ID A0A0A2KUU6_PENIT Unreviewed; 383 AA.
AC A0A0A2KUU6;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=tRNA (uracil-O(2)-)-methyltransferase {ECO:0000256|ARBA:ARBA00017788, ECO:0000256|RuleBase:RU368004};
DE EC=2.1.1.211 {ECO:0000256|ARBA:ARBA00012795, ECO:0000256|RuleBase:RU368004};
GN ORFNames=PITC_053930 {ECO:0000313|EMBL:KGO68140.1};
OS Penicillium italicum (Blue mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=40296 {ECO:0000313|EMBL:KGO68140.1, ECO:0000313|Proteomes:UP000030104};
RN [1] {ECO:0000313|EMBL:KGO68140.1, ECO:0000313|Proteomes:UP000030104}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PHI-1 {ECO:0000313|EMBL:KGO68140.1,
RC ECO:0000313|Proteomes:UP000030104};
RX PubMed=25338147; DOI=10.1094/MPMI-09-14-0261-FI;
RA Ballester A.R., Marcet-Houben M., Levin E., Sela N., Selma-Lazaro C.,
RA Carmona L., Wisniewski M., Droby S., Gonzalez-Candelas L., Gabaldon T.;
RT "Genome, transcriptome, and functional analyses of Penicillium expansum
RT provide new insights into secondary metabolism and pathogenicity.";
RL Mol. Plant Microbe Interact. 28:232-248(2015).
CC -!- FUNCTION: Adenosyl-L-methionine (AdoMet)-dependent tRNA (uracil-O(2)-)-
CC methyltransferase. {ECO:0000256|RuleBase:RU368004}.
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 Evidence={ECO:0000256|ARBA:ARBA00000660,
CC ECO:0000256|RuleBase:RU368004};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC ECO:0000256|RuleBase:RU368004}.
CC -!- SIMILARITY: Belongs to the TRM44 family.
CC {ECO:0000256|ARBA:ARBA00009056, ECO:0000256|RuleBase:RU368004}.
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:KGO68140.1}.
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DR EMBL; JQGA01001233; KGO68140.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0A2KUU6; -.
DR STRING; 40296.A0A0A2KUU6; -.
DR HOGENOM; CLU_721803_0_0_1; -.
DR OMA; CLIELWR; -.
DR OrthoDB; 1353816at2759; -.
DR PhylomeDB; A0A0A2KUU6; -.
DR Proteomes; UP000030104; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0141101; F:tRNA(Ser) (uridine(44)-2'-O-)-methyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0030488; P:tRNA methylation; IEA:UniProtKB-UniRule.
DR InterPro; IPR011671; tRNA_uracil_MeTrfase.
DR PANTHER; PTHR21210:SF0; TRNA (URACIL-O(2)-)-METHYLTRANSFERASE-RELATED; 1.
DR PANTHER; PTHR21210; UNCHARACTERIZED; 1.
DR Pfam; PF07757; AdoMet_MTase; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|RuleBase:RU368004};
KW Methyltransferase {ECO:0000256|RuleBase:RU368004,
KW ECO:0000313|EMBL:KGO68140.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000030104};
KW S-adenosyl-L-methionine {ECO:0000256|RuleBase:RU368004};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU368004};
KW tRNA processing {ECO:0000256|RuleBase:RU368004}.
FT REGION 219..240
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 220..236
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 383 AA; 42808 MW; C95B3327077E797C CRC64;
MERRLTSRNV SLDWVERDNQ DEGNVSAHLI QNTYARLKLQ YAEKLRQYWV EQLESPNQAL
EQLSLAACLI ELWRSMYGAQ PATEQEQPSK NTVPFPGFVD LACGNGILVY ILLMEGYKGL
GFDACRRMTW ETFPAEVQEC LEEKIFIPRP FVDVLDLQEM GVEIHTGDFP DNTFIISDHA
DELTVWTPIM AALSSPSSPL PFFVVPCCSR SLAGSSYRYP PPKESNSVQQ SANGNPAARK
AYDAIEQNSQ PASGDLRALR AIKIEEKTES GFLNSMIGSL AAKTMSVAEE IGFDVEKTWL
RTPGAINMAL IGGRRRVTRE WLKNAGSRGS PTTREQADSV FKNVMEVVER ECLKYGGIQV
AANLWVERAK SLHRGQGTVH QAK
//
