ID A0A249LEU6_9ACTN Unreviewed; 409 AA.
AC A0A249LEU6;
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:ASY27583.1};
GN ORFNames=PHILAsVB114_02760 {ECO:0000313|EMBL:ASY27583.1};
OS Candidatus Planktophila limnetica.
OC Bacteria; Actinomycetota; Actinomycetes; Candidatus Nanopelagicales;
OC Candidatus Nanopelagicaceae; Planktophila.
OX NCBI_TaxID=573600 {ECO:0000313|EMBL:ASY27583.1, ECO:0000313|Proteomes:UP000217221};
RN [1] {ECO:0000313|EMBL:ASY27583.1, ECO:0000313|Proteomes:UP000217221}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MMS-VB-114 {ECO:0000313|EMBL:ASY27583.1};
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; CP016782; ASY27583.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A249LEU6; -.
DR KEGG; plim:PHILAsVB114_02760; -.
DR OrthoDB; 9804590at2; -.
DR Proteomes; UP000217221; 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}; Reference proteome {ECO:0000313|Proteomes:UP000217221};
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..71
FT /note="TRAM"
FT /evidence="ECO:0000259|PROSITE:PS50926"
FT ACT_SITE 363
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 241
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 270
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 294
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 336
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
SQ SEQUENCE 409 AA; 44473 MW; AE616436CD463ABE CRC64;
MESKAQISLQ VGQRLTVDIE KIAHGGHFIA RHESESGKKA VIFVRHAIPG EKVEIEITST
SSNFIRADVV QVITPSPDRV VAPCKFAHRD GCGGCDFQHI SASRQRTLKS EVITEQFARI
AKIPMTVEVE EVDQPLHWRT RVTATTDHNG AIGFYSSRSH RVISVDECLI AVPEIGIKEM
SKQKLSPDVR IEIAYSSEGE RMVAEAPKSG DGKFRQNSGP AVLHEKIGDR LLQVSQRSFW
QGHKRAPEIL AAVVSDFAEI KNGDLVLDLY GGVGLFTASS LNAVGSQGSI HLVEGSKDAT
SDAKNNFAGQ SNVQITTGDV AKIITRIQSA DVVILDPPRE GAGKDVVQQL ARIGARGIVY
VACDPAALAR DTVYLAESGY SMRKIRAFDL FPMTHHIESV ALFTPSKVS
//
