RH53_ARATH
ID RH53_ARATH Reviewed; 616 AA.
AC Q9LUW5;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=DEAD-box ATP-dependent RNA helicase 53, mitochondrial;
DE EC=3.6.4.13;
DE Flags: Precursor;
GN Name=RH53; OrderedLocusNames=At3g22330; ORFNames=MCB17.5;
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=10819329; DOI=10.1093/dnares/7.2.131;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence
RT features of the regions of 4,504,864 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:131-135(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].
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).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND CLEAVAGE OF TRANSIT PEPTIDE AFTER
RP ALA-81.
RX PubMed=25732537; DOI=10.1093/jxb/erv064;
RA Carrie C., Venne A.S., Zahedi R.P., Soll J.;
RT "Identification of cleavage sites and substrate proteins for two
RT mitochondrial intermediate peptidases in Arabidopsis thaliana.";
RL J. Exp. Bot. 66:2691-2708(2015).
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: Mitochondrion {ECO:0000305|PubMed:25732537}.
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; AB022215; BAB01770.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE76622.1; -; Genomic_DNA.
DR EMBL; AY062502; AAL32580.1; -; mRNA.
DR EMBL; AY093256; AAM13255.1; -; mRNA.
DR RefSeq; NP_188872.2; NM_113131.5.
DR AlphaFoldDB; Q9LUW5; -.
DR SMR; Q9LUW5; -.
DR STRING; 3702.AT3G22330.1; -.
DR iPTMnet; Q9LUW5; -.
DR PaxDb; Q9LUW5; -.
DR PRIDE; Q9LUW5; -.
DR ProteomicsDB; 237001; -.
DR EnsemblPlants; AT3G22330.1; AT3G22330.1; AT3G22330.
DR GeneID; 821802; -.
DR Gramene; AT3G22330.1; AT3G22330.1; AT3G22330.
DR KEGG; ath:AT3G22330; -.
DR Araport; AT3G22330; -.
DR TAIR; locus:2087852; AT3G22330.
DR eggNOG; KOG0331; Eukaryota.
DR HOGENOM; CLU_003041_29_1_1; -.
DR InParanoid; Q9LUW5; -.
DR OMA; ATMPGWI; -.
DR OrthoDB; 1139373at2759; -.
DR PhylomeDB; Q9LUW5; -.
DR PRO; PR:Q9LUW5; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LUW5; baseline and differential.
DR Genevisible; Q9LUW5; AT.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR GO; GO:0005730; C:nucleolus; HDA:TAIR.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0009505; C:plant-type cell wall; HDA:TAIR.
DR GO; GO:0032991; C:protein-containing complex; 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:0003729; F:mRNA binding; IDA:TAIR.
DR GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR GO; GO:0000373; P:Group II intron splicing; IMP:TAIR.
DR GO; GO:0009409; P:response to cold; IEP:TAIR.
DR GO; GO:0006364; P:rRNA processing; 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; 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 1: Evidence at protein level;
KW ATP-binding; Helicase; Hydrolase; Mitochondrion; Nucleotide-binding;
KW Reference proteome; RNA-binding; Transit peptide.
FT TRANSIT 1..81
FT /note="Mitochondrion"
FT /evidence="ECO:0000269|PubMed:25732537"
FT CHAIN 82..616
FT /note="DEAD-box ATP-dependent RNA helicase 53,
FT mitochondrial"
FT /id="PRO_0000239193"
FT DOMAIN 135..309
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 338..482
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 489..616
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 104..132
FT /note="Q motif"
FT MOTIF 257..260
FT /note="DEAD box"
FT COMPBIAS 527..542
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 557..610
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 148..155
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 616 AA; 65359 MW; E09A8CE1EC635C31 CRC64;
MITTVLRRSL LDASKRNLSA SLTSINTVLF HNLAPAATRV SDLALIGSSD VKAGFPFGVE
AKGIHFQSGP LDFRASMVSQ AGFAISESSE RRVGDSESVG GDGLAISELG ISPEIVKALS
SKGIEKLFPI QKAVLEPAME GRDMIGRART GTGKTLAFGI PIIDKIIKYN AKHGRGRNPL
CLVLAPTREL ARQVEKEFRE SAPSLDTICL YGGTPIGQQM RQLDYGVDVA VGTPGRVIDL
MKRGALNLSE VQFVVLDEAD QMLQVGFAED VEIILEKLPE KRQSMMFSAT MPSWIRSLTK
KYLNNPLTVD LVGDSDQKLA DGITTYSIIA DSYGRASIIG PLVTEHAKGG KCIVFTQTKR
DADRLSYALA RSFKCEALHG DISQSQRERT LAGFRDGHFN ILVATDVAAR GLDVPNVDLI
IHYELPNNTE TFVHRTGRTG RAGKKGSAIL IYSQDQSRAV KIIEREVGSR FTELPSIAVE
RGSASMFEGI GSRSGGSFGG GMRDRGSSFG GRSGGGGYGG SSGGYGGGRS GGSSNRYSGD
SDRSGFGSFG MRSPEGYGSD RSSQSGGRSS FGGGRSGGSS NNRSSGFGDF GSDRSSQSGG
RSSFGGFGSN DGKRSY
