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
//