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Database: UniProt
Entry: Q8LA13
LinkDB: Q8LA13
Original site: Q8LA13 
ID   RH11_ARATH              Reviewed;         612 AA.
AC   Q8LA13; Q8W4P3; Q9M2G5; Q9ZS09;
DT   30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   16-OCT-2019, entry version 125.
DE   RecName: Full=DEAD-box ATP-dependent RNA helicase 11;
DE            EC=3.6.4.13;
GN   Name=RH11; OrderedLocusNames=At3g58510; ORFNames=F14P22.100;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae;
OC   Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
OC   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.,
RA   Fartmann B., Valle G., Bloecker H., Perez-Alonso M., Obermaier B.,
RA   Delseny M., Boutry M., Grivell L.A., Mache R., Puigdomenech P.,
RA   De Simone V., Choisne N., Artiguenave F., Robert C., Brottier P.,
RA   Wincker P., Cattolico L., Weissenbach J., Saurin W., Quetier F.,
RA   Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Benes V.,
RA   Wurmbach E., Drzonek H., Erfle H., Jordan N., Bangert S.,
RA   Wiedelmann R., Kranz H., Voss H., Holland R., Brandt P., Nyakatura G.,
RA   Vezzi A., D'Angelo M., Pallavicini A., Toppo S., Simionati B.,
RA   Conrad A., Hornischer K., Kauer G., Loehnert T.-H., Nordsiek G.,
RA   Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J., Climent J.,
RA   Navarro P., Collado C., Perez-Perez A., Ottenwaelder B., Duchemin D.,
RA   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.,
RA   Mannhaupt G., Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W.,
RA   Mayer K.F.X., Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J.,
RA   Rooney T., Rizzo M., Walts A., Utterback T., Fujii C.Y., Shea T.P.,
RA   Creasy T.H., Haas B., Maiti R., Wu D., Peterson J., Van Aken S.,
RA   Pai G., Militscher J., Sellers P., Gill J.E., Feldblyum T.V.,
RA   Preuss D., Lin X., Nierman W.C., Salzberg S.L., White O., Venter J.C.,
RA   Fraser C.M., Kaneko T., Nakamura Y., Sato S., Kato T., Asamizu E.,
RA   Sasamoto S., Kimura T., Idesawa K., Kawashima K., Kishida Y.,
RA   Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Muraki A.,
RA   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
RT   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
RT   reference genome.";
RL   Plant J. 89:789-804(2017).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA   Feldmann K.A.;
RT   "Full-length cDNA from Arabidopsis thaliana.";
RL   Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 105-612.
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.,
RA   Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
RA   Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
RA   Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
RA   Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
RA   Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
RA   Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
RA   Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
RA   Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
RA   Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
RA   Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
RA   Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
RT   "Empirical analysis of transcriptional activity in the Arabidopsis
RT   genome.";
RL   Science 302:842-846(2003).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 389-612.
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   [6]
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.,
RA   Lecharny A.;
RT   "DEAD-box RNA helicases in Arabidopsis thaliana: establishing a link
RT   between quantitative expression, gene structure and evolution of a
RT   family of genes.";
RL   Plant Biotechnol. J. 2:401-415(2004).
RN   [7]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=cv. Landsberg erecta;
RX   PubMed=17272265; DOI=10.1074/mcp.m600408-mcp200;
RA   Maor R., Jones A., Nuehse T.S., Studholme D.J., Peck S.C., Shirasu K.;
RT   "Multidimensional protein identification technology (MudPIT) analysis
RT   of ubiquitinated proteins in plants.";
RL   Mol. Cell. Proteomics 6:601-610(2007).
RN   [8]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA   Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C.,
RA   Meinnel T., Giglione C.;
RT   "Comparative large-scale characterisation of plant vs. mammal proteins
RT   reveals similar and idiosyncratic N-alpha acetylation features.";
RL   Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN   [9]
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
RT   family in Zea mays and Glycine max: a comparison with Arabidopsis and
RT   Oryza 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
CC       box family of RNA helicases and controls ATP binding and
CC       hydrolysis.
CC   -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX3/DED1
CC       subfamily. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAL32524.1; Type=Frameshift; Evidence={ECO:0000305};
CC       Sequence=AAM47956.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=CAB68189.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
DR   EMBL; AL137082; CAB68189.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002686; AEE79791.1; -; Genomic_DNA.
DR   EMBL; CP002686; AEE79792.1; -; Genomic_DNA.
DR   EMBL; CP002686; AEE79793.1; -; Genomic_DNA.
DR   EMBL; AY088091; AAM65637.1; -; mRNA.
DR   EMBL; AY062446; AAL32524.1; ALT_FRAME; mRNA.
DR   EMBL; AY114637; AAM47956.1; ALT_INIT; mRNA.
DR   EMBL; AJ010463; CAA09202.1; -; mRNA.
DR   PIR; T45671; T45671.
DR   PIR; T51742; T51742.
DR   RefSeq; NP_001030884.1; NM_001035807.1.
DR   RefSeq; NP_567067.1; NM_115713.2.
DR   RefSeq; NP_974455.1; NM_202726.2.
DR   SMR; Q8LA13; -.
DR   BioGrid; 10335; 1.
DR   IntAct; Q8LA13; 1.
DR   STRING; 3702.AT3G58510.2; -.
DR   iPTMnet; Q8LA13; -.
DR   PaxDb; Q8LA13; -.
DR   PRIDE; Q8LA13; -.
DR   EnsemblPlants; AT3G58510.1; AT3G58510.1; AT3G58510.
DR   EnsemblPlants; AT3G58510.2; AT3G58510.2; AT3G58510.
DR   EnsemblPlants; AT3G58510.3; AT3G58510.3; AT3G58510.
DR   GeneID; 825020; -.
DR   Gramene; AT3G58510.1; AT3G58510.1; AT3G58510.
DR   Gramene; AT3G58510.2; AT3G58510.2; AT3G58510.
DR   Gramene; AT3G58510.3; AT3G58510.3; AT3G58510.
DR   KEGG; ath:AT3G58510; -.
DR   Araport; AT3G58510; -.
DR   TAIR; locus:2076351; AT3G58510.
DR   eggNOG; KOG0335; Eukaryota.
DR   eggNOG; ENOG410XNTI; LUCA.
DR   HOGENOM; HOG000268804; -.
DR   InParanoid; Q8LA13; -.
DR   KO; K11594; -.
DR   OMA; PQNDHAG; -.
DR   OrthoDB; 595675at2759; -.
DR   PhylomeDB; Q8LA13; -.
DR   PRO; PR:Q8LA13; -.
DR   Proteomes; UP000006548; Chromosome 3.
DR   ExpressionAtlas; Q8LA13; baseline and differential.
DR   Genevisible; Q8LA13; AT.
DR   GO; GO:0005829; C:cytosol; HDA:TAIR.
DR   GO; GO:0005730; C:nucleolus; IDA:TAIR.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0043186; C:P granule; IBA:GO_Central.
DR   GO; GO:0005777; C:peroxisome; IDA:TAIR.
DR   GO; GO:0005886; C:plasma membrane; IDA:TAIR.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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; IEA:UniProtKB-EC.
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   1: Evidence at protein level;
KW   Acetylation; ATP-binding; Complete proteome; Helicase; Hydrolase;
KW   Nucleotide-binding; Reference proteome; RNA-binding.
FT   INIT_MET      1      1       Removed. {ECO:0000244|PubMed:22223895}.
FT   CHAIN         2    612       DEAD-box ATP-dependent RNA helicase 11.
FT                                /FTId=PRO_0000239153.
FT   DOMAIN      182    366       Helicase ATP-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00541}.
FT   DOMAIN      377    542       Helicase C-terminal.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00542}.
FT   NP_BIND     195    202       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00541}.
FT   MOTIF       151    179       Q motif.
FT   MOTIF       310    313       DEAD box.
FT   COMPBIAS     46    100       Gly-rich.
FT   COMPBIAS    548    606       Gly-rich.
FT   MOD_RES       2      2       N-acetylserine.
FT                                {ECO:0000244|PubMed:22223895}.
FT   CONFLICT    227    227       A -> V (in Ref. 4; AAL32524/AAM47956).
FT                                {ECO:0000305}.
SQ   SEQUENCE   612 AA;  66026 MW;  3DC76BF66ADE963F CRC64;
     MSASWADVAD SEKAVSQSKP PYVPPHLRNR PSEPVAAPLP QNDHAGYGGQ PAGSRWAPPS
     SGGGGASGGG YRNDGGRTGY GYGAGGGGGG GGGWNNRSGG WDRREREVNP FGDDAELEPV
     FTEQENTGIN FDAYEDIPVE TSGGDVPPPV NTFADIDLGD ALNLNIRRCK YVRPTPVQRH
     AIPILLAERD LMACAQTGSG KTAAFCFPII SGIMKDQHVE RPRGSRAVYP FAVILSPTRE
     LACQIHDEAK KFSYQTGVKV VVAYGGTPIH QQLRELERGC DILVATPGRL NDLLERARVS
     MQMIRFLALD EADRMLDMGF EPQIRKIVEQ MDMPPRGVRQ TMLFSATFPS QIQRLAADFM
     SNYIFLAVGR VGSSTDLITQ RVEFVQESDK RSHLMDLLHA QRETQDKQSL TLVFVETKRG
     ADTLENWLCM NEFPATSIHG DRTQQEREVA LRSFKTGRTP ILVATDVAAR GLDIPHVAHV
     VNFDLPNDID DYVHRIGRTG RAGKSGIATA FFNENNAQLA RSLAELMQEA NQEVPEWLTR
     YASRASFGGG KKRSGGRFGG RDFRREGSYS RGGGGGGGGG GSDYYGGGGY GGGGYGGAPS
     GGYGAGVTSA WD
//
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