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Database: UniProt
Entry: Q1JL90_STRPC
LinkDB: Q1JL90_STRPC
Original site: Q1JL90_STRPC 
ID   Q1JL90_STRPC            Unreviewed;       462 AA.
AC   Q1JL90;
DT   13-JUN-2006, integrated into UniProtKB/TrEMBL.
DT   13-JUN-2006, sequence version 1.
DT   27-MAR-2024, entry version 91.
DE   SubName: Full=23S rRNA m(5)U 1939 methyltransferase {ECO:0000313|EMBL:ABF32329.1};
DE            EC=2.1.1.- {ECO:0000313|EMBL:ABF32329.1};
GN   OrderedLocusNames=MGAS9429_Spy1142 {ECO:0000313|EMBL:ABF32329.1};
OS   Streptococcus pyogenes serotype M12 (strain MGAS9429).
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=370551 {ECO:0000313|EMBL:ABF32329.1, ECO:0000313|Proteomes:UP000002433};
RN   [1] {ECO:0000313|EMBL:ABF32329.1, ECO:0000313|Proteomes:UP000002433}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGAS9429 {ECO:0000313|EMBL:ABF32329.1,
RC   ECO:0000313|Proteomes:UP000002433};
RX   PubMed=16636287; DOI=10.1073/pnas.0510279103;
RA   Beres S.B., Richter E.W., Nagiec M.J., Sumby P., Porcella S.F., DeLeo F.R.,
RA   Musser J.M.;
RT   "Molecular genetic anatomy of inter- and intraserotype variation in the
RT   human bacterial pathogen group A Streptococcus.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:7059-7064(2006).
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; CP000259; ABF32329.1; -; Genomic_DNA.
DR   RefSeq; WP_011527669.1; NC_008021.1.
DR   AlphaFoldDB; Q1JL90; -.
DR   KEGG; spk:MGAS9429_Spy1142; -.
DR   HOGENOM; CLU_014689_7_0_9; -.
DR   Proteomes; UP000002433; 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};
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          12..70
FT                   /note="TRAM"
FT                   /evidence="ECO:0000259|PROSITE:PS50926"
FT   ACT_SITE        419
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10015"
FT   ACT_SITE        419
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         294
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         323
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         344
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         392
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
SQ   SEQUENCE   462 AA;  51813 MW;  8B8D72BE1E466F20 CRC64;
     MVSPRKGKRI RMLKKNDIIQ VAISDLSHEG AGVAKHDGFV FFVDNALPEE VIDMRVLKVN
     KNSGFGKVEA YHYLSPARNA DVNLTYLRTG IADLGHLTYE DQLTFKKKQV QDSLYKIAGI
     SDVTVESTIG MTEPLAYRNK AQVPVRRVNG QLETGFFRKH SHDLIPISDY YIQDKEIDRL
     INFTRDLLRR FDIKPYDETE QTGLLRNIVV RRGHYSGEMM LVLVTTRPKV FRVDQVIEKI
     VEAFPAVVSI IQNINDKNTN AIFGKDFKTL YGKDTITDSM LGNNYAISAQ SFYQVNTIMA
     EKLYQTAIAF SDLSKDDIVI DAYSGIGTIG LSFAKTVKAV YGVEVIEAAV RDAQQNAALN
     GITNAYFVAD TAEHAMATWA KDGIKPSVIL VDPPRKGLTE SFIQASVAMG PQKIIYISCN
     PATMARDIKR YQELGYKLTK VQPVDLFPQT HHVECVVLLI KE
//
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