ID A0A1Y6FPC1_9SPHN Unreviewed; 413 AA.
AC A0A1Y6FPC1;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=23S rRNA m(5)U-1939 methyltransferase {ECO:0000313|EMBL:SMQ74682.1};
GN ORFNames=SAMN06297468_2860 {ECO:0000313|EMBL:SMQ74682.1};
OS Altererythrobacter xiamenensis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Erythrobacteraceae; Altererythrobacter.
OX NCBI_TaxID=1316679 {ECO:0000313|EMBL:SMQ74682.1, ECO:0000313|Proteomes:UP000194420};
RN [1] {ECO:0000313|Proteomes:UP000194420}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Varghese N., Submissions S.;
RL Submitted (APR-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; FXWG01000003; SMQ74682.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y6FPC1; -.
DR Proteomes; UP000194420; 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 CDD; cd02440; AdoMet_MTases; 1.
DR Gene3D; 2.40.50.1070; -; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR030390; MeTrfase_TrmA_AS.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
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; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS51687; SAM_MT_RNA_M5U; 1.
DR PROSITE; PS01230; TRMA_1; 1.
PE 3: Inferred from homology;
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|PROSITE-
KW ProRule:PRU01024}; Reference proteome {ECO:0000313|Proteomes:UP000194420};
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 ACT_SITE 371
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10015"
FT ACT_SITE 371
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 252
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
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 299
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 345
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
SQ SEQUENCE 413 AA; 44697 MW; CEFFD415694461E1 CRC64;
MRYRVLSPPH YEAHHLSDTS EIIRIAAKGD GVTADGKHVS GAVPGDVLRS DGSLDLGPHH
VSPPCRHFGT CGGCQLQHAD EVTLRQFVTD RVLNAAEGQE ITPEEVLETH LSPPRSRRRA
TLHAMRIADG AVLGFRESGS HRIVDLAECH VIAPELFDTI APIRDFVGKH GGKGAVDVEL
TLTDQGVDCG LKNLTVEGLE ATEAALELAQ RNGFARLTLD MGFGPEAMWE PEPVTITLGG
VPVGFPSGSF LQATQDAEAV MIADTREWLQ GASPIADLFS GLGTFAYSLA DPAKLLAVEA
ARDAFLACKS AAGRSGKPVH ALHRDLFRNP LQPDELNRFG AVLLDPPRAG AKDQIDRIAE
STLERVVYVS CNPSSWARDA KRLVEAGFTL KKLRPVGQFR WSTHVELTSY FTR
//
