RNR1_ARATH
ID RNR1_ARATH Reviewed; 803 AA.
AC Q6NQJ6; Q9LZA0;
DT 03-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Ribonuclease II, chloroplastic/mitochondrial;
DE Short=AtmtRNaseII;
DE Short=RNase II;
DE EC=3.1.13.1;
DE AltName: Full=Protein EMBRYO DEFECTIVE 2730;
DE AltName: Full=Ribonucleotide reductase 1;
DE Flags: Precursor;
GN Name=RNR1; Synonyms=EMB2730; OrderedLocusNames=At5g02250;
GN ORFNames=T1E22.10;
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], FUNCTION, DISRUPTION PHENOTYPE, AND SUBCELLULAR
RP LOCATION.
RC STRAIN=cv. Columbia;
RX PubMed=15037609; DOI=10.1074/jbc.m401182200;
RA Perrin R., Meyer E.H., Zaepfel M., Kim Y.-J., Mache R.,
RA Grienenberger J.-M., Gualberto J.M., Gagliardi D.;
RT "Two exoribonucleases act sequentially to process mature 3'-ends of atp9
RT mRNAs in Arabidopsis mitochondria.";
RL J. Biol. Chem. 279:25440-25446(2004).
RN [2]
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 [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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RC STRAIN=cv. Columbia;
RX PubMed=15891117; DOI=10.1093/nar/gki576;
RA Bollenbach T.J., Lange H., Gutierrez R., Erhardt M., Stern D.B.,
RA Gagliardi D.;
RT "RNR1, a 3'-5' exoribonuclease belonging to the RNR superfamily, catalyzes
RT 3' maturation of chloroplast ribosomal RNAs in Arabidopsis thaliana.";
RL Nucleic Acids Res. 33:2751-2763(2005).
CC -!- FUNCTION: 3'-5' exoribonuclease that catalyzes 3' maturation of
CC chloroplast and mitochondrion ribosomal RNAs; degrades short
CC nucleotidic extensions to generate the mature 3'-ends. Involved in the
CC maturation of 23S, 16S and 5S rRNAs. {ECO:0000269|PubMed:15037609,
CC ECO:0000269|PubMed:15891117}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Exonucleolytic cleavage in the 3'- to 5'-direction to yield
CC nucleoside 5'-phosphates.; EC=3.1.13.1;
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:15037609}.
CC Plastid, chloroplast {ECO:0000269|PubMed:15891117}.
CC -!- TISSUE SPECIFICITY: Expressed in seedlings, roots, leaves and flowers.
CC {ECO:0000269|PubMed:15891117}.
CC -!- DISRUPTION PHENOTYPE: Shorter 3' nucleotide extensions of mitochondrial
CC mRNAs and reduced accumulation of several chloroplast rRNA species.
CC Germinates only on sucrose-containing media, with white cotyledons and
CC pale green rosette leaves. {ECO:0000269|PubMed:15037609,
CC ECO:0000269|PubMed:15891117}.
CC -!- SIMILARITY: Belongs to the RNR ribonuclease family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB85530.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL162874; CAB85530.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED90450.1; -; Genomic_DNA.
DR EMBL; BT010457; AAQ62877.1; -; mRNA.
DR EMBL; AK176383; BAD44146.1; -; mRNA.
DR PIR; T48246; T48246.
DR RefSeq; NP_195845.2; NM_120303.5.
DR AlphaFoldDB; Q6NQJ6; -.
DR SMR; Q6NQJ6; -.
DR STRING; 3702.AT5G02250.1; -.
DR PaxDb; Q6NQJ6; -.
DR PRIDE; Q6NQJ6; -.
DR ProteomicsDB; 228014; -.
DR EnsemblPlants; AT5G02250.1; AT5G02250.1; AT5G02250.
DR GeneID; 830864; -.
DR Gramene; AT5G02250.1; AT5G02250.1; AT5G02250.
DR KEGG; ath:AT5G02250; -.
DR Araport; AT5G02250; -.
DR TAIR; locus:2180172; AT5G02250.
DR eggNOG; KOG2102; Eukaryota.
DR HOGENOM; CLU_015903_0_0_1; -.
DR OMA; YLPTGMI; -.
DR OrthoDB; 254420at2759; -.
DR PhylomeDB; Q6NQJ6; -.
DR BRENDA; 3.1.13.1; 399.
DR PRO; PR:Q6NQJ6; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q6NQJ6; baseline and differential.
DR Genevisible; Q6NQJ6; AT.
DR GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR GO; GO:0000178; C:exosome (RNase complex); IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; IDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0000175; F:3'-5'-exoribonuclease activity; IDA:TAIR.
DR GO; GO:0008859; F:exoribonuclease II activity; IEA:UniProtKB-EC.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0009658; P:chloroplast organization; IMP:TAIR.
DR GO; GO:0006364; P:rRNA processing; IMP:TAIR.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR001900; RNase_II/R.
DR Pfam; PF00773; RNB; 1.
DR SMART; SM00955; RNB; 1.
DR SUPFAM; SSF50249; SSF50249; 1.
PE 2: Evidence at transcript level;
KW Chloroplast; Exonuclease; Hydrolase; Mitochondrion; Nuclease; Plastid;
KW Reference proteome; RNA-binding; rRNA processing; Transit peptide.
FT TRANSIT 1..35
FT /note="Chloroplast and mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 36..803
FT /note="Ribonuclease II, chloroplastic/mitochondrial"
FT /id="PRO_0000419509"
FT CONFLICT 513
FT /note="I -> T (in Ref. 1; no nucleotide entry)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 803 AA; 90679 MW; 59E836830E242021 CRC64;
MMSVRAINGC SIIRTATSAG GPPVSLFRHR IQRLRASHLR EFSKLRLNFP LIRADRRFLG
NSDAPSCSTC IHSLVESVSE ELESISRRKG SRMRVRASVK VKLTSYGEVL EDKLVNQELE
AGLLLEFKKD ADRVLLAVLH RRDGKKNWMV FDQNGVSCSI KPQQITYIVP NVYNFDHTGL
TDFLQRAQDN LDPQLLEFAW MELLEKNKPV TPEELAEMIY GRADPLESYC AHFLLSQDEI
YFSILESKGS RSIYSPRPTE QVEELLRRQR VKEAEDKEFQ EFIQLLKSAK KAPSHAKPPK
SSWLADDKVQ DRIGSLEAYA IDAWASTDQQ KLAGTILKSM GLQKTSVSAL NLLIDIGYFP
VHVNLELLKL NLPTHHSEAI TEAAEALLSE SSDIDAVRRI DLTHLKVYAI DVDEADELDD
ALSATRLQDG RIKIWIHVAD PARYVTPGSK VDREARRRGT SVFLPTATYP MFPEKLAMEG
MSLRQGENCN AVSVSVVLRS DGCITEYSVD NSIIRPTYML TYESASELLH LNLEEEAELK
LLSEAAFIRS QWRREQGAVD TTTLETRIKV VNPEDPEPLI NLYVENQADL AMRLVFEMMI
LCGEVVATFG SQHNIPLPYR GQPQSNIDVS AFAHLPEGPV RSSSIVKVMR AAEMNFRCPV
RHGVLGIPGY VQFTSPIRRY MDLTAHYQIK AFLRGGDNFP FSAGELEGIA ASVNMQSKVV
RKLSNTGLRY WVIEFLRRQE KGKKYTALVL RFVKDRIASL LLVEVGFQAT AWVSEGKQVG
DEIEVRVEEA HPRDDLILFK EVI
