RH6_ARATH
ID RH6_ARATH Reviewed; 528 AA.
AC Q94BV4; O80838; Q9SB95;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2006, sequence version 2.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=DEAD-box ATP-dependent RNA helicase 6;
DE EC=3.6.4.13;
GN Name=RH6; OrderedLocusNames=At2g45810; ORFNames=F4I18.21;
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=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
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 [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 384-528.
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 [5]
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 [6]
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 -!- FUNCTION: ATP-dependent RNA helicase involved in mRNA turnover, and
CC more specifically in mRNA decapping. {ECO:0000250}.
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}. Note=Is
CC 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}.
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. DDX6/DHH1
CC subfamily. {ECO:0000305}.
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DR EMBL; AC004665; AAC28543.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC10604.1; -; Genomic_DNA.
DR EMBL; AY039862; AAK63966.1; -; mRNA.
DR EMBL; BT002709; AAO11625.1; -; mRNA.
DR EMBL; AJ010459; CAA09198.1; -; mRNA.
DR PIR; T02466; T02466.
DR PIR; T51740; T51740.
DR RefSeq; NP_182105.1; NM_130144.4.
DR AlphaFoldDB; Q94BV4; -.
DR SMR; Q94BV4; -.
DR BioGRID; 4525; 2.
DR IntAct; Q94BV4; 1.
DR STRING; 3702.AT2G45810.1; -.
DR iPTMnet; Q94BV4; -.
DR PaxDb; Q94BV4; -.
DR PRIDE; Q94BV4; -.
DR ProteomicsDB; 236948; -.
DR EnsemblPlants; AT2G45810.1; AT2G45810.1; AT2G45810.
DR GeneID; 819189; -.
DR Gramene; AT2G45810.1; AT2G45810.1; AT2G45810.
DR KEGG; ath:AT2G45810; -.
DR Araport; AT2G45810; -.
DR TAIR; locus:2050715; AT2G45810.
DR eggNOG; KOG0326; Eukaryota.
DR HOGENOM; CLU_003041_30_0_1; -.
DR InParanoid; Q94BV4; -.
DR OMA; NCIDIQA; -.
DR OrthoDB; 583315at2759; -.
DR PhylomeDB; Q94BV4; -.
DR PRO; PR:Q94BV4; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q94BV4; baseline and differential.
DR Genevisible; Q94BV4; AT.
DR GO; GO:0010494; C:cytoplasmic stress granule; IBA:GO_Central.
DR GO; GO:0000932; C:P-body; IBA:GO_Central.
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; HDA:TAIR.
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:0017148; P:negative regulation of translation; IBA:GO_Central.
DR GO; GO:0033962; P:P-body assembly; IBA:GO_Central.
DR GO; GO:0034063; P:stress granule assembly; IBA:GO_Central.
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; IPR000629; RNA-helicase_DEAD-box_CS.
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; PS00039; DEAD_ATP_HELICASE; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS51195; Q_MOTIF; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Cytoplasm; Helicase; Hydrolase; mRNA processing;
KW mRNA transport; Nucleotide-binding; Phosphoprotein; Reference proteome;
KW RNA-binding; Translation regulation; Transport.
FT CHAIN 1..528
FT /note="DEAD-box ATP-dependent RNA helicase 6"
FT /id="PRO_0000239147"
FT DOMAIN 185..355
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 365..525
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..80
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 154..182
FT /note="Q motif"
FT MOTIF 303..306
FT /note="DEAD box"
FT COMPBIAS 32..46
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 55..80
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 198..205
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT MOD_RES 260
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9CAI7"
FT CONFLICT 160
FT /note="F -> L (in Ref. 3; AAK63966/AAO11625)"
FT /evidence="ECO:0000305"
FT CONFLICT 384..388
FT /note="TLFSK -> FYLLQ (in Ref. 4; CAA09198)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 528 AA; 60421 MW; 3301FFB9D8E37E27 CRC64;
MNNNNNNRGR FPPGIGAAGP GPDPNFQSRN PNPPQPQQYL QSRTPFPQQP QPQPPQYLQS
QSDAQQYVQR GYPQQIQQQQ QLQQQQQQQQ QQQEQQWSRR AQLPGDPSYI DEVEKTVQSE
AISDSNNEDW KATLKLPPRD NRYQTEDVTA TKGNEFEDYF LKRDLLRGIY EKGFEKPSPI
QEESIPIALT GSDILARAKN GTGKTGAFCI PTLEKIDPEN NVIQAVILVP TRELALQTSQ
VCKELSKYLK IEVMVTTGGT SLRDDIMRLY QPVHLLVGTP GRILDLAKKG VCVLKDCAML
VMDEADKLLS VEFQPSIEEL IQFLPESRQI LMFSATFPVT VKSFKDRYLK KPYIINLMDQ
LTLMGVTQYY AFVEERQKVH CLNTLFSKLQ INQSIIFCNS VNRVELLAKK ITELGYSCFY
IHAKMVQDHR NRVFHDFRNG ACRNLVCTDL FTRGIDIQAV NVVINFDFPR TSESYLHRVG
RSGRFGHLGL AVNLVTYEDR FKMYQTEQEL GTEIKPIPSL IDKAIYCQ
