ID A0A2K5JKN4_COLAP Unreviewed; 417 AA.
AC A0A2K5JKN4;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=tRNA (uracil(54)-C(5))-methyltransferase {ECO:0000256|ARBA:ARBA00033763};
DE EC=2.1.1.35 {ECO:0000256|ARBA:ARBA00033763};
OS Colobus angolensis palliatus (Peters' Angolan colobus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Colobinae; Colobus.
OX NCBI_TaxID=336983 {ECO:0000313|Ensembl:ENSCANP00000029391.1, ECO:0000313|Proteomes:UP000233080};
RN [1] {ECO:0000313|Ensembl:ENSCANP00000029391.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-adenosyl-L-methionine + uridine(54) in tRNA = 5-
CC methyluridine(54) in tRNA + H(+) + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:42712, Rhea:RHEA-COMP:10167, Rhea:RHEA-COMP:10193,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:65315, ChEBI:CHEBI:74447; EC=2.1.1.35;
CC Evidence={ECO:0000256|ARBA:ARBA00033652};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42713;
CC Evidence={ECO:0000256|ARBA:ARBA00033652};
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}.
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DR AlphaFoldDB; A0A2K5JKN4; -.
DR Ensembl; ENSCANT00000052544.1; ENSCANP00000029391.1; ENSCANG00000038293.1.
DR Proteomes; UP000233080; Unplaced.
DR GO; GO:0030697; F:tRNA (uracil(54)-C5)-methyltransferase activity, S-adenosyl methionine-dependent; 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; IPR025714; Methyltranfer_dom.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR045850; TRM2_met.
DR InterPro; IPR025823; TRM2B_chor.
DR InterPro; IPR010280; U5_MeTrfase_fam.
DR PANTHER; PTHR45904; TRNA (URACIL-5-)-METHYLTRANSFERASE; 1.
DR PANTHER; PTHR45904:SF1; TRNA (URACIL-5-)-METHYLTRANSFERASE HOMOLOG B; 1.
DR Pfam; PF13847; Methyltransf_31; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS51687; SAM_MT_RNA_M5U; 1.
DR PROSITE; PS51621; SAM_MT_RNA_M5U_1; 1.
PE 3: Inferred from homology;
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|PROSITE-
KW ProRule:PRU01024}; Reference proteome {ECO:0000313|Proteomes:UP000233080};
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 298..363
FT /note="Methyltransferase"
FT /evidence="ECO:0000259|Pfam:PF13847"
FT ACT_SITE 406
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 278
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 328
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 378
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
SQ SEQUENCE 417 AA; 46749 MW; 3612B16C5E1519CA CRC64;
MAGLKRRVPM HSLRYFISMV GLFSKSGLLP WYARNPPGWS QLFLGTVCKG DFTHVIATKC
QKGQKSQKKP SHLGPLDGSW QERLADVVTP LWRLSYEEQL KPVISGYRNK STFSVNRGPD
GNPKTVGYYL GTWRDGNIVC VQSNNLKNIP EKHSQVAQYY EVFLRQSPLE PCLVFHEGGY
WRELIVRTNS QGHTMAIITF HPQKLSQEEL HVQKEAVKEF FIRGPGAACD LTSLYFQEST
MTRCSHQQSP YQLLFGEPYI FEELLSLKIR ISPDAFFQIN TAGAEMLYRT VGELTGVNSD
TILLDICCGT GVIGLSLAQH TSQVLGIELV EQAVEDARWT AAFNGITNSE FHTGRAEKIL
PGLLKSKEDG QSIVAVVNPA RAGLHYKVIQ AIRNCRAIRT LVFVSCKLHG ESTRNVI
//