ID A0A0R2IM81_9LACO Unreviewed; 456 AA.
AC A0A0R2IM81;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=RNA methyltransferase, TrmA family protein {ECO:0000313|EMBL:KRN66043.1};
GN ORFNames=IV80_GL001602 {ECO:0000313|EMBL:KRN66043.1};
OS Pediococcus cellicola.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Pediococcus.
OX NCBI_TaxID=319652 {ECO:0000313|EMBL:KRN66043.1, ECO:0000313|Proteomes:UP000051568};
RN [1] {ECO:0000313|EMBL:KRN66043.1, ECO:0000313|Proteomes:UP000051568}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17757 {ECO:0000313|EMBL:KRN66043.1,
RC ECO:0000313|Proteomes:UP000051568};
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:KRN66043.1}.
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DR EMBL; JQBR01000006; KRN66043.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0R2IM81; -.
DR STRING; 319652.IV80_GL001602; -.
DR PATRIC; fig|319652.3.peg.1623; -.
DR OrthoDB; 9804590at2; -.
DR Proteomes; UP000051568; 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}; Reference proteome {ECO:0000313|Proteomes:UP000051568};
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 6..64
FT /note="TRAM"
FT /evidence="ECO:0000259|PROSITE:PS50926"
FT ACT_SITE 412
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10015"
FT ACT_SITE 412
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 287
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 316
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 337
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 385
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
SQ SEQUENCE 456 AA; 51601 MW; 4F84C315147E2BCC CRC64;
MKFKAPVTKN ETYDVTIMDL TYQGMGVAKI DNFPIFVANS LPGEEITMKV TKVAKTYAFG
RVQTWKSKSP DRVEIKDKQY TQTGITPLQH LAYPAQLEFK QHQIQELFYK AHLDEVEVSP
TVGMEKPYGY RNKAQIPVRS VNGQLTTGFY RRNSHDLVPI EDFYIQDPEI DKAILVVRDI
LRQYHTAPYN ETNHTGVIKT IMVRRGHFTH EMMIVLITRA KKIPMNFEIV EEIRKQLPEV
KSIIQNVNAA QTNVLLGKEE KILWGSNVIH DELLGLRFAI SADSFYQVNP VQTDKLYDLA
IQKAGLTGKE TVIDAYCGIG TISLAMAKHA KKVYGVEIVD KAIQDAKINA KLNDIRNVRF
TVGKAEEKMA DWQHDGLKPD VIVVDPPRKG LAPEFITAAA EMAPKRVVYV SCNPATLVRD
VQTFMDNGYH VAQPVIPLDQ FPQTPHVESV TVLEHK
//