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Database: UniProt
Entry: A0A139NTY6_9STRE
LinkDB: A0A139NTY6_9STRE
Original site: A0A139NTY6_9STRE 
ID   A0A139NTY6_9STRE        Unreviewed;       435 AA.
AC   A0A139NTY6;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   SubName: Full=RNA methyltransferase, TrmA family {ECO:0000313|EMBL:KXT79347.1};
GN   ORFNames=STRDD13_00004 {ECO:0000313|EMBL:KXT79347.1};
OS   Streptococcus sp. DD13.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=1777881 {ECO:0000313|EMBL:KXT79347.1, ECO:0000313|Proteomes:UP000070387};
RN   [1] {ECO:0000313|EMBL:KXT79347.1, ECO:0000313|Proteomes:UP000070387}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DD13 {ECO:0000313|EMBL:KXT79347.1,
RC   ECO:0000313|Proteomes:UP000070387};
RA   Denapaite D., Rieger M., Koendgen S., Brueckner R., Ochigava I.,
RA   Kappeler P., Maetz-Rensing K., Leendertz F., Hakenbeck R.;
RT   "Highly variable Streptococcus oralis are common among viridans
RT   streptococci isolated from primates.";
RL   Submitted (JAN-2016) 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:KXT79347.1}.
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DR   EMBL; LQRH01000001; KXT79347.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A139NTY6; -.
DR   STRING; 1777881.STRDD13_00004; -.
DR   PATRIC; fig|1777881.3.peg.4; -.
DR   Proteomes; UP000070387; 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   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:SF45; -; 1.
DR   PANTHER; PTHR11061; RNA M5U 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:UP000070387};
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..45
FT                   /note="TRAM"
FT                   /evidence="ECO:0000259|PROSITE:PS50926"
FT   ACT_SITE        393
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10015"
FT   ACT_SITE        393
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         268
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         297
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         318
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         366
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
SQ   SEQUENCE   435 AA;  48777 MW;  EA3CE895BB0444B5 CRC64;
     MGINGEGIGF YKKTLVFVPG ALKGEEVFCQ VTAVQRNFVT ARLLTIQKKS KARVTPACAI
     YEECGGCQLM HLRYDKQLEF KDDLIRQALA KFKPEGYADY EIRPTLGMAH PLHYRAKLQF
     QTRTVGGSVQ AGLFAQGSHR LVSVKDCLVQ DDLTQKIVNR VVDLLDRYKI PIYNERKIAG
     VRTIMVRRAE KTDQVQLIIV TSKAVRLTGL VKDLTADFPQ IKTIAVNYNR SKSSEIYGEE
     TEILWGQDTI AEEVLDYRFA LSPRAFYQLN PQQTEALYSQ AVAALDVTAK DHLIDAYCGV
     GTIGFAFAGK VKSVRGMDII PEAISDAKKN ASAMGFENTY YETGKAEEII PRWYAEGYRA
     DALIVDPPRT GLDDQLLSTI LTYQPEKMVY VSCNTSTLAR DLVHLAKVYQ VVYIQSVDMF
     PHTARTEAVV KLVKK
//
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