ID A0A1H1X2Q8_9MICO Unreviewed; 437 AA.
AC A0A1H1X2Q8;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=tRNA/tmRNA/rRNA uracil-C5-methylase, TrmA/RlmC/RlmD family {ECO:0000313|EMBL:SDT03472.1};
GN ORFNames=SAMN04489751_3568 {ECO:0000313|EMBL:SDT03472.1};
OS Brevibacterium sandarakinum.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Brevibacteriaceae;
OC Brevibacterium.
OX NCBI_TaxID=629680 {ECO:0000313|EMBL:SDT03472.1, ECO:0000313|Proteomes:UP000199700};
RN [1] {ECO:0000313|EMBL:SDT03472.1, ECO:0000313|Proteomes:UP000199700}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22082 {ECO:0000313|EMBL:SDT03472.1,
RC ECO:0000313|Proteomes:UP000199700};
RA de Groot N.N.;
RL Submitted (OCT-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}.
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DR EMBL; LT629739; SDT03472.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H1X2Q8; -.
DR STRING; 629680.SAMN04489751_3568; -.
DR Proteomes; UP000199700; 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; IPR030390; MeTrfase_TrmA_AS.
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; 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.
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 7..66
FT /note="TRAM"
FT /evidence="ECO:0000259|PROSITE:PS50926"
FT ACT_SITE 395
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10015"
FT ACT_SITE 395
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 279
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 307
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 329
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 368
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
SQ SEQUENCE 437 AA; 45768 MW; 7C9C9E664B1D0950 CRC64;
MSAHSAEEIP AMDLTLHVES PAAGGSSIAR HEGQVVFVTG AVPGETVRAR TEAGPAAKFL
RADVIEVLDA SEFRVTDRRS RFLAGDAGDR PLFGGMELAH VDLAHSRELK AEVLRDQLSR
IGHIDRSVDV AAAPGENTGL NWRTRVQMAV DNTGRLGMLA PRSHDVVPLA SAPLATSAIA
EVALSSLRLP GADRLEFAWA GDRGAVIVRG QCDPVALTDL AQTLPSQWSI LADARNGTGR
KGAGATGGHT KLAVVRGEDQ LIEEVSGRDY RVAADGFWQV HEQAPQLLSA QVNSALSDQT
RVITDLYCGV GLLGISAASA TGAGLYGVEG AKSAIENAKV NAKGLNANFD ASRADRARIP
KSDVIILDPP RSGAGKAVTR ALLESSATTI VYVSCDAATL ARDLAVLVGG GFAIESLSGF
DLFPLTAHLE TVTVLRR
//
