ID A0A316UAC8_9BASI Unreviewed; 365 AA.
AC A0A316UAC8;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=rRNA methyltransferase 2, mitochondrial {ECO:0000256|ARBA:ARBA00041184};
GN ORFNames=BCV69DRAFT_297481 {ECO:0000313|EMBL:PWN22180.1};
OS Pseudomicrostroma glucosiphilum.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Exobasidiomycetes; Microstromatales; Microstromatales incertae sedis;
OC Pseudomicrostroma.
OX NCBI_TaxID=1684307 {ECO:0000313|EMBL:PWN22180.1, ECO:0000313|Proteomes:UP000245942};
RN [1] {ECO:0000313|EMBL:PWN22180.1, ECO:0000313|Proteomes:UP000245942}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCA 4718 {ECO:0000313|EMBL:PWN22180.1,
RC ECO:0000313|Proteomes:UP000245942};
RX PubMed=29771364; DOI=10.1093/molbev/msy072;
RA Kijpornyongpan T., Mondo S.J., Barry K., Sandor L., Lee J., Lipzen A.,
RA Pangilinan J., LaButti K., Hainaut M., Henrissat B., Grigoriev I.V.,
RA Spatafora J.W., Aime M.C.;
RT "Broad genomic sampling reveals a smut pathogenic ancestry of the fungal
RT clade Ustilaginomycotina.";
RL Mol. Biol. Evol. 0:0-0(2018).
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. RNA methyltransferase RlmE family.
CC {ECO:0000256|ARBA:ARBA00009258}.
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; KZ819323; PWN22180.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A316UAC8; -.
DR STRING; 1684307.A0A316UAC8; -.
DR OrthoDB; 119516at2759; -.
DR Proteomes; UP000245942; Unassembled WGS sequence.
DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0042254; P:ribosome biogenesis; IEA:UniProt.
DR GO; GO:0001510; P:RNA methylation; IEA:InterPro.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR HAMAP; MF_01547; RNA_methyltr_E; 1.
DR InterPro; IPR002877; RNA_MeTrfase_FtsJ_dom.
DR InterPro; IPR015507; rRNA-MeTfrase_E.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR10920; RIBOSOMAL RNA METHYLTRANSFERASE; 1.
DR PANTHER; PTHR10920:SF18; RRNA METHYLTRANSFERASE 2, MITOCHONDRIAL; 1.
DR Pfam; PF01728; FtsJ; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
PE 3: Inferred from homology;
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW Reference proteome {ECO:0000313|Proteomes:UP000245942};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..365
FT /note="rRNA methyltransferase 2, mitochondrial"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5016389545"
FT DOMAIN 103..345
FT /note="Ribosomal RNA methyltransferase FtsJ"
FT /evidence="ECO:0000259|Pfam:PF01728"
SQ SEQUENCE 365 AA; 39682 MW; 1E2026298C45B8B9 CRC64;
MYTAAVGAWG CVAVVQAPAL ASTSFSLACS QATQVASRAL AGAARNFTTD AVCLAKKKSA
STSRYTSRQS SDPYVLARTS QSHASSLALP SSSSQDDLPG EKFVSRSAFK LFQLEEKHHF
LAPRKGKGRG RERVILDLGA APGGWTQMAL RLLRNSSSSV ESSTEGQAEE GVVRRPPIFA
LDLLPLHPSV QALPGVNFIQ GDFESEDVKK ELAERVRLHR SQGGEEAIDD KVDVILSDML
ANTTGSSLRD GALSLSLLHH LYHFAQRHLV ASPSSFLVLK IFPSPEAEAF RRRMLQYSAS
SGKKRASVEE QSGAIKGGAF ETVKTEKPPG SRKESREVYW VCKGFRGSEK CWTLDEWYEM
EEAAG
//