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Database: UniProt
Entry: A0A074ZZ00_9TREM
LinkDB: A0A074ZZ00_9TREM
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ID   A0A074ZZ00_9TREM        Unreviewed;       672 AA.
AC   A0A074ZZ00;
DT   01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2014, sequence version 1.
DT   24-JAN-2024, entry version 31.
DE   RecName: Full=tRNA (uracil(54)-C(5))-methyltransferase {ECO:0000256|ARBA:ARBA00033763};
DE            EC=2.1.1.35 {ECO:0000256|ARBA:ARBA00033763};
GN   ORFNames=T265_02521 {ECO:0000313|EMBL:KER31197.1};
OS   Opisthorchis viverrini.
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Trematoda;
OC   Digenea; Opisthorchiida; Opisthorchiata; Opisthorchiidae; Opisthorchis.
OX   NCBI_TaxID=6198 {ECO:0000313|EMBL:KER31197.1, ECO:0000313|Proteomes:UP000054324};
RN   [1] {ECO:0000313|EMBL:KER31197.1, ECO:0000313|Proteomes:UP000054324}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Young N.D., Nagarajan N., Lin S.J., Korhonen P.K., Jex A.R., Hall R.S.,
RA   Safavi-Hemami H., Kaewkong W., Bertrand D., Gao S., Seet Q., Wongkham S.,
RA   Teh B.T., Wongkham C., Intapan P.M., Maleewong W., Yang X., Hu M., Wang Z.,
RA   Hofmann A., Sternberg P.W., Tan P., Wang J., Gasser R.B.;
RT   "Opisthorchis viverrini - life in the bile duct.";
RL   Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
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   EMBL; KL596649; KER31197.1; -; Genomic_DNA.
DR   RefSeq; XP_009165048.1; XM_009166784.1.
DR   AlphaFoldDB; A0A074ZZ00; -.
DR   STRING; 6198.A0A074ZZ00; -.
DR   GeneID; 20316709; -.
DR   KEGG; ovi:T265_02521; -.
DR   CTD; 20316709; -.
DR   OrthoDB; 120922at2759; -.
DR   Proteomes; UP000054324; Unassembled WGS sequence.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0008173; F:RNA methyltransferase activity; IEA:InterPro.
DR   GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IEA:InterPro.
DR   GO; GO:0001510; P:RNA methylation; IEA:GOC.
DR   GO; GO:0006396; P:RNA processing; IEA:InterPro.
DR   CDD; cd12439; RRM_TRMT2A; 1.
DR   Gene3D; 2.40.50.1070; -; 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 2.
DR   InterPro; IPR030391; MeTrfase_TrmA_CS.
DR   InterPro; IPR035979; RBD_domain_sf.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   InterPro; IPR045850; TRM2_met.
DR   InterPro; IPR034262; TRMT2A_RRM.
DR   InterPro; IPR010280; U5_MeTrfase_fam.
DR   PANTHER; PTHR45904; TRNA (URACIL-5-)-METHYLTRANSFERASE; 1.
DR   PANTHER; PTHR45904:SF2; TRNA (URACIL-5-)-METHYLTRANSFERASE HOMOLOG A; 1.
DR   Pfam; PF05958; tRNA_U5-meth_tr; 1.
DR   SUPFAM; SSF54928; RNA-binding domain, RBD; 1.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR   PROSITE; PS51687; SAM_MT_RNA_M5U; 1.
DR   PROSITE; PS01231; TRMA_2; 1.
PE   3: Inferred from homology;
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|PROSITE-
KW   ProRule:PRU01024}; Reference proteome {ECO:0000313|Proteomes:UP000054324};
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        615
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         487
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         511
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         587
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
SQ   SEQUENCE   672 AA;  75784 MW;  D9EE44141F36B416 CRC64;
     MLHWSTNEAS NRKALLELTH WFRRELTDLK ASGSNSTSAS RLHFSGLGQP STEVTAEQAN
     SLDPSVLPDT VEQPNIKCDC FRLLHTGQSI ASRPQRPGCD HPDCPYQYLQ RDTFTSEAYK
     IQLKNIHKYT GFKQLKKLLD SLNVKYRKVK LLPEVTFITF CTIEDRDAAI AILDGYVWRG
     KSFEAKVAIG KADPLLHKRH ATADGFEAAG GKRTCVSEAL SSADQADRLR DIVTPLYRLP
     YNPDQLLEKN NHVISILALM RTRLIESNPS ISDSLLTLGL QRDSSDKLCA CPLLEIVPSP
     ITAEYRNKSE LTIGCDLEGQ GPIVGFRLTK YRDGLTAVGS FHHVDILPKS TVSILDEVQR
     FIDSFRNVQS ESRCPTLTTY DPITHSGHWR HLLIRESRLG DLLLLLDIHP QQLKQEEMDY
     LCERFRNWFV DNSGQVDPKV TSLYFSTRRN TSEKFDTSNT RLLFGKDHIV EKCCGLEFRI
     SLDAFFQVNT LAAELLYEEV SKFASGAYDN FSGTHSNTDC SQSDKDQPST PASDCHRTTY
     LLDICCGTGT IALCIENAQF YAGQADKVLF DVMSTIPKES NIVAVVDPPR SGIRNTVIQT
     LRRCTRLERI VYVSCNLEAA MQDFIDFARP TSNRFQGAPF IPTLARPVDL FPQTRHVEVV
     ILLQRIRYPQ TS
//
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