ID A0A021VRM7_9CELL Unreviewed; 418 AA.
AC A0A021VRM7;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE SubName: Full=SAM-dependent methyltransferase {ECO:0000313|EMBL:EYR63791.1};
GN ORFNames=N866_18250 {ECO:0000313|EMBL:EYR63791.1};
OS Actinotalea ferrariae CF5-4.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Cellulomonadaceae;
OC Actinotalea.
OX NCBI_TaxID=948458 {ECO:0000313|EMBL:EYR63791.1, ECO:0000313|Proteomes:UP000019753};
RN [1] {ECO:0000313|EMBL:EYR63791.1, ECO:0000313|Proteomes:UP000019753}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CF5-4 {ECO:0000313|EMBL:EYR63791.1,
RC ECO:0000313|Proteomes:UP000019753};
RA Chen F., Li Y., Wang G.;
RT "Actinotalea ferrariae CF5-4.";
RL Submitted (JAN-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}.
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:EYR63791.1}.
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DR EMBL; AXCW01000067; EYR63791.1; -; Genomic_DNA.
DR RefSeq; WP_034225139.1; NZ_AXCW01000067.1.
DR AlphaFoldDB; A0A021VRM7; -.
DR OrthoDB; 9804590at2; -.
DR Proteomes; UP000019753; 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; 2.
DR InterPro; IPR030391; MeTrfase_TrmA_CS.
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; PS01231; TRMA_2; 1.
PE 3: Inferred from homology;
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|PROSITE-
KW ProRule:PRU01024}; Reference proteome {ECO:0000313|Proteomes:UP000019753};
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 6..67
FT /note="TRAM"
FT /evidence="ECO:0000259|PROSITE:PS50926"
FT ACT_SITE 375
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 249
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 280
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 304
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 348
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
SQ SEQUENCE 418 AA; 43922 MW; 01A983F3B73797AB CRC64;
MSQASNPSPS EGTVVLDVGP VAHGGHCVAR HEGRVVFVRH ALPGERVRAR LTEAAPTAKF
WRADAVEVLE ASPDRVASPW PEAGPGGVGG GELGHVALPA QRAWKAAVVE EQLRRLAHDD
RAVVVEGAPG DDARGGLRWR TRVELVADAE GRAGMHRHRS HDVVALEAMP LAVEDAGVEG
VLSRRWTAGA RLTLVAPSGG DRPLLLVDGV PWLRNAPDTR PTARASVRET LRRGDRELSW
RVAGDGFWQV HREAPGVLVG AVGDVLAQDG LAGARVVDLY AGSGLFSLPL ADAVGPAGAV
AAVEGDARAV RDLRRNVHDR PQVRLHHGGV LDVLRSGAVG PADVVVLDPP RVGAGRAVVD
GVVALGAERV VLVACDPASL ARDVALLVDA GHVLEGLRAF DLFPMTHHVE AVALLRRA
//
