ID A0A1M3PU79_9PROT Unreviewed; 429 AA.
AC A0A1M3PU79;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=TRAM domain-containing protein {ECO:0000259|Pfam:PF01938};
GN ORFNames=BGP12_20710 {ECO:0000313|EMBL:OJY70188.1};
OS Rhodospirillales bacterium 70-18.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales.
OX NCBI_TaxID=1895826 {ECO:0000313|EMBL:OJY70188.1, ECO:0000313|Proteomes:UP000184399};
RN [1] {ECO:0000313|EMBL:OJY70188.1, ECO:0000313|Proteomes:UP000184399}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=70-18 {ECO:0000313|EMBL:OJY70188.1};
RA Kantor R.S., Huddy R.J., Iyer R., Thomas B.C., Brown C.T., Anantharaman K.,
RA Tringe S., Hettich R.L., Harrison S.T., Banfield J.F.;
RT "Genome-resolved meta-omics ties microbial dynamics to process performance
RT in biotechnology for thiocyanate degradation.";
RL Submitted (SEP-2016) 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:OJY70188.1}.
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DR EMBL; MKWE01000031; OJY70188.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1M3PU79; -.
DR STRING; 1895826.BGP12_20710; -.
DR Proteomes; UP000184399; 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: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 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.
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 12..45
FT /note="TRAM"
FT /evidence="ECO:0000259|Pfam:PF01938"
FT ACT_SITE 387
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 263
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 313
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 361
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
SQ SEQUENCE 429 AA; 44538 MW; 2D9DFAD179F0657C CRC64;
MTAPAGAPAA AELRVSRIGS DGDGVGHLPD GIVVYLPGTL PGETVLAHPQ FKRGDGWAGT
ADLLATSDDR AAPPCPHFGP CGGCALQHWR DDSYLAWKTA LLETALRRAG YGEMPAPAIR
TPPGARRRVD LAIRRQGPAL LLGLHGKRSA DIVDLHACPV LHPDLFALIA PLRTLLRGLG
GLRRHGSAIL NLLDSGPDLL LRTDAALTTA DRTKLAAFAQ AHGLPRITAA IGDGPHESAA
LLRPPTTAMS GITVTPPPGA FLQASAEGEA AIIAAVLAGL PKLAGKARIA ELYAGCGTLT
FALAKQARIA AFEGDIEAHA ALRQAANNSG LAGRVEALRR DLTRQPLSAK ELAAFGAVVL
DPPHGGAVTQ AALIAASGVA RIIYVSCNPA TLGRDAKLFR DAGYKLLAAT PIDQFLWSPR
LESVTVFAR
//