RH32_ARATH
ID RH32_ARATH Reviewed; 739 AA.
AC Q9FFT9;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=DEAD-box ATP-dependent RNA helicase 32;
DE EC=3.6.4.13;
GN Name=RH32; OrderedLocusNames=At5g54910; ORFNames=MBG8.18;
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=9330910; DOI=10.1093/dnares/4.3.215;
RA Sato S., Kotani H., Nakamura Y., Kaneko T., Asamizu E., Fukami M.,
RA Miyajima N., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. I. Sequence
RT features of the 1.6 Mb regions covered by twenty physically assigned P1
RT clones.";
RL DNA Res. 4:215-230(1997).
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. DDX10/DBP4
CC subfamily. {ECO:0000305}.
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DR EMBL; AB005232; BAB08770.1; -; Genomic_DNA.
DR EMBL; CP002688; AED96555.1; -; Genomic_DNA.
DR RefSeq; NP_200302.1; NM_124873.3.
DR AlphaFoldDB; Q9FFT9; -.
DR SMR; Q9FFT9; -.
DR STRING; 3702.AT5G54910.1; -.
DR iPTMnet; Q9FFT9; -.
DR PaxDb; Q9FFT9; -.
DR PRIDE; Q9FFT9; -.
DR ProteomicsDB; 236171; -.
DR EnsemblPlants; AT5G54910.1; AT5G54910.1; AT5G54910.
DR GeneID; 835582; -.
DR Gramene; AT5G54910.1; AT5G54910.1; AT5G54910.
DR KEGG; ath:AT5G54910; -.
DR Araport; AT5G54910; -.
DR TAIR; locus:2160225; AT5G54910.
DR eggNOG; KOG0343; Eukaryota.
DR HOGENOM; CLU_003041_26_1_1; -.
DR InParanoid; Q9FFT9; -.
DR OMA; MIVPLDQ; -.
DR OrthoDB; 973872at2759; -.
DR PhylomeDB; Q9FFT9; -.
DR PRO; PR:Q9FFT9; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FFT9; baseline and differential.
DR Genevisible; Q9FFT9; AT.
DR GO; GO:0005730; C:nucleolus; HDA:TAIR.
DR GO; GO:0005634; C:nucleus; 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; IEA:UniProtKB-KW.
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; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR025313; DUF4217.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000629; RNA-helicase_DEAD-box_CS.
DR InterPro; IPR014014; RNA_helicase_DEAD_Q_motif.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF13959; DUF4217; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM01178; DUF4217; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR PROSITE; PS00039; DEAD_ATP_HELICASE; 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; Coiled coil; Helicase; Hydrolase; Nucleotide-binding;
KW Reference proteome; RNA-binding.
FT CHAIN 1..739
FT /note="DEAD-box ATP-dependent RNA helicase 32"
FT /id="PRO_0000239172"
FT DOMAIN 102..277
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 303..461
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 656..725
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 643..689
FT /evidence="ECO:0000255"
FT MOTIF 71..99
FT /note="Q motif"
FT MOTIF 225..228
FT /note="DEAD box"
FT COMPBIAS 693..713
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 115..122
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 739 AA; 83582 MW; 2D779D4E94A1E13C CRC64;
MVKIKKTKGM RKQIRLNEVE EINLLKQWIE SQKPDSGFNP LSLRPLPKDS KIGKSEDGKN
GTVFSRYAGV RKFAQLPISD KTKRGLKDAK YVDMTDVQSA AIPHALCGRD ILGAARTGSG
KTLAFVIPIL EKLHRERWSP EDGVGCIIIS PTRELAAQTF GVLNKVGKFH KFSAGLLIGG
REGVDVEKER VHEMNILVCA PGRLLQHMDE TPNFECPQLQ ILILDEADRV LDSAFKGQLD
PIISQLPKHR QTLLFSATQT KKVKDLARLS LRDPEYISVH AEAVTATPTS LMQTVMIVPV
EKKLDMLWSF IKTHLNSRIL VFLSTKKQVK FVHEAFNKLR PGIPLKSLHG KMSQEKRMGV
YSQFIERQSV LFCTDVLARG LDFDKAVDWV VQVDCPEDVA SYIHRVGRTA RFYTQGKSLL
FLTPSEEKMI EKLQEAKVPI KLIKANNQKL QEVSRLLAAL LVKYPDLQGV AQRAFITYLR
SIHKRRDKEI FDVSKLSIEN FSASLGLPMT PRIRFTNLKT KKKGVYESSI AMEIENAQEY
EAPLVVKKDL LGEDLEEEDF ALKPRKEGKV VEKSTKEEEV LIPGNRVLKN KKLKINLHRP
FGSRVVLDEE GNSLAPLASV AAEAGTEVAL DEERMNDYYK KVGAEMRKAD IEDKKVDKER
RREKRMKQKI KRKRGAMEDE EEEEEEDHDG SGSSDDETGR NSKRAKKIVS DNEENGGKIN
TDSLSVADLE EMALKFITQ
