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RecName: Full=Ribonuclease E/G-like protein, chloroplastic; Short=RNase E/G-like protein; AltName: Full=RNase E; Flags: Precursor

UniProtKB/Swiss-Prot: F4IV66.1

Identical Proteins FASTA Graphics 

LOCUS       RNE_ARATH               1001 aa            linear   PLN 27-NOV-2024
DEFINITION  RecName: Full=Ribonuclease E/G-like protein, chloroplastic;
            Short=RNase E/G-like protein; AltName: Full=RNase E; Flags:
            Precursor.
ACCESSION   F4IV66
VERSION     F4IV66.1
DBSOURCE    UniProtKB: locus RNE_ARATH, accession F4IV66;
            class: standard.
            extra accessions:F4IV67,F4IV69,Q8GZQ4,Q8RWB3,Q9M498,Q9SI08
            created: Mar 6, 2013.
            sequence updated: Jun 28, 2011.
            annotation updated: Nov 27, 2024.
            xrefs: AF450479.1, AAN76770.1, AC007213.6, AAD27911.1, CP002685.1,
            AEC05813.1, AEC05814.1, AEC05815.1, AEC05816.1, AEC05817.1,
            ANM63269.1, ANM63270.1, ANM63271.1, AY093213.1, AAM13212.1,
            BT008793.1, AAP68232.1, AJ252122.1, CAB76425.1, F84455,
            NP_001189510.1, NP_001318196.1, NP_001325370.1, NP_001325371.1,
            NP_178508.2, NP_850987.1, NP_850988.1, NP_850989.1
            xrefs (non-sequence databases): AlphaFoldDB:F4IV66, SMR:F4IV66,
            STRING:3702.F4IV66, PaxDb:3702-AT2G04270.5, ProteomicsDB:227998,
            EnsemblPlants:AT2G04270.1, EnsemblPlants:AT2G04270.1,
            EnsemblPlants:AT2G04270, EnsemblPlants:AT2G04270.2,
            EnsemblPlants:AT2G04270.2, EnsemblPlants:AT2G04270.3,
            EnsemblPlants:AT2G04270.3, EnsemblPlants:AT2G04270.4,
            EnsemblPlants:AT2G04270.4, EnsemblPlants:AT2G04270.5,
            EnsemblPlants:AT2G04270.5, EnsemblPlants:AT2G04270.6,
            EnsemblPlants:AT2G04270.6, EnsemblPlants:AT2G04270.8,
            EnsemblPlants:AT2G04270.8, EnsemblPlants:AT2G04270.9,
            EnsemblPlants:AT2G04270.9, GeneID:814965, Gramene:AT2G04270.1,
            Gramene:AT2G04270.2, Gramene:AT2G04270.3, Gramene:AT2G04270.4,
            Gramene:AT2G04270.5, Gramene:AT2G04270.6, Gramene:AT2G04270.8,
            Gramene:AT2G04270.9, KEGG:ath:AT2G04270, Araport:AT2G04270,
            TAIR:AT2G04270, eggNOG:ENOG502QPXM, InParanoid:F4IV66, OMA:CERVELH,
            OrthoDB:1206148at2759, PRO:PR:F4IV66, Proteomes:UP000006548,
            ExpressionAtlas:F4IV66, GO:0009507, GO:0009570, GO:0046872,
            GO:0003723, GO:0004521, GO:2001070, GO:0010239, GO:0009658,
            GO:1901259, FunFam:2.60.40.10:FF:001568, Gene3D:2.60.40.10,
            Gene3D:2.40.50.140, Gene3D:3.40.1260.20, InterPro:IPR013784,
            InterPro:IPR002044, InterPro:IPR013783, InterPro:IPR012340,
            InterPro:IPR019307, InterPro:IPR004659, NCBIfam:TIGR00757,
            PANTHER:PTHR30001, PANTHER:PTHR30001:SF1, Pfam:PF00686,
            Pfam:PF10150, SMART:SM01065, SUPFAM:SSF50249, SUPFAM:SSF49452,
            PROSITE:PS51166
KEYWORDS    Alternative splicing; Chloroplast; Coiled coil; Endonuclease;
            Hydrolase; Magnesium; Metal-binding; mRNA processing; Nuclease;
            Plastid; Reference proteome; RNA-binding; Transit peptide; Zinc.
SOURCE      Arabidopsis thaliana (thale cress)
  ORGANISM  Arabidopsis thaliana
            Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
            Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae;
            Pentapetalae; rosids; malvids; Brassicales; Brassicaceae;
            Camelineae; Arabidopsis.
REFERENCE   1  (residues 1 to 1001)
  AUTHORS   Walter,M. and Kudla,J.
  TITLE     Direct Submission
  JOURNAL   Submitted (??-NOV-2001) to the EMBL/GenBank/DDBJ databases
  REMARK    NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
REFERENCE   2  (residues 1 to 1001)
  AUTHORS   Lin,X., Kaul,S., Rounsley,S., Shea,T.P., Benito,M.I., Town,C.D.,
            Fujii,C.Y., Mason,T., Bowman,C.L., Barnstead,M., Feldblyum,T.V.,
            Buell,C.R., Ketchum,K.A., Lee,J., Ronning,C.M., Koo,H.L.,
            Moffat,K.S., Cronin,L.A., Shen,M., Pai,G., Van Aken,S., Umayam,L.,
            Tallon,L.J., Gill,J.E., Adams,M.D., Carrera,A.J., Creasy,T.H.,
            Goodman,H.M., Somerville,C.R., Copenhaver,G.P., Preuss,D.,
            Nierman,W.C., White,O., Eisen,J.A., Salzberg,S.L., Fraser,C.M. and
            Venter,J.C.
  TITLE     Sequence and analysis of chromosome 2 of the plant Arabidopsis
            thaliana
  JOURNAL   Nature 402 (6763), 761-768 (1999)
   PUBMED   10617197
  REMARK    NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].;
            STRAIN=cv. Columbia
REFERENCE   3  (residues 1 to 1001)
  AUTHORS   Cheng,C.Y., Krishnakumar,V., Chan,A.P., Thibaud-Nissen,F.,
            Schobel,S. and Town,C.D.
  TITLE     Araport11: a complete reannotation of the Arabidopsis thaliana
            reference genome
  JOURNAL   Plant J 89 (4), 789-804 (2017)
   PUBMED   27862469
  REMARK    GENOME REANNOTATION.;
            STRAIN=cv. Columbia
REFERENCE   4  (residues 1 to 1001)
  AUTHORS   Yamada,K., Lim,J., Dale,J.M., Chen,H., Shinn,P., Palm,C.J.,
            Southwick,A.M., Wu,H.C., Kim,C., Nguyen,M., Pham,P., Cheuk,R.,
            Karlin-Newmann,G., Liu,S.X., Lam,B., Sakano,H., Wu,T., Yu,G.,
            Miranda,M., Quach,H.L., Tripp,M., Chang,C.H., Lee,J.M., Toriumi,M.,
            Chan,M.M., Tang,C.C., Onodera,C.S., Deng,J.M., Akiyama,K.,
            Ansari,Y., Arakawa,T., Banh,J., Banno,F., Bowser,L., Brooks,S.,
            Carninci,P., Chao,Q., Choy,N., Enju,A., Goldsmith,A.D., Gurjal,M.,
            Hansen,N.F., Hayashizaki,Y., Johnson-Hopson,C., Hsuan,V.W.,
            Iida,K., Karnes,M., Khan,S., Koesema,E., Ishida,J., Jiang,P.X.,
            Jones,T., Kawai,J., Kamiya,A., Meyers,C., Nakajima,M., Narusaka,M.,
            Seki,M., Sakurai,T., Satou,M., Tamse,R., Vaysberg,M.,
            Wallender,E.K., Wong,C., Yamamura,Y., Yuan,S., Shinozaki,K.,
            Davis,R.W., Theologis,A. and Ecker,J.R.
  TITLE     Empirical analysis of transcriptional activity in the Arabidopsis
            genome
  JOURNAL   Science 302 (5646), 842-846 (2003)
   PUBMED   14593172
  REMARK    NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).;
            STRAIN=cv. Columbia
REFERENCE   5  (residues 1 to 1001)
  AUTHORS   Mudd,E.A., Sullivan,S., Gisby,M.F., Mironov,A., Kwon,C.S.,
            Chung,W.I. and Day,A.
  TITLE     A 125 kDa RNase E/G-like protein is present in plastids and is
            essential for chloroplast development and autotrophic growth in
            Arabidopsis
  JOURNAL   J Exp Bot 59 (10), 2597-2610 (2008)
   PUBMED   18515828
  REMARK    NUCLEOTIDE SEQUENCE [MRNA] OF 45-619 (ISOFORM 5), FUNCTION,
            SUBCELLULAR LOCATION, TISSUE SPECIFICITY, ALTERNATIVE SPLICING, AND
            DISRUPTION PHENOTYPE.
REFERENCE   6  (residues 1 to 1001)
  AUTHORS   Schein,A., Sheffy-Levin,S., Glaser,F. and Schuster,G.
  TITLE     The RNase E/G-type endoribonuclease of higher plants is located in
            the chloroplast and cleaves RNA similarly to the E. coli enzyme
  JOURNAL   RNA 14 (6), 1057-1068 (2008)
   PUBMED   18441049
  REMARK    FUNCTION, MUTAGENESIS OF LYS-551 AND LYS-557, SUBUNIT, 3D-STRUCTURE
            MODELING, AND SUBCELLULAR LOCATION.
REFERENCE   7  (residues 1 to 1001)
  AUTHORS   Walter,M., Piepenburg,K., Schottler,M.A., Petersen,K., Kahlau,S.,
            Tiller,N., Drechsel,O., Weingartner,M., Kudla,J. and Bock,R.
  TITLE     Knockout of the plastid RNase E leads to defective RNA processing
            and chloroplast ribosome deficiency
  JOURNAL   Plant J 64 (5), 851-863 (2010)
   PUBMED   21105931
  REMARK    FUNCTION, AND DISRUPTION PHENOTYPE.
REFERENCE   8  (residues 1 to 1001)
  AUTHORS   Stoppel,R., Manavski,N., Schein,A., Schuster,G., Teubner,M.,
            Schmitz-Linneweber,C. and Meurer,J.
  TITLE     RHON1 is a novel ribonucleic acid-binding protein that supports
            RNase E function in the Arabidopsis chloroplast
  JOURNAL   Nucleic Acids Res 40 (17), 8593-8606 (2012)
   PUBMED   22735703
  REMARK    MUTAGENESIS OF 693-VAL--GLN-698, SUBCELLULAR LOCATION, INTERACTION
            WITH RHON1, AND DISRUPTION PHENOTYPE.;
            STRAIN=cv. Columbia
COMMENT     On or before Mar 13, 2013 this sequence version replaced
            gi:75151654, gi:75158660, gi:75184260, gi:75206015.
            [FUNCTION] Involved in intercistronic processing of primary
            transcripts from chloroplast operons. The endonucleolytic activity
            of the enzyme depends on the number of phosphates at the 5' end, is
            inhibited by structured RNA, and preferentially cleaves A/U-rich
            sequences. {ECO:0000269|PubMed:18441049,
            ECO:0000269|PubMed:18515828, ECO:0000269|PubMed:21105931}.
            [COFACTOR] Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
            Evidence={ECO:0000250|UniProtKB:P21513}; Note=Binds 1 Mg(2+) ion
            per subunit. {ECO:0000250|UniProtKB:P21513}.
            [COFACTOR] Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
            Evidence={ECO:0000250|UniProtKB:P21513}; Note=Binds 2 Zn(2+) ions
            per homotetramer. Zinc ions are bound between subunits.
            {ECO:0000250|UniProtKB:P21513}.
            [SUBUNIT] Part of a chloroplastic degradosome-like complex.
            Interacts with RHON1 (PubMed:18441049, PubMed:22735703). A
            homotetramer formed by a dimer of dimers (By similarity).
            {ECO:0000250|UniProtKB:P21513, ECO:0000269|PubMed:18441049,
            ECO:0000269|PubMed:22735703}.
            [SUBCELLULAR LOCATION] Plastid, chloroplast stroma
            {ECO:0000269|PubMed:18441049, ECO:0000269|PubMed:18515828,
            ECO:0000269|PubMed:22735703}.
            [ALTERNATIVE PRODUCTS] Event=Alternative splicing; Named
            isoforms=5; Name=1; IsoId=F4IV66-1; Sequence=Displayed; Name=2;
            IsoId=F4IV66-2; Sequence=VSP_045664; Name=3; IsoId=F4IV66-3;
            Sequence=VSP_045663, VSP_045665; Name=4; IsoId=F4IV66-4;
            Sequence=VSP_045662; Name=5; IsoId=F4IV66-5; Sequence=VSP_045662,
            VSP_045666, VSP_045667.
            [TISSUE SPECIFICITY] Expressed in cotyledons, rosette and cauline
            leaves. {ECO:0000269|PubMed:18515828}.
            [DISRUPTION PHENOTYPE] Reduced photosynthetic activity and retarded
            growth. Increased number and decreased size of chloroplasts. Loss
            of autotrophic growth. Pale cotyledons when grown on
            sucrose-complemented medium. {ECO:0000269|PubMed:18515828,
            ECO:0000269|PubMed:21105931, ECO:0000269|PubMed:22735703}.
            [SIMILARITY] Belongs to the RNase E/G family. {ECO:0000305}.
            [SEQUENCE CAUTION] Sequence=AAD27911.1; Type=Erroneous gene model
            prediction; Evidence={ECO:0000305}.
FEATURES             Location/Qualifiers
     source          1..1001
                     /organism="Arabidopsis thaliana"
                     /db_xref="taxon:3702"
     gene            1..1001
                     /gene="RNE"
                     /locus_tag="At2g04270"
                     /gene_synonym="RNEE/G"
                     /gene_synonym="T23O15.10"
     Protein         1..1001
                     /product="Ribonuclease E/G-like protein, chloroplastic"
                     /EC_number="3.1.26.-"
                     /note="RNase E/G-like protein"
                     /UniProtKB_evidence="Evidence at protein level"
     Region          1..288
                     /region_name="Splicing variant"
                     /note="Missing (in isoform 4 and isoform 5).
                     /evidence=ECO:0000303|PubMed:14593172,
                     ECO:0000303|PubMed:18515828. /id=VSP_045662."
     Region          1..130
                     /region_name="Splicing variant"
                     /note="Missing (in isoform 3). /evidence=ECO:0000305.
                     /id=VSP_045663."
     Region          1..48
                     /region_name="Transit peptide"
                     /note="Chloroplast. /evidence=ECO:0000255."
     Region          49..1001
                     /region_name="Mature chain"
                     /note="Ribonuclease E/G-like protein, chloroplastic.
                     /id=PRO_0000421383."
     Region          62..71
                     /region_name="Splicing variant"
                     /note="PLRFLLSVFS -> VSAQQ (in isoform 2).
                     /evidence=ECO:0000303|Ref.1. /id=VSP_045664."
     Region          76..185
                     /region_name="Domain"
                     /note="CBM20.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00594."
     Region          82..177
                     /region_name="CBM20"
                     /note="The family 20 carbohydrate-binding module (CBM20),
                     also known as the starch-binding domain, is found in a
                     large number of starch degrading enzymes including
                     alpha-amylase, beta-amylase, glucoamylase, and CGTase
                     (cyclodextrin glucanotransferase). CBM20 is...; cl15347"
                     /db_xref="CDD:449530"
     Site            order(92..97,120,127)
                     /site_type="other"
                     /note="starch-binding site 2 [chemical binding]"
                     /db_xref="CDD:99883"
     Site            order(110,142,157..158,162)
                     /site_type="other"
                     /note="starch-binding site 1 [chemical binding]"
                     /db_xref="CDD:99883"
     Region          131..139
                     /region_name="Splicing variant"
                     /note="VKIASGVNF -> MIMNGKLKS (in isoform 3).
                     /evidence=ECO:0000305. /id=VSP_045665."
     Region          336..956
                     /region_name="CafA"
                     /note="Ribonuclease G or E [Translation, ribosomal
                     structure and biogenesis]; COG1530"
                     /db_xref="CDD:441139"
     Site            551
                     /site_type="mutagenized"
                     /note="K->A: Loss of endonucleolytic activity; when
                     associated with A-557.
                     /evidence=ECO:0000269|PubMed:18441049."
     Site            557
                     /site_type="mutagenized"
                     /note="K->A: Loss of endonucleolytic activity; when
                     associated with A-551.
                     /evidence=ECO:0000269|PubMed:18441049."
     Site            693..698
                     /site_type="mutagenized"
                     /note="Missing: In rne-2; loss of endonucleolytic
                     activity. /evidence=ECO:0000269|PubMed:22735703."
     Region          769..789
                     /region_name="Coiled-coil region"
                     /note="/evidence=ECO:0000255."
     Region          886..907
                     /region_name="Splicing variant"
                     /note="AKMEKRGDLENPKSWPRFILRV -> VSVIISILFCYFSFQPNEEHLE
                     (in isoform 5). /evidence=ECO:0000303|PubMed:18515828.
                     /id=VSP_045666."
     Region          908..1001
                     /region_name="Splicing variant"
                     /note="Missing (in isoform 5).
                     /evidence=ECO:0000303|PubMed:18515828. /id=VSP_045667."
ORIGIN      
        1 mdvtevpwrr lpqfsvssra swlvssgfpl ssymfshver gktfrltlcf gvsrlrprsa
       61 iplrfllsvf seqppsrlkg lcevvwivea dlaanehlyv tgdpstlgsw epdcaismyp
      121 tendneweak vkiasgvnfr ynyllkagyg sssdviwrpg pqfslsvpss vnqdrkiiir
      181 dswmsmsiss ksqesygwgs widdaylfpn cvtpaqsede ctsadsaiev prthlndkqv
      241 gaesflcdel aafssensnl salfsdnyqp ieepwliqes itlqhernmq tdseqdvesc
      301 ddnennlntd eqnhqltetl lpdggffqse siattilins sictvqriav leggklvell
      361 lepvktnvqc dsvylgvitk fvphmggafv nigsarhsfm diksnrepfi fppfcdgskk
      421 qaadgspils mndipaphei ehasydfeas slldidsndp gesfhdddde hendeyhvsd
      481 hlaglvngtv vnhgavevgs enghipmerg hsadsldsna svakaskvms skdnkwiqvr
      541 kgtkiivqvv keglgtkgpt ltaypklrsr fwvlltrckr igvskkisgv ertrlkviak
      601 tlqpqgfglt vrtvaaghsl eelqkdldgl lltwknitde aksaalaade gvegaipall
      661 hramgqtlsv vqdyfndkve kmvvdsprty hevthylqdm apdlcnrvel hdkgiplfdl
      721 yeieeeiegi lskrvplsng gslvieqtea lvsidvnggh gmfgqgnsqe kailevnlaa
      781 arqiareirl rdiggiivvd fidmadesnk rlvyeevkka verdrslvkv selsrhglme
      841 itrkrvrpsv tfmisepcsc chatgrveal ettfskieqe icrqlakmek rgdlenpksw
      901 prfilrvdsh mssflttgkr trlailsssl kvwillkvar hftrgtfevk pfmdektvne
      961 rqhqvaisll kkadaiadss gkkkltlipi kkektsgkqr r
//
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