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Database: UniProt
Entry: A0A3N1G8W2_9ACTN
LinkDB: A0A3N1G8W2_9ACTN
Original site: A0A3N1G8W2_9ACTN 
ID   A0A3N1G8W2_9ACTN        Unreviewed;       454 AA.
AC   A0A3N1G8W2;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   SubName: Full=tRNA/tmRNA/rRNA uracil-C5-methylase (TrmA/RlmC/RlmD family) {ECO:0000313|EMBL:ROP26672.1};
GN   ORFNames=EDC03_3309 {ECO:0000313|EMBL:ROP26672.1};
OS   Pseudokineococcus lusitanus.
OC   Bacteria; Actinomycetota; Actinomycetes; Kineosporiales; Kineosporiaceae;
OC   Pseudokineococcus.
OX   NCBI_TaxID=763993 {ECO:0000313|EMBL:ROP26672.1, ECO:0000313|Proteomes:UP000276232};
RN   [1] {ECO:0000313|EMBL:ROP26672.1, ECO:0000313|Proteomes:UP000276232}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CECT 7306 {ECO:0000313|EMBL:ROP26672.1,
RC   ECO:0000313|Proteomes:UP000276232};
RX   PubMed=26203337; DOI=.1186/s40793-015-0017-x;
RA   Whitman W.B., Woyke T., Klenk H.P., Zhou Y., Lilburn T.G., Beck B.J.,
RA   De Vos P., Vandamme P., Eisen J.A., Garrity G., Hugenholtz P.,
RA   Kyrpides N.C.;
RT   "Genomic Encyclopedia of Bacterial and Archaeal Type Strains, Phase III:
RT   the genomes of soil and plant-associated and newly described type
RT   strains.";
RL   Stand. Genomic Sci. 10:26-26(2015).
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:ROP26672.1}.
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DR   EMBL; RJKN01000011; ROP26672.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3N1G8W2; -.
DR   InParanoid; A0A3N1G8W2; -.
DR   OrthoDB; 9804590at2; -.
DR   Proteomes; UP000276232; 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:0006396; P:RNA processing; IEA:InterPro.
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; 2.
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   PANTHER; PTHR11061; RNA M5U METHYLTRANSFERASE; 1.
DR   PANTHER; PTHR11061:SF30; TRNA (URACIL(54)-C(5))-METHYLTRANSFERASE; 1.
DR   Pfam; PF01135; PCMT; 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; 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:UP000276232};
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          10..70
FT                   /note="TRAM"
FT                   /evidence="ECO:0000259|PROSITE:PS50926"
FT   REGION          219..256
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        411
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         281
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
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         334
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         384
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
SQ   SEQUENCE   454 AA;  47684 MW;  CA7A440CC6D39E15 CRC64;
     MSDDATAPGE GARGRLVELE VGAVAHGGHC VARLEGRVVF VRHTLPGERV VARLTEAADG
     AGFWRADAVE VLEASPDRVA PACPVAGPGG CGGCDWQHVD LAAQRRLKAD VLREQMHRLA
     GLDVDARVEE VPVPAAAGTT PEDAARGLGW RTRVAYAVDA GGRLGFRAHR EHRVVPVERC
     PIATPGVVDL GLPAVRWPGW RSVEAVVPGT GDDALVVAEP RPGARRPPRV PDVPAATSVA
     TTSPRGPRQP PGPVSRVRGR TWVREEVRGS GFRVTGAGFW QVHPGAGEAL TAAVLEALAP
     RPGEAALDLY SGAGLLTRAL ATAVGERGRV TAVEGDARAV ADARRNLHDV AGLTLVHGPV
     ERVLEERAGL EADGEPRADV VVLDPPRTGA RARVVAAVAA LRPRAVAYVA CDPAALARDV
     ATFADHGYVL RGLRAFDLFP QTHHLESVAL LEPR
//
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