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Database: UniProt
Entry: A0A143Q7N4_9NOCA
LinkDB: A0A143Q7N4_9NOCA
Original site: A0A143Q7N4_9NOCA 
ID   A0A143Q7N4_9NOCA        Unreviewed;       418 AA.
AC   A0A143Q7N4;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   SubName: Full=Putative RNA methyltransferase/cg2084 {ECO:0000313|EMBL:AMY18916.1};
DE            EC=2.1.1.- {ECO:0000313|EMBL:AMY18916.1};
GN   ORFNames=A3Q40_01526 {ECO:0000313|EMBL:AMY18916.1};
OS   Rhodococcus sp. PBTS 1.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC   Rhodococcus.
OX   NCBI_TaxID=1653478 {ECO:0000313|EMBL:AMY18916.1, ECO:0000313|Proteomes:UP000076180};
RN   [1] {ECO:0000313|EMBL:AMY18916.1, ECO:0000313|Proteomes:UP000076180}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PBTS 1 {ECO:0000313|EMBL:AMY18916.1,
RC   ECO:0000313|Proteomes:UP000076180};
RX   PubMed=27284129;
RA   Stamler R.A., Vereecke D., Zhang Y., Schilkey F., Devitt N., Randall J.J.;
RT   "Complete Genome and Plasmid Sequences for Rhodococcus fascians D188 and
RT   Draft Sequences for Rhodococcus Isolates PBTS 1 and PBTS 2.";
RL   Genome Announc. 4:0-0(2016).
RN   [2] {ECO:0000313|Proteomes:UP000076180}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PBTS 1 {ECO:0000313|Proteomes:UP000076180};
RA   Stamer R., Vereecke D., Zhang Y., Schilkey F., Devitt N., Randall J.;
RT   "Complete Genome and Plasmid Sequences for Rhodococcus fascians D188 and
RT   Draft Sequences for Rhodococcus spp. Isolates PBTS 1 and PBTS 2.";
RL   Submitted (APR-2016) 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}.
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DR   EMBL; CP015219; AMY18916.1; -; Genomic_DNA.
DR   RefSeq; WP_068100887.1; NZ_CP015219.1.
DR   AlphaFoldDB; A0A143Q7N4; -.
DR   STRING; 1653478.A3Q40_01526; -.
DR   KEGG; rhu:A3Q40_01526; -.
DR   PATRIC; fig|1653478.3.peg.1535; -.
DR   Proteomes; UP000076180; Chromosome.
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; IPR030390; MeTrfase_TrmA_AS.
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.
DR   PROSITE; PS01230; TRMA_1; 1.
PE   3: Inferred from homology;
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|PROSITE-
KW   ProRule:PRU01024}; Reference proteome {ECO:0000313|Proteomes:UP000076180};
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          3..62
FT                   /note="TRAM"
FT                   /evidence="ECO:0000259|PROSITE:PS50926"
FT   REGION          197..236
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        376
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10015"
FT   ACT_SITE        376
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         253
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         282
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         306
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         349
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
SQ   SEQUENCE   418 AA;  43734 MW;  57AB52DAD7BC5557 CRC64;
     MSESWAGRVL EVVVGTPGHG GFCVARYDGR VIFVRHSLPG ETVRALITED TGGSFCRADA
     VEIVDASPER IAPLCPIAGP GASGCCDLSH TSEAGARAWK AAVVSEQLRR IARVETDVDV
     ETWGERTGWR TRLRLGVGAD GHAGFHRARS AELVTDLACP QSPAVAYDGL ADRTWTPGAD
     LAVALDSDGA RHVVEIAPPG SSSRAGGGAR RAASSRRARR SAPRAHRAVV GSGRARQRVG
     DREWTVDAHG FWQAHRHAPD RYSAVVREWA DVRPGDTVWD LYAGAGVFAA AVAGDAGSSG
     SVVGVEAGAD AVRDGRAALA DLPAVDLRAA PVEHAIADLP ADPATVILDP PRAGAGKAVV
     AAVADAGPRR VVHVGCDPAS FARDVGLYLS HGYRLEHLRA FDAFPLTSHV ECIAALVR
//
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