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Database: UniProt
Entry: A0A0J0Y4S5_9SPHI
LinkDB: A0A0J0Y4S5_9SPHI
Original site: A0A0J0Y4S5_9SPHI 
ID   A0A0J0Y4S5_9SPHI        Unreviewed;       470 AA.
AC   A0A0J0Y4S5;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   SubName: Full=RNA methyltransferase {ECO:0000313|EMBL:KLT65230.1};
GN   ORFNames=AB669_16270 {ECO:0000313|EMBL:KLT65230.1};
OS   Pedobacter sp. BMA.
OC   Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC   Sphingobacteriaceae; Pedobacter.
OX   NCBI_TaxID=1663685 {ECO:0000313|EMBL:KLT65230.1, ECO:0000313|Proteomes:UP000036014};
RN   [1] {ECO:0000313|EMBL:KLT65230.1, ECO:0000313|Proteomes:UP000036014}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BMA {ECO:0000313|EMBL:KLT65230.1,
RC   ECO:0000313|Proteomes:UP000036014};
RA   Anderson B.M., Pipes S.E., Miller J.R., Newman J.D.;
RT   "Pedobacter sp. BMA.";
RL   Submitted (JUN-2015) 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:KLT65230.1}.
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DR   EMBL; LECU01000006; KLT65230.1; -; Genomic_DNA.
DR   RefSeq; WP_047800307.1; NZ_LECU01000006.1.
DR   AlphaFoldDB; A0A0J0Y4S5; -.
DR   STRING; 1663685.AB669_16270; -.
DR   PATRIC; fig|1663685.3.peg.3408; -.
DR   OrthoDB; 9804590at2; -.
DR   Proteomes; UP000036014; 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:UP000036014};
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        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   470 AA;  53399 MW;  F802D7ACF8CD80DF CRC64;
     MSRRKPGTVT VIPNVQIIDI AEEGKGVGKA DELVIFVDKA VPGDVVDVRL TKKKKNFAEA
     IIDQLHQKSE LRTDPFCPHF GTCGGCKWQH MGYDSQLKFK QKNVEAALQR LGKIDTSNTE
     PILGSAQDRY YRNKLEFTFS NKRWLDRTDI ERDEDFDMNA LGFHVPLRFD KILDIEHCYL
     QAEPSNSIRN AVRKYALENG LSFYDLRNHE GALRNLIIRT SSTGEVMVAV VFAYPEEDQV
     EGLMGFLKQA FPQITALLYI VNQKKNDTIF DQEVNLFAGR DHIFEEMDGI RFKIGVKSFY
     QTNSEQAFEL YKITRDFAGF KGDELVYDLY TGAGTIANFV AKSVKQVVGV EYVPTAIEDA
     KFNSQLNGID NTIFYAGDMK DILTEEFVLA HGRPDVVITD PPRAGMHADV VQRLLEMESD
     KIVYVSCNAA TQARDLELLK EKYDVVRIKP VDMFPHTQHV ENVVLLKLRG
//
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