RH29_ORYSI
ID RH29_ORYSI Reviewed; 851 AA.
AC A2YV85; Q0J5P3; Q68Q05; Q6ZA73;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 2.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=DEAD-box ATP-dependent RNA helicase 29;
DE Short=RNAH;
DE EC=3.6.4.13;
GN ORFNames=OsI_028228;
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. IR36; TISSUE=Anther;
RA Yau C.P., Zhuang C.X., Zee S.Y., Yip W.K.;
RT "Isolation of anther-specific genes during early pollen development in
RT rice.";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
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).
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 -!- 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. DDX54/DBP10
CC subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAU01909.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AY644647; AAU01909.1; ALT_INIT; mRNA.
DR EMBL; CM000133; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; A2YV85; -.
DR SMR; A2YV85; -.
DR STRING; 39946.A2YV85; -.
DR Proteomes; UP000007015; Chromosome 8.
DR GO; GO:0005634; C:nucleus; IEA:InterPro.
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 Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR012541; DBP10_C.
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; IPR014014; RNA_helicase_DEAD_Q_motif.
DR Pfam; PF08147; DBP10CT; 1.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR SMART; SM01123; DBP10CT; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; SSF52540; 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; Reference proteome;
KW RNA-binding.
FT CHAIN 1..851
FT /note="DEAD-box ATP-dependent RNA helicase 29"
FT /id="PRO_0000302059"
FT DOMAIN 80..253
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 277..426
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..49
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 702..851
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 49..77
FT /note="Q motif"
FT MOTIF 201..204
FT /note="DEAD box"
FT COMPBIAS 28..46
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 771..827
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 93..100
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT CONFLICT 30
FT /note="P -> L (in Ref. 1; AAU01909)"
FT /evidence="ECO:0000305"
FT CONFLICT 44
FT /note="K -> R (in Ref. 1; AAU01909)"
FT /evidence="ECO:0000305"
FT CONFLICT 342
FT /note="K -> E (in Ref. 1; AAU01909)"
FT /evidence="ECO:0000305"
FT CONFLICT 462
FT /note="R -> K (in Ref. 1; AAU01909)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 851 AA; 95478 MW; 94214319EA0874B4 CRC64;
MARLNPSKPS SRGGKPRSSS ADAMAEHKPP PGRPKREGEG ASKKKAKSGG FESMGLCEEV
YRGVRHKGYR VPTPIQRKAM PLILAGHDIA AMARTGSGKT AAFLVPMIQR LRRHDAGAGI
RALILSPTRD LATQTLKFAQ QLGKFTDLKI SLIVGGDSME SQFEELAENP DIIIATPGRL
VHHLAEVEDL NLRTVEYVVF DEADSLFSLG LIQQLHDILH KLSDTRQTLL FSATLPQALA
DFAKAGLRDP QIVRLDLDKK ISPDLKLAFF TLRQEEKLAA LLYLVRERIS SEEQTIIFVS
TKHHVEFLNI LFREEGLEPS LSYGAMDQEA RNIHISKFRA RKTMILIVTD VAARGLDIPL
LDNVVNWDFP AKPKLFVHRV GRVARQGRSG TAYTFVTSED MAYLLDLHLF LSKPLRPAPT
EEELLKDMEG MNLKIDRALA NGETVYGRFP QTIIDLVSDG IREVINGCTD LIALEKPCTN
AFHLYLKTRP MPSTESIRRV KDLPREGLHP IFRDVLGSDE LSALAFSERL KSFRPKQTIL
EAEGEAARGS NQWLDVMKKK REVHEGIINL VHQKNNVDHE PKEELVENIS NWERKDVCGN
KRKLQSFRDE EYYISSVPQN QHLEAGLSVR ANEGFVENRL DAAVLDLVDD ETSGMQAQKT
RYHWKKNKFV KLNSGDRVTA TGKIKTESGA KLKPTKTGIY KKWQQKTHRS IDTGRKYGGF
AEEGASTTGS HQRGNRKHTA AGRGRRYIPN ADVPSEIRNP EQIQKSRQQK AMDIARMKNR
STKESKFQKF QKNNRRHDGP SKDGKFQKNR RPDGNGKNRR PDGNGKGRGK GKGNANGFGK
GKGKMKGKGT R