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Database: UniProt
Entry: TRM44_XENLA
LinkDB: TRM44_XENLA
Original site: TRM44_XENLA 
ID   TRM44_XENLA             Reviewed;         668 AA.
AC   Q4KLT3; Q7ZY77;
DT   19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT   02-AUG-2005, sequence version 1.
DT   27-MAR-2024, entry version 65.
DE   RecName: Full=Probable tRNA (uracil-O(2)-)-methyltransferase;
DE            EC=2.1.1.211;
DE   AltName: Full=Methyltransferase-like protein 19;
GN   Name=trmt44; Synonyms=mettl19;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Egg, and Embryo;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
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:0000305}.
CC   -!- SIMILARITY: Belongs to the TRM44 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH43909.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
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DR   EMBL; BC043909; AAH43909.1; ALT_SEQ; mRNA.
DR   EMBL; BC099012; AAH99012.1; -; mRNA.
DR   RefSeq; NP_001082524.1; NM_001089055.1.
DR   AlphaFoldDB; Q4KLT3; -.
DR   DNASU; 398534; -.
DR   GeneID; 398534; -.
DR   KEGG; xla:398534; -.
DR   AGR; Xenbase:XB-GENE-991929; -.
DR   CTD; 398534; -.
DR   Xenbase; XB-GENE-991929; trmt44.L.
DR   OrthoDB; 1353816at2759; -.
DR   Proteomes; UP000186698; Chromosome 1L.
DR   Bgee; 398534; Expressed in egg cell and 19 other cell types or tissues.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0141101; F:tRNA(Ser) (uridine(44)-2'-O-)-methyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   GO; GO:0008033; P:tRNA processing; IEA:UniProtKB-KW.
DR   Gene3D; 4.10.1000.10; Zinc finger, CCCH-type; 1.
DR   InterPro; IPR011671; tRNA_uracil_MeTrfase.
DR   InterPro; IPR000571; Znf_CCCH.
DR   PANTHER; PTHR21210:SF0; TRNA (URACIL-O(2)-)-METHYLTRANSFERASE-RELATED; 1.
DR   PANTHER; PTHR21210; UNCHARACTERIZED; 1.
DR   Pfam; PF07757; AdoMet_MTase; 1.
DR   PROSITE; PS50103; ZF_C3H1; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Metal-binding; Methyltransferase; Reference proteome;
KW   S-adenosyl-L-methionine; Transferase; tRNA processing; Zinc; Zinc-finger.
FT   CHAIN           1..668
FT                   /note="Probable tRNA (uracil-O(2)-)-methyltransferase"
FT                   /id="PRO_0000249896"
FT   ZN_FING         620..649
FT                   /note="C3H1-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT   REGION          441..460
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        143
FT                   /note="T -> K (in Ref. 1; AAH43909)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        429
FT                   /note="R -> Q (in Ref. 1; AAH43909)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        531
FT                   /note="K -> R (in Ref. 1; AAH43909)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        560
FT                   /note="A -> T (in Ref. 1; AAH43909)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   668 AA;  76767 MW;  4C309BD6A0888D54 CRC64;
     MPELASVLVR DERSVLPGGF WAAVAVWLEK PQVLNKRLCG STVGKKWDHV GEESESEGID
     VETALAALLE DMSGPGRDEE MLKLISGYGK REEDSGSLTL RTLIPKSNPH FPSCQPRCEI
     VIRDLPNSVV TFLPLDEANQ FKTNNIYQIR LAHVQDDEWS ISLYTLCSEA WESDGVVYPK
     ITWMKNELLS KLAKWSTEDK KSEFKSTLSL VPVDKYSRLY QNLKEKYRDM VKVWPEVTDP
     EKFVYEDVAI ATYLLIIWEE ERSQNQLKVK QSFVDLGCGN GLLVHILSNE GHPGRGIDVR
     RRKIWDMYGP QTILEESAIL PNDDYLFPDT DWLIGNHSDE LTPWLPVIAS RSSYSCRYFV
     LPCCFFNFYG KYNRKSSKKT QYREYLDFVK EVGQQCGFNV EEDCLRIPST KRVCLIGMSR
     TYPLTQEKRI DEQRTRYIKS QHTDSLHIST KSSLDKDDPP PLNCHAKNGQ VDNVDSSLVQ
     SEKLPGSWMP GFQPREKEEP IRNCALLPRD FIDETVLQVA KLLLYSNTKE KETPITDQSE
     TVWNTGRSLT LREVAEHLHA DTLQKLKNEC GGLQTLLRNN HQVFKVINSN VSIRDWQKDT
     PTNTKKRKPE AKRTVPSDVL KTRLCWFYVH HPNGCPRVAK SCPYAHGAEE LRPSFISRRK
     NPRNKLCT
//
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