NIH_ARATH
ID NIH_ARATH Reviewed; 1576 AA.
AC F4IDQ6; Q9SHK6; Q9SMG9;
DT 20-JAN-2016, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=DExH-box ATP-dependent RNA helicase DExH2 {ECO:0000305};
DE EC=3.6.4.13 {ECO:0000305};
DE AltName: Full=DEIH-box RNA/DNA helicase {ECO:0000312|EMBL:BAA84364.1};
DE EC=3.6.4.12 {ECO:0000305};
GN Name=NIH {ECO:0000312|EMBL:BAA84364.1};
GN OrderedLocusNames=At1g06670 {ECO:0000312|Araport:AT1G06670};
GN ORFNames=F12K11.4 {ECO:0000312|EMBL:AAF24828.1};
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 [MRNA], MOTIF, SUBCELLULAR LOCATION, FUNCTION, AND
RP SUBUNIT.
RC STRAIN=cv. Columbia {ECO:0000312|EMBL:BAA84364.1};
RC TISSUE=Root {ECO:0000312|EMBL:BAA84364.1};
RX PubMed=10471743; DOI=10.1093/nar/27.18.3728;
RA Isono K., Yamamoto H., Satoh K., Kobayashi H.;
RT "An Arabidopsis cDNA encoding a DNA-binding protein that is highly similar
RT to the DEAH family of RNA/DNA helicase genes.";
RL Nucleic Acids Res. 27:3728-3735(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [3]
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 [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: May function as an ATP-dependent RNA/DNA helicase. Binds DNA
CC in vitro in a non-specific manner. {ECO:0000269|PubMed:10471743}.
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 -!- 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=3.6.4.12;
CC Evidence={ECO:0000305};
CC -!- SUBUNIT: Homodimer. {ECO:0000303|PubMed:10471743}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10471743}.
CC -!- DOMAIN: PH (probe helix) motif serves as a DNA recognition helix.
CC {ECO:0000303|PubMed:10471743}.
CC -!- SIMILARITY: Belongs to the DExH box helicase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF24828.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BAA84364.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; D84225; BAA84364.1; ALT_FRAME; mRNA.
DR EMBL; AC007592; AAF24828.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE28021.1; -; Genomic_DNA.
DR PIR; E86201; E86201.
DR RefSeq; NP_172152.1; NM_100544.3.
DR AlphaFoldDB; F4IDQ6; -.
DR SMR; F4IDQ6; -.
DR STRING; 3702.AT1G06670.1; -.
DR iPTMnet; F4IDQ6; -.
DR PaxDb; F4IDQ6; -.
DR PRIDE; F4IDQ6; -.
DR ProteomicsDB; 251061; -.
DR EnsemblPlants; AT1G06670.1; AT1G06670.1; AT1G06670.
DR GeneID; 837177; -.
DR Gramene; AT1G06670.1; AT1G06670.1; AT1G06670.
DR KEGG; ath:AT1G06670; -.
DR Araport; AT1G06670; -.
DR TAIR; locus:2009200; AT1G06670.
DR eggNOG; KOG0920; Eukaryota.
DR HOGENOM; CLU_001832_1_6_1; -.
DR InParanoid; F4IDQ6; -.
DR OrthoDB; 278674at2759; -.
DR PRO; PR:F4IDQ6; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; F4IDQ6; baseline and differential.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003677; F:DNA binding; IDA:TAIR.
DR GO; GO:0003678; F:DNA helicase activity; ISS: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:0006259; P:DNA metabolic process; ISS:TAIR.
DR CDD; cd06007; R3H_DEXH_helicase; 1.
DR Gene3D; 1.25.40.20; -; 1.
DR Gene3D; 3.30.1370.50; -; 1.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR011709; DEAD-box_helicase_OB_fold.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR007502; Helicase-assoc_dom.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR034083; R3H_DEXH_helicase.
DR InterPro; IPR001374; R3H_dom.
DR InterPro; IPR036867; R3H_dom_sf.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF04408; HA2; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF07717; OB_NTP_bind; 1.
DR Pfam; PF01424; R3H; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00847; HA2; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00393; R3H; 1.
DR SUPFAM; SSF48403; SSF48403; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR SUPFAM; SSF82708; SSF82708; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS51061; R3H; 1.
PE 1: Evidence at protein level;
KW ATP-binding; DNA-binding; Helicase; Hydrolase; Nucleotide-binding; Nucleus;
KW Reference proteome; Repeat; RNA-binding.
FT CHAIN 1..1576
FT /note="DExH-box ATP-dependent RNA helicase DExH2"
FT /id="PRO_0000435292"
FT DOMAIN 15..78
FT /note="R3H"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00382"
FT DOMAIN 227..396
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 561..735
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1137..1165
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1177..1223
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1260..1576
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 343..346
FT /note="DEIH box"
FT /evidence="ECO:0000305"
FT MOTIF 1349..1360
FT /note="PH1"
FT /evidence="ECO:0000303|PubMed:10471743"
FT MOTIF 1454..1465
FT /note="PH2"
FT /evidence="ECO:0000303|PubMed:10471743"
FT MOTIF 1530..1537
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000303|PubMed:10471743"
FT COMPBIAS 1137..1157
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1182..1209
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1260..1299
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1300..1315
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1362..1383
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1384..1429
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1468..1493
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1510..1524
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1540..1565
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 240..247
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 1576 AA; 174510 MW; 3CF741A18D424BAC CRC64;
MAKKKKDTKH TRLCEATGAW ATKVLEDFRA SGNDSYVFEQ QLTNSERGII HQMCRTMGLR
SKSNGSGEER RLSLFKGDGI SKSDKRRMYE ARNQKEKEGD GISKSYSKHR YETRFQKAGG
IRKTRISPKK LKCVSFPPEA KAVLHDLFTR YPPCDGDTTG TSLGIYTTGN VNSNWKDDFF
KKPHMTKHDI ENNVVSLSSR LKKERHFREI FEARSKLPIA SFRDAIISAV ESNQVVLIAG
ETGCGKTTQV PQYLLDHMWH SKKEACKIIC TQPRRISAIS VSDRISWERG ETIGRTVGYK
VRLQSEGGRE SSVVFCTNGI LLRVLIGKGV NSSVPDITHI IVDEIHERDS YSDFMLMILR
DLLPSNPHLR LILMSATLDA ERFSEYFGGC PVVRVPGFTY PVRTFFLDDA LSVLNSDKNS
HLLSAVKRDF KDEDKVSLDE AIDLAWTNDE FDCLVDLVSS EGSHEAYNYQ NSTTGLTPLM
VFAGKGRVSD VCKLLSVGAD CTLKSKEGIT ALELAEKENQ FETAQIIREH AGNIQSNSQQ
AQDLLDKYMA TIKPEEVDVG LIVKLMKKIC SDSKDGAILV FLPGWEEISK TKEKLLDDRF
FAHSAKFIIL CLHSRVPAEE QKKVFNRPPR GCRKIVLATN IAESAVTIDD VVYVIDSGRM
KEKSYDPYND VSTLQSSWVS KANAKQRAGR AGRCQAGICY HLYSKLRAAS LPEYRVPEVM
RMPVDELCLQ VKMLDPNCNV NDFLQKLMDP PVAQSIENAL IILKDIGALT PEEELTELGQ
KFGQLPVHPR ISKMIYFAIL VNCLDPALIL ACAADEKDPF TMPLSPGDRK KAAAAKHELA
SLYGDHSDHL ATVAAFQCWK NAKASGQAKE FCSKYFISQV VMKRLDDLCR KLQGELNRHG
VIPSSSSNCS LNAHDPGILR AVIAVGLYPM LGRMCPLSKN RTRSVIETIA GAKVRVPSLS
NNVDMSSTKF DEALIVFDEI TRGDWGVVIR SCTVLPTIPV LLFSREIAVS TTESYDAVKS
DDEEDHKVGN VGDAMDIDKE VGRPGEKIML GPENSVKVVV DRWLPFKVTA FEIAQMYILR
ERLMASILFK VKHPKENLPP HLGASMYAIA SVLSYDSLAQ SSVQTVAVQP ITSVVDATSP
RDDIPSTNPN ELREHDPNTT PMGSKLELAN KLGLGNMEES LPSNFADGNE QPDPNTSPVE
DVSAATKQKK MQSESKRCKS LNNVDLGNIE ENFGNMEENP PSDLAIGNEQ TLPKLASNLD
MGNMEENTPS DLANGNEKTE PNSANSMDLG NMEENTPSDL ANGNKKKEPK SVSKLDLGSE
KVSIPSNLVN GNEQHDLNIA PGEDASAAKQ PEKKRSRSKK RKSGNNLDLG KMEKSKPSDL
ANENEQTEPK SANNLDLGNM KENTPSDLAN ENEQTELRLP NNSDYGNMEE SLPLNLANGD
EQPDPTTAPM EAAKQPKKKR SRSKKCKSVN NLDLGNMEEN KPSDLANGNE QKDPESVNRL
DPGKEKESIP SNLVSGNEQP DSNTAPAKKP KKKKRKLANN FDSVNNMEEK MPSTNVLSQG
NKSGLIEEKP SIPSDQ
