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Database: UniProt
Entry: W0EQY0_9BACT
LinkDB: W0EQY0_9BACT
Original site: W0EQY0_9BACT 
ID   W0EQY0_9BACT            Unreviewed;       476 AA.
AC   W0EQY0;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   27-MAR-2024, entry version 42.
DE   SubName: Full=RNA methyltransferase {ECO:0000313|EMBL:AHF11526.1};
GN   ORFNames=BARVI_00165 {ECO:0000313|EMBL:AHF11526.1};
OS   Barnesiella viscericola DSM 18177.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Barnesiellaceae;
OC   Barnesiella.
OX   NCBI_TaxID=880074 {ECO:0000313|EMBL:AHF11526.1, ECO:0000313|Proteomes:UP000018901};
RN   [1] {ECO:0000313|EMBL:AHF11526.1, ECO:0000313|Proteomes:UP000018901}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 18177 {ECO:0000313|Proteomes:UP000018901};
RG   DOE Joint Genome Institute;
RA   Eisen J., Huntemann M., Han J., Chen A., Kyrpides N., Mavromatis K.,
RA   Markowitz V., Palaniappan K., Ivanova N., Schaumberg A., Pati A.,
RA   Liolios K., Nordberg H.P., Cantor M.N., Hua S.X., Woyke T.;
RL   Submitted (DEC-2013) 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}.
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DR   EMBL; CP007034; AHF11526.1; -; Genomic_DNA.
DR   RefSeq; WP_025277266.1; NZ_CP007034.1.
DR   AlphaFoldDB; W0EQY0; -.
DR   STRING; 880074.BARVI_00165; -.
DR   KEGG; bvs:BARVI_00165; -.
DR   PATRIC; fig|880074.11.peg.35; -.
DR   eggNOG; COG2265; Bacteria.
DR   HOGENOM; CLU_014689_7_2_10; -.
DR   OrthoDB; 9804590at2; -.
DR   Proteomes; UP000018901; 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          5..63
FT                   /note="TRAM"
FT                   /evidence="ECO:0000259|PROSITE:PS50926"
FT   ACT_SITE        427
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10015"
FT   ACT_SITE        427
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         301
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         330
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         351
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         400
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
SQ   SEQUENCE   476 AA;  55054 MW;  855C8EE1201EA3A2 CRC64;
     MARKKKELPL LEQIEITGVA AEGKALARVN DLVVFVPFAA PGDIVDLQVT RKKHSYAEAR
     IVKFHAYSPL RVQPFCEHFG VCGGCKWQHV TYDFQLQFKR QQVEDNLTRI GKIPLPEVLP
     TKGSAKQRFY RNKLEYSFSN RSWLTYEQLQ SAQEFDCRNA LGFHIPGMFD KVLDIKKCWL
     QDDISNRIRL SIRQFAIDHD YPFFDLKEQT GLMRNMIVRT ASTGEIMLIV VFFEPDMERI
     EALMQHIADE FPQITSLLYI INQKHNDTIT DQEVHLYRGR DYIWESMEGL RFKIGPKSFY
     QTNSEQAYEL YKVAREFASL TGDELVYDLY TGTGTIANFV ARQSRKVIGI EYVPEAIEDA
     KENARINGLD NTLFYAGDMK DILTEEFIGE HGRPDVIITD PPRAGMHDDV IKTILFAEPR
     RIVYVSCNPA TQARDLSLLD VKYRVERVQP VDMFPHTHHV ENVVLLMRKE EEPAEA
//
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