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Database: UniProt
Entry: A0A099XYT5_9FLAO
LinkDB: A0A099XYT5_9FLAO
Original site: A0A099XYT5_9FLAO 
ID   A0A099XYT5_9FLAO        Unreviewed;       484 AA.
AC   A0A099XYT5;
DT   07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT   07-JAN-2015, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   SubName: Full=RNA methyltransferase, TrmA family {ECO:0000313|EMBL:KGL63174.1};
GN   ORFNames=PHEL85_0207 {ECO:0000313|EMBL:KGL63174.1};
OS   Polaribacter sp. Hel1_85.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae.
OX   NCBI_TaxID=1250005 {ECO:0000313|EMBL:KGL63174.1, ECO:0000313|Proteomes:UP000029991};
RN   [1] {ECO:0000313|EMBL:KGL63174.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Hel1_85 {ECO:0000313|EMBL:KGL63174.1};
RA   Xing P., Hahnke R.L., Unfried F., Markert S., Huang S., Barbeyron T.,
RA   Harder J., Becher D., Schweder T., Gloenk F.O., Amann R.I., Teeling H.;
RT   "Niches of two polysaccharide-degrading Polaribacter strains isolated from
RT   the North Sea during a spring diatom bloom.";
RL   ISME J. 0:0-0(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:KGL63174.1}.
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DR   EMBL; JPDS01000001; KGL63174.1; -; Genomic_DNA.
DR   RefSeq; WP_036819917.1; NZ_JPDS01000001.1.
DR   AlphaFoldDB; A0A099XYT5; -.
DR   STRING; 1250005.PHEL85_0207; -.
DR   eggNOG; COG2265; Bacteria.
DR   OrthoDB; 9804590at2; -.
DR   Proteomes; UP000029991; 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};
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          9..71
FT                   /note="TRAM"
FT                   /evidence="ECO:0000259|PROSITE:PS50926"
FT   ACT_SITE        441
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10015"
FT   ACT_SITE        441
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         310
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         343
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         366
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         414
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
SQ   SEQUENCE   484 AA;  54972 MW;  D66638A936E9C688 CRC64;
     MPRRERNKFV KKNQVLELKI EDYAFGGKGI ARIHSEEGSF VVFVPNTLPG QLVKAQISKS
     SKKYAEAKLI DVLEPSDDEV EVTFQDIPGA PYIQLPINLQ HQYKKESTLS LFKRIGKVEN
     IEDLFDEFIA SPNVFHYRNK MEYGFSAIGY DRVNKTDKDE FTLGFKRRGV WWIGDNLEKD
     SGLFDKQMED NLKNIRKYCQ DTGLEPWHGP RKTGFFRYFV VRKSFKTDEL LCNLVTTSPE
     LENFDLNKFA SFLKDIFGER LAGLLHTIND ETGDRTIATA GSLDLVYGKD KIVEELLGLN
     FEISMKSFFQ TNPKCAEKLY SKVVEYVLED KTKVNNTVVM DLFCGTGTIG QIVASRSENA
     KIVGVDIVAS AIEDAKKNAK RNNIDGLKFF AADVGKFLIA HPEYKNKIKT IILDPARAGI
     APKTLQKIIN LNADRMVYVS CNPATQARDT ELLREAGYQI KKISLVDQFP HTSHIETVVL
     FEKI
//
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