ID   RH21_ARATH              Reviewed;         733 AA.
AC   P93008;
DT   30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   03-AUG-2022, entry version 148.
DE   RecName: Full=DEAD-box ATP-dependent RNA helicase 21;
DE            EC=3.6.4.13;
GN   Name=RH21; OrderedLocusNames=At2g33730; ORFNames=T1B8.4;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10617197; DOI=10.1038/45471;
RA   Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA   Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA   Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA   Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA   Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA   Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA   Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT   "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL   Nature 402:761-768(1999).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT   genome.";
RL   Plant J. 89:789-804(2017).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=14593172; DOI=10.1126/science.1088305;
RA   Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA   Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA   Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA   Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA   Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA   Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA   Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA   Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA   Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA   Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA   Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA   Ecker J.R.;
RT   "Empirical analysis of transcriptional activity in the Arabidopsis
RT   genome.";
RL   Science 302:842-846(2003).
RN   [4]
RP   GENE FAMILY, AND NOMENCLATURE.
RX   PubMed=17168887; DOI=10.1111/j.1467-7652.2004.00084.x;
RA   Mingam A., Toffano-Nioche C., Brunaud V., Boudet N., Kreis M., Lecharny A.;
RT   "DEAD-box RNA helicases in Arabidopsis thaliana: establishing a link
RT   between quantitative expression, gene structure and evolution of a family
RT   of genes.";
RL   Plant Biotechnol. J. 2:401-415(2004).
RN   [5]
RP   GENE FAMILY.
RX   PubMed=24265739; DOI=10.1371/journal.pone.0078982;
RA   Xu R., Zhang S., Huang J., Zheng C.;
RT   "Genome-wide comparative in silico analysis of the RNA helicase gene family
RT   in Zea mays and Glycine max: a comparison with Arabidopsis and Oryza
RT   sativa.";
RL   PLoS ONE 8:E78982-E78982(2013).
CC   -!- FUNCTION: ATP-dependent RNA helicase involved in mRNA splicing. May
CC       destabilize the U1/5'-splice site duplex to permit an effective
CC       competition for the 5'-splice site by the U6 snRNA, resulting in the
CC       switch between U1 and U6 at the 5'-splice site. May also act to unwind
CC       the U4/U6 base-pairing interaction in the U4/U6/U5 snRNP, facilitating
CC       the first covalent step of splicing (By similarity). {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 {ECO:0000250}. Nucleus {ECO:0000250}.
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. DDX23/PRP28
CC       subfamily. {ECO:0000305}.
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DR   EMBL; U78721; AAC69128.1; -; Genomic_DNA.
DR   EMBL; CP002685; AEC08875.1; -; Genomic_DNA.
DR   EMBL; AY065194; AAL38370.1; -; mRNA.
DR   EMBL; AY093244; AAM13243.1; -; mRNA.
DR   PIR; H84748; H84748.
DR   RefSeq; NP_180929.1; NM_128931.3.
DR   AlphaFoldDB; P93008; -.
DR   SMR; P93008; -.
DR   BioGRID; 3285; 4.
DR   STRING; 3702.AT2G33730.1; -.
DR   PaxDb; P93008; -.
DR   PRIDE; P93008; -.
DR   ProteomicsDB; 236975; -.
DR   EnsemblPlants; AT2G33730.1; AT2G33730.1; AT2G33730.
DR   GeneID; 817938; -.
DR   Gramene; AT2G33730.1; AT2G33730.1; AT2G33730.
DR   KEGG; ath:AT2G33730; -.
DR   Araport; AT2G33730; -.
DR   TAIR; locus:2057640; AT2G33730.
DR   eggNOG; KOG0333; Eukaryota.
DR   HOGENOM; CLU_003041_11_2_1; -.
DR   InParanoid; P93008; -.
DR   OMA; KKFNFEW; -.
DR   OrthoDB; 820037at2759; -.
DR   PhylomeDB; P93008; -.
DR   PRO; PR:P93008; -.
DR   Proteomes; UP000006548; Chromosome 2.
DR   ExpressionAtlas; P93008; baseline and differential.
DR   Genevisible; P93008; AT.
DR   GO; GO:0071013; C:catalytic step 2 spliceosome; IBA:GO_Central.
DR   GO; GO:0005737; C:cytoplasm; HDA:TAIR.
DR   GO; GO:0005634; C:nucleus; HDA:TAIR.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR   GO; GO:0140223; F:general transcription initiation factor activity; IMP:TAIR.
DR   GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR   GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR   GO; GO:0000398; P:mRNA splicing, via spliceosome; IMP:TAIR.
DR   GO; GO:1903800; P:positive regulation of miRNA maturation; IMP:TAIR.
DR   GO; GO:2000636; P:positive regulation of primary miRNA processing; IMP:TAIR.
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   ATP-binding; Coiled coil; Cytoplasm; Helicase; Hydrolase; mRNA processing;
KW   mRNA splicing; Nucleotide-binding; Nucleus; Reference proteome;
KW   RNA-binding.
FT   CHAIN           1..733
FT                   /note="DEAD-box ATP-dependent RNA helicase 21"
FT                   /id="PRO_0000239162"
FT   DOMAIN          344..539
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          566..710
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   REGION          39..147
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          705..733
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          129..159
FT                   /evidence="ECO:0000255"
FT   COILED          219..248
FT                   /evidence="ECO:0000255"
FT   MOTIF           313..341
FT                   /note="Q motif"
FT   MOTIF           470..473
FT                   /note="DEAD box"
FT   COMPBIAS        708..722
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         357..364
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ   SEQUENCE   733 AA;  85277 MW;  D5944A4BC3F875EC CRC64;
     MKRTINEVVG STSVNTLDSS IAKKPVFLTK KQREELALKR RQDQISEQRV RREQLGRPEP
     ETEDVSNGDT NRDKDRDRDR DRDRERDRDR ERDRGRDRDR DRDRDRDRDR ERERDRERDR
     RERDREPDRR NREKEREEEV KAREKARVEK LVEREKEKEL DAIKEQYLGG KKPKKRVIRP
     SEKFRFSFDW ENTEDTSRDM NVLYQNPHEA QLLFGRGFRA GMDRREQKKQ AAKHEKEMRD
     EIRKKDGIVE KPEEAAAQRV REEAADTYDS FDMRVDRHWS DKRLEEMTER DWRIFREDFN
     ISYKGSRIPR PMRSWEESKL TSELLKAVER AGYKKPSPIQ MAAIPLGLQQ RDVIGIAETG
     SGKTAAFVLP MLAYISRLPP MSEENETEGP YAVVMAPTRE LAQQIEEETV KFAHYLGFRV
     TSIVGGQSIE EQGLKITQGC EIVIATPGRL IDCLERRYAV LNQCNYVVLD EADRMIDMGF
     EPQVAGVLDA MPSSNLKPEN EEEELDEKKI YRTTYMFSAT MPPGVERLAR KYLRNPVVVT
     IGTAGKTTDL ISQHVIMMKE SEKFFRLQKL LDELGEKTAI VFVNTKKNCD SIAKNLDKAG
     YRVTTLHGGK SQEQREISLE GFRAKRYNVL VATDVVGRGI DIPDVAHVIN YDMPKHIEMY
     THRIGRTGRA GKSGVATSFL TLHDTEVFYD LKQMLVQSNS AVPPELARHE ASRFKPGTVP
     DRPPRHSDTV YIN