DEAHB_ARATH
ID DEAHB_ARATH Reviewed; 1787 AA.
AC P0CE10; Q9SV27;
DT 02-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 02-MAR-2010, sequence version 1.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=ATP-dependent RNA helicase DEAH11, chloroplastic;
DE EC=3.6.4.13;
DE Flags: Precursor;
GN OrderedLocusNames=At4g01020 {ECO:0000312|Araport:AT4G01020};
GN ORFNames=F3I3.40 {ECO:0000312|EMBL:CAB45785.1};
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=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(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 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 -!- 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: Plastid, chloroplast {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DEAH subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB45785.1; Type=Erroneous gene model prediction; Note=The predicted gene At4g01020 has been split into 2 genes: At4g01020 and At4g01026.; Evidence={ECO:0000305};
CC Sequence=CAB80911.1; Type=Erroneous gene model prediction; Note=The predicted gene At4g01020 has been split into 2 genes: At4g01020 and At4g01026.; Evidence={ECO:0000305};
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DR EMBL; AL080237; CAB45785.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161491; CAB80911.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE81967.1; -; Genomic_DNA.
DR PIR; T10542; T10542.
DR RefSeq; NP_567206.1; NM_116330.3.
DR AlphaFoldDB; P0CE10; -.
DR SMR; P0CE10; -.
DR STRING; 3702.AT4G01020.1; -.
DR PaxDb; P0CE10; -.
DR PRIDE; P0CE10; -.
DR ProteomicsDB; 222200; -.
DR EnsemblPlants; AT4G01020.1; AT4G01020.1; AT4G01020.
DR GeneID; 826439; -.
DR Gramene; AT4G01020.1; AT4G01020.1; AT4G01020.
DR KEGG; ath:AT4G01020; -.
DR Araport; AT4G01020; -.
DR TAIR; locus:2125211; AT4G01020.
DR eggNOG; KOG0922; Eukaryota.
DR eggNOG; KOG1812; Eukaryota.
DR HOGENOM; CLU_001832_9_0_1; -.
DR InParanoid; P0CE10; -.
DR OMA; VENNGVF; -.
DR OrthoDB; 28987at2759; -.
DR PhylomeDB; P0CE10; -.
DR PRO; PR:P0CE10; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; P0CE10; baseline and differential.
DR Genevisible; P0CE10; AT.
DR GO; GO:0009507; C:chloroplast; 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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR Gene3D; 1.10.10.2130; -; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR011709; DEAD-box_helicase_OB_fold.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR042035; DEAH_win-hel_dom.
DR InterPro; IPR002464; DNA/RNA_helicase_DEAH_CS.
DR InterPro; IPR007502; Helicase-assoc_dom.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR002867; IBR_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR044066; TRIAD_supradom.
DR InterPro; IPR013087; Znf_C2H2_type.
DR InterPro; IPR018957; Znf_C3HC4_RING-type.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF04408; HA2; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF01485; IBR; 1.
DR Pfam; PF07717; OB_NTP_bind; 1.
DR Pfam; PF00097; zf-C3HC4; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00847; HA2; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00647; IBR; 2.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS00690; DEAH_ATP_HELICASE; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS51873; TRIAD; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 3: Inferred from homology;
KW ATP-binding; Chloroplast; Helicase; Hydrolase; Metal-binding;
KW Nucleotide-binding; Plastid; Reference proteome; Repeat; Transferase;
KW Transit peptide; Ubl conjugation pathway; Zinc; Zinc-finger.
FT TRANSIT 1..33
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 34..1787
FT /note="ATP-dependent RNA helicase DEAH11, chloroplastic"
FT /id="PRO_0000391720"
FT DOMAIN 313..477
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 507..673
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT ZN_FING 1561..1609
FT /note="RING-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT ZN_FING 1628..1693
FT /note="IBR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT ZN_FING 1719..1747
FT /note="RING-type 2; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT REGION 1..75
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1557..1764
FT /note="TRIAD supradomain"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT MOTIF 424..427
FT /note="DEAH box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT COMPBIAS 1..64
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1732
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 326..333
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT BINDING 1561
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 1564
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 1577
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 1579
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 1582
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 1585
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 1604
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 1609
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 1649
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 1654
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 1672
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 1675
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 1680
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 1683
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 1688
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 1693
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 1719
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 1722
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 1737
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 1739
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
SQ SEQUENCE 1787 AA; 202131 MW; EF6319FEC8C196C9 CRC64;
MRNSFPPSDG GRSTTDRRQQ SFPSSSTNRY NSRSAQSSPP LNHCTTWNQQ HSQYHNTNFP
PNYRRDRAPS SGFSPPVTRA RPNFIVQLLH PAAANSDTKL SKKQEIESIA LLCEIPEESV
HVPQFGCIAA SFSFRQWVDA RSAVVALWDY RLQGRHDFVP ELIPNVVVPS DMDELKDRLR
DLFSSHVLSL MENGQGVKKV RMEIDDKSRQ VASFSSKRGL KFEVFEKKKA LEAERDLVVN
RLDEFNNAMK SILRYLIGQD GYEFDVDDED DEDVAVFSLE GAYDWRRIHY LILRECRRLE
DGLPIYAYRR QILKKIHCEQ IMVLIGETGS GKSTQLVQFL ADSGVAASES IVCTQPRKIA
AMTLTDRVRE ESSGCYEENT VSCTPTFSST EEISSKVVYM TDNCLLQHYM KDRSLSGISC
VIIDEAHERS LNTDLLLALL RKLLSRRIDL RLVIMSATAD ANQLSQYLFD CGILHVNGRN
FPVEIVYSPS GTEENSVVGR IASYAGDVVK MAVEIHKTEK EGTILAFLTS QAEVEWACER
FVAPSAIALP LHGKLSFEEQ FMVFQNYPGR RKVIFATNIA ETSLTIPGVK YVIDSGMVKE
SKYEPRTGMS ILKVCQVSQS SARQRAGRAG RTEPGRCYRL YSKTDFDSMN LNQEPEIRRV
HLGVALLRML ALGIDNIAAF EFVDAPVPEA IAMAIQNLVQ LGAVVEKNGV LELTQEGHCL
VKLGLEPKLG KLILGCFRHR MGKEGIVLAA VMANASSIFC RVGNFDDKMK ADRLKVQFCN
DNGDLFTLLS VYKEWASLPR DRRNKWCWEN SLNAKSMRRC EDTVKELEIC IERELTLVSP
SYWVWNPNEG TKHDKYLKMV ILASLAENVA MYTGYDQLGY EVALTSQQVQ LHPSCSLLAF
GQKPSWVVFG ELLSIVDQYL VCVTAFDFEA LYMLDPPPPF DASQMDERRL RVKKVVGCSS
TVLKRFCGKS NRSLLSIVSR ARSLCSDERI GIQVDVDQNE IRLYASPLDM EKVSALVNDA
LECEKKWMRN ECLEKYLFHG RGQIPIALFG SGAQIKHLEV DQRFLTVDVH YYGDDVVDDR
ELLTFLEKKI DGCICSIYKF AANKQDCDEK EKWGRITFLT PESAMKATEI QKFDFKGSVL
KVFPSLSTGG GIFKMPYFSS VTAKIRWPRK ESSGRGCLKC PSGDIHSILG DITSLEIGTN
YVHIQRDQLS NDSILISGLG DLSEAEVLDV LEFRTQRRDL NFFIFRKKYS VQCPSPTACE
EELHKRIFAR MSAKNPEPNC VQVQVFEPKE DNYFMRALIK FDGRLHLEAA KALQELNGEV
LPGCLPWQKI KCEQLFQSSI ICSASIYNTV KRQLNVLLAR FERQKGGECC LEPTHNGAYR
VKITAYATRP VAEMRRELEE LLRGKPINHP GFTPRVVQHL MSRDGINLMR KIQQETETYI
LLDRHNLTVR ICGTSEKIAK AEQELVQSLM DYHESKQLEI HLRGPEIRPD LMKEVVKRFG
PELQGIKEKV HGVDLKLNTR YHVIQVHGSK EMRQEVQKMV NELAREKSAL GEKPDEIELE
CPICLSEVDD GYSLEGCSHL FCKACLLEQF EASMRNFDAF PILCSHIDCG APIVVADMRA
LLSQEKLDEL ISASLSAFVT SSDGKLRFCS TPDCPSIYRV AGPQESGEPF ICGACHSETC
TRCHLEYHPL ITCERYKKFK ENPDLSLKDW AKGKDVKECP ICKSTIEKTD GCNHLQCRCG
KHICWTCLDV FTQAEPCYAH LRTIHGGIGL VELGVPEHPV AQPVHRL
