RNC1_ARATH
ID RNC1_ARATH Reviewed; 537 AA.
AC Q9SZV0;
DT 17-FEB-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Ribonuclease III domain-containing protein RNC1, chloroplastic {ECO:0000305};
DE AltName: Full=Chloroplast ribonuclease III domain protein {ECO:0000305};
DE Flags: Precursor;
GN Name=RNC1 {ECO:0000305};
GN OrderedLocusNames=At4g37510 {ECO:0000312|Araport:AT4G37510};
GN ORFNames=F6G17.160 {ECO:0000312|EMBL:CAB38218.1};
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=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(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].
RC STRAIN=cv. Columbia;
RA Shinn P., Chen H., Kim C.J., Quinitio C., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Binds specific group II introns in chloroplasts and
CC facilitates their splicing. Acts on both subgroup IIA and subgroup IIB
CC introns. The substrates of the subgroup II also require the CRM domain
CC proteins CAF1 or CAF2. Binds both single-stranded and double-stranded
CC RNA non-specifically, but lacks endonuclease activity. Required for
CC plastid ribosome biogenesis. {ECO:0000250|UniProtKB:A6YSL1}.
CC -!- SUBUNIT: Interacts with RNA. Part of large ribonucleo-protein particles
CC that contain CAF1 and/or CAF2. {ECO:0000250|UniProtKB:A6YSL1}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000255}.
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DR EMBL; AL035601; CAB38218.1; -; Genomic_DNA.
DR EMBL; AL161591; CAB80416.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE86803.1; -; Genomic_DNA.
DR EMBL; BT025333; ABF57289.1; -; mRNA.
DR PIR; T04745; T04745.
DR RefSeq; NP_195467.1; NM_119915.4.
DR AlphaFoldDB; Q9SZV0; -.
DR SMR; Q9SZV0; -.
DR STRING; 3702.AT4G37510.1; -.
DR iPTMnet; Q9SZV0; -.
DR PaxDb; Q9SZV0; -.
DR PRIDE; Q9SZV0; -.
DR ProteomicsDB; 228167; -.
DR EnsemblPlants; AT4G37510.1; AT4G37510.1; AT4G37510.
DR GeneID; 829906; -.
DR Gramene; AT4G37510.1; AT4G37510.1; AT4G37510.
DR KEGG; ath:AT4G37510; -.
DR Araport; AT4G37510; -.
DR TAIR; locus:2126397; AT4G37510.
DR eggNOG; ENOG502QSFE; Eukaryota.
DR HOGENOM; CLU_018164_0_0_1; -.
DR InParanoid; Q9SZV0; -.
DR OMA; YMAFQHP; -.
DR OrthoDB; 470747at2759; -.
DR PhylomeDB; Q9SZV0; -.
DR PRO; PR:Q9SZV0; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9SZV0; baseline and differential.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0003725; F:double-stranded RNA binding; IBA:GO_Central.
DR GO; GO:0003729; F:mRNA binding; IDA:TAIR.
DR GO; GO:0004525; F:ribonuclease III activity; IBA:GO_Central.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0010468; P:regulation of gene expression; IBA:GO_Central.
DR GO; GO:0006396; P:RNA processing; IBA:GO_Central.
DR GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR GO; GO:0006364; P:rRNA processing; IEA:InterPro.
DR CDD; cd00593; RIBOc; 2.
DR Gene3D; 1.10.1520.10; -; 2.
DR InterPro; IPR011907; RNase_III.
DR InterPro; IPR000999; RNase_III_dom.
DR InterPro; IPR036389; RNase_III_sf.
DR PANTHER; PTHR11207; PTHR11207; 1.
DR SMART; SM00535; RIBOc; 1.
DR SUPFAM; SSF69065; SSF69065; 2.
DR PROSITE; PS50142; RNASE_3_2; 1.
PE 2: Evidence at transcript level;
KW Chloroplast; mRNA processing; mRNA splicing; Plastid; Reference proteome;
KW Repeat; Ribonucleoprotein; RNA-binding; Transit peptide.
FT TRANSIT 1..51
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 52..537
FT /note="Ribonuclease III domain-containing protein RNC1,
FT chloroplastic"
FT /id="PRO_0000435537"
FT DOMAIN 141..283
FT /note="RNase III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00177"
FT DOMAIN 415..515
FT /note="RNase III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00177"
SQ SEQUENCE 537 AA; 62432 MW; 749613600D3214FF CRC64;
MELCSSSPSS SLLRICSSSA PEISFSSSIS QFPSKTQSIL TKSRFQNLRI CASVTAETQG
LPRDSPQRLL KELAQRKTAT GPKKKVPPKR FILRPPLDDK KLAERFLNSP QLSLKSFPLL
SSCLPSSKLN NADKTWIDEY LLEVKQALGY SLEPSESLGD DNPAKHFDTL LYLAFQHPSC
DRARARHVKN GHSRLWFLGQ YVLELALTEF FLQRYPRESP GPMRERVFAL IGKRYLPKWI
KAASLQNLIF PYDDMDKLIR KEREPPVKSV FWALFGAIYL CFGMPEVYRV LFEVFGMDPD
ADECQPRSRR QLEDVDYVSV EFEGKKLGWQ DIATYKPPED ALFAHPRLFR ACVPPGMHRF
RGNIWDFDSK PKVMQTLGYP LTMNDRIKEI TEARNIELGL GLQLCFLHPS KHKFEHPRFC
FERLEYVGQK IQDIAMAERL LMKHLDAPGK WLQEKHRRLL MNKFCGRYLR EKRLHNFIIY
SEEVHDRYEH NRRLRNPATT AVQQAIHGLA YTIYGKPDVR RLMFEVFDFE QIQPKAV