ID G3TPA2_LOXAF Unreviewed; 616 AA.
AC G3TPA2;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 66.
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=TRMT2A {ECO:0000313|Ensembl:ENSLAFP00000017193.2};
OS Loxodonta africana (African elephant).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Afrotheria; Proboscidea; Elephantidae; Loxodonta.
OX NCBI_TaxID=9785 {ECO:0000313|Ensembl:ENSLAFP00000017193.2, ECO:0000313|Proteomes:UP000007646};
RN [1] {ECO:0000313|Ensembl:ENSLAFP00000017193.2, ECO:0000313|Proteomes:UP000007646}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000017193.2,
RC ECO:0000313|Proteomes:UP000007646};
RA Di Palma F., Heiman D., Young S., Johnson J., Lander E.S., Lindblad-Toh K.;
RT "The Genome Sequence of Loxodonta africana (African elephant).";
RL Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLAFP00000017193.2}
RP IDENTIFICATION.
RC STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000017193.2};
RG Ensembl;
RL Submitted (NOV-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; G3TPA2; -.
DR STRING; 9785.ENSLAFP00000017193; -.
DR Ensembl; ENSLAFT00000021599.2; ENSLAFP00000017193.2; ENSLAFG00000022939.2.
DR eggNOG; KOG2187; Eukaryota.
DR GeneTree; ENSGT00530000063723; -.
DR HOGENOM; CLU_014689_4_2_1; -.
DR InParanoid; G3TPA2; -.
DR OMA; TPLWNMP; -.
DR TreeFam; TF314569; -.
DR Proteomes; UP000007646; Unassembled WGS sequence.
DR GO; GO:0008169; F:C-methyltransferase activity; IEA:Ensembl.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0030697; F:tRNA (uracil(54)-C5)-methyltransferase activity, S-adenosyl methionine-dependent; IEA:Ensembl.
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; 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; 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:UP000007646};
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 64..137
FT /note="RRM"
FT /evidence="ECO:0000259|PROSITE:PS50102"
FT REGION 1..43
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 136..155
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 586..616
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 138..155
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 593..616
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 529
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 402
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 452
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 501
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
SQ SEQUENCE 616 AA; 67837 MW; FE72460E7B7CEB1F CRC64;
MSETHENEVK GPMESCGQDD SSTLGSPMAP APQEEEGTGA AAVTRPGTGL YSYIREDLFT
SEIFKLELQN VPRHASFSDV RRFLGRFGLQ PHKTKLFGQP PCAFVTFRSA AERDKALRVL
HGALWKGRPL SVRLARPKAD PMAKRRRREG EGEPPVTHIA DVVTPLWTVP YAEQLERKRL
ECEQVLQRLA KEIGSTNRAL LPWLLTQRHK HNKACCPLEG VRPSPLQTEY RNKCEFLVGV
GVDGEDNTVG CRLGRYKGGT CAVAAPFETM HIPEAAKQVV RAFQEFIRST PYSAYDPETY
AGYWKQLTVR TSRRGQAMAI AYFHPQKLSQ EELAGLKTCL AQHFTEGPGK ASGVTCLYFV
EEGQRKTPSQ EGLPLEHMAG DRYIHEDLLG LTFQISPHAF FQVNTPAAEV LYTVIQDWAQ
LDAESTVLDV CCGTGTIGLA LARKVKKVVG IELCQEAVED ARVNACMNKL SNVEFHCGRA
EDLVATLVSR LATQQLIAIL DPPRAGLHSK VILAIRRAAN LKRLLYVSCN PRAAMSNFVD
LCRAPSNRVK GTPFRPVKAV AVDLFPQTPH CEMLILFERV DYPNGAGAQD PSVLPPPSSP
GPPDGTLQQP GAPPSS
//
