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Database: UniProt
Entry: A8LPG0_DINSH
LinkDB: A8LPG0_DINSH
Original site: A8LPG0_DINSH 
ID   A8LPG0_DINSH            Unreviewed;       414 AA.
AC   A8LPG0;
DT   04-DEC-2007, integrated into UniProtKB/TrEMBL.
DT   04-DEC-2007, sequence version 1.
DT   27-MAR-2024, entry version 77.
DE   SubName: Full=23S rRNA (Uracil-5-)-methyltransferase RumA {ECO:0000313|EMBL:ABV95225.1};
DE            EC=2.1.1.- {ECO:0000313|EMBL:ABV95225.1};
GN   Name=rumA {ECO:0000313|EMBL:ABV95225.1};
GN   OrderedLocusNames=Dshi_3492 {ECO:0000313|EMBL:ABV95225.1};
OS   Dinoroseobacter shibae (strain DSM 16493 / NCIMB 14021 / DFL 12).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Dinoroseobacter.
OX   NCBI_TaxID=398580 {ECO:0000313|EMBL:ABV95225.1, ECO:0000313|Proteomes:UP000006833};
RN   [1] {ECO:0000313|Proteomes:UP000006833}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 16493 / NCIMB 14021 / DFL 12
RC   {ECO:0000313|Proteomes:UP000006833};
RX   PubMed=19741735; DOI=10.1038/ismej.2009.94;
RA   Wagner-Dobler I., Ballhausen B., Berger M., Brinkhoff T., Buchholz I.,
RA   Bunk B., Cypionka H., Daniel R., Drepper T., Gerdts G., Hahnke S., Han C.,
RA   Jahn D., Kalhoefer D., Kiss H., Klenk H.P., Kyrpides N., Liebl W.,
RA   Liesegang H., Meincke L., Pati A., Petersen J., Piekarski T.,
RA   Pommerenke C., Pradella S., Pukall R., Rabus R., Stackebrandt E., Thole S.,
RA   Thompson L., Tielen P., Tomasch J., von Jan M., Wanphrut N., Wichels A.,
RA   Zech H., Simon M.;
RT   "The complete genome sequence of the algal symbiont Dinoroseobacter shibae:
RT   a hitchhiker's guide to life in the sea.";
RL   ISME J. 4:61-77(2010).
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; CP000830; ABV95225.1; -; Genomic_DNA.
DR   RefSeq; WP_012180149.1; NC_009952.1.
DR   AlphaFoldDB; A8LPG0; -.
DR   STRING; 398580.Dshi_3492; -.
DR   KEGG; dsh:Dshi_3492; -.
DR   eggNOG; COG2265; Bacteria.
DR   HOGENOM; CLU_014689_8_0_5; -.
DR   OrthoDB; 9804590at2; -.
DR   Proteomes; UP000006833; 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   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; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   InterPro; IPR010280; U5_MeTrfase_fam.
DR   PANTHER; PTHR11061; RNA M5U METHYLTRANSFERASE; 1.
DR   PANTHER; PTHR11061:SF30; TRNA (URACIL(54)-C(5))-METHYLTRANSFERASE; 1.
DR   Pfam; PF05958; tRNA_U5-meth_tr; 1.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR   PROSITE; PS51687; SAM_MT_RNA_M5U; 1.
DR   PROSITE; PS01230; TRMA_1; 1.
PE   3: Inferred from homology;
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|PROSITE-
KW   ProRule:PRU01024}; Reference proteome {ECO:0000313|Proteomes:UP000006833};
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   ACT_SITE        367
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10015"
FT   ACT_SITE        367
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         246
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         273
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         293
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         341
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
SQ   SEQUENCE   414 AA;  43666 MW;  7BF49734F08FDC6F CRC64;
     MSETQPDTLT ITRLGLHGDG IAPGPVYAAR TLPGEEIRGE ITGDRIAAPK IVTPCPNRVK
     PPCPHYARCG GCALQHAADP FVADWKVQVV IDALSAHGLS APMRPIRTSP PRTRRRATLS
     GRRLKKGTLL GFHTRASDTI VDIPGCEVLA PAITEALPSL AEFLPLLGSR KGELALAVTV
     SEAGLDVDIR GGKPLDPALR LSLTALTQRL DLARLSLDGK VFLTLRPPAQ HFGPASVTPP
     PGAFLQATAP GEAALLAAVT EAVGPARRIA DLFAGCGTFA LPLATRAEVH AVEGDADMLA
     ALDAGWRKTP GLSKVTTEAR DLFRRPLLPD DLARFGAVVI DPPRAGAEAQ TAALASAQPD
     RIAAVSCNPV TFARDAKTLC DAGYALRWVQ VVDQFRWSPH VELAAAFTAP HIQP
//
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