ID A0A2I1UQZ0_STROR Unreviewed; 451 AA. AC A0A2I1UQZ0; DT 28-FEB-2018, integrated into UniProtKB/TrEMBL. DT 28-FEB-2018, sequence version 1. DT 08-MAY-2019, entry version 7. DE SubName: Full=23S rRNA (Uracil(1939)-C(5))-methyltransferase RlmD {ECO:0000313|EMBL:PLA08294.1}; GN ORFNames=CYK17_00885 {ECO:0000313|EMBL:PLA08294.1}; OS Streptococcus oralis subsp. dentisani. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=1458253 {ECO:0000313|EMBL:PLA08294.1, ECO:0000313|Proteomes:UP000235088}; RN [1] {ECO:0000313|EMBL:PLA08294.1, ECO:0000313|Proteomes:UP000235088} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=UMB0008 {ECO:0000313|EMBL:PLA08294.1, RC ECO:0000313|Proteomes:UP000235088}; RA Thomas-White K., Wolfe A.J.; RT "Phylogenetic diversity of female urinary microbiome."; RL Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Belongs to the class I-like SAM-binding CC methyltransferase superfamily. RNA M5U methyltransferase family. CC {ECO:0000256|PROSITE-ProRule:PRU01024, CC ECO:0000256|SAAS:SAAS00561307}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:PLA08294.1}. 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; PKIF01000001; PLA08294.1; -; Genomic_DNA. DR RefSeq; WP_070838606.1; NZ_PKIF01000001.1. DR Proteomes; UP000235088; 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 Complete proteome {ECO:0000313|Proteomes:UP000235088}; KW Methyltransferase {ECO:0000256|PROSITE-ProRule:PRU01024, KW ECO:0000256|SAAS:SAAS00234999, ECO:0000313|EMBL:PLA08294.1}; KW S-adenosyl-L-methionine {ECO:0000256|PROSITE-ProRule:PRU01024, KW ECO:0000256|SAAS:SAAS00235009}; KW Transferase {ECO:0000256|PROSITE-ProRule:PRU01024, KW ECO:0000256|SAAS:SAAS00506843, ECO:0000313|EMBL:PLA08294.1}. FT DOMAIN 1 59 TRAM. {ECO:0000259|PROSITE:PS50926}. FT ACT_SITE 408 408 {ECO:0000256|PROSITE-ProRule:PRU10015}. FT ACT_SITE 408 408 Nucleophile. {ECO:0000256|PROSITE- FT ProRule:PRU01024}. FT BINDING 283 283 S-adenosyl-L-methionine. FT {ECO:0000256|PROSITE-ProRule:PRU01024}. FT BINDING 312 312 S-adenosyl-L-methionine; via carbonyl FT oxygen. {ECO:0000256|PROSITE-ProRule: FT PRU01024}. FT BINDING 333 333 S-adenosyl-L-methionine. FT {ECO:0000256|PROSITE-ProRule:PRU01024}. FT BINDING 381 381 S-adenosyl-L-methionine. FT {ECO:0000256|PROSITE-ProRule:PRU01024}. SQ SEQUENCE 451 AA; 51159 MW; 33B75E0993936D5A 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 QPVDLFPQTH HVEAVSLLVK E //