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Database: UniProt
Entry: F3Y9F6_MELPT
LinkDB: F3Y9F6_MELPT
Original site: F3Y9F6_MELPT 
ID   F3Y9F6_MELPT            Unreviewed;       460 AA.
AC   F3Y9F6;
DT   28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT   28-JUN-2011, sequence version 1.
DT   27-MAR-2024, entry version 67.
DE   SubName: Full=RNA methyltransferase, TrmA family {ECO:0000313|EMBL:BAK21134.1};
GN   OrderedLocusNames=MPTP_0666 {ECO:0000313|EMBL:BAK21134.1};
OS   Melissococcus plutonius (strain ATCC 35311 / CIP 104052 / LMG 20360 / NCIMB
OS   702443).
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae;
OC   Melissococcus.
OX   NCBI_TaxID=940190 {ECO:0000313|EMBL:BAK21134.1, ECO:0000313|Proteomes:UP000008456};
RN   [1] {ECO:0000313|EMBL:BAK21134.1, ECO:0000313|Proteomes:UP000008456}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35311 / CIP 104052 / LMG 20360 / NCIMB 702443
RC   {ECO:0000313|Proteomes:UP000008456};
RX   PubMed=21622755; DOI=10.1128/JB.05151-11;
RA   Okumura K., Arai R., Okura M., Kirikae T., Takamatsu D., Osaki M.,
RA   Miyoshi-Akiyama T.;
RT   "Complete genome sequence of Melissococcus plutonius ATCC 35311.";
RL   J. Bacteriol. 193:4029-4030(2011).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=ATCC 35311;
RA   Okumura K., Arai R., Osaki M., Okura M., Kirikae T., Takamatsu D.,
RA   Akiyama T.;
RT   "Whole genome sequence of Melissococcus plutonius ATCC 35311.";
RL   Submitted (APR-2011) 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; AP012200; BAK21134.1; -; Genomic_DNA.
DR   RefSeq; WP_013773572.1; NC_015516.1.
DR   AlphaFoldDB; F3Y9F6; -.
DR   STRING; 940190.MPTP_0666; -.
DR   KEGG; mps:MPTP_0666; -.
DR   HOGENOM; CLU_014689_7_0_9; -.
DR   OrthoDB; 9804590at2; -.
DR   Proteomes; UP000008456; Chromosome.
DR   GO; GO:0008173; F:RNA methyltransferase activity; IEA:InterPro.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   GO; GO:0034470; P:ncRNA processing; IEA:UniProt.
DR   GO; GO:0009451; P:RNA modification; IEA:UniProt.
DR   CDD; cd02440; AdoMet_MTases; 1.
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; 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   NCBIfam; TIGR00479; rumA; 1.
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.
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:UP000008456};
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..63
FT                   /note="TRAM"
FT                   /evidence="ECO:0000259|PROSITE:PS50926"
FT   ACT_SITE        412
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10015"
FT   ACT_SITE        412
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         287
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         316
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         337
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         385
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
SQ   SEQUENCE   460 AA;  52512 MW;  50ED810CD4A3A2BE CRC64;
     MKEYPINKND KITVEIIDLT HEGLGIAKID HYPIFIENSL PGEIVDILIV KVGNKFAFGK
     VIEWQKISPE RRDLKNYVLL QTGIAPLQHM SYGEQLLFKQ KQVKNVMKKI AKLPDTPVLP
     TIGMAVPKGY RNKAQIPARK VDNQLETGFF RKNSHELIPI QDFYIQDPKI DQAILVIRDI
     LRRFQVKPYN EQEHTGNLRQ IIIRRGHYSH EMMVILVTRT KKLFNHEQLV KEIMQKLPET
     ISIIQNINPD KTNVIMGEES ILLYGNPYIN DQLLGKNYHI SAASFYQVNT EQTEYLYKTA
     IEFAGLSPTD QVVDAYCGIG TIALSLAEQV KHVYGVEIIE AAILDARENA AINQIENCTF
     NIGKAEEVMI DWQKAGISPN IIFVDPPRKG LTESFIETCT EMDPNRIIYI SCNPATLARD
     LKLFAELGYE TRKIQPVDLF PQTYHVETVA LLQKIDHLSG
//
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