ID A0A0A2VSK0_BEABA Unreviewed; 562 AA.
AC A0A0A2VSK0;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=tRNA (Uracil(54)-C(5))-methyltransferase {ECO:0000313|EMBL:KGQ03754.1};
GN ORFNames=BBAD15_g11011 {ECO:0000313|EMBL:KGQ03754.1};
OS Beauveria bassiana D1-5.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Cordycipitaceae; Beauveria.
OX NCBI_TaxID=1245745 {ECO:0000313|EMBL:KGQ03754.1, ECO:0000313|Proteomes:UP000030106};
RN [1] {ECO:0000313|EMBL:KGQ03754.1, ECO:0000313|Proteomes:UP000030106}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=D1-5 {ECO:0000313|EMBL:KGQ03754.1,
RC ECO:0000313|Proteomes:UP000030106};
RA Li Q., Wang L., Zhang Z., Wang Q., Ren J., Wang M., Xu W., Wang J., Lu Y.,
RA Du Q., Sun Z.;
RT "Genome sequencing and analysis of entomopathogenic fungi Beauveria
RT bassiana D1-5.";
RL Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases.
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: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KGQ03754.1}.
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; ANFO01001170; KGQ03754.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0A2VSK0; -.
DR STRING; 1245745.A0A0A2VSK0; -.
DR eggNOG; KOG2187; Eukaryota.
DR HOGENOM; CLU_014689_3_1_1; -.
DR Proteomes; UP000030106; Unassembled WGS sequence.
DR GO; GO:0051908; F:double-stranded DNA 5'-3' exodeoxyribonuclease activity; IEA:EnsemblFungi.
DR GO; GO:0000014; F:single-stranded DNA endodeoxyribonuclease activity; IEA:EnsemblFungi.
DR GO; GO:0030697; F:tRNA (uracil(54)-C5)-methyltransferase activity, S-adenosyl methionine-dependent; IEA:EnsemblFungi.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0006400; P:tRNA modification; IEA:EnsemblFungi.
DR CDD; cd02440; AdoMet_MTases; 1.
DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 2.
DR InterPro; IPR030390; MeTrfase_TrmA_AS.
DR InterPro; IPR030391; MeTrfase_TrmA_CS.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR002792; TRAM_dom.
DR InterPro; IPR025795; tRNA_(uracil-5-)_MeTrfase.
DR InterPro; IPR010280; U5_MeTrfase_fam.
DR PANTHER; PTHR11061; RNA M5U METHYLTRANSFERASE; 1.
DR PANTHER; PTHR11061:SF30; TRNA (URACIL(54)-C(5))-METHYLTRANSFERASE; 1.
DR Pfam; PF01938; TRAM; 1.
DR Pfam; PF05958; tRNA_U5-meth_tr; 1.
DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS51687; SAM_MT_RNA_M5U; 1.
DR PROSITE; PS51622; SAM_MT_RNA_M5U_2; 1.
DR PROSITE; PS50926; TRAM; 1.
DR PROSITE; PS01230; TRMA_1; 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:UP000030106};
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 95..160
FT /note="TRAM"
FT /evidence="ECO:0000259|PROSITE:PS50926"
FT REGION 1..63
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..46
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 512
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10015"
FT ACT_SITE 512
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 376
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 415
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 436
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 485
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
SQ SEQUENCE 562 AA; 61452 MW; AA71A391814F575E CRC64;
MSSAAAAAVA APTTVSAPSG THTNGASHHQ RPAKRPNNAN RNGANRKSKQ QRTKRERNIT
EGSTEEVLRC DIDALLKARG EAASGSETDA AATLEADLPE PYTEIEVEIH ELSSTGDGLG
MVAGSNQVYV VPFTVPGDTA RVKVIRHIRG EGHSHADFVS VVKASPLRDD ARIKCQYFAS
CGGCQFQMLD YAEQLRRKRR IVVKAYDNFS NLPKELIPEI HDTIGSPLQY GYRTKLTPHF
DGPPGFRPGK RGKSQGAAFS ACPDIGFMQK GRRKVLDIED CPIGTEAVRL GNARERRRMQ
DEYTKYVRGA TLLLRENTTR HPKDSEAAKA PLAPHTVKSE VGDFVDVKSC ETDSKATTTE
YIDDYIFTNP AGSFFQNNNS ILPVFTSYIR DRILPTAATT DGSSSPPIKY LIDAYSGSGL
FTITLSSVFQ HSIGIDIAGA SIEYARKNAA LNGLGEDRCR FLAADAGELF RSVTYSADET
VVVLDPPRKG CDASFLAQLR RFGPRRVLYV SCNVHTQARD VGVLVRGEGE GRRYEIESLV
GFDFFPQTGH VEGVAILNRV EE
//
