DEAHC_ARATH
ID DEAHC_ARATH Reviewed; 1775 AA.
AC F4KGU4; Q9LX92;
DT 09-DEC-2015, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=ATP-dependent RNA helicase DEAH12, chloroplastic;
DE EC=3.6.4.13;
DE Flags: Precursor;
GN OrderedLocusNames=At5g10370 {ECO:0000312|Araport:AT5G10370};
GN ORFNames=F12B17_280 {ECO:0000312|EMBL:CAB89406.1};
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=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(2000).
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=CAB89406.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL353995; CAB89406.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED91533.1; -; Genomic_DNA.
DR PIR; T50002; T50002.
DR RefSeq; NP_196599.2; NM_121075.3.
DR AlphaFoldDB; F4KGU4; -.
DR SMR; F4KGU4; -.
DR STRING; 3702.AT5G10370.1; -.
DR iPTMnet; F4KGU4; -.
DR PaxDb; F4KGU4; -.
DR PRIDE; F4KGU4; -.
DR ProteomicsDB; 224222; -.
DR EnsemblPlants; AT5G10370.1; AT5G10370.1; AT5G10370.
DR GeneID; 830901; -.
DR Gramene; AT5G10370.1; AT5G10370.1; AT5G10370.
DR KEGG; ath:AT5G10370; -.
DR Araport; AT5G10370; -.
DR TAIR; locus:2142459; AT5G10370.
DR eggNOG; KOG0922; Eukaryota.
DR eggNOG; KOG1812; Eukaryota.
DR HOGENOM; CLU_001832_9_0_1; -.
DR InParanoid; F4KGU4; -.
DR OMA; GHDNEEN; -.
DR OrthoDB; 28987at2759; -.
DR PRO; PR:F4KGU4; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; F4KGU4; baseline and differential.
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..1775
FT /note="ATP-dependent RNA helicase DEAH12, chloroplastic"
FT /id="PRO_0000434938"
FT DOMAIN 316..480
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 510..676
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT ZN_FING 1564..1612
FT /note="RING-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT ZN_FING 1631..1696
FT /note="IBR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT ZN_FING 1722..1750
FT /note="RING-type 2; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT REGION 1..77
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1560..1767
FT /note="TRIAD supradomain"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT MOTIF 427..430
FT /note="DEAH box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT ACT_SITE 1735
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 329..336
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
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 1567
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 1580
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="2"
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 1588
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 1607
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 1612
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 1652
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 1657
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 1678
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
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 1686
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 1691
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 1696
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
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 1725
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 1740
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 1742
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
SQ SEQUENCE 1775 AA; 201362 MW; F3EB71C0F11BDD1C CRC64;
MRNSFPPSDG GRSATDRRQQ SSHSSSTNRY NSRSAQSSPP LNHRPTWNQQ HSQYPNSNFP
PNYRRDRNPS SGYSPPVTRA RPNFIVQLLH PAAANSDTKL CFSTKKQEIE SLALLCEIPE
ESIHVPQFGC IAGSFSFRQW VDARSAVVAL WDYRLQGKHE FVPELIPNVI VPSDMNELKD
RLRDLFSSHI LSLMENGEGV KKVRLEIEEK SRQVVSFSSK RGLKFEVFEK KKAIEAERDL
VVNRLEEFNN AMKSILRYLI GQDGYEFDLD DEEEGDVAVF CLEGAYDWRR IHCLIRRECR
RLEDGLPIYA YRRQILKKIH REQIMVLIGE TGSGKSTQLV QFLADSGVAA SESIVCTQPR
KIAAMTLADR VREESSGCYE ENTVSCTPTF SSTEEISSKV VYMTDNCLLQ HYMKDRSLSG
ISCVIIDEAH ERSLNTDLLL ALLKKLLSRR IDLRLVIMSA TADAKQLSQY FFSCGILLVN
GRNFPVEIVY SPSDTEENSV VGGIASYVGD VVKMAVEIHK TEKEGTILAF LTSQAEVEWA
CERFITPSAI ALPLHGKLSF EEQFRVFQNH PGRRKVIFAT NIAETSLTIP GVKYVIDSGM
VKESKYEPRT GMSILKVCRV SQSSARQRAG RAGRTEPGRC YRLYSKNDFD SMNLNQEPEI
RRVHLGVALL RMLALGVNNI AEFNFVDAPV PEAIAMAVQN LVQLGAVVEK NGVHELTQEG
HCLVKLGLEP KLGKLILGCF RHRMGKEGIV LAAVMANASS IFCRVGNFDD KMKADRLKVQ
FCNQNGDLFT LLSVYKEWAS LPRERRNKWC WENSLNAKSM RRCEDTVKEL EICIERELTL
VSPSYWVWNP NEGTKHDKHL KMVILASLAE NVAMYTGYNQ LGYEVALTGQ QVQLHPSCSL
LAFGQKPSWV VFGELLSIVD QYLVCVTACD FEALYMLDPP PPFDVSQMDE RRLRIKKVVG
CSSTVLKRFC GKSNRSLLSI VSRARSLCSD ERIGIQVDVD QNEIRLYAPP LDMEKVSALV
NDALECEKKW MHNECLEKYL YHGRGQVPIA LFGSGAQIKH LEVDQRFLTV DVLYYGDDVV
DDRELLTFLE KKIDGSICSI YKFAANKQDC DEKEKWGRIT FLTPESAMKA TEIQKFYFKG
SVLKLFPSLS TGGGIFKMPY FSSVTAKIRW PRRESSGRGC LKCPSGDIHR ILGDISSLEI
GTNYVHIQRD QQSNDSILIS GLGDLSEAEV LDVLEFRTQR RDLNFFIFRK KYSVQCPSPT
ACEEELHKRI FARMSAKNPE PNCVQVQVFE PKEDNYFMRA LIKFDGRLHF EAAKALQELN
GEVLPGCLPW QKIKCEQLFQ SSIICSASIY NTVKRQLNVL LARFERQKGG ECCLEPTHNG
AYRVKITAYA TRPVAEMRRE LEELLRGRPI NHPGFTRRVL QHLMSRDGIN LMRKIQQETE
TYILLDRHNL TVRICGTSEK IAKAEQELIQ ALMDYHESKQ LEIHLRGPEI RPDLMKEVVK
RFGPELQGIK EKVHGVDLKL NTRYHVIQVH GSKEMRQEVQ KMVNELAREK SALGEKPDEI
EVECPICLSE VDDGYSLEGC SHLFCKACLL EQFEASMRNF DAFPILCSHI DCGAPIVLAD
MRALLSQEKL DELFSASLSS FVTSSDGKFR FCSTPDCPSV YRVAGPQESG EPFICGACHS
EICTRCHLEY HPLITCERYK KFKENPDLSL KDWAKGKNVK ECPICKSTIE KTDGCNHMKC
RCGKHICWTC LDVFTQEEPC YAHLRTIHGG IGLVE
