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Database: UniProt
Entry: A0A0A2DUJ5_9PORP
LinkDB: A0A0A2DUJ5_9PORP
Original site: A0A0A2DUJ5_9PORP 
ID   A0A0A2DUJ5_9PORP        Unreviewed;       476 AA.
AC   A0A0A2DUJ5;
DT   04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT   04-FEB-2015, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   SubName: Full=RNA methyltransferase {ECO:0000313|EMBL:KGN67909.1};
GN   ORFNames=JT26_08270 {ECO:0000313|EMBL:KGN67909.1};
OS   Porphyromonas sp. COT-108 OH1349.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Porphyromonadaceae;
OC   Porphyromonas.
OX   NCBI_TaxID=1537504 {ECO:0000313|EMBL:KGN67909.1, ECO:0000313|Proteomes:UP000030126};
RN   [1] {ECO:0000313|EMBL:KGN67909.1, ECO:0000313|Proteomes:UP000030126}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=COT-108 OH1349 {ECO:0000313|Proteomes:UP000030126};
RA   Wallis C., Deusch O., O'Flynn C., Davis I., Jospin G., Darling A.E.,
RA   Coil D.A., Alexiev A., Horsfall A., Kirkwood N., Harris S., Eisen J.A.;
RT   "Porphyromonas sp. COT-108_OH1349 Genome sequencing.";
RL   Submitted (AUG-2014) 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}.
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:KGN67909.1}.
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DR   EMBL; JRAH01000031; KGN67909.1; -; Genomic_DNA.
DR   RefSeq; WP_036848429.1; NZ_JRAH01000031.1.
DR   AlphaFoldDB; A0A0A2DUJ5; -.
DR   OrthoDB; 9804590at2; -.
DR   Proteomes; UP000030126; 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:UP000030126};
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..65
FT                   /note="TRAM"
FT                   /evidence="ECO:0000259|PROSITE:PS50926"
FT   ACT_SITE        434
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10015"
FT   ACT_SITE        434
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         308
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         358
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         407
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
SQ   SEQUENCE   476 AA;  54772 MW;  0483FA4B99E1E265 CRC64;
     MSRKRQKERK ILEAVRIEEM AAEGKSLARL ENGKVLFVPF TAPGDLVDVQ LGRSRSSFAE
     GRVVKMLEPS PHRVEPRCRH FGTCGGCKWQ HVPYTMQLAM KERQVYDQLE RIGKIELKDR
     RSILGSKEIF EYRNKMEYTF SNKRWVTAEE MQEIGDGDVG CRAGLGFHIP GMFDKVLNIE
     ECHLQIDLSN RIRLFVRDFC LARPGQYPFF DLKEQVGYMR NLVIRTSSTG EVMVLVIFHE
     EDEEKSRTLL DAILERFGNE ITTLLYIVNP KRNDTYNDLD VVTYYGPGFI MEAMEELRFK
     VGPKSFYQTN SKQAYELYSQ VREMAGIQPH EVVYDLYTGT GTIACFLSKS ASKIVGIEYV
     EDAVIDARHN AEDNQLDNLT FFAGDMKDVL NDEFIRTHGK PDVIITDPPR AGMHQDVVET
     ILRAAPERIV YVSCNPATQA RDLAIMDSHY SVERVQPVDM FPHTHHVENI VLLHRR
//
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