RH25_ARATH
ID RH25_ARATH Reviewed; 563 AA.
AC Q94C75; Q9ZS00;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2006, sequence version 2.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=DEAD-box ATP-dependent RNA helicase 25;
DE EC=3.6.4.13;
GN Name=RH25; OrderedLocusNames=At5g08620; ORFNames=MAH20.18;
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 [MRNA].
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9405937; DOI=10.1093/dnares/4.4.291;
RA Kotani H., Nakamura Y., Sato S., Kaneko T., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. II. Sequence
RT features of the regions of 1,044,062 bp covered by thirteen physically
RT assigned P1 clones.";
RL DNA Res. 4:291-300(1997).
RN [3]
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 [4]
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 [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 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. {ECO:0000305}.
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DR EMBL; AJ010473; CAA09212.1; -; mRNA.
DR EMBL; AB006697; BAB10011.1; -; Genomic_DNA.
DR EMBL; CP002688; AED91330.1; -; Genomic_DNA.
DR EMBL; AY035114; AAK59619.1; -; mRNA.
DR EMBL; AY142638; AAN13096.1; -; mRNA.
DR PIR; T51348; T51348.
DR RefSeq; NP_196479.1; NM_120949.4.
DR AlphaFoldDB; Q94C75; -.
DR SMR; Q94C75; -.
DR BioGRID; 16041; 6.
DR STRING; 3702.AT5G08620.1; -.
DR PaxDb; Q94C75; -.
DR PRIDE; Q94C75; -.
DR ProteomicsDB; 236964; -.
DR EnsemblPlants; AT5G08620.1; AT5G08620.1; AT5G08620.
DR GeneID; 830763; -.
DR Gramene; AT5G08620.1; AT5G08620.1; AT5G08620.
DR KEGG; ath:AT5G08620; -.
DR Araport; AT5G08620; -.
DR TAIR; locus:2159527; AT5G08620.
DR eggNOG; KOG0342; Eukaryota.
DR HOGENOM; CLU_003041_26_6_1; -.
DR InParanoid; Q94C75; -.
DR OMA; CFVGGAN; -.
DR OrthoDB; 537587at2759; -.
DR PhylomeDB; Q94C75; -.
DR PRO; PR:Q94C75; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q94C75; baseline and differential.
DR Genevisible; Q94C75; AT.
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; IDA:TAIR.
DR GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
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 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; Phosphoprotein;
KW Reference proteome; RNA-binding.
FT CHAIN 1..563
FT /note="DEAD-box ATP-dependent RNA helicase 25"
FT /id="PRO_0000239165"
FT DOMAIN 111..294
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 328..479
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 21..57
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 80..108
FT /note="Q motif"
FT MOTIF 242..245
FT /note="DEAD box"
FT COMPBIAS 21..55
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 124..131
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT MOD_RES 25
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9FNM7"
FT CONFLICT 119
FT /note="D -> N (in Ref. 4; AAK59619)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 563 AA; 62495 MW; A0E4BD8BF745A41E CRC64;
MNSDGPKSGK KRREIRAKLV KKLTSDEDGS GKLVKDNNKS LKRGREGKSD VDEPLIKKPA
STTPLVTQIA KTSDSYLSKT RFDQFPLSPL TLKGIEDAGF KTMTVVQEAT LPLILQGKDI
LAKAKTGTGK TVAFLLPSIE AVIKAPPASR DNRHPPIIVL VVCPTRELAC QAAAEANILL
KYHPSIGVQV VIGGTKLPTE QRRLQKSPCQ ILVATPGRLK DHIDNTSGFA TRLMGVKVLV
LDEADHLLDM GFRREIERII AAVPKQRQTF LFSATVSDEV RQICHVALKR DHEFVNCVQE
GAGETHQKVS QMYMIASLDR HFSLLYGLLK KHITDNVGYK VIIFCTTAMV TRLVADLLGK
LSLNVREIHS RKPQSYRTRV SDEFRKSKSI ILVTSDVSAR GVDYPDVSLV VQMGLPSDRE
QYIHRLGRTG RKGKEGEGVL LLAPWEEYFL SSVKDLPITK SSLPPIDHEA VKKVQKGLIQ
VEMTNKEAAY QAWLGYYKSQ KKIARDTTRL VELANEFSRS MGLSIPPAIP VNILGKMGLK
NVPGIRVAPG FDKKPAKRNY RSR
