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RH8_ORYSJ
ID   RH8_ORYSJ               Reviewed;         508 AA.
AC   Q6H7S2; B7EKD5; Q6H7S3;
DT   03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   03-APR-2007, sequence version 2.
DT   03-AUG-2022, entry version 121.
DE   RecName: Full=DEAD-box ATP-dependent RNA helicase 8;
DE            EC=3.6.4.13;
GN   OrderedLocusNames=Os02g0641800, LOC_Os02g42860;
GN   ORFNames=OJ1112_G03.6-1, OJ1112_G03.6-2,
GN   OsJ_07688 {ECO:0000312|EMBL:EEE57460.1};
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=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   [2]
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   [3]
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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
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   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
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).
CC   -!- FUNCTION: ATP-dependent RNA helicase involved in mRNA turnover, and
CC       more specifically in mRNA decapping. {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: Cytoplasm, P-body {ECO:0000250}. Note=Is
CC       concentrated in several cytoplasmic foci called P bodies (or
CC       cytoplasmic processing bodies) which represent sites of mRNA decapping
CC       and 5' to 3' exonucleotidic decay. {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q6H7S2-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q6H7S2-2; Sequence=VSP_024161;
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. DDX6/DHH1
CC       subfamily. {ECO:0000305}.
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DR   EMBL; AP004133; BAD25226.1; -; Genomic_DNA.
DR   EMBL; AP004133; BAD25227.1; -; Genomic_DNA.
DR   EMBL; AP008208; BAF09466.1; -; Genomic_DNA.
DR   EMBL; AP014958; BAS79992.1; -; Genomic_DNA.
DR   EMBL; AP014958; BAS79993.1; -; Genomic_DNA.
DR   EMBL; CM000139; EEE57460.1; -; Genomic_DNA.
DR   EMBL; AK066504; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; AK072124; BAG92832.1; -; mRNA.
DR   RefSeq; XP_015627069.1; XM_015771583.1. [Q6H7S2-1]
DR   AlphaFoldDB; Q6H7S2; -.
DR   SMR; Q6H7S2; -.
DR   STRING; 4530.OS02T0641800-02; -.
DR   PaxDb; Q6H7S2; -.
DR   PRIDE; Q6H7S2; -.
DR   EnsemblPlants; Os02t0641800-01; Os02t0641800-01; Os02g0641800. [Q6H7S2-2]
DR   EnsemblPlants; Os02t0641800-02; Os02t0641800-02; Os02g0641800. [Q6H7S2-1]
DR   GeneID; 4330120; -.
DR   Gramene; Os02t0641800-01; Os02t0641800-01; Os02g0641800. [Q6H7S2-2]
DR   Gramene; Os02t0641800-02; Os02t0641800-02; Os02g0641800. [Q6H7S2-1]
DR   KEGG; osa:4330120; -.
DR   eggNOG; KOG0326; Eukaryota.
DR   InParanoid; Q6H7S2; -.
DR   OMA; TAIRIQI; -.
DR   OrthoDB; 583315at2759; -.
DR   Proteomes; UP000000763; Chromosome 2.
DR   Proteomes; UP000007752; Chromosome 2.
DR   Proteomes; UP000059680; Chromosome 2.
DR   Genevisible; Q6H7S2; OS.
DR   GO; GO:0010494; C:cytoplasmic stress granule; IBA:GO_Central.
DR   GO; GO:0000932; C:P-body; 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:0003729; F:mRNA binding; IBA:GO_Central.
DR   GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR   GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
DR   GO; GO:0017148; P:negative regulation of translation; IBA:GO_Central.
DR   GO; GO:0033962; P:P-body assembly; IBA:GO_Central.
DR   GO; GO:0034063; P:stress granule assembly; 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; 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   Alternative splicing; ATP-binding; Cytoplasm; Helicase; Hydrolase;
KW   mRNA processing; mRNA transport; Nucleotide-binding; Reference proteome;
KW   RNA-binding; Translation regulation; Transport.
FT   CHAIN           1..508
FT                   /note="DEAD-box ATP-dependent RNA helicase 8"
FT                   /id="PRO_0000282459"
FT   DOMAIN          165..335
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          345..505
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   REGION          1..123
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           134..162
FT                   /note="Q motif"
FT   MOTIF           283..286
FT                   /note="DEAD box"
FT   COMPBIAS        23..50
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        100..114
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         178..185
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   VAR_SEQ         31..55
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:12869764"
FT                   /id="VSP_024161"
FT   CONFLICT        118
FT                   /note="P -> S (in Ref. 5; AK066504)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   508 AA;  58167 MW;  C748F6A47FC6CE24 CRC64;
     MDPRARYPPG IGNGRGGNPN YYNRGPPLQQ QHNHHQQQQT SAPHHQQYVQ RQPQQHHHHN
     HHQQHQQQQQ QWLRRNQIAR EAAGTDRNSE PKAVAQSPAV DGIDSSSQDW KAQLKLPPQD
     TRYRTEDVTA TKGNEFEDYF LKRELLMGIY EKGFERPSPI QEESIPIALT GSDILARAKN
     GTGKTAAFCI PALEKIDQEK NAIQVVILVP TRELALQTSQ VCKELGKHLK IQVMVTTGGT
     SLKDDIIRLY QPVHLLVGTP GRILDLTKKG ICILKDCSML IMDEADKLLS PEFQPSVEQL
     IRYLPASRQI LMFSATFPVT VKEFKDKYLP KPYVINLMDE LTLKGITQFY AFVEERQKVH
     CLNTLFSKLQ INQSIIFCNS VNRVELLAKK ITELGYSCFY IHAKMLQDHR NRVFHDFRNG
     ACRNLVCTDL FTRGIDIQAV NVVINFDFPK TAETYLHRVG RSGRFGHLGL AVNLITYEDR
     FNLYRIEQEL GTEIKPIPPQ IDQAIYCQ
 
 
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