ID   RH3_HELAN               Reviewed;         234 AA.
AC   P85199;
DT   10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT   10-AUG-2010, sequence version 1.
DT   03-AUG-2022, entry version 25.
DE   RecName: Full=DEAD-box ATP-dependent RNA helicase 3 {ECO:0000250|UniProtKB:Q0DM51};
DE            EC=3.6.1.-;
DE   Flags: Fragment;
OS   Helianthus annuus (Common sunflower).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; campanulids; Asterales; Asteraceae; Asteroideae;
OC   Heliantheae alliance; Heliantheae; Helianthus.
OX   NCBI_TaxID=4232;
RN   [1] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. ANN1312 {ECO:0000269|Ref.1};
RA   Michelmore R.W., Knapp S., Rieseberg L., Bradford K., Kesseli R., Boore J.,
RA   Kozik A., Matvienko M., Lavelle D., Lai Z.;
RT   "Sunflower (Helianthus annuus) ESTs (set 2) from the compositae genome
RT   project http://compgenomics.ucdavis.edu/.";
RL   Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000305}
RP   IDENTIFICATION BY MASS SPECTROMETRY, AND INDUCTION.
RA   Garcia J.S., Souza G.H.M.F., Eberlin M.N., Arruda M.A.Z.;
RT   "Evaluation of metal-ion stress in sunflower (Heliantus annus L.) leaves
RT   through proteomic changes.";
RL   Metallomics 1:107-113(2009).
CC   -!- INDUCTION: Down-regulated in response to mixed metal ion contamination
CC       (cadmium, copper, lead and zinc), but not in response to zinc ion
CC       contamination. {ECO:0000269|Ref.2}.
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. DDX21/DDX50
CC       subfamily. {ECO:0000255}.
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DR   EMBL; DY911458; -; NOT_ANNOTATED_CDS; mRNA.
DR   AlphaFoldDB; P85199; -.
DR   SMR; P85199; -.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003724; F:RNA helicase activity; IEA:InterPro.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR014014; RNA_helicase_DEAD_Q_motif.
DR   Pfam; PF00270; DEAD; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51195; Q_MOTIF; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Helicase; Hydrolase; Nucleotide-binding; RNA-binding.
FT   CHAIN           <1..>234
FT                   /note="DEAD-box ATP-dependent RNA helicase 3"
FT                   /id="PRO_0000397231"
FT   DOMAIN          151..>234
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   MOTIF           120..148
FT                   /note="Q motif"
FT                   /evidence="ECO:0000255"
FT   BINDING         164..171
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   NON_TER         1
FT                   /evidence="ECO:0000305"
FT   NON_TER         234
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   234 AA;  24786 MW;  A988479B09A361C9 CRC64;
     TRGGYLNKFT TVVASIIGVS SLYKVPTKPT TLSPPFISPK PGFMSLPPRK HEVVGGASSS
     LVAAAVSARN SVISEDLFEG LALFDKASSL EDDGGDNVSE FQASIDDVND GGGGGGDDEL
     AVSRLGLPQK LVETLEKRGI TKLFPIQRAV LVPALEGRDI IGRAKTGTGK TLAFAIPIIK
     RLTEEDEDNR NSLAGRLPRV LVLAPTRELA KQVETEIKEP APYLRTVCVY GGVS