ID A0A0B6TRY9_9CORY Unreviewed; 405 AA.
AC A0A0B6TRY9;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE SubName: Full=Putative RNA methyltransferase {ECO:0000313|EMBL:AJK69034.1};
DE EC=2.1.1.- {ECO:0000313|EMBL:AJK69034.1};
GN ORFNames=B840_07180 {ECO:0000313|EMBL:AJK69034.1};
OS Corynebacterium marinum DSM 44953.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=1224162 {ECO:0000313|EMBL:AJK69034.1, ECO:0000313|Proteomes:UP000031928};
RN [1] {ECO:0000313|EMBL:AJK69034.1, ECO:0000313|Proteomes:UP000031928}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44953 {ECO:0000313|EMBL:AJK69034.1,
RC ECO:0000313|Proteomes:UP000031928};
RA Schaffert L., Albersmeier A., Kalinowski J., Ruckert C.;
RT "Complete genome sequence of Corynebacterium marinum DSM 44953.";
RL Submitted (MAY-2014) 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; CP007790; AJK69034.1; -; Genomic_DNA.
DR RefSeq; WP_042621566.1; NZ_CP007790.1.
DR AlphaFoldDB; A0A0B6TRY9; -.
DR STRING; 1224162.B840_07180; -.
DR KEGG; cmq:B840_07180; -.
DR HOGENOM; CLU_014689_7_0_11; -.
DR OrthoDB; 9804590at2; -.
DR Proteomes; UP000031928; 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:UP000031928};
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..61
FT /note="TRAM"
FT /evidence="ECO:0000259|PROSITE:PS50926"
FT ACT_SITE 362
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10015"
FT ACT_SITE 362
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 238
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 270
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 294
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 335
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
SQ SEQUENCE 405 AA; 43435 MW; F2D5C2F9ABBE7B67 CRC64;
MTELERGQTR ELTITRMAHG GEGIAELDGR VVFVRGAYPG DVVDATITQV KKRFARAELD
SVSTPGPLRV EQSCPAAAAG AGCCDFGDLD PAQEVDLKAD ILVGQLTRLG RAIDLPAPEL
INLEPARGWR TRVRLGVDKE GRAGFRARAS HDVVHIPCTQ VVPGLLDGLV GENARAFTPG
AEVVAVLDSE GVRHVVETRK APRGRRVEKV TDVLEGSGTV TERADGHTFR FPATAFWQAH
TQAPDAYTGV IRRWLSDLGD SDNTVGWDLY GGVGLFVPAL ADSLGEGATI HSVDYSPAAA
ELTQDTLEPY GLEIHNAMVE KTVETLPTPR VVVLDPPRTG AGDDVVAGVA KKQPERIIHV
GCDPATFSRD VAAWGENGYR IARLAVINAF PGTHHFEVVA ELTRK
//