TRM44_ASHGO
ID TRM44_ASHGO Reviewed; 531 AA.
AC Q751E7;
DT 19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=tRNA (uracil-O(2)-)-methyltransferase;
DE EC=2.1.1.211;
GN Name=TRM44; OrderedLocusNames=AGL241W;
OS Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS (Yeast) (Eremothecium gossypii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX NCBI_TaxID=284811;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=15001715; DOI=10.1126/science.1095781;
RA Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA Gaffney T.D., Philippsen P.;
RT "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT cerevisiae genome.";
RL Science 304:304-307(2004).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=23749448; DOI=10.1534/g3.112.002881;
RA Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT loci, numerous translocations, lack of transposons, and distinct gene
RT duplications.";
RL G3 (Bethesda) 3:1225-1239(2013).
CC -!- FUNCTION: Probable adenosyl-L-methionine (AdoMet)-dependent tRNA
CC (uracil-O(2)-)-methyltransferase. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-adenosyl-L-methionine + uridine(44) in tRNA(Ser) = 2'-O-
CC methyluridine(44) in tRNA(Ser) + H(+) + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:43100, Rhea:RHEA-COMP:10339, Rhea:RHEA-COMP:10340,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:65315, ChEBI:CHEBI:74478; EC=2.1.1.211;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the TRM44 family. {ECO:0000305}.
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DR EMBL; AE016820; AAS54250.1; -; Genomic_DNA.
DR RefSeq; NP_986426.1; NM_211488.1.
DR AlphaFoldDB; Q751E7; -.
DR STRING; 33169.AAS54250; -.
DR EnsemblFungi; AAS54250; AAS54250; AGOS_AGL241W.
DR GeneID; 4622719; -.
DR KEGG; ago:AGOS_AGL241W; -.
DR eggNOG; KOG3790; Eukaryota.
DR HOGENOM; CLU_018580_2_0_1; -.
DR InParanoid; Q751E7; -.
DR OMA; WIPLLGY; -.
DR Proteomes; UP000000591; Chromosome VII.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016300; F:tRNA (uracil) methyltransferase activity; IBA:GO_Central.
DR GO; GO:0052665; F:tRNA (uracil-2'-O-)-methyltransferase activity; IEA:RHEA.
DR GO; GO:0030488; P:tRNA methylation; IBA:GO_Central.
DR GO; GO:0002128; P:tRNA nucleoside ribose methylation; IEA:EnsemblFungi.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR011671; tRNA_uracil_MeTrfase.
DR PANTHER; PTHR21210; PTHR21210; 1.
DR Pfam; PF07757; AdoMet_MTase; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Methyltransferase; Reference proteome; S-adenosyl-L-methionine;
KW Transferase; tRNA processing.
FT CHAIN 1..531
FT /note="tRNA (uracil-O(2)-)-methyltransferase"
FT /id="PRO_0000249900"
SQ SEQUENCE 531 AA; 59306 MW; 7F4C5196336FCA49 CRC64;
MTFEFCGGES SILGGAWVCI YQTAEDVGFQ REHFEQAMDN VIRHPNINST VLLRADIVAE
REYDCRTGEA VRDGNCGAAA DVAEGMLSVG LEDVAARSVH TELDLAVKLE FVRRLVPRNP
YKDALINQTC LVLNTREPSE TALVVYLPHF SEREDCPFYI PPVAAVGILL HGGRLSVHYI
PFAGEGAALA DEGQRAVRTA RRLLQTAEKH SKGCMNGYTK RVEHDVVVDK VLFQERYIQL
KKKYSQWLVD NWAESTDPRK HVFEDIAIAA FLIELWSKIY GQHAEDKFRF CDMGCGNGVL
CYILLMEGYA GEGIDARRRK SWGMFPENVR SCLKEQLVIP SLLLRPHPEI RKMASHMEHN
GGFFPVHVSS SQLMAPATIV YSAADLITSP QVNIAEFPPN TFLIGNHSDE LTCWIPLLGQ
PFMVIPCCSH NFHGARVRYR PSRESATRLG NSTYAGLVDY VEYLAKAVGW ETEKEMLRIP
STRNAAIIGY KNPALGQFPT QQVYDEVLKN GGAEGWIQSA TALLKGTPKS H