DIM1C_ARATH
ID DIM1C_ARATH Reviewed; 343 AA.
AC O65090; Q9LPD3; Q9LQ70;
DT 24-JUN-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Ribosomal RNA small subunit methyltransferase, chloroplastic {ECO:0000305};
DE EC=2.1.1.- {ECO:0000305};
DE AltName: Full=Dimethyladenosine transferase 1C {ECO:0000305};
DE AltName: Full=Protein PALEFACE 1 {ECO:0000303|PubMed:9596631};
DE Flags: Precursor;
GN Name=PFC1 {ECO:0000303|PubMed:9596631}; Synonyms=DIM1C {ECO:0000305};
GN OrderedLocusNames=At1g01860 {ECO:0000312|Araport:AT1G01860};
GN ORFNames=F22M8.1 {ECO:0000312|EMBL:AAF76480.1},
GN T1N6.27 {ECO:0000312|EMBL:AAF78414.1};
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 {ECO:0000312|EMBL:AAC09322.1};
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=9596631; DOI=10.2307/3870658;
RA Tokuhisa J.G., Vijayan P., Feldmann K.A., Browse J.A.;
RT "Chloroplast development at low temperatures requires a homolog of DIM1, a
RT yeast gene encoding the 18S rRNA dimethylase.";
RL Plant Cell 10:699-711(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(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=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
RN [5]
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).
CC -!- FUNCTION: Required for methylation of the 3' adenosines in the small
CC subunit of plastid rRNA. Essential for chloroplast biogenesis at low
CC temperatures. {ECO:0000269|PubMed:9596631}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000305|PubMed:9596631}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype when grown at 22 degrees
CC Celsius. Chilling-induced chlorosis and reduced growth at 5 degrees
CC Celsius. {ECO:0000269|PubMed:9596631}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. rRNA adenine N(6)-methyltransferase family.
CC {ECO:0000255|PROSITE-ProRule:PRU01026}.
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DR EMBL; AF051326; AAC09322.1; -; mRNA.
DR EMBL; AC009273; AAF78414.1; -; Genomic_DNA.
DR EMBL; AC020622; AAF76480.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE27344.1; -; Genomic_DNA.
DR EMBL; AK117412; BAC42078.1; -; mRNA.
DR EMBL; BT005097; AAO50630.1; -; mRNA.
DR PIR; D86150; D86150.
DR PIR; E86150; E86150.
DR PIR; T51591; T51591.
DR RefSeq; NP_171690.1; NM_100068.3.
DR AlphaFoldDB; O65090; -.
DR SMR; O65090; -.
DR STRING; 3702.AT1G01860.1; -.
DR PaxDb; O65090; -.
DR PRIDE; O65090; -.
DR ProteomicsDB; 223951; -.
DR EnsemblPlants; AT1G01860.1; AT1G01860.1; AT1G01860.
DR GeneID; 839283; -.
DR Gramene; AT1G01860.1; AT1G01860.1; AT1G01860.
DR KEGG; ath:AT1G01860; -.
DR Araport; AT1G01860; -.
DR TAIR; locus:2025437; AT1G01860.
DR eggNOG; KOG0820; Eukaryota.
DR HOGENOM; CLU_041220_6_0_1; -.
DR InParanoid; O65090; -.
DR OMA; CAFNGKR; -.
DR OrthoDB; 628543at2759; -.
DR PhylomeDB; O65090; -.
DR PRO; PR:O65090; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; O65090; baseline and differential.
DR Genevisible; O65090; AT.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0016422; F:mRNA (2'-O-methyladenosine-N6-)-methyltransferase activity; ISS:TAIR.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0000179; F:rRNA (adenine-N6,N6-)-dimethyltransferase activity; IBA:GO_Central.
DR GO; GO:0009409; P:response to cold; IMP:TAIR.
DR GO; GO:0031167; P:rRNA methylation; IBA:GO_Central.
DR Gene3D; 1.10.8.100; -; 1.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR001737; KsgA/Erm.
DR InterPro; IPR023165; rRNA_Ade_diMease-like_C.
DR InterPro; IPR020596; rRNA_Ade_Mease_Trfase_CS.
DR InterPro; IPR020598; rRNA_Ade_methylase_Trfase_N.
DR InterPro; IPR011530; rRNA_adenine_dimethylase.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR11727; PTHR11727; 1.
DR Pfam; PF00398; RrnaAD; 1.
DR SMART; SM00650; rADc; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR TIGRFAMs; TIGR00755; ksgA; 1.
DR PROSITE; PS01131; RRNA_A_DIMETH; 1.
DR PROSITE; PS51689; SAM_RNA_A_N6_MT; 1.
PE 2: Evidence at transcript level;
KW Chloroplast; Methyltransferase; Plastid; Reference proteome; RNA-binding;
KW rRNA processing; S-adenosyl-L-methionine; Transferase; Transit peptide.
FT TRANSIT 1..48
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 49..343
FT /note="Ribosomal RNA small subunit methyltransferase,
FT chloroplastic"
FT /evidence="ECO:0000255"
FT /id="PRO_0000433249"
FT BINDING 78
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01026"
FT BINDING 80
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01026"
FT BINDING 105
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01026"
FT BINDING 126
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01026"
FT BINDING 151
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01026"
FT BINDING 183
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01026"
SQ SEQUENCE 343 AA; 38023 MW; 55BE66930A569556 CRC64;
MMNAVITSAT INCNSLSPSW TCGDNSPSKL LLGEISAALS RRRTVKVSCG KSSPDDYHST
LKSLNSRGRF PRKSLGQHYM LNSDINDQLA SAADVKEGDF VLEIGPGTGS LTNVLINLGA
TVLAIEKDPH MVDLVSERFA GSDKFKVLQE DFVKCHIRSH MLSILETRRL SHPDSALAKV
VSNLPFNIST DVVKLLLPMG DIFSKVVLLL QDEAALRLVE PALRTSEYRP INILINFYSE
PEYNFRVPRE NFFPQPKVDA AVVTFKLKHP RDYPDVSSTK NFFSLVNSAF NGKRKMLRKS
LQHISSSPDI EKALGVAGLP ATSRPEELTL DDFVKLHNVI ARE
