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Database: UniProt
Entry: A0A0P6S3M4_9STRE
LinkDB: A0A0P6S3M4_9STRE
Original site: A0A0P6S3M4_9STRE 
ID   A0A0P6S3M4_9STRE        Unreviewed;       451 AA.
AC   A0A0P6S3M4;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   SubName: Full=RNA methyltransferase {ECO:0000313|EMBL:KPJ22713.1};
GN   ORFNames=AKK44_03440 {ECO:0000313|EMBL:KPJ22713.1};
OS   Streptococcus phocae.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=119224 {ECO:0000313|EMBL:KPJ22713.1, ECO:0000313|Proteomes:UP000049578};
RN   [1] {ECO:0000313|EMBL:KPJ22713.1, ECO:0000313|Proteomes:UP000049578}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51973 {ECO:0000313|EMBL:KPJ22713.1,
RC   ECO:0000313|Proteomes:UP000049578};
RA   Avendano-Herrera R.;
RT   "Genome sequence of Streptococcus phocae subsp. phocae ATCC 51973T isolated
RT   from liver specimen obtained from seal.";
RL   Submitted (AUG-2015) 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:KPJ22713.1}.
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DR   EMBL; LHQM01000010; KPJ22713.1; -; Genomic_DNA.
DR   RefSeq; WP_054278523.1; NZ_LHQM01000010.1.
DR   AlphaFoldDB; A0A0P6S3M4; -.
DR   STRING; 119224.AKK44_03440; -.
DR   PATRIC; fig|119224.3.peg.214; -.
DR   Proteomes; UP000049578; 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: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};
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..59
FT                   /note="TRAM"
FT                   /evidence="ECO:0000259|PROSITE:PS50926"
FT   ACT_SITE        408
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10015"
FT   ACT_SITE        408
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         283
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         312
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         333
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         381
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
SQ   SEQUENCE   451 AA;  50917 MW;  00A05F23BDA300B3 CRC64;
     MLTKNDIVEV MISDLSHDGS GVAKNDGFVF FVENALPGEV IQMRVLKVNK NSGFGKVEAY
     LTKSPSRHEG IDTAYLRTGI ADFGHLIYPE QLQFKKKQVQ DNLYKTAGIS DIEVMDTVGM
     EHPYAYRNKA QVPVRRVNGQ LETGFFRKNT HDLLPISDFY IQDKEIDRLV NFLRDLFRRF
     EVKPYDEKEQ TGLIRNIVVR KGHYSGEIML VLVTNRPKVF RVDQVIAKIT EAFPNIVSVI
     QNINDQNTNA IFGKTFKTLY GRDTITDTML GNQYEISAQS FYQVNTVMAE KLYQTAIDFS
     DLSKNDVVID AYSGIGTIGL SFAKEVKKVY GVELLERAVQ DAQKNAAING ITNVHFVTDS
     AENAMEKWRK EGIKPSVIIV DPPRKGLTES FIKASVAMNP DKITYISCNP ATMARDIKSY
     QDLGYALKKV QPFDLFPQTH HVECVALLVK A
//
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