ID   RH29_ARATH              Reviewed;         845 AA.
AC   O49289;
DT   30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   03-AUG-2022, entry version 132.
DE   RecName: Full=Putative DEAD-box ATP-dependent RNA helicase 29;
DE            EC=3.6.4.13;
GN   Name=RH29; OrderedLocusNames=At1g77030; ORFNames=F22K20.13;
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=11130712; DOI=10.1038/35048500;
RA   Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA   Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA   Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA   Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA   Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA   Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA   Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA   Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA   Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA   Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA   Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA   Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA   Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA   Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA   Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT   "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL   Nature 408:816-820(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. DDX54/DBP10
CC       subfamily. {ECO:0000305}.
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DR   EMBL; AC002291; AAC00620.1; -; Genomic_DNA.
DR   EMBL; CP002684; AEE35927.1; -; Genomic_DNA.
DR   PIR; D96799; D96799.
DR   RefSeq; NP_177829.5; NM_106354.6.
DR   AlphaFoldDB; O49289; -.
DR   SMR; O49289; -.
DR   STRING; 3702.AT1G77030.1; -.
DR   PaxDb; O49289; -.
DR   PRIDE; O49289; -.
DR   ProteomicsDB; 236929; -.
DR   EnsemblPlants; AT1G77030.1; AT1G77030.1; AT1G77030.
DR   GeneID; 844039; -.
DR   Gramene; AT1G77030.1; AT1G77030.1; AT1G77030.
DR   KEGG; ath:AT1G77030; -.
DR   Araport; AT1G77030; -.
DR   TAIR; locus:2025227; AT1G77030.
DR   eggNOG; KOG0337; Eukaryota.
DR   HOGENOM; CLU_003041_5_2_1; -.
DR   InParanoid; O49289; -.
DR   OMA; MRWDKKS; -.
DR   OrthoDB; 268859at2759; -.
DR   PhylomeDB; O49289; -.
DR   PRO; PR:O49289; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; O49289; baseline and differential.
DR   Genevisible; O49289; 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   GO; GO:0006364; P:rRNA processing; IBA:GO_Central.
DR   Gene3D; 3.40.50.300; -; 2.
DR   InterPro; IPR012541; DBP10_C.
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; PF08147; DBP10CT; 1.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   SMART; SM01123; DBP10CT; 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   3: Inferred from homology;
KW   ATP-binding; Helicase; Hydrolase; Nucleotide-binding; Reference proteome;
KW   RNA-binding.
FT   CHAIN           1..845
FT                   /note="Putative DEAD-box ATP-dependent RNA helicase 29"
FT                   /id="PRO_0000239169"
FT   DOMAIN          59..232
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          256..411
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   REGION          675..845
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           28..56
FT                   /note="Q motif"
FT   MOTIF           180..183
FT                   /note="DEAD box"
FT   COMPBIAS        692..756
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         72..79
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ   SEQUENCE   845 AA;  93503 MW;  3CA33435AC400497 CRC64;
     MVEGKGFLVS SVTELHRKEK QKKKGKSGGF ESLNLGPNVF NAIKKKGYKV PTPIQRKTMP
     LILSGVDVVA MARTGSGKTA AFLIPMLEKL KQHVPQGGVR ALILSPTRDL AEQTLKFTKE
     LGKFTDLRVS LLVGGDSMED QFEELTKGPD VIIATPGRLM HLLSEVDDMT LRTVEYVVFD
     EADSLFGMGF AEQLHQILTQ LSENRQTLLF SATLPSALAE FAKAGLREPQ LVRLDVENKI
     SPDLKLSFLT VRPEEKYSAL LYLVREHISS DQQTLIFVST KHHVEFVNSL FKLENIEPSV
     CYGDMDQDAR KIHVSRFRAR KTMLLIVTDI AARGIDIPLL DNVINWDFPP RPKIFVHRVG
     RAARAGRTGC AYSFVTPEDM PYMLDLHLFL SKPVRPAPTE DEVLKNMEEV MTKTSQAIDS
     GVTVYGRFPQ KTIDLIFNRT REMIDSSAEL DSLERTSTKA FRLYSKTKPS PSKESIRRAK
     DLPREGLHPI FRSIIETGEL EAMSFFQKIK NFRPKQTILE AEGEVAKSKH VKGPAGQWVD
     VMKKKRAIHE EIINTRHQQN QKTSNNHLEM EAEPTTSFVD GTVEGSKVSG KKRKAQETFK
     DDEFFISSIP VNHHSEAGLS LRGNEGFGSN RLDAAVLDLV ADDGQGIKQQ QSNYHWDKKG
     KKYIKLNNGD RVTASGKIKT ESGAKATAKK TGIYKRWQER SHKKVSRDSG DADETTRMSG
     RGGRDGKRRQ GSVPNAHVRS EIKDLDQVRK ERQQKANKVS YLQSKRGGRG GRGGARGGRG
     GGARGGRGGS RDFGGGGRDF GSSSDRGGRS GGRDFGGRRG GASTSSRGGK RGGGRGGGGK
     RGRGR