RH7_ARATH
ID RH7_ARATH Reviewed; 671 AA.
AC Q39189; Q94BX7; Q9LVB7;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2006, sequence version 2.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=DEAD-box ATP-dependent RNA helicase 7;
DE EC=3.6.4.13;
GN Name=RH7; Synonyms=PRH75; OrderedLocusNames=At5g62190; ORFNames=MMI9.2;
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 [MRNA].
RC TISSUE=Hypocotyl;
RX PubMed=9121476; DOI=10.1128/mcb.17.4.2257;
RA Lorkovic Z.J., Herrmann R.G., Oelmueller R.;
RT "PRH 75, a new nuclear-localized member of the DEAD-box protein family from
RT higher plants.";
RL Mol. Cell. Biol. 17:2257-2265(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10718197; DOI=10.1093/dnares/7.1.31;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. X. Sequence
RT features of the regions of 3,076,755 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:31-63(2000).
RN [3]
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 [4]
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 [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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-40 AND SER-42, 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 [7]
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 -!- SUBCELLULAR LOCATION: Nucleus {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. DDX21/DDX50
CC subfamily. {ECO:0000305}.
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DR EMBL; X99938; CAA68194.1; -; mRNA.
DR EMBL; AB019235; BAA97183.1; -; Genomic_DNA.
DR EMBL; CP002688; AED97579.1; -; Genomic_DNA.
DR EMBL; AY039576; AAK62631.1; -; mRNA.
DR EMBL; AY056137; AAL07216.1; -; mRNA.
DR EMBL; BT008581; AAP40408.1; -; mRNA.
DR RefSeq; NP_201025.1; NM_125613.3.
DR AlphaFoldDB; Q39189; -.
DR SMR; Q39189; -.
DR BioGRID; 21584; 4.
DR IntAct; Q39189; 2.
DR STRING; 3702.AT5G62190.1; -.
DR iPTMnet; Q39189; -.
DR PaxDb; Q39189; -.
DR PRIDE; Q39189; -.
DR ProteomicsDB; 236896; -.
DR EnsemblPlants; AT5G62190.1; AT5G62190.1; AT5G62190.
DR GeneID; 836340; -.
DR Gramene; AT5G62190.1; AT5G62190.1; AT5G62190.
DR KEGG; ath:AT5G62190; -.
DR Araport; AT5G62190; -.
DR TAIR; locus:2167903; AT5G62190.
DR eggNOG; KOG0331; Eukaryota.
DR HOGENOM; CLU_003041_20_0_1; -.
DR InParanoid; Q39189; -.
DR OMA; KQVHTDF; -.
DR OrthoDB; 1139373at2759; -.
DR PhylomeDB; Q39189; -.
DR BRENDA; 3.6.4.13; 399.
DR PRO; PR:Q39189; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q39189; baseline and differential.
DR Genevisible; Q39189; AT.
DR GO; GO:0005730; C:nucleolus; IDA:TAIR.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0017151; F:DEAD/H-box RNA helicase binding; ISS:TAIR.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0003724; F:RNA helicase activity; IDA:TAIR.
DR GO; GO:0016070; P:RNA metabolic process; IDA:TAIR.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR012562; GUCT.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000629; RNA-helicase_DEAD-box_CS.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF08152; GUCT; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF54928; SSF54928; 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 1: Evidence at protein level;
KW ATP-binding; Helicase; Hydrolase; Nucleotide-binding; Nucleus;
KW Phosphoprotein; Reference proteome; RNA-binding.
FT CHAIN 1..671
FT /note="DEAD-box ATP-dependent RNA helicase 7"
FT /id="PRO_0000239148"
FT DOMAIN 127..309
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 339..479
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..84
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 627..671
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 96..124
FT /note="Q motif"
FT MOTIF 255..258
FT /note="DEAD box"
FT BINDING 140..147
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT MOD_RES 40
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19376835"
FT MOD_RES 42
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19376835"
FT CONFLICT 104
FT /note="S -> P (in Ref. 2; AAK62631)"
FT /evidence="ECO:0000305"
FT CONFLICT 196
FT /note="A -> E (in Ref. 2; AAK62631)"
FT /evidence="ECO:0000305"
FT CONFLICT 214
FT /note="Y -> I (in Ref. 1; CAA68194)"
FT /evidence="ECO:0000305"
FT CONFLICT 249..250
FT /note="LQ -> FK (in Ref. 1; CAA68194)"
FT /evidence="ECO:0000305"
FT CONFLICT 446
FT /note="A -> P (in Ref. 1; CAA68194)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 671 AA; 72891 MW; FBFD888C79F7E35C CRC64;
MPSLMLSDKK EEKKMKKKMA LDTPELDSKK GKKEQKLKLS DSDEEESEKK KSKKKDKKRK
ASEEEDEVKS DSSSEKKKSS KKVKLGVEDV EVDNPNAVSK FRISAPLREK LKANGIEALF
PIQASTFDMV LDGADLVGRA RTGQGKTLAF VLPILESLVN GPAKSKRKMG YGRSPSVLVL
LPTRELAKQV AADFDAYGGS LGLSSCCLYG GDSYPVQEGK LKRGVDIVVG TPGRIKDHIE
RQNLDFSYLQ FRVLDEADEM LRMGFVEDVE LILGKVEDST KVQTLLFSAT LPSWVKNISN
RFLKRDQKTI DLVGNDKMKA SNSVRHIAIP CNKAAMARLI PDIISCYSSG GQTIIFAETK
VQVSELSGLL DGSRALHGEI PQSQREVTLA GFRNGKFATL VATNVAARGL DINDVQLIIQ
CEPPREVEAY IHRSGRTGRA GNTGVAVTLY DSRKSSVSRI EKEAGIKFEH LAAPQPDEIA
RSGGMEAAEK VKQVCDSVVP AFLEAAKELL ETSGLSAEVL LAKALAKTAG FTEIKKRSLL
TSMENYVTLH LEAGKPIYSP SFVYGLLRRV LPDDKVEMIE GLSLTADKTG AVFDVKQSDL
DLFIAGAQKS AGSMSLEVVK VMPKLQEREP LPQKRFGGGG RGNRFGGGGG NRFGGGGGRG
RGGSGGRGQR Y
