ID A0A249KPI9_9ACTN Unreviewed; 404 AA.
AC A0A249KPI9;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=Methyltransferase {ECO:0000313|EMBL:ASY18694.1};
GN ORFNames=A1sIA105_03980 {ECO:0000313|EMBL:ASY18694.1};
OS Candidatus Planktophila versatilis.
OC Bacteria; Actinomycetota; Actinomycetes; Candidatus Nanopelagicales;
OC Candidatus Nanopelagicaceae; Planktophila.
OX NCBI_TaxID=1884905 {ECO:0000313|EMBL:ASY18694.1, ECO:0000313|Proteomes:UP000217175};
RN [1] {ECO:0000313|EMBL:ASY18694.1, ECO:0000313|Proteomes:UP000217175}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MMS-IA-105 {ECO:0000313|EMBL:ASY18694.1};
RA Neuenschwander S.M., Salcher M., Ghai R., Pernthaler J.;
RT "High microdiversification within the ubiquitous acI lineage of
RT Actinobacteria.";
RL Submitted (JUL-2016) 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}.
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DR EMBL; CP016775; ASY18694.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A249KPI9; -.
DR Proteomes; UP000217175; Chromosome.
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; 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};
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 8..66
FT /note="TRAM"
FT /evidence="ECO:0000259|PROSITE:PS50926"
FT ACT_SITE 358
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 236
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 265
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 289
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"
SQ SEQUENCE 404 AA; 43862 MW; 30BEB7460FF6F493 CRC64;
MSSPKKASIE VGARLRVEIE KVAHGGHFIA RHEGAVIFVR HAIPGESVEI EVTSVGASFN
RADVVEVITP SADRVTAPCR YAHRLGCGGC DFQHITPARQ RDLKSEVISE QFSRIAKMEI
DVEVEEVSAP LGWRTRCSAH STKSGALGFF QARSHKVTPV DDCRILVPEM KFAELAQRGV
KGDQRLEISI SNTGERTIAT ANSRDESPMR LSDGPEIAHY QVGDKVFNVS QKSFWQSHKD
APRVLSDVVV ELGQFQTGDH VLDLYGGVGL FAAAILPIIG EAGAVDIVEG SKAATADASS
NFADNSNVTV ITADVAKAIT RFTQANVIVL DPPREGAGKE VLQNCARIAP RVIIYVACDP
AALARDTGYL REFGYTLEKI RAFDLFPMTH HIECVARFVA DKVS
//
