DEXHD_ARATH
ID DEXHD_ARATH Reviewed; 2172 AA.
AC O48534; Q93YW2;
DT 20-JAN-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=DExH-box ATP-dependent RNA helicase DExH13 {ECO:0000305};
DE EC=3.6.4.13 {ECO:0000305};
DE AltName: Full=BRR2 homolog B {ECO:0000305};
DE Short=AtBRR2B {ECO:0000305};
DE AltName: Full=Pre-mRNA-splicing helicase BRR2B {ECO:0000305};
GN Name=BRR2B {ECO:0000305}; OrderedLocusNames=At2g42270;
GN ORFNames=T24P15.18 {ECO:0000312|EMBL:AAB88651.1};
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=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] OF 1556-2172.
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.
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: RNA helicase that plays an essential role in pre-mRNA
CC splicing as component of the U5 snRNP and U4/U6-U5 tri-snRNP complexes.
CC Involved in spliceosome assembly, activation and disassembly.
CC {ECO:0000250|UniProtKB:P32639}.
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 Evidence={ECO:0000305};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
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DR EMBL; AC002561; AAB88651.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC10098.1; -; Genomic_DNA.
DR EMBL; AY059740; AAL24152.2; -; mRNA.
DR PIR; T00936; T00936.
DR RefSeq; NP_181756.1; NM_129789.2.
DR AlphaFoldDB; O48534; -.
DR SMR; O48534; -.
DR IntAct; O48534; 1.
DR MINT; O48534; -.
DR STRING; 3702.AT2G42270.1; -.
DR PaxDb; O48534; -.
DR PRIDE; O48534; -.
DR ProteomicsDB; 224252; -.
DR EnsemblPlants; AT2G42270.1; AT2G42270.1; AT2G42270.
DR GeneID; 818828; -.
DR Gramene; AT2G42270.1; AT2G42270.1; AT2G42270.
DR KEGG; ath:AT2G42270; -.
DR Araport; AT2G42270; -.
DR TAIR; locus:2059969; AT2G42270.
DR eggNOG; KOG0951; Eukaryota.
DR HOGENOM; CLU_000335_1_0_1; -.
DR InParanoid; O48534; -.
DR OMA; QICEETL; -.
DR OrthoDB; 154891at2759; -.
DR PhylomeDB; O48534; -.
DR PRO; PR:O48534; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O48534; baseline and differential.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR GO; GO:0005681; C:spliceosomal complex; 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:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003724; F:RNA helicase activity; IBA:GO_Central.
DR GO; GO:0000388; P:spliceosome conformational change to release U4 (or U4atac) and U1 (or U11); IBA:GO_Central.
DR Gene3D; 1.10.10.10; -; 2.
DR Gene3D; 2.60.40.150; -; 2.
DR Gene3D; 3.40.50.300; -; 4.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR041094; Brr2_helicase_PWI.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR014756; Ig_E-set.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR004179; Sec63-dom.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR Pfam; PF00270; DEAD; 2.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF18149; Helicase_PWI; 1.
DR Pfam; PF02889; Sec63; 2.
DR SMART; SM00382; AAA; 2.
DR SMART; SM00487; DEXDc; 2.
DR SMART; SM00490; HELICc; 2.
DR SMART; SM00973; Sec63; 2.
DR SUPFAM; SSF46785; SSF46785; 2.
DR SUPFAM; SSF52540; SSF52540; 4.
DR SUPFAM; SSF81296; SSF81296; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 2.
DR PROSITE; PS51194; HELICASE_CTER; 2.
PE 2: Evidence at transcript level;
KW ATP-binding; Helicase; Hydrolase; mRNA processing; mRNA splicing;
KW Nucleotide-binding; Nucleus; Reference proteome; Repeat; RNA-binding;
KW Spliceosome.
FT CHAIN 1..2172
FT /note="DExH-box ATP-dependent RNA helicase DExH13"
FT /id="PRO_0000435300"
FT DOMAIN 515..698
FT /note="Helicase ATP-binding 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 742..946
FT /note="Helicase C-terminal 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT DOMAIN 1007..1308
FT /note="SEC63 1"
FT /evidence="ECO:0000255"
FT DOMAIN 1361..1538
FT /note="Helicase ATP-binding 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 1575..1772
FT /note="Helicase C-terminal 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT DOMAIN 1840..2157
FT /note="SEC63 2"
FT /evidence="ECO:0000255"
FT REGION 20..83
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 640..643
FT /note="DEIH box"
FT /evidence="ECO:0000305"
FT MOTIF 1480..1483
FT /note="DELH box"
FT /evidence="ECO:0000305"
FT COMPBIAS 28..83
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 528..535
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT BINDING 1374..1381
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 2172 AA; 247389 MW; 733F608BCE0C79D7 CRC64;
MTNLGGGGAE EQARLKQYGY KVNSSLVLNS DERRRDTHES SGEPESLRGR IDPKSFGDRV
VRGRPHELDE RLNKSKKKKE RCDDLVSARE SKRVRLREVS VLNDTEDGVY QPKTKETRVA
FEIMLGLIQQ QLGGQPLDIV CGAADEILAV LKNESVKNHE KKVEIEKLLN VITDQVFSQF
VSIGKLITDY EEGGDSLSGK ASEDGGLDYD IGVALECEED DDESDLDMVQ DEKDEEDEDV
VELNKTGVVQ VGVAINGEDA RQAKEDTSLN VLDIDAYWLQ RKISQEYEQK IDAQECQELA
EELLKILAEG NDRDVEIKLL EHLQFEKFSL VKFLLQNRLK VVWCTRLARG RDQEERNQIE
EEMLGLGSEL AAIVKELHAK RATAKEREEK REKDIKEEAQ HLMDDDSGVD GDRGMRDVDD
LDLENGWLKG QRQVMDLESL AFNQGGFTRE NNKCELPDRS FRIRGKEFDE VHVPWVSKKF
DSNEKLVKIS DLPEWAQPAF RGMQQLNRVQ SKVYGTALFK ADNILLCAPT GAGKTNVAVL
TILHQLGLNM NPGGTFNHGN YKIVYVAPMK ALVAEVVDSL SQRLKDFGVT VKELSGDQSL
TGQEIKETQI IVTTPEKWDI ITRKSGDRTY TQLVRLLIID EIHLLDDNRG PVLESIVART
LRQIESTKEH IRLVGLSATL PNCDDVASFL RVDLKNGLFI FDRSYRPVPL GQQYIGINVK
KPLRRFQLMN DICYQKVVAV AGKHQVLIFV HSRKETAKTA RAIRDTAMAN DTLSRFLKED
SQSREILKCL AGLLKNNDLK ELLPYGFAIH HAGLTRTDRE IVENQFRWGN LQVLISTATL
AWGVNLPAHT VIIKGTQVYN PERGEWMELS PLDVMQMIGR AGRPQYDQQG EGIIITGYSK
LQYYLRLMNE QLPIESQFIS KLADQLNAEI VLGTIQNARE ACHWLGYTYL YVRMVRNPTL
YGVSPDALAK DLLLEERRAD LIHSAATILD KNNLIKYDRK SGHFQVTDLG RIASYYYISH
GTIAAYNENL KPTMNDIELC RLFSLSEEFK YVTVRQDEKM ELAKLLDRVP IPVKETLEDP
SAKINVLLQV YISKLKLEGL SLTSDMVYIT QSAGRLLRAI FEIVLKRGWA QLSQKALNLS
KMVGKRMWSV QTPLWQFPGI PKEILMKLEK NDLVWERYYD LSSQELGELI CNPKMGRPLH
KYIHQFPKLK LAAHVQPISR SVLQVELTVT PDFHWDDKAN KYVEPFWIIV EDNDGEKILH
HEYFLFKKRV IDEDHTLNFT VPISEPIPPQ YFIRVVSDKW LDSPTVLPVS FRHLILPEKY
PPPTELLDLQ PLPVMALRNP SYETLYQDFK HFNPVQTQVF TVLYNTSDNV VVAAPTGSGK
TICAEFAILR NHLEGPDSAM RVVYIAPLEA IAKEQFRDWE KKFGKGLGLR VVELTGETLL
DLKLLEKGQI IISTPEKWDA LSRRWKQRKY IQQVSLFIVD ELHLIGGQGG QVLEVIVSRM
RYISSQVGNK IRIVALSTSL ANAKDLGEWI GASSCGVFNF PPNVRPVPLE IHIHGVDILS
FEARMQAMTK PTYTAIVQHA KNKKPAIVFV PTRKHVRLTA VDLIAYSHMD NMKSPDFLLG
NLEELEPFLI QICEETLKET LRHGIGYLHE GLSNLDQEIV TQLFEAGRIQ VCVMSSSLCW
GTPLKAHLVV VMGTHFYDGR ENSHSDYPIS NLLQMMGRGS RPLLDDAGKC VIFCHAPRKE
YYKKFLYEAL PVESHLQHFL HDNFNAEVVA RVIENKQDAV DYLTWSFMYR RLPQNPNYYN
LLGVSHRHLS DHLSELVENT LSDLEVSKCI EIDNELDLSP LNLGMIASYY YINYTTIERF
SSLLASKTKM KGLLEILTSA SEYDLIPIRP GEEDAVRRLI NHQRFSFQNP RCTDPRVKTS
ALLQAHFSRQ KISGNLVMDQ CEVLLSATRL LQAMVDVISS NGCLNLALLA MEVSQMVTQG
MWDRDSMLLQ LPHFTKDLAK RCHENPGNNI ETIFDLVEME DDKRQELLQM SDAQLLDIAR
FCNRFPNIDL TYEIVGSNEV SPGKDITLQV LLERDMEGRT EVGPVDAPRY PKTKEEGWWL
VVGEAKTNQL MAIKRISLQR KAQVKLEFAV PTETGEKSYT LYFMCDSYLG CDQEYSFTVD
VKDSDAADHM EE
