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Database: UniProt
Entry: D5AGU1_STRGZ
LinkDB: D5AGU1_STRGZ
Original site: D5AGU1_STRGZ 
ID   D5AGU1_STRGZ            Unreviewed;       452 AA.
AC   D5AGU1;
DT   15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT   15-JUN-2010, sequence version 1.
DT   27-MAR-2024, entry version 62.
DE   SubName: Full=tRNA (Uracil-5-)-methyltransferase/TrmA {ECO:0000313|EMBL:ADE31056.1};
GN   OrderedLocusNames=SSGZ1_0596 {ECO:0000313|EMBL:ADE31056.1};
OS   Streptococcus suis (strain GZ1).
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=423211 {ECO:0000313|EMBL:ADE31056.1, ECO:0000313|Proteomes:UP000002359};
RN   [1] {ECO:0000313|EMBL:ADE31056.1, ECO:0000313|Proteomes:UP000002359}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GZ1 {ECO:0000313|EMBL:ADE31056.1,
RC   ECO:0000313|Proteomes:UP000002359};
RX   PubMed=19016627; DOI=10.1086/594370;
RA   Ye C., Zheng H., Zhang J., Jing H., Wang L., Xiong Y., Wang W., Zhou Z.,
RA   Sun Q., Luo X., Du H., Gottschalk M., Xu J.;
RT   "Clinical, experimental, and genomic differences between intermediately
RT   pathogenic, highly pathogenic, and epidemic Streptococcus suis.";
RL   J. Infect. Dis. 199:97-107(2009).
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; CP000837; ADE31056.1; -; Genomic_DNA.
DR   RefSeq; WP_011922145.1; NC_017617.1.
DR   AlphaFoldDB; D5AGU1; -.
DR   GeneID; 8153961; -.
DR   KEGG; ssw:SSGZ1_0596; -.
DR   PATRIC; fig|423211.3.peg.583; -.
DR   HOGENOM; CLU_014689_7_0_9; -.
DR   Proteomes; UP000002359; 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   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; 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.
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   452 AA;  50730 MW;  EC4BDAA7D3B3A484 CRC64;
     MLKKNDIVEV EVVDLTHEGQ GVAKIDGFVF FVDNALPGEK ISMRILKLKK NIGFGKVEQW
     QSFSQDRNQD LDFTYLRTGI ADLGHLTYPA QLAFKKKQVE NSLRKIAGIS EIAVADTLGM
     DSPLAYRNKA AVPVRRVNGQ LETGFFRKNS HDLVPIEDFY IQHKEIDALV LATRDLLRKL
     DLKPYDEKEQ TGLVRNIVVR RGHYSGQLML VLVTTRPKIF RVETLIERLT SQFPNLVSIV
     QNINDQNTNA IFGQEFRLLH GSETIADTML GNEFEISAPS FYQVNTEMAE KLYQTAIDFA
     ELSADDVVID AYSGIGTIGL SFAKQVKHVY GVEVVEKAVL DSQKNAARNG IDNVTYVCDS
     AESAMQKWVA DGVKPTVIFV DPPRKGLTES FIKASTSVKP EKIVYISCNV ATMARDIKLY
     EELGYKLTKV QPADLFPNTH HIEVVGLLEK RN
//
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