ID D5V7E7_ARCNC Unreviewed; 373 AA.
AC D5V7E7;
DT 13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT 13-JUL-2010, sequence version 1.
DT 27-MAR-2024, entry version 77.
DE SubName: Full=tRNA (Uracil-5-)-methyltransferase {ECO:0000313|EMBL:ADG94567.1};
DE EC=2.1.1.35 {ECO:0000313|EMBL:ADG94567.1};
GN OrderedLocusNames=Arnit_2919 {ECO:0000313|EMBL:ADG94567.1};
OS Arcobacter nitrofigilis (strain ATCC 33309 / DSM 7299 / CCUG 15893 / LMG
OS 7604 / NCTC 12251 / CI) (Campylobacter nitrofigilis).
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Arcobacteraceae; Arcobacter.
OX NCBI_TaxID=572480 {ECO:0000313|EMBL:ADG94567.1, ECO:0000313|Proteomes:UP000000939};
RN [1] {ECO:0000313|EMBL:ADG94567.1, ECO:0000313|Proteomes:UP000000939}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33309 / DSM 7299 / CCUG 15893 / LMG 7604 / NCTC 12251 / CI
RC {ECO:0000313|Proteomes:UP000000939};
RX PubMed=21304714; DOI=10.4056/sigs.912121;
RA Pati A., Gronow S., Lapidus A., Copeland A., Glavina Del Rio T., Nolan M.,
RA Lucas S., Tice H., Cheng J.F., Han C., Chertkov O., Bruce D., Tapia R.,
RA Goodwin L., Pitluck S., Liolios K., Ivanova N., Mavromatis K., Chen A.,
RA Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D., Detter J.C.,
RA Rohde M., Goker M., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA Klenk H.P., Kyrpides N.C.;
RT "Complete genome sequence of Arcobacter nitrofigilis type strain (CI).";
RL Stand. Genomic Sci. 2:300-308(2010).
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. RNA M5U methyltransferase family. {ECO:0000256|PROSITE-
CC 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; CP001999; ADG94567.1; -; Genomic_DNA.
DR RefSeq; WP_013136712.1; NC_014166.1.
DR AlphaFoldDB; D5V7E7; -.
DR STRING; 572480.Arnit_2919; -.
DR KEGG; ant:Arnit_2919; -.
DR eggNOG; COG2265; Bacteria.
DR HOGENOM; CLU_043022_0_0_7; -.
DR OrthoDB; 9804590at2; -.
DR Proteomes; UP000000939; Chromosome.
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: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; 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.
PE 3: Inferred from homology;
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|PROSITE-
KW ProRule:PRU01024}; Reference proteome {ECO:0000313|Proteomes:UP000000939};
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 330
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10015"
FT ACT_SITE 330
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 197
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 224
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 245
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 305
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
SQ SEQUENCE 373 AA; 43790 MW; 1100D8849C28F67F CRC64;
MTCDYFGKCG SCTLYHMNYE EQLAYKLSRE KQRFQDITTM DFEIIRSEEE HFRNRAEFRF
WKNYDDEKNP TLSYGMTSFD KNILEVDKCS IVSKQIDELM PKLLDEISQS EILNYKIYSV
EFLGSTTNDM LVTLIYHKKL DTTWEKVAKE VQERLNIKII GRSRKQKIVL KEDFIKEELN
INDNVFKFHY KEGGFTQPNT KVNIKMIEWV LNNIETKDDL CELYCGGGNF TIPLSTKFNK
VLATEISKTS INSALLNCEL NNITNIDFIR MSAEEFVEAL NSVREFRRLK DINLSDYNFS
TIFVDPPRSG LDDTTRELVK NYEQIIYISC NPETLHRDLK ELIKSHQILN FSLFDQFSYS
GHIETGVILK KSC
//
