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Database: UniProt
Entry: A0A011Q6P8_9LACT
LinkDB: A0A011Q6P8_9LACT
Original site: A0A011Q6P8_9LACT 
ID   A0A011Q6P8_9LACT        Unreviewed;       462 AA.
AC   A0A011Q6P8;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   24-JAN-2024, entry version 36.
DE   SubName: Full=RNA methyltransferase, TrmA family {ECO:0000313|EMBL:EXJ22986.1};
GN   ORFNames=ADIAL_1609 {ECO:0000313|EMBL:EXJ22986.1};
OS   Alkalibacterium sp. AK22.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Carnobacteriaceae;
OC   Alkalibacterium.
OX   NCBI_TaxID=1229520 {ECO:0000313|EMBL:EXJ22986.1, ECO:0000313|Proteomes:UP000020164};
RN   [1] {ECO:0000313|EMBL:EXJ22986.1, ECO:0000313|Proteomes:UP000020164}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AK22 {ECO:0000313|Proteomes:UP000020164};
RA   Singh A., Pinnaka A.K.;
RL   Submitted (JAN-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: 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:EXJ22986.1}.
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DR   EMBL; JANL01000036; EXJ22986.1; -; Genomic_DNA.
DR   RefSeq; WP_034302222.1; NZ_JANL01000036.1.
DR   AlphaFoldDB; A0A011Q6P8; -.
DR   STRING; 1229520.ADIAL_1609; -.
DR   PATRIC; fig|1229520.3.peg.1572; -.
DR   eggNOG; COG2265; Bacteria.
DR   OrthoDB; 9804590at2; -.
DR   Proteomes; UP000020164; 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   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:SF48; 23S RRNA (URACIL(747)-C(5))-METHYLTRANSFERASE RLMC; 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.
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:UP000020164};
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          11..69
FT                   /note="TRAM"
FT                   /evidence="ECO:0000259|PROSITE:PS50926"
FT   ACT_SITE        418
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10015"
FT   ACT_SITE        418
FT                   /note="Nucleophile"
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         322
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         343
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         391
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
SQ   SEQUENCE   462 AA;  51931 MW;  09FC79A08E0A8149 CRC64;
     MAKNKTHKKA PVSKNEVLKA EIVDLTHEGA GVAKIDYYPV FIEGALIGET VEFKIVKTKK
     TFAFGKLIKV IEKSPDRVEV VDKVYAQTGT MPLQHLSYPA QLAFKKKQVE TVLQKIGKLE
     GIKVNEVIGM DSPLGYRNKA QVPVRKIDGR LTTGFFRKNS HDVLPIEDFQ IQDPEIDQAI
     VRIRDIMRQF HVKPYNEKAH TGWLRHIIVR RGHSSKELMV VLVTTNHDFH REEEIVTAIK
     KALPELVSLI QNINPEKTNV ILGSESRILW GEDNYKDQLM GFTFSIGHQS FYQVNSVQTE
     QLYRTAVDYA GLTGQETVID AYCGIGTLTL ALAQKAEKVY GLEIIEPAIE NARLNALNNS
     VSNVEFKVGP AEEIITEWAE AQLQADVIVV DPPRKGLAPE FIESVLTMKP EKMVYVSCNP
     ATLARDLKLL TEGGYTVEAV QPVDMFPQTY HVECVVLMSM MK
//
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