RNC1_MAIZE
ID RNC1_MAIZE Reviewed; 525 AA.
AC A6YSL1;
DT 17-FEB-2016, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=Ribonuclease III domain-containing protein RNC1, chloroplastic {ECO:0000305};
DE AltName: Full=Chloroplast ribonuclease III domain protein {ECO:0000303|PubMed:17693527};
DE Flags: Precursor;
GN Name=RNC1 {ECO:0000303|PubMed:17693527}; Synonyms=Zm.27802;
OS Zea mays (Maize).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX NCBI_TaxID=4577;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, AND
RP DISRUPTION PHENOTYPE.
RX PubMed=17693527; DOI=10.1105/tpc.107.053736;
RA Watkins K.P., Kroeger T.S., Cooke A.M., Williams-Carrier R.E., Friso G.,
RA Belcher S.E., van Wijk K.J., Barkan A.;
RT "A ribonuclease III domain protein functions in group II intron splicing in
RT maize chloroplasts.";
RL Plant Cell 19:2606-2623(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. B73;
RX PubMed=19965430; DOI=10.1126/science.1178534;
RA Schnable P.S., Ware D., Fulton R.S., Stein J.C., Wei F., Pasternak S.,
RA Liang C., Zhang J., Fulton L., Graves T.A., Minx P., Reily A.D.,
RA Courtney L., Kruchowski S.S., Tomlinson C., Strong C., Delehaunty K.,
RA Fronick C., Courtney B., Rock S.M., Belter E., Du F., Kim K., Abbott R.M.,
RA Cotton M., Levy A., Marchetto P., Ochoa K., Jackson S.M., Gillam B.,
RA Chen W., Yan L., Higginbotham J., Cardenas M., Waligorski J., Applebaum E.,
RA Phelps L., Falcone J., Kanchi K., Thane T., Scimone A., Thane N., Henke J.,
RA Wang T., Ruppert J., Shah N., Rotter K., Hodges J., Ingenthron E.,
RA Cordes M., Kohlberg S., Sgro J., Delgado B., Mead K., Chinwalla A.,
RA Leonard S., Crouse K., Collura K., Kudrna D., Currie J., He R.,
RA Angelova A., Rajasekar S., Mueller T., Lomeli R., Scara G., Ko A.,
RA Delaney K., Wissotski M., Lopez G., Campos D., Braidotti M., Ashley E.,
RA Golser W., Kim H., Lee S., Lin J., Dujmic Z., Kim W., Talag J., Zuccolo A.,
RA Fan C., Sebastian A., Kramer M., Spiegel L., Nascimento L., Zutavern T.,
RA Miller B., Ambroise C., Muller S., Spooner W., Narechania A., Ren L.,
RA Wei S., Kumari S., Faga B., Levy M.J., McMahan L., Van Buren P.,
RA Vaughn M.W., Ying K., Yeh C.-T., Emrich S.J., Jia Y., Kalyanaraman A.,
RA Hsia A.-P., Barbazuk W.B., Baucom R.S., Brutnell T.P., Carpita N.C.,
RA Chaparro C., Chia J.-M., Deragon J.-M., Estill J.C., Fu Y., Jeddeloh J.A.,
RA Han Y., Lee H., Li P., Lisch D.R., Liu S., Liu Z., Nagel D.H., McCann M.C.,
RA SanMiguel P., Myers A.M., Nettleton D., Nguyen J., Penning B.W.,
RA Ponnala L., Schneider K.L., Schwartz D.C., Sharma A., Soderlund C.,
RA Springer N.M., Sun Q., Wang H., Waterman M., Westerman R., Wolfgruber T.K.,
RA Yang L., Yu Y., Zhang L., Zhou S., Zhu Q., Bennetzen J.L., Dawe R.K.,
RA Jiang J., Jiang N., Presting G.G., Wessler S.R., Aluru S.,
RA Martienssen R.A., Clifton S.W., McCombie W.R., Wing R.A., Wilson R.K.;
RT "The B73 maize genome: complexity, diversity, and dynamics.";
RL Science 326:1112-1115(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=18937034; DOI=10.1007/s11103-008-9415-4;
RA Alexandrov N.N., Brover V.V., Freidin S., Troukhan M.E., Tatarinova T.V.,
RA Zhang H., Swaller T.J., Lu Y.-P., Bouck J., Flavell R.B., Feldmann K.A.;
RT "Insights into corn genes derived from large-scale cDNA sequencing.";
RL Plant Mol. Biol. 69:179-194(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. B73;
RX PubMed=19936069; DOI=10.1371/journal.pgen.1000740;
RA Soderlund C., Descour A., Kudrna D., Bomhoff M., Boyd L., Currie J.,
RA Angelova A., Collura K., Wissotski M., Ashley E., Morrow D., Fernandes J.,
RA Walbot V., Yu Y.;
RT "Sequencing, mapping, and analysis of 27,455 maize full-length cDNAs.";
RL PLoS Genet. 5:E1000740-E1000740(2009).
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:0000269|PubMed:17693527}.
CC -!- SUBUNIT: Interacts with RNA. Part of large ribonucleo-protein particles
CC that contain CAF1 and/or CAF2. {ECO:0000269|PubMed:17693527}.
CC -!- INTERACTION:
CC A6YSL1; B6TTV8: WTF1; NbExp=4; IntAct=EBI-15761735, EBI-15761679;
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma
CC {ECO:0000269|PubMed:17693527}.
CC -!- DISRUPTION PHENOTYPE: Pale green, albino, and albino stunted seedling
CC phenotypes. Lack of plastid ribosomes. {ECO:0000269|PubMed:17693527}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; EF650835; ABR53724.1; -; mRNA.
DR EMBL; EU971053; ACG43171.1; -; mRNA.
DR EMBL; BT041100; ACF86105.1; -; mRNA.
DR EMBL; BT064625; ACN29322.1; -; mRNA.
DR RefSeq; NP_001106055.1; NM_001112585.1.
DR AlphaFoldDB; A6YSL1; -.
DR DIP; DIP-48742N; -.
DR IntAct; A6YSL1; 4.
DR STRING; 4577.GRMZM2G035820_P01; -.
DR PaxDb; A6YSL1; -.
DR PRIDE; A6YSL1; -.
DR GeneID; 100125654; -.
DR KEGG; zma:100125654; -.
DR eggNOG; ENOG502QSFE; Eukaryota.
DR HOGENOM; CLU_018164_0_0_1; -.
DR OrthoDB; 470747at2759; -.
DR BRENDA; 3.1.26.3; 6752.
DR Proteomes; UP000007305; Unplaced.
DR ExpressionAtlas; A6YSL1; baseline and differential.
DR GO; GO:0009570; C:chloroplast stroma; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0003725; F:double-stranded RNA binding; IDA:UniProtKB.
DR GO; GO:0004525; F:ribonuclease III activity; IBA:GO_Central.
DR GO; GO:0003727; F:single-stranded RNA binding; IDA:UniProtKB.
DR GO; GO:0000373; P:Group II intron splicing; IMP:UniProtKB.
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:0042254; P:ribosome biogenesis; IMP:UniProtKB.
DR GO; GO:0006396; P:RNA processing; IBA:GO_Central.
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 1: Evidence at protein level;
KW Chloroplast; mRNA processing; mRNA splicing; Plastid; Reference proteome;
KW Repeat; Ribonucleoprotein; RNA-binding; Transit peptide.
FT TRANSIT 1..28
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 29..525
FT /note="Ribonuclease III domain-containing protein RNC1,
FT chloroplastic"
FT /id="PRO_0000435536"
FT DOMAIN 125..271
FT /note="RNase III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00177"
FT DOMAIN 403..503
FT /note="RNase III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00177"
SQ SEQUENCE 525 AA; 61018 MW; E3CA6753D5CD860A CRC64;
MGPPAMAFQA LTLTPLPFSL HSSSRRVRVL AVAADQTPPP APPSEPANSP SRLLRELAQR
KKAVSPKKKH PPRRFILKPP LDDERLTRRF LSSPQLSLKA LPLLSSCLPS APLSTADRTW
MDEYLLEAKQ ALGYPLAPSE TLGEGDDCPA RHFDVLFYLA FQHLDPSSER TRMRHVRNGH
SRLWFLGQYV LELAFCEFFL QRYPRESPGP MRERVFALIG KKVLPRWLKA ASLHNLVFPY
DDLDKMIRKD REPPSKAVFW AIFGAIYLCF GMPEVYRVLF EAFGMDPDDE SCQPKLRRQL
EDVDYVSVEF EKRQLTWQDV AAYRPPPDAL FAHPRLFRAC VPPGMHRFRG NIWDFDSRPK
VMTTLGYPLP MNDRIPEITE ARNIELGLGL QLCFLHPSKH KFEHPRFCYE RLEYVGQKIQ
DLVMAERLLM KHLDAPGRWL AEKHRRTLMN KYCGRYLRDK HLQHYIIYGE TVQDRFEHNR
RLRNPSTTSV QQALHGLAYC VYGKPDVRRL MFEVFDFEQV QPKAV
