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Database: UniProt
Entry: Q9C551
LinkDB: Q9C551
Original site: Q9C551 
ID   RH5_ARATH               Reviewed;         537 AA.
AC   Q9C551; Q9ZS13;
DT   30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   11-DEC-2019, entry version 123.
DE   RecName: Full=DEAD-box ATP-dependent RNA helicase 5;
DE            EC=3.6.4.13;
GN   Name=RH5; OrderedLocusNames=At1g31970; ORFNames=F5M6.3, T12O21.12;
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=11130712; DOI=10.1038/35048500;
RA   Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA   Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA   Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA   Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA   Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA   Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA   Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA   Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA   Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA   Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA   Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA   Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA   Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA   Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA   Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT   "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL   Nature 408:816-820(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].
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   NUCLEOTIDE SEQUENCE [MRNA] OF 127-537.
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   [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   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-533, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19376835; DOI=10.1104/pp.109.138677;
RA   Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA   Grossmann J., Gruissem W., Baginsky S.;
RT   "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT   chloroplast kinase substrates and phosphorylation networks.";
RL   Plant Physiol. 150:889-903(2009).
RN   [7]
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   -!- FUNCTION: ATP-dependent RNA helicase required for 60S ribosomal subunit
CC       synthesis. Involved in efficient pre-rRNA processing, predominantly at
CC       site A3, which is necessary for the normal formation of 25S and 5.8S
CC       rRNAs (By similarity). {ECO:0000250}.
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   -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250}.
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. DDX5/DBP2
CC       subfamily. {ECO:0000305}.
DR   EMBL; AC074309; AAG50784.1; -; Genomic_DNA.
DR   EMBL; AC079041; AAG50723.1; -; Genomic_DNA.
DR   EMBL; CP002684; AEE31423.1; -; Genomic_DNA.
DR   EMBL; AY080680; AAL86356.1; -; mRNA.
DR   EMBL; AY117298; AAM51373.1; -; mRNA.
DR   EMBL; AJ010458; CAA09197.1; -; mRNA.
DR   PIR; A86444; A86444.
DR   PIR; T51739; T51739.
DR   RefSeq; NP_174479.1; NM_102933.3.
DR   SMR; Q9C551; -.
DR   BioGrid; 25321; 3.
DR   IntAct; Q9C551; 3.
DR   STRING; 3702.AT1G31970.1; -.
DR   iPTMnet; Q9C551; -.
DR   PaxDb; Q9C551; -.
DR   PRIDE; Q9C551; -.
DR   EnsemblPlants; AT1G31970.1; AT1G31970.1; AT1G31970.
DR   GeneID; 840087; -.
DR   Gramene; AT1G31970.1; AT1G31970.1; AT1G31970.
DR   KEGG; ath:AT1G31970; -.
DR   Araport; AT1G31970; -.
DR   TAIR; locus:2034481; AT1G31970.
DR   eggNOG; KOG0331; Eukaryota.
DR   eggNOG; COG0513; LUCA.
DR   HOGENOM; HOG000268804; -.
DR   InParanoid; Q9C551; -.
DR   KO; K14811; -.
DR   OMA; AYGAFFK; -.
DR   OrthoDB; 471730at2759; -.
DR   PhylomeDB; Q9C551; -.
DR   PRO; PR:Q9C551; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; Q9C551; baseline and differential.
DR   Genevisible; Q9C551; AT.
DR   GO; GO:0005829; C:cytosol; IDA:TAIR.
DR   GO; GO:0005730; C:nucleolus; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR   GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006364; P:rRNA processing; IBA:GO_Central.
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; IPR000629; RNA-helicase_DEAD-box_CS.
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; 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   1: Evidence at protein level;
KW   ATP-binding; Coiled coil; Helicase; Hydrolase; Nucleotide-binding; Nucleus;
KW   Phosphoprotein; Reference proteome; Ribosome biogenesis; RNA-binding;
KW   rRNA processing.
FT   CHAIN           1..537
FT                   /note="DEAD-box ATP-dependent RNA helicase 5"
FT                   /id="PRO_0000239146"
FT   DOMAIN          145..324
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          349..500
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   NP_BIND         158..165
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   COILED          22..80
FT                   /evidence="ECO:0000255"
FT   MOTIF           116..142
FT                   /note="Q motif"
FT   MOTIF           272..275
FT                   /note="DEAD box"
FT   COMPBIAS        24..84
FT                   /note="Lys-rich"
FT   MOD_RES         533
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:19376835"
FT   CONFLICT        537
FT                   /note="D -> N (in Ref. 4; CAA09197)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   537 AA;  59604 MW;  31EAA4CE91DF37E1 CRC64;
     MAGQKQELPV SGEPLAVESP MTNKKKKKSK KNKHTEENHE VEEVPQEVTN GVEEELSNKE
     KKKKRKREEK ESEKNKKKDV PEKKLEAEDL GEGESEQQKV VVTGKGVEEA KYAALKTFAE
     SNLPENVLDC CKTFEKPSPI QSHTWPFLLD GRDLIGIAKT GSGKTLAFGI PAIMHVLKKN
     KKIGGGSKKV NPTCLVLSPT RELAVQISDV LREAGEPCGL KSICVYGGSS KGPQISAIRS
     GVDIVIGTPG RLRDLIESNV LRLSDVSFVV LDEADRMLDM GFEEPVRFIL SNTNKVRQMV
     MFSATWPLDV HKLAQEFMDP NPIKVIIGSV DLAANHDVMQ IIEVLDERAR DQRLIALLEK
     YHKSQKNRVL VFALYKVEAE RLERFLQQRG WKAVSIHGNK AQSERTRSLS LFKEGSCPLL
     VATDVAARGL DIPDVEVVIN YTFPLTTEDY VHRIGRTGRA GKKGVAHTFF TPLNKGLAGE
     LVNVLREAGQ VVPADLLKFG THVKKKESKL YGAHFKEIAA DAPKATKITF DNSDDED
//
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