RH41_ARATH
ID RH41_ARATH Reviewed; 505 AA.
AC Q3EBD3; Q8VZ85;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=DEAD-box ATP-dependent RNA helicase 41;
DE EC=3.6.4.13;
GN Name=RH41; OrderedLocusNames=At3g02065; ORFNames=F1C9.15;
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=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(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] (ISOFORM 2).
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q3EBD3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q3EBD3-2; Sequence=VSP_019106;
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 -!- MISCELLANEOUS: [Isoform 2]: May be due to an intron retention.
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX59 subfamily.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AC011664; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CP002686; AEE73756.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE73757.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE73758.1; -; Genomic_DNA.
DR EMBL; AY065172; AAL38348.1; -; mRNA.
DR EMBL; BT001184; AAN65071.1; -; mRNA.
DR RefSeq; NP_001030621.1; NM_001035544.2. [Q3EBD3-1]
DR RefSeq; NP_850499.1; NM_180168.2. [Q3EBD3-2]
DR RefSeq; NP_974208.1; NM_202479.2. [Q3EBD3-1]
DR AlphaFoldDB; Q3EBD3; -.
DR SMR; Q3EBD3; -.
DR BioGRID; 6488; 2.
DR IntAct; Q3EBD3; 1.
DR STRING; 3702.AT3G02065.2; -.
DR PaxDb; Q3EBD3; -.
DR PRIDE; Q3EBD3; -.
DR ProteomicsDB; 236857; -. [Q3EBD3-1]
DR EnsemblPlants; AT3G02065.1; AT3G02065.1; AT3G02065. [Q3EBD3-2]
DR EnsemblPlants; AT3G02065.2; AT3G02065.2; AT3G02065. [Q3EBD3-1]
DR EnsemblPlants; AT3G02065.3; AT3G02065.3; AT3G02065. [Q3EBD3-1]
DR GeneID; 821155; -.
DR Gramene; AT3G02065.1; AT3G02065.1; AT3G02065. [Q3EBD3-2]
DR Gramene; AT3G02065.2; AT3G02065.2; AT3G02065. [Q3EBD3-1]
DR Gramene; AT3G02065.3; AT3G02065.3; AT3G02065. [Q3EBD3-1]
DR KEGG; ath:AT3G02065; -.
DR Araport; AT3G02065; -.
DR TAIR; locus:2828586; AT3G02065.
DR eggNOG; KOG0331; Eukaryota.
DR InParanoid; Q3EBD3; -.
DR OMA; DESFCIR; -.
DR PhylomeDB; Q3EBD3; -.
DR PRO; PR:Q3EBD3; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q3EBD3; baseline and differential.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0003724; F:RNA helicase activity; IBA:GO_Central.
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 InterPro; IPR007529; Znf_HIT.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF04438; zf-HIT; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
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 Alternative splicing; ATP-binding; Helicase; Hydrolase; Metal-binding;
KW Nucleotide-binding; Reference proteome; RNA-binding; Zinc; Zinc-finger.
FT CHAIN 1..505
FT /note="DEAD-box ATP-dependent RNA helicase 41"
FT /id="PRO_0000239181"
FT DOMAIN 141..318
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 342..492
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT ZN_FING 27..56
FT /note="HIT-type"
FT MOTIF 110..138
FT /note="Q motif"
FT MOTIF 267..270
FT /note="DEAD box"
FT BINDING 154..161
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT VAR_SEQ 1..137
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14593172"
FT /id="VSP_019106"
SQ SEQUENCE 505 AA; 55218 MW; FA7915BD5D533F56 CRC64;
MNEEGCVPHN SDVVKQKSID QRAPLSGEPK CVICSRYGEY ICDETNDDVC SLECKQALLR
RVDSARVFPA TDECFYVRDP GSSSHDAQLL RRKLDIHVQG QGSAVPPPVL TFTSCGLPPK
LLLNLETAGY DFPTPIQMQA IPAALTGKSL LASADTGSGK TASFLVPIIS RCTTYHSEHP
SDQRRNPLAM VLAPTRELCV QVEDQAKMLG KGLPFKTALV VGGDPMSGQL YRIQQGVELI
IGTPGRVVDL LSKHTIELDN IMTFVLDEVD CMLQRGFRDQ VMQIFQALSQ PQVLLFSATI
SREVEKVGGS LAKEIILVSI GNPNKPNKAV NQLAIWVDAK QKKQKLFDIL RSQNHFKPPA
VVYVSSRVGA DLLANAITVV TGVKALSIHG EKPMKERRDV MGSFLGGEVP VLVSTGVLGR
GVDLLVVRQV IVFDMPSTIK EYIHVIGRAS RMGEKGTAIV FVNEDDRNLF PDLVAALKSS
GAAIPKELIN LTSREMHNKK RRVGY
