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Database: UniProt
Entry: A0A268TBI1_9HELI
LinkDB: A0A268TBI1_9HELI
Original site: A0A268TBI1_9HELI 
ID   A0A268TBI1_9HELI        Unreviewed;       369 AA.
AC   A0A268TBI1;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   SubName: Full=tRNA (Uridine(54)-C5)-methyltransferase TrmA {ECO:0000313|EMBL:PAF42053.1};
GN   ORFNames=BKH45_05595 {ECO:0000313|EMBL:PAF42053.1};
OS   Helicobacter sp. 11S03491-1.
OC   Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=1476196 {ECO:0000313|EMBL:PAF42053.1, ECO:0000313|Proteomes:UP000216568};
RN   [1] {ECO:0000313|EMBL:PAF42053.1, ECO:0000313|Proteomes:UP000216568}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=11S03491-1 {ECO:0000313|EMBL:PAF42053.1,
RC   ECO:0000313|Proteomes:UP000216568};
RX   PubMed=28827684; DOI=10.1038/s41598-017-09091-7;
RA   Gilbert M.J., Duim B., Timmerman A.J., Zomer A.L., Wagenaar J.A.;
RT   "Whole genome-based phylogeny of reptile-associated Helicobacter indicates
RT   independent niche adaptation followed by diversification in a
RT   poikilothermic host.";
RL   Sci. Rep. 7:8387-8387(2017).
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:PAF42053.1}.
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DR   EMBL; MLAO01000006; PAF42053.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A268TBI1; -.
DR   OrthoDB; 9804590at2; -.
DR   Proteomes; UP000216568; Unassembled WGS sequence.
DR   GO; GO:0030697; F:tRNA (uracil(54)-C5)-methyltransferase activity, S-adenosyl methionine-dependent; IEA:UniProtKB-EC.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   GO; GO:0009451; P:RNA modification; IEA:UniProt.
DR   GO; GO:0008033; P:tRNA processing; IEA:UniProtKB-KW.
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   HAMAP; MF_01011; RNA_methyltr_TrmA; 1.
DR   InterPro; IPR030390; MeTrfase_TrmA_AS.
DR   InterPro; IPR030391; MeTrfase_TrmA_CS.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   InterPro; IPR011869; TrmA_MeTrfase.
DR   InterPro; IPR010280; U5_MeTrfase_fam.
DR   NCBIfam; TIGR02143; trmA_only; 1.
DR   PANTHER; PTHR47790; TRNA/TMRNA (URACIL-C(5))-METHYLTRANSFERASE; 1.
DR   PANTHER; PTHR47790:SF2; TRNA_TMRNA (URACIL-C(5))-METHYLTRANSFERASE; 1.
DR   Pfam; PF05958; tRNA_U5-meth_tr; 1.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR   PROSITE; PS51687; SAM_MT_RNA_M5U; 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:UP000216568};
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}; tRNA processing {ECO:0000256|ARBA:ARBA00022694}.
FT   ACT_SITE        327
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10015"
FT   ACT_SITE        327
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         191
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         220
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         241
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         301
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
SQ   SEQUENCE   369 AA;  42985 MW;  FD508D6C9728445B CRC64;
     MICENFLECG GCQIDQDYHV QFSQKFQIFQ SLFEHKIQDL EIFYSPPTGF RARGEFRLHR
     ENSKVYLSMN TYGKNNRVKI SSCPILLPIL QEKLEILLAF INTDHLLEHK LYGIKILGGL
     SGDSVITLIY HKKLDNLWEE SATRLSQDMR CSLIGRSRGQ KIIIGKDYIR ESLWIGQQNY
     FYIHQESGFS QPNPYTNIQM IEFVLSKLPP AFQSDMLEMY CGSGNFTIPL AKRFQKVFAT
     EVVKSSIQTL KINAVNNNVQ NIIASRLSGL ETLEALSYKR DFFRLRKVCL EDFNFSHIFL
     DPPRSGIKDP QMLAFIQKFK HIIYISCNPF SLKQDFATLL QTHRIKHSAL FDQFPYTHHL
     ECGFMLERF
//
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