RH58_ARATH
ID RH58_ARATH Reviewed; 472 AA.
AC Q3E9C3; Q84W18;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=DEAD-box ATP-dependent RNA helicase 58, chloroplastic;
DE EC=3.6.4.13;
DE Flags: Precursor;
GN Name=RH58; OrderedLocusNames=At5g19210; ORFNames=T24G5.110;
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=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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 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 [5]
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: Plastid, chloroplast {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q3E9C3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q3E9C3-2; Sequence=VSP_019107;
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 -!- MISCELLANEOUS: [Isoform 2]: May be due to a competing acceptor splice
CC site. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. {ECO:0000305}.
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DR EMBL; AC069326; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CP002688; AED92670.1; -; Genomic_DNA.
DR EMBL; CP002688; AED92671.1; -; Genomic_DNA.
DR EMBL; CP002688; ANM69255.1; -; Genomic_DNA.
DR EMBL; BT004328; AAO42322.1; -; mRNA.
DR RefSeq; NP_001330950.1; NM_001343593.1. [Q3E9C3-2]
DR RefSeq; NP_197422.2; NM_121926.2. [Q3E9C3-2]
DR RefSeq; NP_974812.1; NM_203083.2. [Q3E9C3-1]
DR AlphaFoldDB; Q3E9C3; -.
DR SMR; Q3E9C3; -.
DR STRING; 3702.AT5G19210.2; -.
DR PaxDb; Q3E9C3; -.
DR PRIDE; Q3E9C3; -.
DR ProteomicsDB; 236931; -. [Q3E9C3-1]
DR EnsemblPlants; AT5G19210.1; AT5G19210.1; AT5G19210. [Q3E9C3-2]
DR EnsemblPlants; AT5G19210.2; AT5G19210.2; AT5G19210. [Q3E9C3-1]
DR EnsemblPlants; AT5G19210.3; AT5G19210.3; AT5G19210. [Q3E9C3-2]
DR GeneID; 832041; -.
DR Gramene; AT5G19210.1; AT5G19210.1; AT5G19210. [Q3E9C3-2]
DR Gramene; AT5G19210.2; AT5G19210.2; AT5G19210. [Q3E9C3-1]
DR Gramene; AT5G19210.3; AT5G19210.3; AT5G19210. [Q3E9C3-2]
DR KEGG; ath:AT5G19210; -.
DR Araport; AT5G19210; -.
DR TAIR; locus:2182202; AT5G19210.
DR eggNOG; KOG0327; Eukaryota.
DR HOGENOM; CLU_003041_2_1_1; -.
DR InParanoid; Q3E9C3; -.
DR OMA; RRFLHDC; -.
DR OrthoDB; 1223767at2759; -.
DR PhylomeDB; Q3E9C3; -.
DR PRO; PR:Q3E9C3; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q3E9C3; baseline and differential.
DR Genevisible; Q3E9C3; AT.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0005681; C:spliceosomal complex; 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; IBA:GO_Central.
DR GO; GO:0003724; F:RNA helicase activity; IBA:GO_Central.
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 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 Alternative splicing; ATP-binding; Chloroplast; Helicase; Hydrolase;
KW Nucleotide-binding; Plastid; Reference proteome; RNA-binding;
KW Transit peptide.
FT TRANSIT 1..54
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 55..472
FT /note="DEAD-box ATP-dependent RNA helicase 58,
FT chloroplastic"
FT /id="PRO_0000239197"
FT DOMAIN 107..286
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 314..472
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT MOTIF 76..104
FT /note="Q motif"
FT MOTIF 231..234
FT /note="DEAD box"
FT BINDING 120..127
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT VAR_SEQ 1..157
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14593172"
FT /id="VSP_019107"
SQ SEQUENCE 472 AA; 52811 MW; 074057EA6DB630BB CRC64;
MASQLLNVPH LAFFPKISYA SVFSTLKPSF FHSTSTRRAL KSSPSSRIIN LQAVAETSSE
IESNSVTETT VPLTLRQICQ GFVPEHILHR MEEIGFVFPT DIQREALPTL FTGRDCILHA
QTGSGKTLTY LLLIFSLINP QRSSVQAVIV VPTRELGMQV TKVARMLAAK SEIDVKGCTV
MALLDGGTLR RHKSWLKAEP PAILVATVAS LCHMLEKHIF RIDSVRVLVV DEVDFLFYSS
KQVGSVRKLL TSFSSCDKRQ TVFASASIPQ HKHFVHDCIQ QKWTKRDVVH VHVSAIMPMP
LCLLHRFVMC EKTNKHQVLL ALLESDAPES AIIFVGEQSE KSKKAGNDPS TTLLMEFLKT
SYKGSLEILL LEGDMNFNSR AASLTEIRQG GGFLLVSTDI AARGIDLPET THIFNFDLPQ
TVTDYLHRAG RAGRKPFSDR KCIVANLITS EERFVLQRYE NELMFSCEEM ML
