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Database: UniProt
Entry: A0A2K6EBF8_MACNE
LinkDB: A0A2K6EBF8_MACNE
Original site: A0A2K6EBF8_MACNE 
ID   A0A2K6EBF8_MACNE        Unreviewed;       443 AA.
AC   A0A2K6EBF8;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   RecName: Full=tRNA (uracil(54)-C(5))-methyltransferase {ECO:0000256|ARBA:ARBA00033763};
DE            EC=2.1.1.35 {ECO:0000256|ARBA:ARBA00033763};
GN   Name=TRMT2B {ECO:0000313|Ensembl:ENSMNEP00000045501.1};
OS   Macaca nemestrina (Pig-tailed macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9545 {ECO:0000313|Ensembl:ENSMNEP00000045501.1, ECO:0000313|Proteomes:UP000233120};
RN   [1] {ECO:0000313|Ensembl:ENSMNEP00000045501.1}
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; A0A2K6EBF8; -.
DR   Ensembl; ENSMNET00000070013.1; ENSMNEP00000045501.1; ENSMNEG00000045257.1.
DR   GeneTree; ENSGT00530000063723; -.
DR   OMA; LHYRVIR; -.
DR   Proteomes; UP000233120; Unplaced.
DR   Bgee; ENSMNEG00000045257; Expressed in heart and 12 other cell types or tissues.
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:UP000233120};
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          282..347
FT                   /note="Methyltransferase"
FT                   /evidence="ECO:0000259|Pfam:PF13847"
FT   ACT_SITE        390
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         262
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         312
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         362
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
SQ   SEQUENCE   443 AA;  49861 MW;  915933DF281BB15B CRC64;
     MNSRCSVHIY IIKELPELFY SRLADVVTPL WRLSYEEQLK VKFEAQKKIL QRLESYIQML
     NGVNVTTAVP KSESLPCLLH PIIPSPVING YRNKSTFSVN RGPDGNPKTV GYYLGTWRDG
     NIVCVRSNNL KNIPEKHSQV AQYYEVFLRQ SPLEPCLVFH EGGYWRELIV RTNSQGHTMA
     IITFHPQKLS QEELHVQKET VKEFFIRGPG AACDLTSLYF QESTMTRCSH QQSPYQLLFG
     EPYIFEELLS LKIRISPDAF FQINTAGAEM LYRTVGELTG VNSDTILLDI CCGTGVIGLS
     LAQHTSQVLG IELVEQAVED ARWTAAFNGI TNSEFHTGRA EKILPGLLKS KEDGQSVVAV
     VNPARAGLHY KVIQAIRNCR AIRTLVFVSC KLHGESTRNI IELCCPPDSA KKLLGEPFVL
     QQAVPVDLFP HTPHCELVLL FTR
//
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