ID DIM1A_ARATH Reviewed; 353 AA.
AC O22268;
DT 24-JUN-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 30-NOV-2016, entry version 123.
DE RecName: Full=Ribosomal RNA small subunit methyltransferase {ECO:0000305};
DE EC=2.1.1.- {ECO:0000269|PubMed:22829145};
DE AltName: Full=18S nuclear rRNA (adenine(1785)-N(6)/adenine(1786)-N(6))-dimethyltransferase {ECO:0000305};
DE AltName: Full=Adenosine dimethyl transferase 1A {ECO:0000305};
DE AltName: Full=Dimethyladenosine transferase 1A {ECO:0000303|PubMed:19929881};
GN Name=DIM1A {ECO:0000303|PubMed:19929881};
GN OrderedLocusNames=At2g47420 {ECO:0000312|TAIR:AT2G47420};
GN ORFNames=T30B22.28 {ECO:0000312|EMBL:AAC62868.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
OC Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
OC Arabidopsis.
OX NCBI_TaxID=3702 {ECO:0000312|Proteomes:UP000006548};
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L.,
RA Moffat K.S., Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L.,
RA Tallon L.J., Gill J.E., Adams M.D., Carrera A.J., Creasy T.H.,
RA Goodman H.M., Somerville C.R., Copenhaver G.P., Preuss D.,
RA Nierman W.C., White O., Eisen J.A., Salzberg S.L., Fraser C.M.,
RA Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis
RT thaliana.";
RL Nature 402:761-768(1999).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RG The Arabidopsis Information Resource (TAIR);
RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases.
RN [3]
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.,
RA Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
RA Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
RA Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
RA Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
RA Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
RA Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
RA Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
RA Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
RA Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
RA Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
RA Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RC STRAIN=cv. Columbia;
RX PubMed=19929881; DOI=10.1111/j.1365-313X.2009.04079.x;
RA Richter U., Kuhn K., Okada S., Brennicke A., Weihe A., Borner T.;
RT "A mitochondrial rRNA dimethyladenosine methyltransferase in
RT Arabidopsis.";
RL Plant J. 61:558-569(2010).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF GLY-66, TISSUE
RP SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=22829145; DOI=10.1105/tpc.112.101022;
RA Wieckowski Y., Schiefelbein J.;
RT "Nuclear ribosome biogenesis mediated by the DIM1A rRNA dimethylase is
RT required for organized root growth and epidermal patterning in
RT Arabidopsis.";
RL Plant Cell 24:2839-2856(2012).
CC -!- FUNCTION: N6-adenine methyltransferase which modifies the AA
CC dinucleotide at the plant nuclear 18S rRNA nucleotides A1785 and
CC A1786 (PubMed:22829145). Required for generating appropriate
CC patterns of gene expression during root development, including the
CC cell-specific expression of transcriptional regulators involved in
CC root hair and non-hair cells patterning (PubMed:22829145).
CC {ECO:0000269|PubMed:22829145, ECO:0000305|PubMed:19929881}.
CC -!- CATALYTIC ACTIVITY: 4 S-adenosyl-L-methionine +
CC adenine(1785)/adenine(1786) in nuclear 18S rRNA = 4 S-adenosyl-L-
CC homocysteine + N(6)-dimethyladenine(1785)/N(6)-
CC dimethyladenine(1786) in nuclear 18S rRNA.
CC {ECO:0000269|PubMed:22829145}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19929881,
CC ECO:0000269|PubMed:22829145}. Nucleus, nucleolus
CC {ECO:0000269|PubMed:19929881, ECO:0000269|PubMed:22829145}.
CC -!- TISSUE SPECIFICITY: Expressed in rapidly dividing tissues,
CC including root meristems and lateral root primordia, developing
CC cotyledons and leaves, petals, anther, pollen grains and silique
CC abscission zone. {ECO:0000269|PubMed:22829145}.
CC -!- MISCELLANEOUS: The inability to isolate a null mutant suggests
CC that DIM1A is essential for viability.
CC {ECO:0000305|PubMed:22829145}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding
CC methyltransferase superfamily. rRNA adenine N(6)-methyltransferase
CC family. {ECO:0000305}.
DR EMBL; AC002535; AAC62868.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC10839.1; -; Genomic_DNA.
DR EMBL; AY039949; AAK64053.1; -; mRNA.
DR EMBL; AY113864; AAM44912.1; -; mRNA.
DR PIR; T00442; T00442.
DR RefSeq; NP_182264.1; NM_130310.3.
DR UniGene; At.12423; -.
DR ProteinModelPortal; O22268; -.
DR SMR; O22268; -.
DR STRING; 3702.AT2G47420.1; -.
DR PaxDb; O22268; -.
DR DNASU; 819355; -.
DR EnsemblPlants; AT2G47420.1; AT2G47420.1; AT2G47420.
DR GeneID; 819355; -.
DR Gramene; AT2G47420.1; AT2G47420.1; AT2G47420.
DR KEGG; ath:AT2G47420; -.
DR TAIR; AT2G47420; -.
DR eggNOG; KOG0820; Eukaryota.
DR eggNOG; COG0030; LUCA.
DR HOGENOM; HOG000227963; -.
DR InParanoid; O22268; -.
DR KO; K14191; -.
DR OMA; PRFDICV; -.
DR OrthoDB; EOG09360F1H; -.
DR PhylomeDB; O22268; -.
DR PRO; PR:O22268; -.
DR Proteomes; UP000006548; Chromosome 2.
DR Genevisible; O22268; AT.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005730; C:nucleolus; IDA:TAIR.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0000179; F:rRNA (adenine-N6,N6-)-dimethyltransferase activity; IMP:TAIR.
DR GO; GO:0051301; P:cell division; IMP:TAIR.
DR GO; GO:0001708; P:cell fate specification; IMP:TAIR.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR001737; KsgA/Erm.
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.
DR PANTHER; PTHR11727; PTHR11727; 2.
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 1: Evidence at protein level;
KW Complete proteome; Methyltransferase; Nucleus; Reference proteome;
KW RNA-binding; rRNA processing; S-adenosyl-L-methionine; Transferase.
FT CHAIN 1 353 Ribosomal RNA small subunit
FT methyltransferase.
FT /FTId=PRO_0000433250.
FT COMPBIAS 277 305 Asp-rich. {ECO:0000255|PROSITE-
FT ProRule:PRU00004}.
FT BINDING 35 35 S-adenosyl-L-methionine; via carbonyl
FT oxygen. {ECO:0000255|PROSITE-
FT ProRule:PRU01026}.
FT BINDING 37 37 S-adenosyl-L-methionine; via amide
FT nitrogen. {ECO:0000255|PROSITE-
FT ProRule:PRU01026}.
FT BINDING 62 62 S-adenosyl-L-methionine; via carbonyl
FT oxygen. {ECO:0000255|PROSITE-
FT ProRule:PRU01026}.
FT BINDING 83 83 S-adenosyl-L-methionine.
FT {ECO:0000255|PROSITE-ProRule:PRU01026}.
FT BINDING 111 111 S-adenosyl-L-methionine.
FT {ECO:0000255|PROSITE-ProRule:PRU01026}.
FT BINDING 126 126 S-adenosyl-L-methionine.
FT {ECO:0000255|PROSITE-ProRule:PRU01026}.
FT MUTAGEN 66 66 G->E: In dim1A; loss of adenine
FT methylation, but no effect on pre-rRNA
FT processing.
FT {ECO:0000269|PubMed:22829145}.
CC --------------------------------------------------------------------------
CC The following FT lines are automated annotations from the MyHits database.
CC --------------------------------------------------------------------------
FT MYHIT 27 254 ipfam:RrnaAD [T]
FT MYHIT 58 85 ipat:RRNA_A_DIMETH [T]
FT MYHIT 42 211 ismart:rADc [T]
FT MYHIT 28 349 iprf:SAM_RNA_A_N6_MT [T]
SQ SEQUENCE 353 AA; 39687 MW; 7BF9B910CF184DD4 CRC64;
MAGGKIRKEK PKASNRAPSN HYQGGISFHK SKGQHILKNP LLVDSIVQKA GIKSTDVILE
IGPGTGNLTK KLLEAGKEVI AVELDSRMVL ELQRRFQGTP FSNRLKVIQG DVLKTELPRF
DICVANIPYQ ISSPLTFKLL FHPTSFRCAV IMYQREFAMR LVAQPGDNLY CRLSVNTQLY
ARVSHLLKVG KNNFRPPPKV DSSVVRIEPR RPGPQVNKKE WDGFLRVCFI RKNKTLGSIF
KQKSVLSMLE KNFKTLQAVL ASLQNNGEPA LNTTSMDLGD QSMGMEDDDN EMDDDDMEMD
EGEGDGGETS EFKEKVMNVL KEGGFEEKRS SKLSQQEFLY LLSLFNKSGI HFT
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