ID Q03ZS5_LEUMM Unreviewed; 496 AA.
AC Q03ZS5;
DT 14-NOV-2006, integrated into UniProtKB/TrEMBL.
DT 14-NOV-2006, sequence version 1.
DT 27-MAR-2024, entry version 104.
DE SubName: Full=23S rRNA m(5)U-1939 methyltransferase {ECO:0000313|EMBL:ABJ61297.1};
DE EC=2.1.1.- {ECO:0000313|EMBL:ABJ61297.1};
GN OrderedLocusNames=LEUM_0147 {ECO:0000313|EMBL:ABJ61297.1};
OS Leuconostoc mesenteroides subsp. mesenteroides (strain ATCC 8293 / DSM
OS 20343 / BCRC 11652 / CCM 1803 / JCM 6124 / NCDO 523 / NBRC 100496 / NCIMB
OS 8023 / NCTC 12954 / NRRL B-1118 / 37Y).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Leuconostoc.
OX NCBI_TaxID=203120 {ECO:0000313|EMBL:ABJ61297.1, ECO:0000313|Proteomes:UP000000362};
RN [1] {ECO:0000313|EMBL:ABJ61297.1, ECO:0000313|Proteomes:UP000000362}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8293 / DSM 20343 / BCRC 11652 / CCM 1803 / JCM 6124 / NCDO
RC 523 / NBRC 100496 / NCIMB 8023 / NCTC 12954 / NRRL B-1118 / 37Y
RC {ECO:0000313|Proteomes:UP000000362};
RX PubMed=17030793; DOI=10.1073/pnas.0607117103;
RA Makarova K., Slesarev A., Wolf Y., Sorokin A., Mirkin B., Koonin E.,
RA Pavlov A., Pavlova N., Karamychev V., Polouchine N., Shakhova V.,
RA Grigoriev I., Lou Y., Rohksar D., Lucas S., Huang K., Goodstein D.M.,
RA Hawkins T., Plengvidhya V., Welker D., Hughes J., Goh Y., Benson A.,
RA Baldwin K., Lee J.H., Diaz-Muniz I., Dosti B., Smeianov V., Wechter W.,
RA Barabote R., Lorca G., Altermann E., Barrangou R., Ganesan B., Xie Y.,
RA Rawsthorne H., Tamir D., Parker C., Breidt F., Broadbent J., Hutkins R.,
RA O'Sullivan D., Steele J., Unlu G., Saier M., Klaenhammer T., Richardson P.,
RA Kozyavkin S., Weimer B., Mills D.;
RT "Comparative genomics of the lactic acid bacteria.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:15611-15616(2006).
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; CP000414; ABJ61297.1; -; Genomic_DNA.
DR RefSeq; WP_011679108.1; NC_008531.1.
DR AlphaFoldDB; Q03ZS5; -.
DR EnsemblBacteria; ABJ61297; ABJ61297; LEUM_0147.
DR GeneID; 61177374; -.
DR KEGG; lme:LEUM_0147; -.
DR eggNOG; COG2265; Bacteria.
DR HOGENOM; CLU_014689_7_1_9; -.
DR Proteomes; UP000000362; 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 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; 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:SF45; -; 1.
DR PANTHER; PTHR11061; RNA M5U 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.
DR PROSITE; PS01230; TRMA_1; 1.
PE 3: Inferred from homology;
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|PROSITE-
KW ProRule:PRU01024};
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 43..101
FT /note="TRAM"
FT /evidence="ECO:0000259|PROSITE:PS50926"
FT REGION 1..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..19
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 452
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10015"
FT ACT_SITE 452
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 327
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 356
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 377
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 425
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
SQ SEQUENCE 496 AA; 55770 MW; D43D0126AC02396E CRC64;
MTEQNKRPYQ KSRNNNGKKP YYGKNFDPRK SGAPRGNTSE GVNVRVGQNF PLTIKRLGIN
GEGIGYFKRK IVFVPGALPD EVAVVKVTEV EPKYIAAKVL KIREKSPDRV KPLDEFADSV
GGFELEHMNY PAQLRFKKDV LVQSLEKFQP KGWSNYDIRD TIGMDHPYEY RNKAQFPVRK
IGDKLSVGMY KRGSHDLVDL PVVHTQTPAT MKVMRTVREL LDKLSVSIYN EDKNRGTVKT
IVARVSQTTS EVQLTFITNT DGFPGDTALI EAINQALPEV TGIFQNYNPG RTSLVWGEET
LKLWGKDYIE EKVLGKTFQL SPRAFMQLNH TQMSVVYNQA LAALDLTHAD KLVDAYAGVG
TIGLSLADKA GEVRGMEIIP EAVDDANQNA TLNHISNAHY EVGTAEKLFP KWQSEGWIAD
ALVVDPPRTG LDTALRREIL RTQPEKFVYI SCNASTLARD LVDLSKAYQV DYIQSIDMFP
QTARWEGVVK LTKRQK
//
