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Database: UniProt
Entry: A0A090VEY5_9FLAO
LinkDB: A0A090VEY5_9FLAO
Original site: A0A090VEY5_9FLAO 
ID   A0A090VEY5_9FLAO        Unreviewed;       470 AA.
AC   A0A090VEY5;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   SubName: Full=RNA methyltransferase {ECO:0000313|EMBL:GAL61924.1};
GN   ORFNames=JCM19300_670 {ECO:0000313|EMBL:GAL61924.1};
OS   Algibacter lectus.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Algibacter.
OX   NCBI_TaxID=221126 {ECO:0000313|EMBL:GAL61924.1, ECO:0000313|Proteomes:UP000029644};
RN   [1] {ECO:0000313|EMBL:GAL61924.1, ECO:0000313|Proteomes:UP000029644}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 19300 {ECO:0000313|EMBL:GAL61924.1,
RC   ECO:0000313|Proteomes:UP000029644};
RA   Takatani N., Nakanishi M., Meirelles P., Mino S., Suda W., Oshima K.,
RA   Hattori M., Ohkuma M., Hosokawa M., Miyashita K., Thompson F.L., Niwa A.,
RA   Sawabe T., Sawabe T.;
RT   "Draft Genome Sequences of Marine Flavobacterium Algibacter lectus Strains
RT   SS8 and NR4.";
RL   Genome Announc. 2:e01168-14(2014).
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:GAL61924.1}.
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DR   EMBL; BBNQ01000004; GAL61924.1; -; Genomic_DNA.
DR   RefSeq; WP_042503820.1; NZ_BBNQ01000004.1.
DR   AlphaFoldDB; A0A090VEY5; -.
DR   OrthoDB; 9804590at2; -.
DR   Proteomes; UP000029644; 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:UP000029644};
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          3..64
FT                   /note="TRAM"
FT                   /evidence="ECO:0000259|PROSITE:PS50926"
FT   ACT_SITE        428
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10015"
FT   ACT_SITE        428
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         302
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         331
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         352
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         401
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
SQ   SEQUENCE   470 AA;  53457 MW;  F5769554C8578AC1 CRC64;
     MSRRKTRKQV FENVEVIDAG AKGKTIAKAP DGKVIFLPNA VPGDVVDVQT FKKRKAYYEG
     KATVFHKLSD KRTTPACEHF GTCGGCKWQD MAYEHQLFYK QKEVTNNLTR IGHIELPEVT
     PIFGAENQYF YRNKMEFSFS DSRWLTLEEV QSDEDLGDRN ALGFHIPGMW DKILDVKKCH
     LQADPSNAIR NAVKAFALEN DLEFFNTRNQ TGLLRTMMIR TSSTGDIMVM IQFFKEDKEK
     RELILDYLGE TFPEITSLQY VINGKANDTI YDQEVICYKG NDHIFEEMEG LKFKINAKSF
     YQTNSEQAYE LYKITRDFAG LTGNELVYDL YTGTGTIAQF VAKQAKKVVG VEAVPDAITA
     AKENAQFNNI NNVEFFVGDM KNVFNADFIE ANGTPDIIIT DPPRDGMHKD VVQQILNIAP
     AKVVYVSCNS ATQARDLALM DEQYKVVKTQ AVDMFPQTFH VENVVLLEKR
//
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