ID A0A427YY56_STROR Unreviewed; 451 AA. AC A0A427YY56; DT 08-MAY-2019, integrated into UniProtKB/TrEMBL. DT 08-MAY-2019, sequence version 1. DT 12-AUG-2020, entry version 5. DE SubName: Full=23S rRNA (Uracil-C(5))-methyltransferase RlmCD {ECO:0000313|EMBL:RSH96442.1}; DE EC=2.1.1.189 {ECO:0000313|EMBL:RSH96442.1}; GN Name=rlmCD_1 {ECO:0000313|EMBL:RSH96442.1}; GN ORFNames=D8894_08875 {ECO:0000313|EMBL:RSH96442.1}; OS Streptococcus oralis. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=1303 {ECO:0000313|EMBL:RSH96442.1, ECO:0000313|Proteomes:UP000273781}; RN [1] {ECO:0000313|EMBL:RSH96442.1, ECO:0000313|Proteomes:UP000273781} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BCA18 {ECO:0000313|EMBL:RSH96442.1, RC ECO:0000313|Proteomes:UP000273781}; RA Velsko I.; RT "Species Designations Belie Phenotypic and Genotypic Heterogeneity in Oral RT Streptococci."; RL Submitted (NOV-2018) 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:RSH96442.1}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; RJME01000017; RSH96442.1; -; Genomic_DNA. DR Proteomes; UP000273781; Unassembled WGS sequence. DR GO; GO:0008173; F:RNA methyltransferase activity; IEA:InterPro. DR GO; GO:0006396; P:RNA processing; IEA:InterPro. 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. DR InterPro; IPR002792; TRAM_dom. DR InterPro; IPR010280; U5_MeTrfase_fam. DR PANTHER; PTHR11061; PTHR11061; 1. DR Pfam; PF05958; tRNA_U5-meth_tr; 1. DR SUPFAM; SSF50249; SSF50249; 1. DR SUPFAM; SSF53335; SSF53335; 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, ECO:0000313|EMBL:RSH96442.1}; 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, ECO:0000313|EMBL:RSH96442.1}. FT DOMAIN 1..59 FT /note="TRAM" FT /evidence="ECO:0000259|PROSITE:PS50926" FT ACT_SITE 408 FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10015" FT ACT_SITE 408 FT /note="Nucleophile" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024" FT BINDING 283 FT /note="S-adenosyl-L-methionine" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024" FT BINDING 312 FT /note="S-adenosyl-L-methionine; via carbonyl oxygen" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024" FT BINDING 333 FT /note="S-adenosyl-L-methionine" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024" FT BINDING 381 FT /note="S-adenosyl-L-methionine" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024" SQ SEQUENCE 451 AA; 51168 MW; 33B75E0981249D5A CRC64; MLKKNDIVEV EIIDLTHEGA GVAKVDGLVF FVENALPTEK ILMRVLKVNK KIGFGKVEEY FVRSPHRNQD LDLAYLRSGI ADLGHLAYPE QLKFKTKQVK DSLYKIAGIT DVEVAETFGM DHPVQYRNKA QVPVRRVNGV LETGFFRKNS HDLMPLEDFF IQDPVIDQVV VVLRDLLRRF DLKPYDEKEQ SGLIRNLVVR RGHYSGQIMV ILVTKRPKVF RVEQLIEQII KQFPEIVSVM QNINDQNTNA IFGKEWKTLY GQDYITDQML GNDFQIAGPA FYQVNTEMAE KLYQTAIDFA ELKEDDVVID AYSGIGTIGL SVAKHVKEVY GVEVIPEAVE NSQKNASLNK ITNAHYVCDT AENAMKNWLK EGIQPTVILV DPPRKGLTES FIKASAQTGA DRIAYISCNV ATMARDIKLY QELGYELKKV HPVDLFPQTH HVEAVSLLVK E //