RH45_ARATH
ID RH45_ARATH Reviewed; 989 AA.
AC Q9SF41;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=DEAD-box ATP-dependent RNA helicase 45;
DE EC=3.6.4.13;
GN Name=RH45; OrderedLocusNames=At3g09620; ORFNames=F11F8_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=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 [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 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 [4]
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. DDX46/PRP5
CC subfamily. {ECO:0000305}.
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DR EMBL; AC016661; AAF23310.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE74788.1; -; Genomic_DNA.
DR RefSeq; NP_187573.1; NM_111796.1.
DR AlphaFoldDB; Q9SF41; -.
DR SMR; Q9SF41; -.
DR STRING; 3702.AT3G09620.1; -.
DR PaxDb; Q9SF41; -.
DR PRIDE; Q9SF41; -.
DR EnsemblPlants; AT3G09620.1; AT3G09620.1; AT3G09620.
DR GeneID; 820119; -.
DR Gramene; AT3G09620.1; AT3G09620.1; AT3G09620.
DR KEGG; ath:AT3G09620; -.
DR Araport; AT3G09620; -.
DR TAIR; locus:2074899; AT3G09620.
DR eggNOG; KOG0334; Eukaryota.
DR HOGENOM; CLU_003041_0_1_1; -.
DR InParanoid; Q9SF41; -.
DR OMA; NREHERD; -.
DR PhylomeDB; Q9SF41; -.
DR PRO; PR:Q9SF41; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9SF41; baseline and differential.
DR Genevisible; Q9SF41; AT.
DR GO; GO:0005634; C:nucleus; 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:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; 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; 2.
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 3: Inferred from homology;
KW ATP-binding; Coiled coil; Helicase; Hydrolase; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; RNA-binding.
FT CHAIN 1..989
FT /note="DEAD-box ATP-dependent RNA helicase 45"
FT /id="PRO_0000239185"
FT DOMAIN 427..605
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 590..748
FT /note="Helicase C-terminal"
FT REGION 1..248
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 305..330
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 88..182
FT /evidence="ECO:0000255"
FT MOTIF 396..424
FT /note="Q motif"
FT MOTIF 553..556
FT /note="DEAD box"
FT COMPBIAS 1..186
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 195..221
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 440..447
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT MOD_RES 119
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8H0U8"
FT MOD_RES 200
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8H0U8"
SQ SEQUENCE 989 AA; 111625 MW; 9ED3B785DB6640EC CRC64;
MLEKSKSRKE NDRKDRDRSK KENGRRDTTE MRSRVKRCDS EEEERIRIRR DRKSSDFEEE
EYERDSKRRG EDKGRGRRER DRDRGKYLKR DRERREREKE KGRKKQKKER SREDCNEESD
DVKCGLKRKR TERSRHGDDD VEKKTRDEQV EDEQKQLAEE VEKRRRRVQE WQELKRQNEE
AQIESKGPET GKAWTLDGES DDEVKSDSEM DVDRDTKLEN GGDAKMVASE NETAVTVSEN
GGDRAADEDE IDPLDAFMNT MVLPEVEKLS NIVIDGILDF KMNGKETGDQ AKKGFNKAAL
GRIIQGEDSD SDYSEPKSDD DPSLDEDDEE FMKRVKKTKA EKLSLVDHSK IEYEPFRKNF
YIEVKDISRM TQDAVNAYRK ELELKVHGKD VPRPIQFWHQ TGLTSKILDT LKKLNYEKPM
PIQAQALPII MSGRDCIGVA KTGSGKTLGF VLPMLRHIKD QPPVEAGDGP IGLVMAPTRE
LVQQIYSDIR KFSKALGIIC VPVYGGSGVA QQISELKRGT EIVVCTPGRM IDILCTSSGK
ITNLRRVTYL VMDEADRMFD MGFEPQITRI VQNIRPDRQT VLFSATFPRQ VETLARKVLN
KPVEIQVGGR SVVNKDITQL VEIRPESERF SRLLELLGEW YEKGKVLVFV RSQEKSISDF
KSDVCNLLIA TSVAARGLDV KELELVVNFD APNHYEDYVH RVGRTGRAGR KGCAVTFISE
DDAKYAPDLV KALELSEQPV PDDVKAVAEG FMAKVKQGIE QAHGTGYGGS GFKFNEEEDE
VRKAAKKAQA KEYGFEEEKS DSEDENDVVR KAGGDISQQQ ITLAQIAAIA SAASKAPVTA
NQLLPNGGGL ATEPGIPPTD GAGRVAAMIA AANVQQYLAK IQADAIPEHY EAELEINDFP
QNARWKVTHK ETLGPISEWS GASITTRGKF YEAGRIPGPE ERKLYLFVEG PTEISVKTAK
AELKRVLEDI TNQTFSLPGG AQSGRYSVL
