ID Y1394_BIFLO Reviewed; 435 AA.
AC Q8G4I8;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 27-MAR-2024, entry version 91.
DE RecName: Full=Uncharacterized RNA methyltransferase BL1394;
DE EC=2.1.1.-;
GN OrderedLocusNames=BL1394;
OS Bifidobacterium longum (strain NCC 2705).
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=206672;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCC 2705;
RX PubMed=12381787; DOI=10.1073/pnas.212527599;
RA Schell M.A., Karmirantzou M., Snel B., Vilanova D., Berger B., Pessi G.,
RA Zwahlen M.-C., Desiere F., Bork P., Delley M., Pridmore R.D., Arigoni F.;
RT "The genome sequence of Bifidobacterium longum reflects its adaptation to
RT the human gastrointestinal tract.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:14422-14427(2002).
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. RNA M5U methyltransferase family. {ECO:0000255|PROSITE-
CC ProRule:PRU01024}.
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DR EMBL; AE014295; AAN25193.1; -; Genomic_DNA.
DR RefSeq; NP_696557.1; NC_004307.2.
DR AlphaFoldDB; Q8G4I8; -.
DR SMR; Q8G4I8; -.
DR STRING; 206672.BL1394; -.
DR EnsemblBacteria; AAN25193; AAN25193; BL1394.
DR KEGG; blo:BL1394; -.
DR PATRIC; fig|206672.9.peg.252; -.
DR HOGENOM; CLU_014689_7_0_11; -.
DR OrthoDB; 9804590at2; -.
DR PhylomeDB; Q8G4I8; -.
DR Proteomes; UP000000439; Chromosome.
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; 2.40.50.140; 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 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; PS01230; TRMA_1; 1.
PE 3: Inferred from homology;
KW Methyltransferase; Reference proteome; S-adenosyl-L-methionine;
KW Transferase.
FT CHAIN 1..435
FT /note="Uncharacterized RNA methyltransferase BL1394"
FT /id="PRO_0000161958"
FT ACT_SITE 393
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01024"
FT BINDING 261
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01024"
FT BINDING 294
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01024"
FT BINDING 318
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01024"
FT BINDING 366
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01024"
SQ SEQUENCE 435 AA; 47590 MW; CE5FA186886C2663 CRC64;
MPNSNRAQPE RTMMQAEVRI ERYADQGRCV AHIDGRVVFV RFALPDELVR VELDEPHDRD
DRFWTGEVVE VLEPSEDRVT PAWPLAGPLA MGGGVGGADL VHVSLPGQLK WKAITVSEQM
SRLGHIDVAV PIERMPGDKA AGGLNWRTRI EMIADDNGMP SMRRRGTHNR VAIDTMPLAT
RTLLDVAKRE HVWEGGFEPG SQIRLSVPEP RGEIVDTAAA DDNYAVLVDG ELRAGSQLLT
EQVTINGTTF DYQVDANGFW QVHRQAPIAL GTHVINLVNG QLQSAADAVI WDLYSGSGLF
TLPLATMTGE RTRMLSVEGA RVAVKNAQRN LRAMNLNDVD ARAGDVSRTL DHVPAHLAKP
NVVVLDPPRA GARAKVCRQI AAAGASSVVY IACDPTSLAR DTATLIGEGY ELKDIRAFDI
YPMTHHVETV ALFTR
//
