RH37_ARATH
ID RH37_ARATH Reviewed; 633 AA.
AC Q84W89; Q9SIN6;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2006, sequence version 2.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=DEAD-box ATP-dependent RNA helicase 37;
DE EC=3.6.4.13;
GN Name=RH37; OrderedLocusNames=At2g42520; ORFNames=F14N22.21;
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=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
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 -!- 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. DDX3/DED1
CC subfamily. {ECO:0000305}.
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DR EMBL; AC007087; AAD23001.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC10133.1; -; Genomic_DNA.
DR EMBL; CP002685; ANM62393.1; -; Genomic_DNA.
DR EMBL; CP002685; ANM62394.1; -; Genomic_DNA.
DR EMBL; BT004111; AAO42134.1; -; mRNA.
DR PIR; H84854; H84854.
DR RefSeq; NP_001324553.1; NM_001336985.1.
DR RefSeq; NP_001324554.1; NM_001336984.1.
DR RefSeq; NP_181780.1; NM_129813.5.
DR AlphaFoldDB; Q84W89; -.
DR SMR; Q84W89; -.
DR BioGRID; 4189; 8.
DR IntAct; Q84W89; 1.
DR STRING; 3702.AT2G42520.1; -.
DR iPTMnet; Q84W89; -.
DR PaxDb; Q84W89; -.
DR PRIDE; Q84W89; -.
DR ProteomicsDB; 236887; -.
DR EnsemblPlants; AT2G42520.1; AT2G42520.1; AT2G42520.
DR EnsemblPlants; AT2G42520.2; AT2G42520.2; AT2G42520.
DR EnsemblPlants; AT2G42520.3; AT2G42520.3; AT2G42520.
DR GeneID; 818852; -.
DR Gramene; AT2G42520.1; AT2G42520.1; AT2G42520.
DR Gramene; AT2G42520.2; AT2G42520.2; AT2G42520.
DR Gramene; AT2G42520.3; AT2G42520.3; AT2G42520.
DR KEGG; ath:AT2G42520; -.
DR Araport; AT2G42520; -.
DR TAIR; locus:2041549; AT2G42520.
DR eggNOG; KOG0335; Eukaryota.
DR HOGENOM; CLU_003041_16_3_1; -.
DR InParanoid; Q84W89; -.
DR OMA; NHGNSRL; -.
DR OrthoDB; 595675at2759; -.
DR PhylomeDB; Q84W89; -.
DR PRO; PR:Q84W89; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q84W89; baseline and differential.
DR Genevisible; Q84W89; AT.
DR GO; GO:0005829; C:cytosol; IDA:TAIR.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005777; C:peroxisome; HDA: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:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0003724; F:RNA helicase activity; IBA:GO_Central.
DR CDD; cd17967; DEADc_DDX3_DDX4; 1.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR044763; Ded1/Dbp1_DEADc.
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 Acetylation; ATP-binding; Helicase; Hydrolase; Nucleotide-binding;
KW Reference proteome; RNA-binding.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q8LA13"
FT CHAIN 2..633
FT /note="DEAD-box ATP-dependent RNA helicase 37"
FT /id="PRO_0000239177"
FT DOMAIN 190..374
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 401..552
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..110
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 555..600
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 159..187
FT /note="Q motif"
FT MOTIF 318..321
FT /note="DEAD box"
FT COMPBIAS 1..27
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 203..210
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:Q8LA13"
FT CONFLICT 259
FT /note="K -> R (in Ref. 3; AAO42134)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 633 AA; 67626 MW; C2CBC32359F5FC8F CRC64;
MSASWADVAD SENTGSGSSN QNSHPSRPAY VPPHLRNRPA ASEPVAPLPA NDRVGYGGPP
SGSRWAPGGS GVGVGGGGGY RADAGRPGSG SGYGGRGGGG WNNRSGGWDR REREVNPFEN
DDSEPEPAFT EQDNTVINFD AYEDIPIETS GDNVPPPVNT FAEIDLGEAL NLNIRRCKYV
KPTPVQRHAI PILLEGRDLM ACAQTGSGKT AAFCFPIISG IMKDQHVQRP RGSRTVYPLA
VILSPTRELA SQIHDEAKKF SYQTGVKVVV AYGGTPINQQ LRELERGVDI LVATPGRLND
LLERARVSMQ MIRFLALDEA DRMLDMGFEP QIRKIVEQMD MPPRGVRQTL LFSATFPREI
QRLAADFLAN YIFLAVGRVG SSTDLIVQRV EFVLDSDKRS HLMDLLHAQR ENGIQGKQAL
TLVFVETKRG ADSLENWLCI NGFPATSIHG DRTQQEREVA LKAFKSGRTP ILVATDVAAR
GLDIPHVAHV VNFDLPNDID DYVHRIGRTG RAGKSGLATA FFNDGNTSLA RPLAELMQEA
NQEVPEWLTR YASRSSFGGG KNRRSGGRFG GRDFRREGSF GSGRGGYGGG GGGYGGGGGY
GGGGGYGGGG GYGGGYGGAS SGGYGGEPPS AWD
