ID   RH26_ARATH              Reviewed;         850 AA.
AC   Q9FNM7; Q9ZRZ9;
DT   30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2006, sequence version 2.
DT   03-AUG-2022, entry version 124.
DE   RecName: Full=DEAD-box ATP-dependent RNA helicase 26;
DE            EC=3.6.4.13;
GN   Name=RH26; OrderedLocusNames=At5g08610; ORFNames=MAH20.17;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=9405937; DOI=10.1093/dnares/4.4.291;
RA   Kotani H., Nakamura Y., Sato S., Kaneko T., Asamizu E., Miyajima N.,
RA   Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 5. II. Sequence
RT   features of the regions of 1,044,062 bp covered by thirteen physically
RT   assigned P1 clones.";
RL   DNA Res. 4:291-300(1997).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT   genome.";
RL   Plant J. 89:789-804(2017).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 90-684.
RC   STRAIN=cv. Columbia;
RX   PubMed=9862990; DOI=10.1093/nar/27.2.628;
RA   Aubourg S., Kreis M., Lecharny A.;
RT   "The DEAD box RNA helicase family in Arabidopsis thaliana.";
RL   Nucleic Acids Res. 27:628-636(1999).
RN   [4]
RP   GENE FAMILY, AND NOMENCLATURE.
RX   PubMed=17168887; DOI=10.1111/j.1467-7652.2004.00084.x;
RA   Mingam A., Toffano-Nioche C., Brunaud V., Boudet N., Kreis M., Lecharny A.;
RT   "DEAD-box RNA helicases in Arabidopsis thaliana: establishing a link
RT   between quantitative expression, gene structure and evolution of a family
RT   of genes.";
RL   Plant Biotechnol. J. 2:401-415(2004).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-109 AND SER-110, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=16807317; DOI=10.1093/nar/gkl429;
RA   de la Fuente van Bentem S., Anrather D., Roitinger E., Djamei A.,
RA   Hufnagl T., Barta A., Csaszar E., Dohnal I., Lecourieux D., Hirt H.;
RT   "Phosphoproteomics reveals extensive in vivo phosphorylation of Arabidopsis
RT   proteins involved in RNA metabolism.";
RL   Nucleic Acids Res. 34:3267-3278(2006).
RN   [6]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=cv. Columbia;
RX   PubMed=19245862; DOI=10.1016/j.jprot.2009.02.004;
RA   Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E.,
RA   Rathjen J.P., Peck S.C.;
RT   "Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis
RT   thaliana.";
RL   J. Proteomics 72:439-451(2009).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-109 AND SER-110, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19376835; DOI=10.1104/pp.109.138677;
RA   Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA   Grossmann J., Gruissem W., Baginsky S.;
RT   "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT   chloroplast kinase substrates and phosphorylation networks.";
RL   Plant Physiol. 150:889-903(2009).
RN   [8]
RP   GENE FAMILY.
RX   PubMed=24265739; DOI=10.1371/journal.pone.0078982;
RA   Xu R., Zhang S., Huang J., Zheng C.;
RT   "Genome-wide comparative in silico analysis of the RNA helicase gene family
RT   in Zea mays and Glycine max: a comparison with Arabidopsis and Oryza
RT   sativa.";
RL   PLoS ONE 8:E78982-E78982(2013).
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   -!- 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   -!- SIMILARITY: Belongs to the DEAD box helicase family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAB10010.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AB006697; BAB10010.1; ALT_INIT; Genomic_DNA.
DR   EMBL; CP002688; AED91329.1; -; Genomic_DNA.
DR   EMBL; AJ010474; CAA09213.1; -; mRNA.
DR   PIR; T51747; T51747.
DR   RefSeq; NP_196478.2; NM_120948.4.
DR   AlphaFoldDB; Q9FNM7; -.
DR   SMR; Q9FNM7; -.
DR   STRING; 3702.AT5G08610.1; -.
DR   iPTMnet; Q9FNM7; -.
DR   PaxDb; Q9FNM7; -.
DR   PRIDE; Q9FNM7; -.
DR   ProteomicsDB; 236944; -.
DR   EnsemblPlants; AT5G08610.1; AT5G08610.1; AT5G08610.
DR   GeneID; 830762; -.
DR   Gramene; AT5G08610.1; AT5G08610.1; AT5G08610.
DR   KEGG; ath:AT5G08610; -.
DR   Araport; AT5G08610; -.
DR   TAIR; locus:2159517; AT5G08610.
DR   eggNOG; KOG0342; Eukaryota.
DR   HOGENOM; CLU_003041_26_6_1; -.
DR   InParanoid; Q9FNM7; -.
DR   OMA; QPPIIVL; -.
DR   OrthoDB; 537587at2759; -.
DR   PhylomeDB; Q9FNM7; -.
DR   PRO; PR:Q9FNM7; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q9FNM7; baseline and differential.
DR   Genevisible; Q9FNM7; AT.
DR   GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR   GO; GO:0003729; F:mRNA binding; IDA:TAIR.
DR   GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR   Gene3D; 3.40.50.300; -; 2.
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   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
DR   PROSITE; PS51195; Q_MOTIF; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Helicase; Hydrolase; Nucleotide-binding; Phosphoprotein;
KW   Reference proteome; RNA-binding.
FT   CHAIN           1..850
FT                   /note="DEAD-box ATP-dependent RNA helicase 26"
FT                   /id="PRO_0000239166"
FT   DOMAIN          413..596
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          630..777
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   REGION          60..82
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          106..350
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           382..410
FT                   /note="Q motif"
FT   MOTIF           544..547
FT                   /note="DEAD box"
FT   COMPBIAS        106..162
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        174..188
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        197..211
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        288..302
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         426..433
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   MOD_RES         109
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:16807317,
FT                   ECO:0007744|PubMed:19376835"
FT   MOD_RES         110
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:16807317,
FT                   ECO:0007744|PubMed:19376835"
SQ   SEQUENCE   850 AA;  94186 MW;  95617D29469530CD CRC64;
     MSSKFPLGVR FITHSLPCTR LASMNSGALI YSFRSVPVLS KAFPFRLKYI GLGSRVNFST
     RPERSQPEFA RRSGAGGEIR ASKSLIEDEA ELSDWVSDLR TSSLRGKFTS DEDNADPEVV
     RRNVDRDTSR GPRRGREGQS DRFGGAKRGK EGEMDRFGSP NRRRTSGEPA DSFGNKRLGD
     REGSRNGRVQ GKSSESSFRG RSDRNVDSGS SFRGRSDKNV DSGSSFRGRN DRNVDSGSSF
     RGRSDRNVDS GSSFRGRSDR NVDSGSSFRG RNDRNVDSGS SFRGRNDRNV ESGFRREPGS
     ENNRGLGKQT RGLSLEEEDS SDDDENRVGL GNIDDLPSED SSDEDDENDE PLIKKAASAK
     AVQTDKPTGE HVKTSDSYLS KTRFDQFPLS PLSLKAIKDA GFETMTVVQE ATLPIILQGK
     DVLAKAKTGT GKTVAFLLPA IEAVIKSPPA SRDSRQPPII VLVVCPTREL ASQAAAEANT
     LLKYHPSIGV QVVIGGTKLP TEQRRMQTNP CQILVATPGR LKDHIENTSG FATRLMGVKV
     LVLDEADHLL DMGFRRDIER IIAAVPKQRQ TFLFSATVPE EVRQICHVAL KRDHEFINCV
     QEGSGETHQK VTQMYMIASL DRHFSLLHVL LKEHIADNVD YKVIIFCTTA MVTRLVADLL
     SQLSLNVREI HSRKPQSYRT RVSDEFRKSK AIILVTSDVS ARGVDYPDVS LVVQMGLPSD
     REQYIHRLGR TGRKGKEGEG VLLLAPWEEY FMSSVKDLPI TKSPLPPIDP EAVKRVQKGL
     SQVEMKNKEA AYQAWLGYYK SQKMIARDTT RLVELANEFS RSMGLDSPPA IPKNVLGKMG
     LKNVPGLRTK