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RH10_ORYSI
ID   RH10_ORYSI              Reviewed;         472 AA.
AC   A2XKG2;
DT   28-MAR-2018, integrated into UniProtKB/Swiss-Prot.
DT   20-MAR-2007, sequence version 1.
DT   03-AUG-2022, entry version 89.
DE   RecName: Full=DEAD-box ATP-dependent RNA helicase 10 {ECO:0000305};
DE            EC=3.6.4.13 {ECO:0000269|PubMed:26848586};
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   ORFNames=OsI_12939 {ECO:0000312|EMBL:EAY91322.1};
OS   Oryza sativa subsp. indica (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=39946 {ECO:0000312|EMBL:EAY91322.1};
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. 93-11;
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   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, SUBUNIT, SUBCELLULAR
RP   LOCATION, DEVELOPMENTAL STAGE, INDUCTION, DISRUPTION PHENOTYPE, AND
RP   MUTAGENESIS OF GLY-47.
RC   STRAIN=cv. Zhongxian 3037 {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. Partially rescues the yeast rRNA helicase RRP3 mutant which
CC       has repressed cell proliferation at 38 degrees Celsius.
CC       {ECO:0000269|PubMed:26848586}.
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:0000269|PubMed:26848586};
CC   -!- ACTIVITY REGULATION: Helicase activity is activated by temperature
CC       increase. {ECO:0000269|PubMed:26848586}.
CC   -!- SUBUNIT: Interacts with U3 small nucleolar RNA (U3 snoRNA) as part of
CC       the ribosomal small subunit (SSU) processome.
CC       {ECO:0000269|PubMed:26848586}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:26848586}. Nucleus,
CC       nucleolus {ECO:0000269|PubMed:26848586}. Note=Localization is not
CC       affected by temperature. {ECO:0000269|PubMed:26848586}.
CC   -!- DEVELOPMENTAL STAGE: Widely expressed in roots, shoots, leaves, culms,
CC       spikelets and anthers during different developing stages.
CC       {ECO:0000269|PubMed:26848586}.
CC   -!- INDUCTION: By high temperature and the circadian clock. Expression
CC       peaks at zeitgeber time 9 (ZT9) corresponding to afternoon of a
CC       subjective day, the hottest time of daily temperature fluctuation.
CC       {ECO:0000269|PubMed:26848586}.
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       {ECO:0000305}.
CC   -!- DISRUPTION PHENOTYPE: Thermosensitive dwarf mutant. Reduced plant
CC       height, root length and crown root number at 30, 32.5 and 35 degrees
CC       Celsius, whereas they grow similarly to wild-type at 25 degrees Celsius
CC       except for a slightly reduced plant height. At tillering stage, plants
CC       grown in a hot climate show narrowed leaf blades mainly due to a
CC       decrease in vascular bundle and lateral vein numbers, and all
CC       internodes are shortened. Furthermore, cross-sections of leaf sheath,
CC       leaf blades, internodes and root maturation zones do not show a
CC       significant difference in cell elongation, but a reduction in cell
CC       numbers compared to wild-type. {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; CM000128; EAY91322.1; -; Genomic_DNA.
DR   AlphaFoldDB; A2XKG2; -.
DR   SMR; A2XKG2; -.
DR   STRING; 39946.A2XKG2; -.
DR   EnsemblPlants; BGIOSGA010088-TA; BGIOSGA010088-PA; BGIOSGA010088.
DR   Gramene; BGIOSGA010088-TA; BGIOSGA010088-PA; BGIOSGA010088.
DR   HOGENOM; CLU_003041_1_1_1; -.
DR   OMA; YDIELYQ; -.
DR   Proteomes; UP000007015; Chromosome 3.
DR   GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
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; IEA:UniProtKB-KW.
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   1: Evidence at protein 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_0000443718"
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                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00552"
FT   MOTIF           193..196
FT                   /note="DEAD box"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
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   MUTAGEN         47
FT                   /note="G->V: In togr1-1; thermosensitive dwarf mutant."
FT                   /evidence="ECO:0000269|PubMed:26848586"
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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