DR AlphaFoldDB; A2VD92; -.
DR BioGRID; 674470; 1.
DR IntAct; A2VD92; 2.
DR MaxQB; A2VD92; -.
DR DNASU; 100037192; -.
DR GeneID; 100037192; -.
DR KEGG; xla:100037192; -.
DR CTD; 100037192; -.
DR Xenbase; XB-GENE-969102; ddx1.L.
DR OMA; EYCIRAI; -.
DR OrthoDB; 973872at2759; -.
DR Proteomes; UP000186698; Chromosome 5L.
DR Bgee; 100037192; Expressed in muscle tissue and 19 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_0000312360"
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; 82347 MW; E55339BC02B6407B CRC64;
MAAFSEMGVM PEIAQAVEEM DWLLPTDIQA ESIPLILGGG DVLMAAETGS GKTGAFSIPV
IQIVYETLKD QQEGKKGKAS VKTGSTVLNK WQMNPYDRGS AFAIGSDGLC CQSREIKEWH
GCRSTRGVNK GKYYYEVSCH DQGLCRVGWS TLSASLDLGT DKFGFGFGGT GKKSHNKQFD
NYGEEFTMHD TIGCYLDIDN SIVKFSKNGK DLGLAFQIPS HMKNQAFFTS CVLKNAELKF
NFGEEDFKFP PKDGFVALSK APDGHVVKSQ NTGSAQVSQT KSLPNAPKAL IIEPSRELAE
QTLNNVKQFK KYVDNPKLRE LLIIGGVAAK EQLTILENGV DIVVGTPGRI DDLISTGKLS
LSQVRFLVLD EADGLLSQGY SDFINRIYGQ IPQITSDGKR LQVIVCSATL HSFDVKKLSE
KIMHFPTWVD LKGEDSVPET VHHVVVPVNP KKDKQWEKLA KNHIRTDGVH DKDNTRPGGN
SAEVWSEAIK VLKGEYIVRA IKEHKMDQAI IFCRTKLDCD NMEQYFIQQG GGPDKKGHQF
SCVCLHSDRK PPERKHNLER FKKCEVRFLI CTDVAARGID IRGVPYVINV TLPDEKQNYV
HRIGRVGRAE RMGLAISLVA SEKEKVWYHV CSSRGKGCYN TRLKEDGGCT IWYNEMQLLS
EIEEHLTCTI SQVEPDIKVP LDDFDGKVVY GQRRATGGGL YKGHVDILAP TVQELASLEK
EAQTSFLHLG YLSNQLFRSF
