C3H31_ARATH
ID C3H31_ARATH Reviewed; 1015 AA.
AC O22243; C0SV94;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1999, sequence version 2.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=DExH-box ATP-dependent RNA helicase DExH8 {ECO:0000305};
DE EC=3.6.4.13;
DE AltName: Full=Zinc finger CCCH domain-containing protein 31;
DE Short=AtC3H31;
DE EC=3.6.4.12;
GN OrderedLocusNames=At2g47680; ORFNames=F17A22.7;
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].
RA Fujita M., Mizukado S., Seki M., Shinozaki K., Mitsuda N., Takiguchi Y.,
RA Takagi M.;
RT "ORF cloning and analysis of Arabidopsis transcription factor genes.";
RL Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NOMENCLATURE.
RX PubMed=18221561; DOI=10.1186/1471-2164-9-44;
RA Wang D., Guo Y., Wu C., Yang G., Li Y., Zheng C.;
RT "Genome-wide analysis of CCCH zinc finger family in Arabidopsis and rice.";
RL BMC Genomics 9:44-44(2008).
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 -!- 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 -!- 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 -!- SIMILARITY: Belongs to the DExH box helicase family. {ECO:0000305}.
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DR EMBL; AC005309; AAC63624.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC10875.1; -; Genomic_DNA.
DR EMBL; AB493597; BAH30435.1; -; mRNA.
DR PIR; C84918; C84918.
DR PIR; T00416; T00416.
DR RefSeq; NP_182290.1; NM_130336.3.
DR AlphaFoldDB; O22243; -.
DR SMR; O22243; -.
DR STRING; 3702.AT2G47680.1; -.
DR PaxDb; O22243; -.
DR PRIDE; O22243; -.
DR ProteomicsDB; 240559; -.
DR EnsemblPlants; AT2G47680.1; AT2G47680.1; AT2G47680.
DR GeneID; 819381; -.
DR Gramene; AT2G47680.1; AT2G47680.1; AT2G47680.
DR KEGG; ath:AT2G47680; -.
DR Araport; AT2G47680; -.
DR TAIR; locus:2043413; AT2G47680.
DR eggNOG; KOG0920; Eukaryota.
DR HOGENOM; CLU_007384_0_0_1; -.
DR InParanoid; O22243; -.
DR OMA; INPPMYL; -.
DR OrthoDB; 101959at2759; -.
DR PhylomeDB; O22243; -.
DR PRO; PR:O22243; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O22243; baseline and differential.
DR Genevisible; O22243; AT.
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; IEA:UniProtKB-KW.
DR GO; GO:0003678; F:DNA helicase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003729; F:mRNA binding; IDA:TAIR.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
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; IPR000571; Znf_CCCH.
DR InterPro; IPR036855; Znf_CCCH_sf.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00356; ZnF_C3H1; 2.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF90229; SSF90229; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS50103; ZF_C3H1; 2.
PE 2: Evidence at transcript level;
KW ATP-binding; DNA-binding; Helicase; Hydrolase; Metal-binding;
KW Nucleotide-binding; Reference proteome; Repeat; RNA-binding; Zinc;
KW Zinc-finger.
FT CHAIN 1..1015
FT /note="DExH-box ATP-dependent RNA helicase DExH8"
FT /id="PRO_0000371989"
FT DOMAIN 36..197
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 254..419
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT ZN_FING 727..753
FT /note="C3H1-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT ZN_FING 754..782
FT /note="C3H1-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT MOTIF 144..147
FT /note="DEVH box"
FT /evidence="ECO:0000305"
FT BINDING 49..56
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 1015 AA; 115085 MW; D1C342B338C561C9 CRC64;
MAVSSPTSSS SSSESLPLPS SNFASLPIMA MKRRIIDKIL ENRVTLIVGE PGCGKSSQVP
QFLLEANMAP ILCTQPRRFA VVAVAKMVAK SRNSDLGGEI GYHIGHSKIL TEGSKILFKT
AGVLLDEMLD KGLNALKYKV IILDEVHERS VESDLVLVCV KQFLMKNNDL RVVLMSATAD
ITRYRDYFKE LGRGERVEVV AIPSPDQRTI FQRRVLYLEQ VAGLLGVSSD LSAYCPGPSP
SSADTEIKPE LQNLIHDLIL YIHEKEPDIE KSILVFLPTY YSLEQQYHQL EPFFASFEVH
ILHRSIDTEQ ALAAMKICRS RRKVILATNI AESSVTIPKV AYVIDSCRSL QVFWDPSRKR
DAVQLVWVSR SQAEQRRGRT GRTCDGEVYR LVPSAFFNKL EEHEPPSILK LSLRQQVLHI
CCTESRAIND ANALLAKAMD PPDPDVVDDA LRMLLSIQAL RKSPRGRYEP TFYGRLLASF
PLSFDASILV VKFGEMGMLR QGILLGVLMD TLPLPIHHPF GDDSLFLEYV DHYFGGSKTI
SGGRREMVLM ANFCAFQFWQ RVFKDKHRLE NLKQLLSKEK DKDLKLMFPE IEKEWCDFHN
IAQSSFYHVS ELYEDTLSSF HRFRPQFISS SDSQPTYYNP YEFDHTCYIE CQPSEDKYLH
SEDVDNNQPP PEVRKCVSVP FVPPNAFQAN AIAENMASII KEIRTQCTPS ESDNGHGALE
PEDYVEYGEA PVCVYFLNGY CNRGGQCTFT HTLQSTRPAC KFFASSQGCR NGESCLFSHA
MRRRTTSYLP PPQCLPEEDG SSTSPLLDLF PTSSEGCILV FDDSDMHFTS SIANRYPSWR
ILSTSSSSET LFCDSSLADT RIFWGLNHPY QTIISKAGRE NPIPWNEVKC VLWFLNPDSY
ADTPEKQKTI LQNFFEHMAI RLLGDKLYKI RVVLTMNNVR FSLLQVEKLA RESFFFLGES
FPHDSESFGA FQDTLTIQKP MLVSRPISYV FNLHPPSDIQ FGNYTSLLRK SLHNK