ID   RH1_CATRO               Reviewed;          26 AA.
AC   P85441;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   18-MAR-2008, sequence version 1.
DT   03-AUG-2022, entry version 25.
DE   RecName: Full=DEAD-box ATP-dependent RNA helicase 1;
DE            EC=3.6.4.13;
DE   Flags: Fragments;
OS   Catharanthus roseus (Madagascar periwinkle) (Vinca rosea).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Gentianales; Apocynaceae; Rauvolfioideae; Vinceae;
OC   Catharanthinae; Catharanthus.
OX   NCBI_TaxID=4058;
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE.
RA   Varman P.A.M., Ranjitha Kumari B.D.;
RL   Submitted (JAN-2008) to UniProtKB.
CC   -!- FUNCTION: ATP-dependent RNA helicase involved in mRNA turnover, and
CC       more specifically in mRNA decapping. {ECO:0000250|UniProtKB:Q8RXK6}.
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: Cytoplasm, P-body {ECO:0000250|UniProtKB:P39517}.
CC       Note=Is concentrated in several cytoplasmic foci called P bodies (or
CC       cytoplasmic processing bodies) which represent sites of mRNA decapping
CC       and 5' to 3' exonucleotidic decay. {ECO:0000250|UniProtKB:P39517}.
CC   -!- DOMAIN: The Q motif is unique to and characteristic of the DEAD box
CC       family of RNA helicases and controls ATP binding and hydrolysis.
CC       {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX6/DHH1
CC       subfamily. {ECO:0000255}.
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DR   AlphaFoldDB; P85441; -.
DR   GO; GO:0000932; C:P-body; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR   GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
DR   GO; GO:0006417; P:regulation of translation; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   ATP-binding; Cytoplasm; Direct protein sequencing; Helicase; Hydrolase;
KW   mRNA processing; mRNA transport; Nucleotide-binding; RNA-binding;
KW   Translation regulation; Transport.
FT   CHAIN           <1..>26
FT                   /note="DEAD-box ATP-dependent RNA helicase 1"
FT                   /id="PRO_0000324679"
FT   DOMAIN          <11..>26
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   MOTIF           <1..>10
FT                   /note="Q motif"
FT                   /evidence="ECO:0000255"
FT   BINDING         <11..16
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q58Z64,
FT                   ECO:0000255|PROSITE-ProRule:PRU00541"
FT   NON_CONS        10..11
FT                   /evidence="ECO:0000305"
FT   NON_TER         1
FT   NON_TER         26
SQ   SEQUENCE   26 AA;  2875 MW;  4246AAC748E98F2B CRC64;
     RELLMGIFEK NGTGKTAAFV IPLLQK