ID R0JXQ5_ANAPL Unreviewed; 597 AA.
AC R0JXQ5;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE RecName: Full=tRNA (uracil(54)-C(5))-methyltransferase {ECO:0000256|ARBA:ARBA00033763};
DE EC=2.1.1.35 {ECO:0000256|ARBA:ARBA00033763};
DE Flags: Fragment;
GN ORFNames=Anapl_02412 {ECO:0000313|EMBL:EOB02351.1};
OS Anas platyrhynchos (Mallard) (Anas boschas).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Anseriformes; Anatidae;
OC Anatinae; Anas.
OX NCBI_TaxID=8839 {ECO:0000313|EMBL:EOB02351.1, ECO:0000313|Proteomes:UP000296049};
RN [1] {ECO:0000313|Proteomes:UP000296049}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23749191; DOI=10.1038/ng.2657;
RA Huang Y., Li Y., Burt D.W., Chen H., Zhang Y., Qian W., Kim H., Gan S.,
RA Zhao Y., Li J., Yi K., Feng H., Zhu P., Li B., Liu Q., Fairley S.,
RA Magor K.E., Du Z., Hu X., Goodman L., Tafer H., Vignal A., Lee T.,
RA Kim K.W., Sheng Z., An Y., Searle S., Herrero J., Groenen M.A.,
RA Crooijmans R.P., Faraut T., Cai Q., Webster R.G., Aldridge J.R.,
RA Warren W.C., Bartschat S., Kehr S., Marz M., Stadler P.F., Smith J.,
RA Kraus R.H., Zhao Y., Ren L., Fei J., Morisson M., Kaiser P., Griffin D.K.,
RA Rao M., Pitel F., Wang J., Li N.;
RT "The duck genome and transcriptome provide insight into an avian influenza
RT virus reservoir species.";
RL Nat. Genet. 45:776-783(2013).
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; KB742969; EOB02351.1; -; Genomic_DNA.
DR AlphaFoldDB; R0JXQ5; -.
DR Proteomes; UP000296049; Unassembled WGS sequence.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008173; F:RNA methyltransferase activity; 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 CDD; cd12439; RRM_TRMT2A; 1.
DR Gene3D; 2.40.50.1070; -; 1.
DR Gene3D; 3.30.70.330; -; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
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; PF00076; RRM_1; 1.
DR Pfam; PF05958; tRNA_U5-meth_tr; 1.
DR SMART; SM00360; RRM; 1.
DR SUPFAM; SSF54928; RNA-binding domain, RBD; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS50102; RRM; 1.
DR PROSITE; PS51687; SAM_MT_RNA_M5U; 1.
PE 3: Inferred from homology;
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|PROSITE-
KW ProRule:PRU01024}; Reference proteome {ECO:0000313|Proteomes:UP000296049};
KW RNA-binding {ECO:0000256|PROSITE-ProRule:PRU00176};
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 18..90
FT /note="RRM"
FT /evidence="ECO:0000259|PROSITE:PS50102"
FT REGION 89..113
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 546..597
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 96..113
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 548..587
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 489
FT /note="Nucleophile"
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"
FT BINDING 412
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 461
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:EOB02351.1"
FT NON_TER 597
FT /evidence="ECO:0000313|EMBL:EOB02351.1"
SQ SEQUENCE 597 AA; 66813 MW; E2C7B55DDB2D21C1 CRC64;
GPDVYGYTKG ELFTSEIYKV EIQNLPKYIG FNDVKKFLAK YGRPHKIKLF GRQTFAFVTF
KSEEERDKAA RALHGVLWKG RALSVRLAKP KADPMAKKRK KAEGSEAGEA KREPLSKQIA
DVVTPLWSVP YAEQLARKKQ ECEQVLQKLA KEIGNNNRAL LPWLFVQKQK YNKMCCPVEG
VKASPLQTEY RNKCEFLIGI GVNQEDKTVG CRLGKYKGGT CAVVEPFDTI HIPAIAKKVV
KAFQDYIRST PYSVYSPETY EGHWKQLTVR TSRNGHIMAI VYFNPQKLSK EELADLKVSL
AKYFTEGMGR DSGITSLYFV EEGQRKSPNL EDLPLEHVAG DKYIYEELLG LKFRISPHAF
FQVNTQAAEV LYTAIREWAQ LSQESTVLDI CCGTGTIGIS LAKKVKKVIG IELCQEAVQD
AKANAQINEL NNIEFHCGKA EDIVPSLINI LAPQNLITIV DPPRAGLHSK VILAIRRAEQ
LKKLIYVSCN PRAAMNNFID LCRAPSNRVK GASFRPVKAM AVDLFPQTRH CELLIFFERV
EYTNGSSAEA KPDDTQVTTA GCDSECLDST NPSNVDASQT TSMDTCIDTS SKEREST
//
