TRM44_EMENI
ID TRM44_EMENI Reviewed; 606 AA.
AC Q5ASK9; C8VA24;
DT 19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 25-MAY-2022, entry version 77.
DE RecName: Full=tRNA (uracil-O(2)-)-methyltransferase;
DE EC=2.1.1.211;
GN Name=trm44; ORFNames=AN8721;
OS Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS M139) (Aspergillus nidulans).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Nidulantes.
OX NCBI_TaxID=227321;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=16372000; DOI=10.1038/nature04341;
RA Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT fumigatus and A. oryzae.";
RL Nature 438:1105-1115(2005).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA Oliver S.G., Turner G.;
RT "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT effort.";
RL Fungal Genet. Biol. 46:S2-13(2009).
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; AACD01000160; EAA60270.1; -; Genomic_DNA.
DR EMBL; BN001303; CBF78165.1; -; Genomic_DNA.
DR RefSeq; XP_681990.1; XM_676898.1.
DR AlphaFoldDB; Q5ASK9; -.
DR STRING; 162425.CADANIAP00006348; -.
DR EnsemblFungi; CBF78165; CBF78165; ANIA_08721.
DR EnsemblFungi; EAA60270; EAA60270; AN8721.2.
DR GeneID; 2868588; -.
DR KEGG; ani:AN8721.2; -.
DR VEuPathDB; FungiDB:AN8721; -.
DR eggNOG; KOG3790; Eukaryota.
DR HOGENOM; CLU_018580_0_0_1; -.
DR InParanoid; Q5ASK9; -.
DR OMA; WIPLLGY; -.
DR OrthoDB; 1146281at2759; -.
DR Proteomes; UP000000560; Chromosome III.
DR Proteomes; UP000005890; Unassembled WGS sequence.
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 InterPro; IPR011671; tRNA_uracil_MeTrfase.
DR PANTHER; PTHR21210; PTHR21210; 1.
DR Pfam; PF07757; AdoMet_MTase; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Methyltransferase; Reference proteome; S-adenosyl-L-methionine;
KW Transferase; tRNA processing.
FT CHAIN 1..606
FT /note="tRNA (uracil-O(2)-)-methyltransferase"
FT /id="PRO_0000249905"
FT REGION 455..489
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 537..606
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 545..561
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 562..600
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 606 AA; 67778 MW; 88FB8AF6DF603F94 CRC64;
MARALALSRS VQVCKSRLFT VASKSAITKR CLSNPIQYRS VSLFATTYAP SKDLNSRLHS
EHIGDTALYL LLNPGLTSSV LFRADILAQS GKCPTLAALE AQKQQETEEA STATAMTMAQ
NVIEEEKEVK EPVVEIPARE VPGFELHKTL IRRLIPRNQQ LDMPVDQTCH LYSHAGAVEQ
IEKEKELGIP HSRAPKERFM VIYTPHVSSK EELPYYHPLV RSMAFVYEFG YTGEFEGPEN
SIPRIAENPK GTMSIHFLPY ENDVDSISAR LERSLTKLIE VQIRTTKGRL DPCRPSTSSP
YALIKDNVIP RNRVQDTYSR LKNKYAANLN ERWIESTEPS KHVFEDLSIA AFLIELWRDL
YGAVPGDERE QQKQQSSTSK VGSGQFPGFV DIACGNGVLV YILISEGYSG WGFDARRRKT
WSIFPTDVQE RLKEEIYIPK PFMDVLAAQN QGPIQNKNQD ASMQSPLSEP QSGQSNGPNS
GTSTSTSLSN LPKDTFIISN HADELTLWTP ILSTLLNPAN PPPFLAIPCC SHSLSGARHR
FRPQSARPSA TQNPQKQQGE NGTHSQDEEG SSEDMKERKG EEKEKNPETG DLEQMRKDKL
AAQNPH
