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Database: UniProt
Entry: H6NPR2_9BACL
LinkDB: H6NPR2_9BACL
Original site: H6NPR2_9BACL 
ID   H6NPR2_9BACL            Unreviewed;       501 AA.
AC   H6NPR2;
DT   18-APR-2012, integrated into UniProtKB/TrEMBL.
DT   18-APR-2012, sequence version 1.
DT   27-MAR-2024, entry version 63.
DE   SubName: Full=RNA methyltransferase {ECO:0000313|EMBL:AFC33418.1};
GN   ORFNames=PM3016_6814 {ECO:0000313|EMBL:AFC33418.1};
OS   Paenibacillus mucilaginosus 3016.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=1116391 {ECO:0000313|EMBL:AFC33418.1, ECO:0000313|Proteomes:UP000007523};
RN   [1] {ECO:0000313|EMBL:AFC33418.1, ECO:0000313|Proteomes:UP000007523}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=3016 {ECO:0000313|EMBL:AFC33418.1,
RC   ECO:0000313|Proteomes:UP000007523};
RX   PubMed=22535950; DOI=10.1128/JB.00323-12;
RA   Ma M., Wang Z., Li L., Jiang X., Guan D., Cao F., Chen H., Wang X.,
RA   Shen D., Du B., Li J.;
RT   "Complete Genome Sequence of Paenibacillus mucilaginosus 3016, a Bacterium
RT   Functional as Microbial Fertilizer.";
RL   J. Bacteriol. 194:2777-2778(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; CP003235; AFC33418.1; -; Genomic_DNA.
DR   AlphaFoldDB; H6NPR2; -.
DR   STRING; 1116391.PM3016_6814; -.
DR   KEGG; pmq:PM3016_6814; -.
DR   HOGENOM; CLU_014689_7_0_9; -.
DR   Proteomes; UP000007523; Chromosome.
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; 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.
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:UP000007523};
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          36..94
FT                   /note="TRAM"
FT                   /evidence="ECO:0000259|PROSITE:PS50926"
FT   REGION          1..35
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        8..27
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        453
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10015"
FT   ACT_SITE        453
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         328
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         357
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         378
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         426
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
SQ   SEQUENCE   501 AA;  54854 MW;  C98BB8B347FE8F34 CRC64;
     MTRSKKPTTR TKTTDTKSNH KRPGRPAGAE DLSGLPVAKN EDYTADIVGI GHEGEGVGRV
     NGYTLFVPGA LPGEKVRVKV VKVKKQYGYA KLLEVLEASP DRIDAPCPIY KQCGGCQLQH
     LSYEAQMRWK RQLVIDNLTR IGKLQVVGER EEGIIVHPTL GMSDPWRYRN KAQVPIGLAE
     TEEGGLVGGF YAQGSHRIID MEACLIQHEN NDAVVGAVKK IARELGIRPY SEETGRGLLR
     HVIARYGFNT GEIMVVLVTN GRDLPHADEL TGLIRRDVPG VTSIVQNINT RETNVIFGDE
     TRTLWGSDVI YDTIGDIRFA ISARSFYQVN PVQTEVLYGK ALEYAALTGR ETVIDAYCGI
     GTISLFLAQK ADQVYGVEIV PEAIEDARAN ARLNGIRNAS FEAGPAEVVI PAWRGKGIAP
     DVIVVDPPRK GCDPALLETI LAMRPERVVY VSCNPSTLAR DLRVLEDGGF RTVQVQPVDM
     FPHTVHVESV AVLVRGEAGE A
//
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