ID T1L421_TETUR Unreviewed; 448 AA.
AC T1L421;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 24-JAN-2024, entry version 45.
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=107370079 {ECO:0000313|EnsemblMetazoa:tetur37g00500.1};
OS Tetranychus urticae (Two-spotted spider mite).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC Acariformes; Trombidiformes; Prostigmata; Eleutherengona; Raphignathae;
OC Tetranychoidea; Tetranychidae; Tetranychus.
OX NCBI_TaxID=32264 {ECO:0000313|EnsemblMetazoa:tetur37g00500.1, ECO:0000313|Proteomes:UP000015104};
RN [1] {ECO:0000313|Proteomes:UP000015104}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=London {ECO:0000313|Proteomes:UP000015104};
RA Rombauts S.;
RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:tetur37g00500.1}
RP IDENTIFICATION.
RG EnsemblMetazoa;
RL Submitted (JUN-2015) 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 EMBL; CAEY01001062; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_015793546.1; XM_015938060.1.
DR AlphaFoldDB; T1L421; -.
DR STRING; 32264.T1L421; -.
DR EnsemblMetazoa; tetur37g00500.1; tetur37g00500.1; tetur37g00500.
DR GeneID; 107370079; -.
DR KEGG; tut:107370079; -.
DR eggNOG; KOG2187; Eukaryota.
DR HOGENOM; CLU_014689_4_0_1; -.
DR OMA; DQMLPLW; -.
DR OrthoDB; 120922at2759; -.
DR Proteomes; UP000015104; Unassembled WGS sequence.
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; 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; IPR030391; MeTrfase_TrmA_CS.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR045850; TRM2_met.
DR InterPro; IPR010280; U5_MeTrfase_fam.
DR PANTHER; PTHR45904:SF1; TRNA (URACIL(54)-C(5))-METHYLTRANSFERASE HOMOLOG; 1.
DR PANTHER; PTHR45904; TRNA (URACIL-5-)-METHYLTRANSFERASE; 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; 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:UP000015104};
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 288..354
FT /note="Methyltransferase"
FT /evidence="ECO:0000259|Pfam:PF13847"
FT ACT_SITE 394
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 267
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 317
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 366
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
SQ SEQUENCE 448 AA; 50356 MW; 23F80CFB649CD71A CRC64;
MKNVSQSIKT IGSMRRKSFP VDQKMNNLTK FKGLTPLAGF SYSKQLDIKQ KRTSQILETL
TDKLKGMNSS VIPDERGLPC LLERIVASPV TKGYRNTDDF SIWPGLDKNP KTVGYIMGKA
SNSNKIPVCL PPDDCVIVKD SHKILVSKFQ QYLRNHSPLG ICMDFSRGGN WRRFCVRSND
FDELMGIAIL HPQKLSSKEL KEEQNRLKDF FIPISQDINL KSFYFQACPG VRCTNRRAPF
ELLFGDEHID EVINGTKIRI TPEPFLQVNK GAAEMLYRQI IEEIEPQSDM TILDMCCGSG
ILAIQLAPLV EKVIGVDSCE EAIKDAKMNA QTNNITNCNF IHGTMEDYMV KISEDLYSDD
LVMVVNPGSG GLPSGVVNVI RTMSNVSKLI YVSCKPEGQA LKNFAHLCLP YRPNDDIQGD
PFIPVKAIPF DLFPQTERVE LLVSFSRI
//