ID A0A239C5G4_9ACTN Unreviewed; 450 AA.
AC A0A239C5G4;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=23S rRNA m(5)U-1939 methyltransferase {ECO:0000313|EMBL:SNS15132.1};
GN ORFNames=SAMN05216252_103367 {ECO:0000313|EMBL:SNS15132.1};
OS Actinacidiphila glaucinigra.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Actinacidiphila.
OX NCBI_TaxID=235986 {ECO:0000313|EMBL:SNS15132.1, ECO:0000313|Proteomes:UP000198280};
RN [1] {ECO:0000313|EMBL:SNS15132.1, ECO:0000313|Proteomes:UP000198280}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 4.1858 {ECO:0000313|EMBL:SNS15132.1,
RC ECO:0000313|Proteomes:UP000198280};
RA Kim H.J., Triplett B.A.;
RL Submitted (JUN-2017) 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; FZOF01000003; SNS15132.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A239C5G4; -.
DR OrthoDB; 9804590at2; -.
DR Proteomes; UP000198280; 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; 1.
DR InterPro; IPR025714; Methyltranfer_dom.
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; PF13847; Methyltransf_31; 1.
DR Pfam; PF01938; TRAM; 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:UP000198280};
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 11..77
FT /note="TRAM"
FT /evidence="ECO:0000259|PROSITE:PS50926"
FT ACT_SITE 403
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 279
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
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 332
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 376
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
SQ SEQUENCE 450 AA; 48419 MW; DE3B1C44E33E6FEC CRC64;
MQHRSKAPEA DALVGERYEV EVGPVAHGGH CIARTVLPGH DRPQVIFVRH ALPGERVVAE
ITEGGPDSRF LRADAVEVLE ASPDRVEAPC PFSGPGKCGG CDWQHAAPGA QRRLKVQVIT
EQLERLAHLT PEEAGWDGTV EPAPGDKVAK GEVPAWRTRV QYAVDSEGHA GLRRHRSHEV
ERVDRCLIAA PGVSELGVES RDWSGIASVE AIAATGSSDR QVILTPRPGA RLPIVELDRP
VSVLRVDEQG GIHRVHGRGF VRERAIDRTW RVGSGGFWQV HPMAAGLLVE AVMQGLMPRK
GETALDLYCG VGLFAGALAE RVGETGAVLG IESGKRAVED ARHNLGDFDR VRIEQGKVES
ALPRTGITEA DLVVLDPPRT GAGRATVEHV ASLGPRRIAY VACDPAALAR DLGYFAAAGY
APRRLRAFDL FPMTHHVECV AILEPATKDA
//