ID   RH9_ARATH               Reviewed;         610 AA.
AC   Q9LUW6; Q9ZS11;
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 9, mitochondrial;
DE            EC=3.6.4.13;
DE   Flags: Precursor;
GN   Name=RH9; OrderedLocusNames=At3g22310; ORFNames=MCB17.17, MCB17.3;
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   NUCLEOTIDE SEQUENCE [MRNA] OF 248-610.
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   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=cv. Landsberg erecta;
RX   PubMed=17272265; DOI=10.1074/mcp.m600408-mcp200;
RA   Maor R., Jones A., Nuehse T.S., Studholme D.J., Peck S.C., Shirasu K.;
RT   "Multidimensional protein identification technology (MudPIT) analysis of
RT   ubiquitinated proteins in plants.";
RL   Mol. Cell. Proteomics 6:601-610(2007).
RN   [7]
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   [8]
RP   IDENTIFICATION BY MASS SPECTROMETRY, AND CLEAVAGE OF TRANSIT PEPTIDE AFTER
RP   ASP-66.
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; BAB01768.1; -; Genomic_DNA.
DR   EMBL; CP002686; AEE76620.1; -; Genomic_DNA.
DR   EMBL; AY091091; AAM14042.1; -; mRNA.
DR   EMBL; AJ010461; CAA09200.1; -; mRNA.
DR   PIR; T51341; T51341.
DR   RefSeq; NP_188870.1; NM_113129.4.
DR   AlphaFoldDB; Q9LUW6; -.
DR   SMR; Q9LUW6; -.
DR   BioGRID; 7132; 10.
DR   IntAct; Q9LUW6; 8.
DR   STRING; 3702.AT3G22310.1; -.
DR   iPTMnet; Q9LUW6; -.
DR   PaxDb; Q9LUW6; -.
DR   PRIDE; Q9LUW6; -.
DR   ProteomicsDB; 236260; -.
DR   EnsemblPlants; AT3G22310.1; AT3G22310.1; AT3G22310.
DR   GeneID; 821800; -.
DR   Gramene; AT3G22310.1; AT3G22310.1; AT3G22310.
DR   KEGG; ath:AT3G22310; -.
DR   Araport; AT3G22310; -.
DR   TAIR; locus:2087832; AT3G22310.
DR   eggNOG; KOG0331; Eukaryota.
DR   HOGENOM; CLU_003041_29_1_1; -.
DR   InParanoid; Q9LUW6; -.
DR   OrthoDB; 1139373at2759; -.
DR   PhylomeDB; Q9LUW6; -.
DR   PRO; PR:Q9LUW6; -.
DR   Proteomes; UP000006548; Chromosome 3.
DR   ExpressionAtlas; Q9LUW6; baseline and differential.
DR   Genevisible; Q9LUW6; AT.
DR   GO; GO:0005737; C:cytoplasm; IDA:TAIR.
DR   GO; GO:0005829; C:cytosol; HDA:TAIR.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0032991; C:protein-containing complex; IDA:TAIR.
DR   GO; GO:0019034; C:viral replication 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:0003677; F:DNA binding; IDA:TAIR.
DR   GO; GO:0003723; F:RNA binding; IDA:TAIR.
DR   GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR   GO; GO:0000373; P:Group II intron splicing; IBA:GO_Central.
DR   GO; GO:0009409; P:response to cold; IEP:TAIR.
DR   GO; GO:0009651; P:response to salt stress; IMP:TAIR.
DR   GO; GO:0009414; P:response to water deprivation; IMP:TAIR.
DR   GO; GO:0006364; P:rRNA processing; IBA:GO_Central.
DR   GO; GO:0039694; P:viral RNA genome replication; IMP:TAIR.
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..66
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000269|PubMed:25732537"
FT   CHAIN           67..610
FT                   /note="DEAD-box ATP-dependent RNA helicase 9,
FT                   mitochondrial"
FT                   /id="PRO_0000239151"
FT   DOMAIN          147..321
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          350..494
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   REGION          542..610
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           116..144
FT                   /note="Q motif"
FT   MOTIF           269..272
FT                   /note="DEAD box"
FT   COMPBIAS        552..604
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         160..167
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ   SEQUENCE   610 AA;  63609 MW;  E85F6FAAF3C3C432 CRC64;
     MISTVLRRSI LGTSRRTLAA SVTSINAALF HNLAPAAATV SDLANGATNV KSLPSNSSPF
     GVKVRDFHVK SVPSEFRSSI VSSAGFAAQE YAPSYENDGG IGDSESVGSS GGGDGLAIAD
     LGISPEIVKA LKGRGIEKLF PIQKAVLEPA MEGRDMIGRA RTGTGKTLAF GIPIIDKIIK
     FNAKHGRGKN PQCLVLAPTR ELARQVEKEF RESAPSLDTI CLYGGTPIGQ QMRELNYGID
     VAVGTPGRII DLMKRGALNL SEVQFVVLDE ADQMLQVGFA EDVEIILQKL PAKRQSMMFS
     ATMPSWIRSL TKKYLNNPLT IDLVGDSDQK LADGITMYSI AADSYGRASI IGPLVKEHGK
     GGKCIVFTQT KRDADRLAFG LAKSYKCEAL HGDISQAQRE RTLAGFRDGN FSILVATDVA
     ARGLDVPNVD LVIHYELPNN TETFVHRTGR TGRAGKKGSA ILIHGQDQTR AVKMIEKEVG
     SRFNELPSIA VERGSASMFE GVGARSGGSF GGGRSGGGGY GSYGSSSGRS GGGSYGGYGG
     SSGRSGGGGG SYGGSGGSSS RYSGGSDRSS GFGSFGSGGS SGGFGSDRSS QSSGRSSFGG
     FGSNDGKRSY