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Database: UniProt
Entry: A0A0R2EZ03_9LACO
LinkDB: A0A0R2EZ03_9LACO
Original site: A0A0R2EZ03_9LACO 
ID   A0A0R2EZ03_9LACO        Unreviewed;       482 AA.
AC   A0A0R2EZ03;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   SubName: Full=tRNA (Uracil-5-)-methyltransferase related enzyme {ECO:0000313|EMBL:KRN21219.1};
GN   ORFNames=FD14_GL001352 {ECO:0000313|EMBL:KRN21219.1};
OS   Secundilactobacillus similis DSM 23365 = JCM 2765.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Secundilactobacillus.
OX   NCBI_TaxID=1423804 {ECO:0000313|EMBL:KRN21219.1, ECO:0000313|Proteomes:UP000051442};
RN   [1] {ECO:0000313|EMBL:KRN21219.1, ECO:0000313|Proteomes:UP000051442}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 23365 {ECO:0000313|EMBL:KRN21219.1,
RC   ECO:0000313|Proteomes:UP000051442};
RX   PubMed=26415554; DOI=10.1038/ncomms9322;
RA   Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X.,
RA   Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E.,
RA   Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., Ritari J.,
RA   Douillard F.P., Paul Ross R., Yang R., Briner A.E., Felis G.E.,
RA   de Vos W.M., Barrangou R., Klaenhammer T.R., Caufield P.W., Cui Y.,
RA   Zhang H., O'Toole P.W.;
RT   "Expanding the biotechnology potential of lactobacilli through comparative
RT   genomics of 213 strains and associated genera.";
RL   Nat. Commun. 6:8322-8322(2015).
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:KRN21219.1}.
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DR   EMBL; AYZM01000125; KRN21219.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0R2EZ03; -.
DR   STRING; 1423804.FD14_GL001352; -.
DR   PATRIC; fig|1423804.4.peg.1451; -.
DR   Proteomes; UP000051442; 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: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: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.
PE   3: Inferred from homology;
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|PROSITE-
KW   ProRule:PRU01024}; Reference proteome {ECO:0000313|Proteomes:UP000051442};
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          30..88
FT                   /note="TRAM"
FT                   /evidence="ECO:0000259|PROSITE:PS50926"
FT   REGION          1..30
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        440
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10015"
FT   ACT_SITE        440
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         315
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         365
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         413
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
SQ   SEQUENCE   482 AA;  54232 MW;  2C6622EE4D031899 CRC64;
     MKTTQTNQYH SRNNSQNHRP NQRRQQQDVQ VEMGQRFPLT IKRLGINGEG IGYFKRKLVF
     VQGALPNEVV VAEVTGIKPN FLTAKVHRLK TPSPDRVTPR DAYAGEVGGF ELEHLAYPAQ
     LEFKRDVVRQ SLEKYQPKGF RNYLLKPTIG MTDPYGYRNK AQFQIRRATD GHVMAGLYQE
     RSHKLVDLET CSVQMPATMA VMRTVVNLLE ELDVSIYNEK KHSGLVRTVV VRVAAGTDEV
     QVVFVTNGTN FPQQADMIDR LQTAHPEVVS IMQNVNSERT SLIWGDDTYL LAGKPQIREV
     LNDLQFNLSA RAFLQLNPYQ TVTLYAEALK ALDLSPDENV VDAYSGVGTI GLSMAHAAKE
     VRGMDVIDDA VKDARENAAL NDITNATYET GTAETLLPKW LDEGFELDAL VVDPPRTGLD
     DQLIRAILAS KPKKFVYISC NPSTLARDLV KLTRQYRVDY IQSVDMMPQT ARCEAVVKFT
     RI
//
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