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RH16_ARATH
ID   RH16_ARATH              Reviewed;         626 AA.
AC   Q9SW44; Q9ZS05;
DT   30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 134.
DE   RecName: Full=DEAD-box ATP-dependent RNA helicase 16;
DE            EC=3.6.4.13;
GN   Name=RH16; OrderedLocusNames=At4g34910; ORFNames=T11I11.150;
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=10617198; DOI=10.1038/47134;
RA   Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA   Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA   Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA   de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA   Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA   Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA   Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA   Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA   Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA   Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA   Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA   Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA   Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA   Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA   Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA   Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA   Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA   Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA   Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA   Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA   Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA   Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA   Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA   Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA   Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA   Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA   Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA   de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA   Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA   Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA   Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA   Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA   Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA   Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA   Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA   Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA   Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA   O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA   Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA   Martienssen R., McCombie W.R.;
RT   "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL   Nature 402:769-777(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 343-626.
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   -!- 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. DDX56/DBP9
CC       subfamily. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA09206.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; AL079347; CAB45452.1; -; Genomic_DNA.
DR   EMBL; AL161586; CAB80208.1; -; Genomic_DNA.
DR   EMBL; CP002687; AEE86436.1; -; Genomic_DNA.
DR   EMBL; BT002816; AAO22635.1; -; mRNA.
DR   EMBL; BT004442; AAO42436.1; -; mRNA.
DR   EMBL; AJ010467; CAA09206.1; ALT_FRAME; mRNA.
DR   PIR; T10237; T10237.
DR   PIR; T51745; T51745.
DR   RefSeq; NP_195217.1; NM_119657.3.
DR   AlphaFoldDB; Q9SW44; -.
DR   SMR; Q9SW44; -.
DR   BioGRID; 14925; 8.
DR   STRING; 3702.AT4G34910.1; -.
DR   PaxDb; Q9SW44; -.
DR   PRIDE; Q9SW44; -.
DR   ProteomicsDB; 236938; -.
DR   EnsemblPlants; AT4G34910.1; AT4G34910.1; AT4G34910.
DR   GeneID; 829643; -.
DR   Gramene; AT4G34910.1; AT4G34910.1; AT4G34910.
DR   KEGG; ath:AT4G34910; -.
DR   Araport; AT4G34910; -.
DR   TAIR; locus:2116920; AT4G34910.
DR   eggNOG; KOG0346; Eukaryota.
DR   HOGENOM; CLU_003041_17_1_1; -.
DR   InParanoid; Q9SW44; -.
DR   OMA; GYEKDFK; -.
DR   OrthoDB; 973872at2759; -.
DR   PhylomeDB; Q9SW44; -.
DR   PRO; PR:Q9SW44; -.
DR   Proteomes; UP000006548; Chromosome 4.
DR   ExpressionAtlas; Q9SW44; baseline and differential.
DR   Genevisible; Q9SW44; AT.
DR   GO; GO:0005730; C:nucleolus; 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; 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; 2.
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; Coiled coil; Helicase; Hydrolase; Nucleotide-binding;
KW   Reference proteome; RNA-binding.
FT   CHAIN           1..626
FT                   /note="DEAD-box ATP-dependent RNA helicase 16"
FT                   /id="PRO_0000239158"
FT   DOMAIN          77..259
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          293..477
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   REGION          1..48
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          363..388
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          568..626
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          9..47
FT                   /evidence="ECO:0000255"
FT   COILED          356..385
FT                   /evidence="ECO:0000255"
FT   MOTIF           46..74
FT                   /note="Q motif"
FT   MOTIF           207..210
FT                   /note="DEAD box"
FT   COMPBIAS        1..16
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        23..48
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        609..626
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         90..97
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   CONFLICT        386
FT                   /note="S -> T (in Ref. 4; CAA09206)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   626 AA;  69502 MW;  E5F4B8AE7AE45377 CRC64;
     MGKTKLKPVE DVNSEVVDEV EKAEEVEEQR NDREQEEEQK EEEAPKSFEE LGLDSRLIRA
     LTKKGIEKPT LIQQSAIPYI LEGKDVVARA KTGSGKTLAY LLPLLQKLFS ADSVSKKKLA
     PSAFILVPSR ELCQQVYTEV SSLIELCRVQ LKAVQLTSSM SASDMRNALA GLPEILVSTP
     ACIPKCFAAG VLEPTAVSES LSILVLDEAD LLLSYGYEDN LRSVTSIIPR RCQCLLMSAT
     TSSDVEKLKK LILHNPIVLT LTEDNDKEEA VPSNVQQFWI SCSAQDKLLH ILALLKLEVV
     QKKILIFINT IDMGFRLKLF LEKFGIKSAI LNGELPQNSR LHILEQFNAG LFDYLIATDD
     NSQTKKQKEE AKGEANKENK KNNKRSKPKL DAEFGVVRGI DFKKVHTVIN FDMPQSVTGY
     IHRIGRTGRA YSSGSSVSLI SPDEMEGFED IKSFLASDKN KDIDIITPFP LLTENAVESL
     RYRAEDVAKS VTKIAVRESR AQDLRNEIIN SEKLKAHFEA NPRDLDLLRH DKPLSKTAPA
     PHLKDIPEYL VDAKTQEASK MVKLARAAMG NTRRSGGGGG RNNKNKKRSR KGSDPLKTFN
     PNGSKRGAVG QKDGKDSSST KKQKTV
 
 
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