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RH10_ORYSJ
ID   RH10_ORYSJ              Reviewed;         472 AA.
AC   Q7Y183; A3AL75; B7EDZ1;
DT   03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   03-AUG-2022, entry version 116.
DE   RecName: Full=DEAD-box ATP-dependent RNA helicase 10;
DE            EC=3.6.4.13 {ECO:0000250|UniProtKB:A2XKG2};
DE   AltName: Full=DEAD-box RNA helicase TOGR1 {ECO:0000303|PubMed:26848586};
DE   AltName: Full=Protein THERMOTOLERANT GROWTH REQUIRED1 {ECO:0000303|PubMed:26848586};
GN   Name=RH10 {ECO:0000305}; Synonyms=TOGR1 {ECO:0000303|PubMed:26848586};
GN   OrderedLocusNames=Os03g0669000, LOC_Os03g46610;
GN   ORFNames=OsJ_12029 {ECO:0000312|EMBL:EAZ28064.1}, OSJNBa0039O18.13,
GN   OSJNBb0036M02.1;
OS   Oryza sativa subsp. japonica (Rice).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX   NCBI_TaxID=39947;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=16109971; DOI=10.1101/gr.3869505;
RG   The rice chromosome 3 sequencing consortium;
RA   Buell C.R., Yuan Q., Ouyang S., Liu J., Zhu W., Wang A., Maiti R., Haas B.,
RA   Wortman J., Pertea M., Jones K.M., Kim M., Overton L., Tsitrin T.,
RA   Fadrosh D., Bera J., Weaver B., Jin S., Johri S., Reardon M., Webb K.,
RA   Hill J., Moffat K., Tallon L., Van Aken S., Lewis M., Utterback T.,
RA   Feldblyum T., Zismann V., Iobst S., Hsiao J., de Vazeille A.R.,
RA   Salzberg S.L., White O., Fraser C.M., Yu Y., Kim H., Rambo T., Currie J.,
RA   Collura K., Kernodle-Thompson S., Wei F., Kudrna K., Ammiraju J.S.S.,
RA   Luo M., Goicoechea J.L., Wing R.A., Henry D., Oates R., Palmer M.,
RA   Pries G., Saski C., Simmons J., Soderlund C., Nelson W., de la Bastide M.,
RA   Spiegel L., Nascimento L., Huang E., Preston R., Zutavern T., Palmer L.,
RA   O'Shaughnessy A., Dike S., McCombie W.R., Minx P., Cordum H., Wilson R.,
RA   Jin W., Lee H.R., Jiang J., Jackson S.;
RT   "Sequence, annotation, and analysis of synteny between rice chromosome 3
RT   and diverged grass species.";
RL   Genome Res. 15:1284-1291(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=16100779; DOI=10.1038/nature03895;
RG   International rice genome sequencing project (IRGSP);
RT   "The map-based sequence of the rice genome.";
RL   Nature 436:793-800(2005).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=18089549; DOI=10.1093/nar/gkm978;
RG   The rice annotation project (RAP);
RT   "The rice annotation project database (RAP-DB): 2008 update.";
RL   Nucleic Acids Res. 36:D1028-D1033(2008).
RN   [4]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA   Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA   Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA   Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA   Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT   "Improvement of the Oryza sativa Nipponbare reference genome using next
RT   generation sequence and optical map data.";
RL   Rice 6:4-4(2013).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare {ECO:0000312|EMBL:EAZ28064.1};
RX   PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA   Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA   Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA   Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA   Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA   Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA   Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA   Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA   Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA   Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA   Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA   Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA   Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA   Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA   McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT   "The genomes of Oryza sativa: a history of duplications.";
RL   PLoS Biol. 3:266-281(2005).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=12869764; DOI=10.1126/science.1081288;
RG   The rice full-length cDNA consortium;
RT   "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT   japonica rice.";
RL   Science 301:376-379(2003).
RN   [7]
RP   DISRUPTION PHENOTYPE.
RC   STRAIN=cv. Yandao 8 {ECO:0000303|PubMed:26848586}, and
RC   cv. Zhonghua 11 {ECO:0000303|PubMed:26848586};
RX   PubMed=26848586; DOI=10.1371/journal.pgen.1005844;
RA   Wang D., Qin B., Li X., Tang D., Zhang Y., Cheng Z., Xue Y.;
RT   "Nucleolar DEAD-box RNA helicase TOGR1 regulates thermotolerant growth as a
RT   pre-rRNA chaperone in rice.";
RL   PLoS Genet. 12:E1005844-E1005844(2016).
CC   -!- FUNCTION: Has ATP-dependent RNA helicase activity in vitro. Acts as a
CC       thermosensitive RNA chaperone required for normal processing of pre-
CC       rRNA intermediates. Required for normal cell division at high
CC       temperatures. Required for a primary metabolism adaptation to high
CC       temperatures to support thermotolerant growth by regulating gene
CC       expression. {ECO:0000250|UniProtKB:A2XKG2}.
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         Evidence={ECO:0000250|UniProtKB:A2XKG2};
CC   -!- ACTIVITY REGULATION: Helicase activity is activated by temperature
CC       increase. {ECO:0000250|UniProtKB:A2XKG2}.
CC   -!- SUBUNIT: Interacts with U3 small nucleolar RNA (U3 snoRNA) as part of
CC       the ribosomal small subunit (SSU) processome.
CC       {ECO:0000250|UniProtKB:A2XKG2}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:A2XKG2}. Nucleus,
CC       nucleolus {ECO:0000250|UniProtKB:A2XKG2}. Note=Localization is not
CC       affected by temperature. {ECO:0000250|UniProtKB:A2XKG2}.
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   -!- DISRUPTION PHENOTYPE: Plant shows a high temperature-dependent growth
CC       repression. {ECO:0000269|PubMed:26848586}.
CC   -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX47/RRP3
CC       subfamily. {ECO:0000305}.
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DR   EMBL; AC133930; AAP44655.1; -; Genomic_DNA.
DR   EMBL; AC145388; AAU89137.1; -; Genomic_DNA.
DR   EMBL; DP000009; ABF98097.1; -; Genomic_DNA.
DR   EMBL; AP008209; BAF12775.1; -; Genomic_DNA.
DR   EMBL; AP014959; BAS85665.1; -; Genomic_DNA.
DR   EMBL; CM000140; EAZ28064.1; -; Genomic_DNA.
DR   EMBL; AK067769; BAG90588.1; -; mRNA.
DR   RefSeq; XP_015627999.1; XM_015772513.1.
DR   AlphaFoldDB; Q7Y183; -.
DR   SMR; Q7Y183; -.
DR   STRING; 4530.OS03T0669000-01; -.
DR   PaxDb; Q7Y183; -.
DR   PRIDE; Q7Y183; -.
DR   EnsemblPlants; Os03t0669000-01; Os03t0669000-01; Os03g0669000.
DR   GeneID; 4333678; -.
DR   Gramene; Os03t0669000-01; Os03t0669000-01; Os03g0669000.
DR   KEGG; osa:4333678; -.
DR   eggNOG; KOG0330; Eukaryota.
DR   HOGENOM; CLU_003041_1_1_1; -.
DR   InParanoid; Q7Y183; -.
DR   OMA; MAQNTII; -.
DR   OrthoDB; 744428at2759; -.
DR   Proteomes; UP000000763; Chromosome 3.
DR   Proteomes; UP000007752; Chromosome 3.
DR   Proteomes; UP000059680; Chromosome 3.
DR   ExpressionAtlas; Q7Y183; baseline and differential.
DR   Genevisible; Q7Y183; OS.
DR   GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
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; IEA:UniProtKB-KW.
DR   GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006364; P:rRNA processing; IBA:GO_Central.
DR   CDD; cd17954; DEADc_DDX47; 1.
DR   Gene3D; 3.40.50.300; -; 2.
DR   InterPro; IPR044765; DDX47/Rrp3_DEADc.
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   2: Evidence at transcript level;
KW   ATP-binding; Helicase; Hydrolase; Nucleotide-binding; Nucleus;
KW   Reference proteome; RNA-binding; rRNA processing; Stress response.
FT   CHAIN           1..472
FT                   /note="DEAD-box ATP-dependent RNA helicase 10"
FT                   /id="PRO_0000282503"
FT   DOMAIN          72..245
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          256..416
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   REGION          1..40
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          429..472
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           41..69
FT                   /note="Q motif"
FT   MOTIF           193..196
FT                   /note="DEAD box"
FT   COMPBIAS        429..461
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         85..92
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   CONFLICT        96
FT                   /note="A -> G (in Ref. 5; EAZ28064)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   472 AA;  52480 MW;  019998F2508FB19B CRC64;
     MAKKKDVEVE ELDEEVVAAA AAPAADGGEE QEAEPPARRP STFAELGVVP ELVAACDAMG
     WKEPTRIQAE AIPHALEGRD LIGLGQTGSG KTGAFALPII QALLKQDKPQ ALFACVLSPT
     RELAFQIGQQ FEALGSAIGL SCTVLVGGVD RVQQAVSLAK RPHIVVGTPG RLLDHLTDTK
     GFSLNKLKYL VLDEADKLLN VEFQKALDDI LNVIPKERRT FLFSATMTNK VSKLQRACLR
     NPVKVEVASK YSTVDTLRQE FYFVPADYKD CFLVHVLNEL PGSMIMIFVR TCESTRLLAL
     TLRNLRFKAI SISGQMSQDK RLGALNRFKT KDCNILICTD VASRGLDIQG VDVVINYDIP
     MNSKDYVHRV GRTARAGNTG YAVSLVNQYE AMWFKMIEKL LGYEIPDRKV DNAEIMILRE
     RISDSKRIAL TTMKEGGGHK KKRRKNEDDE EEEERNAPVS RKSKSFNKSR RR
 
 
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