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Database: UniProt
Entry: A0A0J5S525_9PAST
LinkDB: A0A0J5S525_9PAST
Original site: A0A0J5S525_9PAST 
ID   A0A0J5S525_9PAST        Unreviewed;       393 AA.
AC   A0A0J5S525;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   24-JAN-2024, entry version 38.
DE   SubName: Full=23S rRNA methyltransferase {ECO:0000313|EMBL:KMK51917.1};
GN   ORFNames=RO21_03765 {ECO:0000313|EMBL:KMK51917.1};
OS   Muribacter muris.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Muribacter.
OX   NCBI_TaxID=67855 {ECO:0000313|EMBL:KMK51917.1, ECO:0000313|Proteomes:UP000036270};
RN   [1] {ECO:0000313|EMBL:KMK51917.1, ECO:0000313|Proteomes:UP000036270}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ackerman80-443D {ECO:0000313|EMBL:KMK51917.1,
RC   ECO:0000313|Proteomes:UP000036270};
RA   Christensen H., Nicklas W., Bisgaard M.;
RT   "Reclassification of Actinobacillus muris as Muribacter muris.";
RL   Submitted (DEC-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. RNA M5U methyltransferase family. {ECO:0000256|PROSITE-
CC       ProRule:PRU01024}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU01024}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KMK51917.1}.
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DR   EMBL; JWIZ01000021; KMK51917.1; -; Genomic_DNA.
DR   RefSeq; WP_047976460.1; NZ_JWIZ01000021.1.
DR   AlphaFoldDB; A0A0J5S525; -.
DR   STRING; 67855.RO21_03765; -.
DR   PATRIC; fig|67855.3.peg.609; -.
DR   Proteomes; UP000036270; Unassembled WGS sequence.
DR   GO; GO:0008173; F:RNA methyltransferase activity; IEA:InterPro.
DR   GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IEA:InterPro.
DR   GO; GO:0034470; P:ncRNA processing; IEA:UniProt.
DR   GO; GO:0001510; P:RNA methylation; IEA:GOC.
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:UP000036270};
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          10..71
FT                   /note="TRAM"
FT                   /evidence="ECO:0000259|PROSITE:PS50926"
FT   ACT_SITE        350
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10015"
FT   ACT_SITE        350
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         255
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         276
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         324
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
SQ   SEQUENCE   393 AA;  44745 MW;  DE6AE9F27E8AF6BC CRC64;
     MALFYSDKRA KKVAQPTALQ RFAVQALDYQ GLGVAKLNGK TWFIENALPD EVVDADILEE
     KRQYGRAQAV RFIQKSAKRQ DPHCAVYHQC GGCQMRHIPI ELQRDTKQST LFRRLQTLQA
     EPIVCEPMLA GNAARYRRRA KFSVMWEKGQ LVIGFRQANS HAIIPLQDCD VLEPALAALL
     PPLQRLFAAW QQKKAVGHIE LVRADNGVAM LLRHIGELKE ADRTHLLAFA EHYHLMLFVM
     TDKDQLEQWY GEPPFYTING LKLGFSIRDF IQINADLNEK MVAQARENAQ RNGISNAAFY
     QTDLDQSFID QPWAAQPFNK VLLDPARQGA YFALAHLCRL APERIVYVSC NPATLVRDAE
     KLIQDGYRLA KCAMIDMFPH TAHLESISLF VKK
//
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