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Database: UniProt
Entry: K0NGP1_DESTT
LinkDB: K0NGP1_DESTT
Original site: K0NGP1_DESTT 
ID   K0NGP1_DESTT            Unreviewed;       462 AA.
AC   K0NGP1;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   27-MAR-2024, entry version 58.
DE   SubName: Full=RumA: predicted 23S rRNA mehtyltransferase {ECO:0000313|EMBL:CCK80406.1};
DE            EC=2.1.1.- {ECO:0000313|EMBL:CCK80406.1};
GN   Name=rumA {ECO:0000313|EMBL:CCK80406.1};
GN   OrderedLocusNames=TOL2_C22450 {ECO:0000313|EMBL:CCK80406.1};
OS   Desulfobacula toluolica (strain DSM 7467 / Tol2).
OC   Bacteria; Thermodesulfobacteriota; Desulfobacteria; Desulfobacterales;
OC   Desulfobacteraceae; Desulfobacula.
OX   NCBI_TaxID=651182 {ECO:0000313|EMBL:CCK80406.1, ECO:0000313|Proteomes:UP000007347};
RN   [1] {ECO:0000313|EMBL:CCK80406.1, ECO:0000313|Proteomes:UP000007347}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 7467 / Tol2 {ECO:0000313|Proteomes:UP000007347};
RX   PubMed=23088741; DOI=10.1111/j.1462-2920.2012.02885.x;
RA   Wohlbrand L., Jacob J.H., Kube M., Mussmann M., Jarling R., Beck A.,
RA   Amann R., Wilkes H., Reinhardt R., Rabus R.;
RT   "Complete genome, catabolic sub-proteomes and key-metabolites of
RT   Desulfobacula toluolica Tol2, a marine, aromatic compound-degrading,
RT   sulfate-reducing bacterium.";
RL   Environ. Microbiol. 15:1334-55(2013).
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; FO203503; CCK80406.1; -; Genomic_DNA.
DR   RefSeq; WP_014957718.1; NC_018645.1.
DR   AlphaFoldDB; K0NGP1; -.
DR   STRING; 651182.TOL2_C22450; -.
DR   KEGG; dto:TOL2_C22450; -.
DR   PATRIC; fig|651182.5.peg.2653; -.
DR   HOGENOM; CLU_014689_8_1_7; -.
DR   OrthoDB; 9804590at2; -.
DR   Proteomes; UP000007347; 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; 2.
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:UP000007347};
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          2..60
FT                   /note="TRAM"
FT                   /evidence="ECO:0000259|PROSITE:PS50926"
FT   ACT_SITE        420
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10015"
FT   ACT_SITE        420
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         298
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
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         348
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         393
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
SQ   SEQUENCE   462 AA;  52752 MW;  8932438E3FB8DCA7 CRC64;
     MSIKKRKAYE LEITDLAFGG RGLAKPDGFP VFIDRCIPGD VVFAKITKKK KSWAEGKLIK
     ILQESSLRKE GKCQYCNFCG GCKWQQIGYD LQLEYKKRHV TESMQHIGGL KDVLVKDVIP
     SDNIYEYRNK MEFSCSSKRW LLPWELENEE IKKDFGIGLH VPGTFDKVID IKRCEIMPDL
     GNQILDDVRN FIKESDLPAY NLRTHEGFWR FLMLRHSVAF DTWMVNIVTT FKQMDVVRDL
     ASVLTQNHPQ IKSVMNNITD AKSGVSIGKE EICLYGKDHI KERLGKFVFK ISPNSFFQTN
     TRSCENLYAK VSEYAALTGK ETVIDLYSGT GTIPIWLSDQ AKMVYGIEIV KSAVVDAKLN
     AQLNGIENCE FFEGDIKDVL PGLKQKPDVM IIDPPRVGMH KDVVQQVLYI SPEKIVYVSC
     NPATLARDLE MLAPEYDIKE IQPVDMFPHT YHIESVALLL KK
//
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