RH34_ARATH
ID RH34_ARATH Reviewed; 392 AA.
AC Q9C8J1; Q9SYE0;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2006, sequence version 2.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=DEAD-box ATP-dependent RNA helicase 34 {ECO:0000303|PubMed:17168887};
DE Short=AtRH34 {ECO:0000303|PubMed:17168887};
DE EC=3.6.4.13 {ECO:0000305};
GN Name=RH34 {ECO:0000303|PubMed:17168887};
GN OrderedLocusNames=At1g51380 {ECO:0000312|Araport:AT1G51380};
GN ORFNames=F11M15.24 {ECO:0000312|EMBL:AAD30651.1},
GN F5D21.11 {ECO:0000312|EMBL:AAG52624.1};
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 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).
CC -!- FUNCTION: ATP-dependent RNA helicase involved in 40S ribosomal subunit
CC biogenesis. Required for the processing and cleavage of 35S pre-rRNA at
CC sites A0, A1, and A2, leading to mature 18S rRNA (By similarity).
CC {ECO:0000250}.
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: Nucleus, nucleolus {ECO:0000250}.
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. DDX48/FAL1
CC subfamily. {ECO:0000305}.
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DR EMBL; AC006085; AAD30651.1; -; Genomic_DNA.
DR EMBL; AC024261; AAG52624.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE32660.1; -; Genomic_DNA.
DR EMBL; AY058890; AAL24276.1; -; mRNA.
DR EMBL; AY079046; AAL79596.1; -; mRNA.
DR PIR; H96551; H96551.
DR RefSeq; NP_175549.1; NM_104016.3.
DR AlphaFoldDB; Q9C8J1; -.
DR SMR; Q9C8J1; -.
DR STRING; 3702.AT1G51380.1; -.
DR PaxDb; Q9C8J1; -.
DR PRIDE; Q9C8J1; -.
DR ProteomicsDB; 236960; -.
DR EnsemblPlants; AT1G51380.1; AT1G51380.1; AT1G51380.
DR GeneID; 841562; -.
DR Gramene; AT1G51380.1; AT1G51380.1; AT1G51380.
DR KEGG; ath:AT1G51380; -.
DR Araport; AT1G51380; -.
DR TAIR; locus:2008296; AT1G51380.
DR eggNOG; KOG0328; Eukaryota.
DR HOGENOM; CLU_003041_1_0_1; -.
DR InParanoid; Q9C8J1; -.
DR OMA; ERHYGTK; -.
DR OrthoDB; 726081at2759; -.
DR PhylomeDB; Q9C8J1; -.
DR PRO; PR:Q9C8J1; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9C8J1; baseline and differential.
DR Genevisible; Q9C8J1; AT.
DR GO; GO:0071013; C:catalytic step 2 spliceosome; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0003724; F:RNA helicase activity; IBA:GO_Central.
DR GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-KW.
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 2: Evidence at transcript level;
KW ATP-binding; Helicase; Hydrolase; Nucleotide-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Ribosome biogenesis; RNA-binding;
KW rRNA processing.
FT CHAIN 1..392
FT /note="DEAD-box ATP-dependent RNA helicase 34"
FT /id="PRO_0000239174"
FT DOMAIN 53..223
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 234..392
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT MOTIF 22..50
FT /note="Q motif"
FT MOTIF 171..174
FT /note="DEAD box"
FT BINDING 66..73
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT MOD_RES 87
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q94A52"
SQ SEQUENCE 392 AA; 44357 MW; 98F9502E389117C9 CRC64;
MEGTLDEENL VFETTKGIKP IKSFDDMGMN DKVLRGVYDY GYKKPSEIQQ RALVPILKGR
DVIAQAQSGT GKTSMIAISV CQIVNISSRK VQVLVLSPSR ELASQTEKTI QAIGAHTNIQ
AHACIGGKSI GEDIKKLERG VHAVSGTPGR VYDMIKRGSL QTKAVKLLVL DESDEMLSKG
LKDQIYDVYR ALPHDIQVCL ISATLPQEIL EMTEKFMTDP VRILVKPDEL TLEGIKQYYV
DVDKEEWKFD TLCDLYGRLT INQAIIFCNT RQKVDWLTEK MRSSNFIVSS MHGDKRQKER
DDIMNQFRSF KSRVLIASDV WARGIDVQTV SHVINYDIPN NPELYIHRIG RAGRFGREGV
AINFVKSSDM KDLKDIERHY GTKIREMPAD LV
