ID A0A0E3ZA56_9FUSO Unreviewed; 452 AA.
AC A0A0E3ZA56;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=RNA methyltransferase {ECO:0000313|EMBL:AKC95420.1};
GN ORFNames=VC03_02535 {ECO:0000313|EMBL:AKC95420.1};
OS Sneathia vaginalis.
OC Bacteria; Fusobacteriota; Fusobacteriia; Fusobacteriales; Leptotrichiaceae;
OC Sneathia.
OX NCBI_TaxID=187101 {ECO:0000313|EMBL:AKC95420.1, ECO:0000313|Proteomes:UP000033103};
RN [1] {ECO:0000313|EMBL:AKC95420.1, ECO:0000313|Proteomes:UP000033103}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SN35 {ECO:0000313|EMBL:AKC95420.1,
RC ECO:0000313|Proteomes:UP000033103};
RX PubMed=23281612;
RG Vaginal Microbiome Consortium (additional members);
RA Harwich M.D.Jr., Serrano M.G., Fettweis J.M., Alves J.M., Reimers M.A.,
RA Buck G.A., Jefferson K.K.;
RT "Genomic sequence analysis and characterization of Sneathia amnii sp.
RT nov.";
RL BMC Genomics 13:S4-S4(2012).
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; CP011280; AKC95420.1; -; Genomic_DNA.
DR RefSeq; WP_046328526.1; NZ_CP011280.1.
DR AlphaFoldDB; A0A0E3ZA56; -.
DR STRING; 187101.VC03_02535; -.
DR KEGG; sns:VC03_02535; -.
DR PATRIC; fig|1069640.6.peg.487; -.
DR HOGENOM; CLU_014689_7_1_0; -.
DR OrthoDB; 9804590at2; -.
DR Proteomes; UP000033103; 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; 1.
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; 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.
PE 3: Inferred from homology;
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|PROSITE-
KW ProRule:PRU01024}; Reference proteome {ECO:0000313|Proteomes:UP000033103};
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 1..59
FT /note="TRAM"
FT /evidence="ECO:0000259|PROSITE:PS50926"
FT ACT_SITE 406
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 284
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 311
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 379
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
SQ SEQUENCE 452 AA; 51772 MW; 27826EF656F9692D CRC64;
MLKVNDVITV TIEKIVFGGE GLARYEDIVV FVPMSCIGDK LEVKVISVKK TYVRALIQKV
LVPSEDRKEH NKISFEENSG CDFNHIKYEK QLEYKDIMLK DMLKSISKLD VSNIYENIIG
ASNVTNYRNK VATPFFVQDG KIKVGFYKRK SHTKFSIEED YLKSIVASKI EEIILKELND
NKFTVYNEDT DTGFLRCLII RNNTKGEAMV CIVVNKNKEL DKLKVVLKKV YDEVDFLKSV
YVSVKNQKNN IILGEKNIHL FGDEYISENI FSIDFKIYVD SFFQINIEQV KKLYKLAISF
LDNTSNVIDA FSGTGTIGMI LAKNVNKVYC IESVKSAVLS GKKTAKKNDI KNIEFICNRV
EKSIASILSK DKIDSIVFDP PRKGIEESVI KEVCSNNIRQ IVYISCEPSR FARDLNIFRQ
LGYELKRIAS VDMFPNTHHI ESVALIEKKK ED
//
