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Database: UniProt
Entry: A0A0Q8AUD1_9MICO
LinkDB: A0A0Q8AUD1_9MICO
Original site: A0A0Q8AUD1_9MICO 
ID   A0A0Q8AUD1_9MICO        Unreviewed;       442 AA.
AC   A0A0Q8AUD1;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   SubName: Full=23S rRNA methyltransferase {ECO:0000313|EMBL:KQZ84842.1};
GN   ORFNames=ASD56_00115 {ECO:0000313|EMBL:KQZ84842.1};
OS   Microbacterium sp. Root166.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Microbacterium.
OX   NCBI_TaxID=1736478 {ECO:0000313|EMBL:KQZ84842.1, ECO:0000313|Proteomes:UP000051650};
RN   [1] {ECO:0000313|Proteomes:UP000051650}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root166 {ECO:0000313|Proteomes:UP000051650};
RA   Garrido-Oter R., Bai Y.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQZ84842.1, ECO:0000313|Proteomes:UP000051650}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root166 {ECO:0000313|EMBL:KQZ84842.1,
RC   ECO:0000313|Proteomes:UP000051650};
RA   Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. RNA M5U methyltransferase family. {ECO:0000256|PROSITE-
CC       ProRule:PRU01024}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KQZ84842.1}.
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DR   EMBL; LMGL01000001; KQZ84842.1; -; Genomic_DNA.
DR   RefSeq; WP_055959784.1; NZ_LMGL01000001.1.
DR   AlphaFoldDB; A0A0Q8AUD1; -.
DR   STRING; 1736478.ASD56_00115; -.
DR   OrthoDB; 9804590at2; -.
DR   Proteomes; UP000051650; Unassembled WGS sequence.
DR   GO; GO:0008173; F:RNA methyltransferase activity; IEA:InterPro.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   GO; GO:0006396; P:RNA processing; IEA:InterPro.
DR   Gene3D; 2.40.50.1070; -; 1.
DR   Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   InterPro; IPR002792; TRAM_dom.
DR   InterPro; IPR010280; U5_MeTrfase_fam.
DR   PANTHER; PTHR11061; RNA M5U METHYLTRANSFERASE; 1.
DR   PANTHER; PTHR11061:SF30; TRNA (URACIL(54)-C(5))-METHYLTRANSFERASE; 1.
DR   Pfam; PF01938; TRAM; 1.
DR   Pfam; PF05958; tRNA_U5-meth_tr; 1.
DR   SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR   PROSITE; PS51687; SAM_MT_RNA_M5U; 1.
DR   PROSITE; PS50926; TRAM; 1.
PE   3: Inferred from homology;
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|PROSITE-
KW   ProRule:PRU01024}; Reference proteome {ECO:0000313|Proteomes:UP000051650};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691,
KW   ECO:0000256|PROSITE-ProRule:PRU01024};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PROSITE-
KW   ProRule:PRU01024}.
FT   DOMAIN          5..64
FT                   /note="TRAM"
FT                   /evidence="ECO:0000259|PROSITE:PS50926"
FT   ACT_SITE        395
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         255
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         291
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         315
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         368
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
SQ   SEQUENCE   442 AA;  47741 MW;  83F56B9FE0526848 CRC64;
     MTESTGDSGQ IIDLEIGDVA HGGVFVARHE GRVVFVPDVL PGERVRVRLT DTSKNSFWRG
     EALEVLDASP HRRAHVWRQA DIDVDPERRP GGAEFGHIDL AEQRRLKLNV LTDALHRFGG
     VDLPVSIGAA EGDATSAPET SDGTRWRTRV SLHVDDEGRV GPYAARSHRV IAVDDLPLAT
     QEVEDAALAL RGGQPGRIDL VQPDDGRVRV IVRPERPAGR GRGRSGPKPV EPKPEIVYER
     VGDRDFRVDA GGFWQVHRLA AHTLTQSVRS VLTGLGEHVS WDADAWHLDL YGGVGLFAAA
     MGDVGGRATR MTTVESDPRA TDNAAENLVE WVGARAETGR VDRWLARLAA EATAAEKERL
     SRGVVLLDPP RAGAGRAVVE SVASLAPGAV VYVACDPVAL ARDVAIFRDA GYDTTAVEAL
     DLFPNSHHVE AVATLMPSRS RR
//
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