GenomeNet

Database: UniProt
Entry: Q90WU3
LinkDB: Q90WU3
Original site: Q90WU3 
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   16-OCT-2019, entry version 110.
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;
OC   Phasianidae; 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
CC       both RNA-RNA and RNA-DNA duplexes. Possesses 5' single-stranded
CC       RNA overhang nuclease activity. Acts as a positive regulator of
CC       transcription. May be involved in 3'-end cleavage and
CC       polyadenylation of pre-mRNAs. Binds DNA and RNA. Component of the
CC       tRNA-splicing ligase complex required to facilitate the enzymatic
CC       turnover of catalytic subunit RTCB (By similarity). Binds (via
CC       helicase ATP-binding domain) on both short and long poly(I:C)
CC       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}.
CC       Cytoplasm {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,
CC       heart, 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
CC       subfamily. {ECO:0000305}.
DR   EMBL; AY057383; AAL15417.1; -; mRNA.
DR   RefSeq; NP_989894.1; NM_204563.1.
DR   BioGrid; 675543; 1.
DR   STRING; 9031.ENSGALP00000026509; -.
DR   PaxDb; Q90WU3; -.
DR   PRIDE; Q90WU3; -.
DR   GeneID; 395249; -.
DR   KEGG; gga:395249; -.
DR   CTD; 1653; -.
DR   eggNOG; KOG0349; Eukaryota.
DR   eggNOG; COG0513; LUCA.
DR   HOGENOM; HOG000251633; -.
DR   InParanoid; Q90WU3; -.
DR   KO; K13177; -.
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: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:0004386; F:helicase activity; ISS:UniProtKB.
DR   GO; GO:0004518; F:nuclease activity; ISS:UniProtKB.
DR   GO; GO:0008143; F:poly(A) binding; ISS:UniProtKB.
DR   GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR   GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
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   InterPro; IPR001870; B30.2/SPRY.
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; Complete proteome; Cytoplasm; DNA-binding;
KW   Exonuclease; Helicase; Hydrolase; Mitochondrion; mRNA processing;
KW   Nuclease; Nucleotide-binding; Nucleus; Reference proteome;
KW   RNA-binding; Transcription; Transcription regulation; tRNA processing.
FT   CHAIN         1    740       ATP-dependent RNA helicase DDX1.
FT                                /FTId=PRO_0000312359.
FT   DOMAIN        2    428       Helicase ATP-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00541}.
FT   DOMAIN       70    247       B30.2/SPRY. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00548}.
FT   DOMAIN      493    681       Helicase C-terminal.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00542}.
FT   NP_BIND      46     53       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00541}.
FT   REGION        1    448       Interaction with dsRNA.
FT                                {ECO:0000250|UniProtKB:Q91VR5}.
FT   MOTIF       370    373       DEAD box. {ECO:0000255|PROSITE-
FT                                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
//
DBGET integrated database retrieval system