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Database: UniProt
Entry: A0A0S8JNE2_9BACE
LinkDB: A0A0S8JNE2_9BACE
Original site: A0A0S8JNE2_9BACE 
ID   A0A0S8JNE2_9BACE        Unreviewed;       467 AA.
AC   A0A0S8JNE2;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   SubName: Full=RNA methyltransferase {ECO:0000313|EMBL:KPL11024.1};
GN   ORFNames=AMS26_20890 {ECO:0000313|EMBL:KPL11024.1};
OS   Bacteroides sp. SM23_62.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Bacteroides.
OX   NCBI_TaxID=1703352 {ECO:0000313|EMBL:KPL11024.1, ECO:0000313|Proteomes:UP000050819};
RN   [1] {ECO:0000313|EMBL:KPL11024.1, ECO:0000313|Proteomes:UP000050819}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SM23_62 {ECO:0000313|EMBL:KPL11024.1};
RX   PubMed=25922666; DOI=10.1186/s40168-015-0077-6;
RA   Baker B.J., Lazar C.S., Teske A.P., Dick G.J.;
RT   "Genomic resolution of linkages in carbon, nitrogen, and sulfur cycling
RT   among widespread estuary sediment bacteria.";
RL   Microbiome 3:14-14(2015).
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:KPL11024.1}.
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DR   EMBL; LJUP01000281; KPL11024.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0S8JNE2; -.
DR   PATRIC; fig|1703352.3.peg.2319; -.
DR   Proteomes; UP000050819; Unassembled WGS sequence.
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};
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          1..61
FT                   /note="TRAM"
FT                   /evidence="ECO:0000259|PROSITE:PS50926"
FT   ACT_SITE        425
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10015"
FT   ACT_SITE        425
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         299
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
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         349
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         398
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
SQ   SEQUENCE   467 AA;  53351 MW;  F4C7623865C7AB57 CRC64;
     MGRKKLPLIE QVEITDIGAR GKAIARIDNF VTFVTNGLPG DVVDVQITRR RKSYQEGRVV
     RFHKQSTRRT EPFCQHFGKC GGCRWQDLKY ADQLHYKQQE VIENLKRIGR LEFPPVNTIR
     ASANEKYYRN KLEFTFSNRR WLSAEEINSG DDFSDRNGLG FHVPGMFDKV IDLHECHLQP
     SLSDAIRQGI RDYARAHGLT FYDLRNGGGL LRTLVIRNTM KGEWMVLVAF SEDDEAQRNL
     LLDHLQMRFP EITSLMYCIN RKANDSIFDQ EIMLHAGRDH IMEQLEDLQF KIGPKSFFQT
     NTAQALELYR TVRDMAGLTG GEVVYDLYAG TGTIGLFLAR QAGKVVGIEY IDEAIGDARV
     NAELNGIDNA LFFSGDIKDI LTVEFVRMHG KPDVLITDPP RAGMHKDVVD VILEISPARI
     VYVSCNPSTQ ARDLQLLSGQ YRILEIQPFD MFPQTFHVEN IVLLEKM
//
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