ID A0A091VCL4_NIPNI Unreviewed; 465 AA.
AC A0A091VCL4;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 26.
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=Y956_07997 {ECO:0000313|EMBL:KFR00163.1};
OS Nipponia nippon (Crested ibis) (Ibis nippon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Pelecaniformes; Threskiornithidae;
OC Nipponia.
OX NCBI_TaxID=128390 {ECO:0000313|EMBL:KFR00163.1, ECO:0000313|Proteomes:UP000053283};
RN [1] {ECO:0000313|EMBL:KFR00163.1, ECO:0000313|Proteomes:UP000053283}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_Y956 {ECO:0000313|EMBL:KFR00163.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KL410835; KFR00163.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091VCL4; -.
DR STRING; 128390.A0A091VCL4; -.
DR eggNOG; KOG2187; Eukaryota.
DR Proteomes; UP000053283; Unassembled WGS sequence.
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:UP000053283};
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 306..369
FT /note="Methyltransferase"
FT /evidence="ECO:0000259|Pfam:PF13847"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 9..23
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 412
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 284
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 334
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 384
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:KFR00163.1"
FT NON_TER 465
FT /evidence="ECO:0000313|EMBL:KFR00163.1"
SQ SEQUENCE 465 AA; 51535 MW; 948E93B841B866E3 CRC64;
RHLRPSSALL SSLPGQGRSL PTEKTATKWK EKKKAREGCR VPGCSWEERL ANVVTPLWRL
AYQEQLQVKY ESQRKILQTL ASRLEDLGIA AQKPGGLCCP LQPVVPSPVI NGYRNKSTFS
VNRGPDGNPK TVGLYVGTGR ARNIVCVKAN HMENIPPKHK QVAQCYEEFI RRSPLDPCIL
FHEGGHWREL VVRTTSCGQT MAIITFHPQE LGQEALATQK ALLKGFFTCG PGRVCDLTSL
YFQESTMTRC SHEQSPFQLL HGEPHIFEEV LGLKFRISPD AFFQVNRGGA EVLYQAVGEL
SQAGGDTVLL DICCGTGTIG LSLAHRVSKI IGIEVVEKAI EDARWNAAFN GISNCEFHSG
KAEAVLPQLL SSWEDARPLL AVVNPSRAGL HYRVVRAIRN CKSVRRLLYI SCKPEGEAMR
NFLELCCPSD PGKKLAGEPF APTLAIPFDM FPHTVHCELV LLFTR
//
