ID A0A286ET27_9ACTN Unreviewed; 456 AA.
AC A0A286ET27;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=tRNA/tmRNA/rRNA uracil-C5-methylase (TrmA/RlmC/RlmD family) {ECO:0000313|EMBL:SOD74077.1};
GN ORFNames=SAMN05892883_3253 {ECO:0000313|EMBL:SOD74077.1};
OS Jatrophihabitans sp. GAS493.
OC Bacteria; Actinomycetota; Actinomycetes; Jatrophihabitantales;
OC Jatrophihabitantaceae; Jatrophihabitans.
OX NCBI_TaxID=1907575 {ECO:0000313|EMBL:SOD74077.1, ECO:0000313|Proteomes:UP000218903};
RN [1] {ECO:0000313|EMBL:SOD74077.1, ECO:0000313|Proteomes:UP000218903}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GAS493 {ECO:0000313|EMBL:SOD74077.1,
RC ECO:0000313|Proteomes:UP000218903};
RA Ehlers B., Leendertz F.H.;
RL Submitted (SEP-2017) 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}.
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DR EMBL; LT907982; SOD74077.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A286ET27; -.
DR InParanoid; A0A286ET27; -.
DR Proteomes; UP000218903; Chromosome i.
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 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; 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 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; 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 17..80
FT /note="TRAM"
FT /evidence="ECO:0000259|PROSITE:PS50926"
FT REGION 214..253
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 396
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 272
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 301
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 325
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 369
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
SQ SEQUENCE 456 AA; 48214 MW; 93B06DF5779BEF15 CRC64;
MPTDPRTSTG RDDVTAPFAV GHRLRLRVTA VAHGGHCVAR VDDDPHGRVV FVRHTLPGEV
VEAAVTEDSG GAFLRADAVE ILQAATERVA PPCPHAGAGR CGGCDWQHVT AGGQRELKRA
VVGEQFARLA QLEVDAEVEE LAGGLLGWRT RTLYATTPGG EVGLRRHRSH TVEVLDHCPL
GVHGVGDSEV LQEPWPGISG LELVQDGPQA ITLLTHRPAP RPSGRRGSTQ RGGGQRHHRR
QPDVVSVHSG SPEVTRPALG RSFSVAAAGF WQVHPLAAET FARAMLDGLA PAAGEVVLDL
YAGAGLFTAL IGERVGLTGR VIGLEADRQA VADAETNLAD LPWCSVRQGK VSAELIADVG
AGCDLVVLDP PRSGAGREIM LAALQLRPRL IGYLACDPSS LARDVATARE AGWELRQLRA
FDAFPMTHHL ECLAVLAPTP TGEHATSATG RRTPVG
//