ID A0A1V1ZFD3_9FLAO Unreviewed; 470 AA.
AC A0A1V1ZFD3;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=23S rRNA (Uracil-5-)-methyltransferase RumA {ECO:0000313|EMBL:OMP30835.1};
GN ORFNames=BKM32_11460 {ECO:0000313|EMBL:OMP30835.1};
OS Mangrovimonas sp. DI 80.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Mangrovimonas.
OX NCBI_TaxID=1779330 {ECO:0000313|EMBL:OMP30835.1, ECO:0000313|Proteomes:UP000188854};
RN [1] {ECO:0000313|EMBL:OMP30835.1, ECO:0000313|Proteomes:UP000188854}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DI 80 {ECO:0000313|EMBL:OMP30835.1,
RC ECO:0000313|Proteomes:UP000188854};
RA Krishnamurthi S., Pal Y., Verma A., Sundharam S.;
RT "Taxonomic characterization of strain DI 80 closely related to
RT Mangrovimonas sp.";
RL Submitted (DEC-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}.
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:OMP30835.1}.
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DR EMBL; MSDT01000005; OMP30835.1; -; Genomic_DNA.
DR RefSeq; WP_076663898.1; NZ_MSDT01000005.1.
DR AlphaFoldDB; A0A1V1ZFD3; -.
DR Proteomes; UP000188854; 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; 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:UP000188854};
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..63
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; 53809 MW; 8DFE8AD44B10E01B CRC64;
MSRRNKKQVF TNVEVIDAGA KGKLVAKAPD GKVIFLSNAV PGDVVDIQTY KKRKAYYEGK
AIAFHKLSEK RSEPKCEHFG VCGGCKWQDM DYQYQLEYKH KEVENNLRRI GHIELPEVTP
ILGSSEQYFY RNKMEFSFSD SRWLTQEEIQ SDEDLGDKNA LGFHIPGMWD KILDVKKCWL
QGDPSNAIRN EVKSFAIVNG MEFFNTRNQA GFLRSLMIRT STTGDLMVMI QFFKEDKAKR
ELLLDHLAET FPEISSLQYV INEKANDTIY DQEVICYKGE DHIFEQMEDL RFKINAKSFY
QTNSKQAYEL YKIARKFANL KGDELVYDLY TGTGTIAQFV AKKAKKVVGV EAVPDAITAA
KENAQLNGIE NVDFYVGDMK NVFNEAFISQ HGHPDVIITD PPRDGMHKDV VQQILNIAPE
KVVYVSCNSA TQARDLALMD EAYKVTKVQA VDMFPQTYHV ENVVLLERRN
//
