DDX1_CHICK
ID DDX1_CHICK Reviewed; 740 AA.
AC Q90WU3;
DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, 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;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Embryonic retina;
RX PubMed=11955614; DOI=10.1016/s0167-4781(01)00346-3;
RA Godbout R., Packer M., Katyal S., Bleoo S.;
RT "Cloning and expression analysis of the chicken DEAD box gene DDX1.";
RL Biochim. Biophys. Acta 1574:63-71(2002).
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 -!- TISSUE SPECIFICITY: Detected in embryonic retina, brain, heart and
CC liver (at protein level). Detected in embryonic retina, brain, heart,
CC kidney and liver. {ECO:0000269|PubMed:11955614}.
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}.
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; AY057383; AAL15417.1; -; mRNA.
DR RefSeq; NP_989894.1; NM_204563.1.
DR AlphaFoldDB; Q90WU3; -.
DR SMR; Q90WU3; -.
DR BioGRID; 675543; 1.
DR STRING; 9031.ENSGALP00000026509; -.
DR PaxDb; Q90WU3; -.
DR GeneID; 395249; -.
DR KEGG; gga:395249; -.
DR CTD; 1653; -.
DR VEuPathDB; HostDB:geneid_395249; -.
DR eggNOG; KOG0349; Eukaryota.
DR InParanoid; Q90WU3; -.
DR OrthoDB; 973872at2759; -.
DR PhylomeDB; Q90WU3; -.
DR PRO; PR:Q90WU3; -.
DR Proteomes; UP000000539; Unplaced.
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 1: Evidence at protein 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_0000312359"
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; 82484 MW; DAC1AC7B3D305365 CRC64;
MAAFSEMGVM PEIAQAVEEM DWLLPTDIQA ESIPLILGGG DVLMAAETGS GKTGAFSIPV
IQIVYETLKD QMEGKKGKAT IKTGGAVLNK WQMNPYDRGS AFAIGSDGLC CQSREVKEWH
GCRATRGVTK GKYYYEVSCH DQGLCRVGWS TMQASLDLGT DKFGFGFGGT GKKSHNKQFD
SYGEEFTMHD TIGCYLDIDK GQIKFSKNGK DLGLAFEFPP HIRNQALFAA CVLKNAELKF
NFGEEDFKFP PKDGYIGLCK APDGNVVKSQ HTGNAQVVQT QNLPNAPKAL IVEPSRELAE
QTLNNVKQFK KYIDNPKLRE LLIIGGVAAR DQLSVLEQGV DIVVGTPGRL DDLVSTGKLN
LSQVRFLVLD EADGLLLQGY SDFINRIHSQ IPQITSDGKR LQVIVCSATL HSFDVKKLSE
KIMHFPTWVD LKGEDSVPET VHHVVVIVNP KTDKLWERLG KNHIRTDEVH AKDNTLPGAN
TPEMWSEAIK ILKGEYTVRA IKEHKMDQAI IFCRTKIDCD NMEQYFIQQG GGPDRKGHQF
SCVCLHGDRK PQERKQNLER FKRGDVRFLI CTDVAARGID IHGVPYVINV TLPDEKQNYV
HRIGRVGRAE RMGLAISLVA KEKEKVWYHV CSSRGKGCYN TRLKEEGGCT IWYNEMQLLG
EIEEHLNCTI SQVEPDIKVP VDDFDGKVTY GQKRALGGGL YKGHVDILAP TVQELAALEK
EAQTSFLHLG YLPNQLFRTF
