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Database: UniProt
Entry: Q109G2
LinkDB: Q109G2
Original site: Q109G2 
ID   RH12_ORYSJ              Reviewed;         521 AA.
AC   Q109G2; A0A0P0XWK1; B7ELN4; Q109G3; Q337E8; Q53RP3; Q9FVY5;
DT   03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   03-APR-2007, sequence version 2.
DT   16-OCT-2019, entry version 84.
DE   RecName: Full=DEAD-box ATP-dependent RNA helicase 12;
DE            EC=3.6.4.13;
GN   OrderedLocusNames=Os10g0503700, LOC_Os10g35990;
GN   ORFNames=OsJ_32082, OSJNBb0073N24.12;
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=12791992; DOI=10.1126/science.1083523;
RA   Yu Y., Rambo T., Currie J., Saski C., Kim H.-R., Collura K.,
RA   Thompson S., Simmons J., Yang T.-J., Nah G., Patel A.J., Thurmond S.,
RA   Henry D., Oates R., Palmer M., Pries G., Gibson J., Anderson H.,
RA   Paradkar M., Crane L., Dale J., Carver M.B., Wood T., Frisch D.,
RA   Engler F., Soderlund C., Palmer L.E., Teytelman L., Nascimento L.,
RA   De la Bastide M., Spiegel L., Ware D., O'Shaughnessy A., Dike S.,
RA   Dedhia N., Preston R., Huang E., Ferraro K., Kuit K., Miller B.,
RA   Zutavern T., Katzenberger F., Muller S., Balija V., Martienssen R.A.,
RA   Stein L., Minx P., Johnson D., Cordum H., Mardis E., Cheng Z.,
RA   Jiang J., Wilson R., McCombie W.R., Wing R.A., Yuan Q., Ouyang S.,
RA   Liu J., Jones K.M., Gansberger K., Moffat K., Hill J., Tsitrin T.,
RA   Overton L., Bera J., Kim M., Jin S., Tallon L., Ciecko A., Pai G.,
RA   Van Aken S., Utterback T., Reidmuller S., Bormann J., Feldblyum T.,
RA   Hsiao J., Zismann V., Blunt S., de Vazeille A.R., Shaffer T., Koo H.,
RA   Suh B., Yang Q., Haas B., Peterson J., Pertea M., Volfovsky N.,
RA   Wortman J., White O., Salzberg S.L., Fraser C.M., Buell C.R.,
RA   Messing J., Song R., Fuks G., Llaca V., Kovchak S., Young S.,
RA   Bowers J.E., Paterson A.H., Johns M.A., Mao L., Pan H., Dean R.A.;
RT   "In-depth view of structure, activity, and evolution of rice
RT   chromosome 10.";
RL   Science 300:1566-1569(2003).
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.,
RA   McCombie W.R., Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S.,
RA   Childs K.L., Davidson R.M., Lin H., Quesada-Ocampo L.,
RA   Vaillancourt B., Sakai H., Lee S.S., Kim J., Numa H., Itoh T.,
RA   Buell C.R., Matsumoto T.;
RT   "Improvement of the Oryza sativa Nipponbare reference genome using
RT   next 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;
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.,
RA   Cong L., Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J.,
RA   Wang J., Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X.,
RA   Wang J., Wang X., Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y.,
RA   Zhang Z., Bao J., Han Y., Dong L., Ji J., Chen P., Wu S., Liu J.,
RA   Xiao Y., Bu D., Tan J., Yang L., Ye C., Zhang J., Xu J., Zhou Y.,
RA   Yu Y., Zhang B., Zhuang S., Wei H., Liu B., Lei M., Yu H., Li Y.,
RA   Xu H., Wei S., He X., Fang L., Zhang Z., Zhang Y., Huang X., Su Z.,
RA   Tong W., Li J., Tong Z., Li S., Ye J., Wang L., Fang L., Lei T.,
RA   Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F., Xu H.,
RA   Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q., Li W.,
RA   Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J., Gao L.,
RA   Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M., McDermott J.,
RA   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).
CC   -!- FUNCTION: ATP-dependent RNA helicase involved in mRNA turnover,
CC       and 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
CC       decapping and 5' to 3' exonucleotidic decay. {ECO:0000250}.
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. DDX6/DHH1
CC       subfamily. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAX95709.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=ABG66172.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=ABG66173.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
DR   EMBL; AC078840; AAG13612.1; -; Genomic_DNA.
DR   EMBL; AC084023; AAX95709.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; DP000086; ABB47852.2; -; Genomic_DNA.
DR   EMBL; DP000086; ABG66172.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; DP000086; ABG66173.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AP008216; BAF26914.2; -; Genomic_DNA.
DR   EMBL; AP014966; BAT11553.1; -; Genomic_DNA.
DR   EMBL; CM000147; EEE51233.1; -; Genomic_DNA.
DR   EMBL; AK073085; BAG93281.1; -; mRNA.
DR   RefSeq; XP_015614831.1; XM_015759345.1.
DR   SMR; Q109G2; -.
DR   STRING; 4530.OS10T0503700-01; -.
DR   PaxDb; Q109G2; -.
DR   PRIDE; Q109G2; -.
DR   EnsemblPlants; Os10t0503700-01; Os10t0503700-01; Os10g0503700.
DR   GeneID; 4349053; -.
DR   Gramene; Os10t0503700-01; Os10t0503700-01; Os10g0503700.
DR   KEGG; osa:4349053; -.
DR   eggNOG; KOG0326; Eukaryota.
DR   eggNOG; ENOG410XRAZ; LUCA.
DR   InParanoid; Q109G2; -.
DR   KO; K12614; -.
DR   OMA; YGRGPQP; -.
DR   OrthoDB; 583315at2759; -.
DR   Proteomes; UP000059680; Chromosome 10.
DR   ExpressionAtlas; Q109G2; baseline and differential.
DR   Genevisible; Q109G2; 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:0003729; F:mRNA binding; IBA:GO_Central.
DR   GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR   GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR   GO; GO:0033962; P:cytoplasmic mRNA processing body assembly; IBA:GO_Central.
DR   GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR   GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
DR   GO; GO:0006417; P:regulation of translation; IEA:UniProtKB-KW.
DR   GO; GO:0034063; P:stress granule assembly; 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   2: Evidence at transcript level;
KW   ATP-binding; Complete proteome; Cytoplasm; Helicase; Hydrolase;
KW   mRNA processing; mRNA transport; Nucleotide-binding;
KW   Reference proteome; RNA-binding; Translation regulation; Transport.
FT   CHAIN         1    521       DEAD-box ATP-dependent RNA helicase 12.
FT                                /FTId=PRO_0000282460.
FT   DOMAIN      178    348       Helicase ATP-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00541}.
FT   DOMAIN      358    518       Helicase C-terminal.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00542}.
FT   NP_BIND     191    198       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00541}.
FT   MOTIF       147    175       Q motif.
FT   MOTIF       296    299       DEAD box.
FT   COMPBIAS     11     52       Gly-rich.
FT   COMPBIAS     54     95       Gln-rich.
FT   CONFLICT    380    380       S -> L (in Ref. 1; AAX95709 and 2;
FT                                BAF26914). {ECO:0000305}.
FT   CONFLICT    449    449       D -> G (in Ref. 1; AAX95709 and 2;
FT                                BAF26914). {ECO:0000305}.
SQ   SEQUENCE   521 AA;  57950 MW;  26221BEF5781ECF6 CRC64;
     MHHPRARYPP GYTSGGGGGG GGGGGGGRGN GGGGFGGGGG GGGGNHGYYG RGPQPQPQQQ
     HYHHQAQQLH QHQQQQQHAQ RNSSSQQQQW LRRDQATAAA ASGEVAARTA AQLEAVDSSS
     EDWKAQLNLP APDTRYRTED VTATKGNEFE DYFLKRELLM GIYEKGFERP SPIQEESIPI
     ALTGSDILAR AKNGTGKTAA FCIPALEKID PEKNAIQVVI LVPTRELALQ TSQVCKELGK
     YLNIQVMVST GGTSLKDDIM RLYQPVHLLV GTPGRILDLT RKGICVLKDC SMLVMDEADK
     LLAPEFQPSI EQLIHFLPAN RQLLMFSATF PVTVKDFKEK YLPRPYVINL MDELTLKGIT
     QYYAFVEERQ KVHCLNTLFS KLQINQSIIF CNSVNRVELL AKKITELGYS CFYIHAKMLQ
     DHRNRVFHDF RNGACRNLVC TDLFTRGIDI QAVNVVINFD FPKTSETYLH RVGRSGRFGH
     LGLAVNLITY EDRFNLYRIE QELGTEIKTI PPQIDLAVYC Q
//
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