ID A0A0B5D8I3_9CORY Unreviewed; 395 AA.
AC A0A0B5D8I3;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE SubName: Full=SAM-dependent methyltransferase {ECO:0000313|EMBL:AJE33357.1};
GN ORFNames=B842_07540 {ECO:0000313|EMBL:AJE33357.1};
OS Corynebacterium humireducens NBRC 106098 = DSM 45392.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=1223515 {ECO:0000313|EMBL:AJE33357.1, ECO:0000313|Proteomes:UP000031524};
RN [1] {ECO:0000313|EMBL:AJE33357.1, ECO:0000313|Proteomes:UP000031524}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MFC-5 {ECO:0000313|Proteomes:UP000031524};
RA Ruckert C., Albersmeier A., Kalinowski J.;
RT "Complete genome sequence of Corynebacterium humireducens DSM 45392(T),
RT isolated from a wastewater-fed microbial fuel cell.";
RL Submitted (APR-2013) 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; CP005286; AJE33357.1; -; Genomic_DNA.
DR RefSeq; WP_040085988.1; NZ_CP005286.1.
DR AlphaFoldDB; A0A0B5D8I3; -.
DR STRING; 1223515.B842_07540; -.
DR KEGG; chm:B842_07540; -.
DR HOGENOM; CLU_014689_7_0_11; -.
DR Proteomes; UP000031524; 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; 2.40.50.140; 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};
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 1..53
FT /note="TRAM"
FT /evidence="ECO:0000259|PROSITE:PS50926"
FT ACT_SITE 353
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10015"
FT ACT_SITE 353
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 227
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 261
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 285
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 326
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
SQ SEQUENCE 395 AA; 42269 MW; 6E28864925560B5A CRC64;
MTELEITRMA HGGEGIAELD GRVVFVRGAY PGDVVEVSIT QDKKRFARAE VVSVTTPGPL
RVAQACPAAA AGAGCCDFGD LDPAAETQLK ADILQGQLTR LGRVAEPPTP ELHPLEPVRG
WRTRVRLGVD KQGRAGFRAR NSHEIIPVAC TQVVPGLLDG LLEATYTPGA EIVAVLDSTG
ERHVVESRRA PRGRRVEKVQ QVLEGSGTVT ERADDHTFRF PATAFWQAHS AAPDAYTGLV
REWLADLGPA DGTPAVGWDL YGGVGLFVPA LADSLGEGAV IHSVDYSQAA AKLTQESLEG
YVVEKHNRMV EKAIGNLPAP RVVVLDPPRT GAGDDVVAGV AKQNPERVIH VGCDPATFSR
DVAAWGEQGY RLKRLAVLNA FPGTHHFEVM AELTR
//
