RH50_ARATH
ID RH50_ARATH Reviewed; 781 AA.
AC Q8GUG7; Q9M901;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2006, sequence version 2.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=DEAD-box ATP-dependent RNA helicase 50;
DE EC=3.6.4.13;
GN Name=RH50; Synonyms=HEL; OrderedLocusNames=At3g06980; ORFNames=F17A9.13;
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 STRAIN=cv. Columbia;
RA Li J., Dodeman C., Bergounioux C.;
RT "DEAD box RNA-helicase expression.";
RL Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(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 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: Probably involved in resistance to biotic and abiotic
CC stresses. {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 -!- 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}.
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DR EMBL; AJ296275; CAC82719.1; -; mRNA.
DR EMBL; AC016827; AAF27002.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE74483.1; -; Genomic_DNA.
DR EMBL; AY048260; AAK82522.1; -; mRNA.
DR EMBL; AY113064; AAM47372.1; -; mRNA.
DR EMBL; BT002520; AAO00880.1; -; mRNA.
DR RefSeq; NP_187354.1; NM_111578.2.
DR AlphaFoldDB; Q8GUG7; -.
DR SMR; Q8GUG7; -.
DR BioGRID; 5218; 3.
DR IntAct; Q8GUG7; 5.
DR STRING; 3702.AT3G06980.1; -.
DR PaxDb; Q8GUG7; -.
DR PRIDE; Q8GUG7; -.
DR ProteomicsDB; 236170; -.
DR EnsemblPlants; AT3G06980.1; AT3G06980.1; AT3G06980.
DR GeneID; 819883; -.
DR Gramene; AT3G06980.1; AT3G06980.1; AT3G06980.
DR KEGG; ath:AT3G06980; -.
DR Araport; AT3G06980; -.
DR TAIR; locus:2077592; AT3G06980.
DR eggNOG; KOG0331; Eukaryota.
DR HOGENOM; CLU_003041_24_2_1; -.
DR InParanoid; Q8GUG7; -.
DR OMA; HMSHNEE; -.
DR OrthoDB; 1223767at2759; -.
DR PhylomeDB; Q8GUG7; -.
DR PRO; PR:Q8GUG7; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q8GUG7; baseline and differential.
DR Genevisible; Q8GUG7; 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; ISS:UniProtKB.
DR GO; GO:0006968; P:cellular defense response; ISS:UniProtKB.
DR GO; GO:0071369; P:cellular response to ethylene stimulus; IEA:EnsemblPlants.
DR GO; GO:0071395; P:cellular response to jasmonic acid stimulus; IEA:EnsemblPlants.
DR GO; GO:0071446; P:cellular response to salicylic acid stimulus; IEA:EnsemblPlants.
DR GO; GO:0050832; P:defense response to fungus; IEA:EnsemblPlants.
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 2: Evidence at transcript level;
KW ATP-binding; Helicase; Hydrolase; Nucleotide-binding; Plant defense;
KW Reference proteome; RNA-binding.
FT CHAIN 1..781
FT /note="DEAD-box ATP-dependent RNA helicase 50"
FT /id="PRO_0000239190"
FT DOMAIN 405..586
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 621..781
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 72..103
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 117..148
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 166..240
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 254..292
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 313..342
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 374..402
FT /note="Q motif"
FT MOTIF 533..536
FT /note="DEAD box"
FT COMPBIAS 77..100
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 170..198
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 213..230
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 254..277
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 313..329
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 418..425
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT CONFLICT 529
FT /note="C -> F (in Ref. 4; AAO00880)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 781 AA; 87429 MW; 85651709B81C804E CRC64;
MLARAPPPYF NFPARNNTIC NRNEIVRLFR NGGGVVARGA GFTRRPLETS SSYDDSTDDG
FVIISAADKE NEFAPPPSSD LLSSIPSESA RRNGSRSRGL TASFGRLKAQ KVKALVGKVT
QKKQHMSHNE EEDEDDASDE NYSADEGFGS SSILDLMRKK LAMKAIPRSG KSAERNEVKR
ASKVRESRES RRDLDRLEGD DEDVDEVSNP DRFTDNQRAG SRSSYSKGGY AANSRGKGDR
LSVARDLDSF EGHGRAIDEV SNPRKFNDNE RAESRSSYSR DSSANSRGRE DRRFVAKELD
TFQGRDKAYD EVYNPRRFTD NERGLRGGSH SKGSDTNSRG WGDRRSVVYT RDMDDWRERN
KTKDTRETGF FSRKTFAEIG CSEDMMKALK EQNFDRPAHI QAMAFSPVID GKSCIIADQS
GSGKTLAYLV PVIQRLREEE LQGHSKSSPG CPRVIVLVPT AELASQVLAN CRSISKSGVP
FRSMVVTGGF RQRTQLENLE QGVDVLIATP GRFTYLMNEG ILGLSNLRCA ILDEVDILFG
DDEFEAALQN LINSSPVTAQ YLFVTATLPL EIYNKLVEVF PDCEVVMGPR VHRVSNALEE
FLVDCSGDDN AEKTPETAFQ NKKTALLQIM EENPVSKTII FCNKIETCRK VENIFKRVDR
KERQLHVLPF HAALSQESRL TNMQEFTSSQ PEENSLFLVC TDRASRGIDF SGVDHVVLFD
FPRDPSEYVR RVGRTARGAR GKGKAFIFVV GKQVGLARRI IERNEKGHPV HDVPNAYEFT
T
