DIM1B_ARATH
ID DIM1B_ARATH Reviewed; 380 AA.
AC Q9FK02; Q8L867;
DT 24-JUN-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Ribosomal RNA small subunit methyltransferase, mitochondrial {ECO:0000305};
DE EC=2.1.1.- {ECO:0000269|PubMed:19929881};
DE AltName: Full=18S mitochondrial rRNA (adenine(1914)-N(6)/adenine(1915)-N(6))-dimethyltransferase {ECO:0000305};
DE AltName: Full=Adenosine dimethyl transferase 1B {ECO:0000305};
DE AltName: Full=Dimethyladenosine transferase 1B {ECO:0000303|PubMed:19929881};
DE Flags: Precursor;
GN Name=DIM1B {ECO:0000303|PubMed:19929881};
GN OrderedLocusNames=At5g66360 {ECO:0000312|Araport:AT5G66360};
GN ORFNames=K1L20.14 {ECO:0000312|EMBL:BAB10912.1};
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|Proteomes:UP000006548};
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9734815; DOI=10.1093/dnares/5.3.203;
RA Kotani H., Nakamura Y., Sato S., Asamizu E., Kaneko T., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. VI. Sequence
RT features of the regions of 1,367,185 bp covered by 19 physically assigned
RT P1 and TAC clones.";
RL DNA Res. 5:203-216(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10718197; DOI=10.1093/dnares/7.1.31;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. X. Sequence
RT features of the regions of 3,076,755 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:31-63(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] (ISOFORM 2).
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 FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND DISRUPTION
RP PHENOTYPE.
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 Arabidopsis.";
RL Plant J. 61:558-569(2010).
CC -!- FUNCTION: N6-adenine methyltransferase which modifies the AA
CC dinucleotide at the plant mitochondrial 18S rRNA nucleotides A1914 and
CC A1915. Not active as mitochondrial transcription factor.
CC {ECO:0000269|PubMed:19929881}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=adenosine(1914)/adenosine(1915) in 18S rRNA + 4 S-adenosyl-L-
CC methionine = 4 H(+) + N(6)-dimethyladenosine(1914)/N(6)-
CC dimethyladenosine(1915) in 18S rRNA + 4 S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:47644, Rhea:RHEA-COMP:11868, Rhea:RHEA-COMP:11869,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:74411, ChEBI:CHEBI:74493;
CC Evidence={ECO:0000269|PubMed:19929881};
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:19929881}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9FK02-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9FK02-2; Sequence=VSP_057696;
CC -!- DISRUPTION PHENOTYPE: No visible phenotype when grown under normal
CC conditions or under cold stress, but lack of methylation of the
CC adenosine dinucleotide present in the mitochondrial 18S rRNA.
CC {ECO:0000269|PubMed:19929881}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. rRNA adenine N(6)-methyltransferase family. {ECO:0000305}.
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DR EMBL; AB013389; BAB10912.1; -; Genomic_DNA.
DR EMBL; AB022211; BAB10912.1; JOINED; Genomic_DNA.
DR EMBL; CP002688; AED98203.1; -; Genomic_DNA.
DR EMBL; CP002688; AED98204.1; -; Genomic_DNA.
DR EMBL; AY120713; AAM53271.1; -; mRNA.
DR EMBL; BT008836; AAP68275.1; -; mRNA.
DR RefSeq; NP_201437.2; NM_126034.3. [Q9FK02-2]
DR RefSeq; NP_975003.1; NM_203274.2. [Q9FK02-1]
DR AlphaFoldDB; Q9FK02; -.
DR SMR; Q9FK02; -.
DR STRING; 3702.AT5G66360.2; -.
DR PaxDb; Q9FK02; -.
DR PRIDE; Q9FK02; -.
DR ProteomicsDB; 220541; -. [Q9FK02-1]
DR EnsemblPlants; AT5G66360.1; AT5G66360.1; AT5G66360. [Q9FK02-2]
DR EnsemblPlants; AT5G66360.2; AT5G66360.2; AT5G66360. [Q9FK02-1]
DR GeneID; 836768; -.
DR Gramene; AT5G66360.1; AT5G66360.1; AT5G66360. [Q9FK02-2]
DR Gramene; AT5G66360.2; AT5G66360.2; AT5G66360. [Q9FK02-1]
DR KEGG; ath:AT5G66360; -.
DR Araport; AT5G66360; -.
DR TAIR; locus:2155031; AT5G66360.
DR eggNOG; KOG0820; Eukaryota.
DR HOGENOM; CLU_041220_2_0_1; -.
DR InParanoid; Q9FK02; -.
DR OMA; EWWAFTR; -.
DR PhylomeDB; Q9FK02; -.
DR PRO; PR:Q9FK02; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FK02; baseline and differential.
DR Genevisible; Q9FK02; AT.
DR GO; GO:0005739; C:mitochondrion; IDA: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:0046085; P:adenosine metabolic process; IMP:TAIR.
DR GO; GO:0031167; P:rRNA methylation; IBA:GO_Central.
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_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 1: Evidence at protein level;
KW Alternative splicing; Methyltransferase; Mitochondrion; Reference proteome;
KW RNA-binding; rRNA processing; S-adenosyl-L-methionine; Transferase;
KW Transit peptide.
FT TRANSIT 1..26
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 27..380
FT /note="Ribosomal RNA small subunit methyltransferase,
FT mitochondrial"
FT /evidence="ECO:0000255"
FT /id="PRO_0000433251"
FT BINDING 70
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01026"
FT BINDING 72
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01026"
FT BINDING 97
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01026"
FT BINDING 118
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01026"
FT BINDING 146
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01026"
FT BINDING 161
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01026"
FT VAR_SEQ 214..241
FT /note="Missing (in isoform 2)"
FT /id="VSP_057696"
SQ SEQUENCE 380 AA; 43315 MW; C7102C6BDE90CE0C CRC64;
MILRLKDQTL IKINSTRSYL SSLVFRRDSH SQARTKPDHD RRRRGYERDV RIEEKKEHDG
LFLCKSKGQH LLTNTRILDS IVRSSDIRPT DTVLEIGPGT GNLTMKLLEA AQNVVAVELD
KRMVEILRKR VSDHGFADKL TIIQKDVLKT DFPHFDLVVA NIPYNISSPL VAKLVYGSNT
FRSATLLLQK EFSRRLLANP GDSDFNRLAV NVKLVADVKF VMDVSKREFV PPPKVDSSVI
RITPKEIIPD VNVQEWLAFT RTCFGKKNKT LGSMFRQKKK VMELQSLSAG RHGSNVEVMN
QTGGDSDSDV EEDGKDDLLC LDTDASMFKE RVIEILRTNG FEEKRPSKLS HRELLHLLSL
FNQAGIFFHD ITSLQMDLHE
