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Database: UniProt
Entry: U1RDN4_9ACTO
LinkDB: U1RDN4_9ACTO
Original site: U1RDN4_9ACTO 
ID   U1RDN4_9ACTO            Unreviewed;       355 AA.
AC   U1RDN4;
DT   13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2013, sequence version 1.
DT   24-JAN-2024, entry version 37.
DE   SubName: Full=TRAM domain protein {ECO:0000313|EMBL:ERH16587.1};
DE   Flags: Fragment;
GN   ORFNames=HMPREF0043_01873 {ECO:0000313|EMBL:ERH16587.1};
OS   Actinobaculum sp. oral taxon 183 str. F0552.
OC   Bacteria; Actinomycetota; Actinomycetes; Actinomycetales; Actinomycetaceae;
OC   Actinobaculum.
OX   NCBI_TaxID=1227261 {ECO:0000313|EMBL:ERH16587.1, ECO:0000313|Proteomes:UP000016495};
RN   [1] {ECO:0000313|EMBL:ERH16587.1, ECO:0000313|Proteomes:UP000016495}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F0552 {ECO:0000313|EMBL:ERH16587.1,
RC   ECO:0000313|Proteomes:UP000016495};
RA   Weinstock G., Sodergren E., Lobos E.A., Fulton L., Fulton R., Courtney L.,
RA   Fronick C., O'Laughlin M., Godfrey J., Wilson R.M., Miner T., Farmer C.,
RA   Delehaunty K., Cordes M., Minx P., Tomlinson C., Chen J., Wollam A.,
RA   Pepin K.H., Bhonagiri V., Zhang X., Warren W., Mitreva M., Mardis E.R.,
RA   Wilson R.K.;
RL   Submitted (JUN-2013) 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:ERH16587.1}.
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DR   EMBL; AWSB01000059; ERH16587.1; -; Genomic_DNA.
DR   RefSeq; WP_021601773.1; NZ_KE951423.1.
DR   AlphaFoldDB; U1RDN4; -.
DR   STRING; 1227261.HMPREF0043_01873; -.
DR   eggNOG; COG2265; Bacteria.
DR   HOGENOM; CLU_014689_7_0_11; -.
DR   OrthoDB; 9804590at2; -.
DR   Proteomes; UP000016495; 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:0001510; P:RNA methylation; IEA:GOC.
DR   GO; GO:0006396; P:RNA processing; IEA:InterPro.
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; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   InterPro; IPR002792; TRAM_dom.
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; PF01938; TRAM; 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.
PE   3: Inferred from homology;
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|PROSITE-
KW   ProRule:PRU01024}; Reference proteome {ECO:0000313|Proteomes:UP000016495};
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..54
FT                   /note="TRAM"
FT                   /evidence="ECO:0000259|PROSITE:PS50926"
FT   BINDING         244
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         297
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         339
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   NON_TER         355
FT                   /evidence="ECO:0000313|EMBL:ERH16587.1"
SQ   SEQUENCE   355 AA;  37982 MW;  9FFDF3BCC80F73C1 CRC64;
     MIDIDLTDIA HGGACVGRAP DGRVVFARFG LPGERVRVEV TGERSSLVRG DVVEVLSGPS
     EHRVQTAWPE AGPLGVGGAE LGHVAFDFQA RWKTHVLRAT LARVGGAGLA AHLADRGVDC
     RVRPMDGDAR TGGWATRTRV EFVVGEDGTP SMHREGTHDL LPVSGFPLAV ADVGDLDLFG
     AWRRAWRPGQ RVRAVAPSGS DPVIAVGQTC WWAPGFRADR YVREDVVVDG RLYPYRVRAS
     GFWQVHRDGA AQLIRTVLRA ARVEPGDGVV ELYAGAGLLT QPLALAVGDS GGVWAFEGMR
     EATDDARANL RDLPWARVQT ASITARFARD LGGRILVADP PRSGLGRDLA STLAA
//
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