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Database: UniProt
Entry: A0A2K5JKN4_COLAP
LinkDB: A0A2K5JKN4_COLAP
Original site: A0A2K5JKN4_COLAP 
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
//
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