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Database: UniProt
Entry: A0A132AG94_SARSC
LinkDB: A0A132AG94_SARSC
Original site: A0A132AG94_SARSC 
ID   A0A132AG94_SARSC        Unreviewed;       408 AA.
AC   A0A132AG94;
DT   11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT   11-MAY-2016, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   RecName: Full=tRNA (uracil(54)-C(5))-methyltransferase {ECO:0000256|ARBA:ARBA00033763};
DE            EC=2.1.1.35 {ECO:0000256|ARBA:ARBA00033763};
GN   ORFNames=QR98_0083840 {ECO:0000313|EMBL:KPM09839.1};
OS   Sarcoptes scabiei (Itch mite) (Acarus scabiei).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC   Acariformes; Sarcoptiformes; Astigmata; Psoroptidia; Sarcoptoidea;
OC   Sarcoptidae; Sarcoptinae; Sarcoptes.
OX   NCBI_TaxID=52283 {ECO:0000313|EMBL:KPM09839.1, ECO:0000313|Proteomes:UP000616769};
RN   [1] {ECO:0000313|EMBL:KPM09839.1, ECO:0000313|Proteomes:UP000616769}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Arlian Lab {ECO:0000313|EMBL:KPM09839.1};
RX   PubMed=26555130; DOI=10.1186/s13071-015-1198-2;
RA   Rider S.D.Jr., Morgan M.S., Arlian L.G.;
RT   "Draft genome of the scabies mite.";
RL   Parasit. Vectors 8:585-585(2015).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=S-adenosyl-L-methionine + uridine(54) in tRNA = 5-
CC         methyluridine(54) in tRNA + H(+) + S-adenosyl-L-homocysteine;
CC         Xref=Rhea:RHEA:42712, Rhea:RHEA-COMP:10167, Rhea:RHEA-COMP:10193,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC         ChEBI:CHEBI:65315, ChEBI:CHEBI:74447; EC=2.1.1.35;
CC         Evidence={ECO:0000256|ARBA:ARBA00033652};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42713;
CC         Evidence={ECO:0000256|ARBA:ARBA00033652};
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. RNA M5U methyltransferase family. {ECO:0000256|PROSITE-
CC       ProRule:PRU01024}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU01024}.
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:KPM09839.1}.
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DR   EMBL; JXLN01014135; KPM09839.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A132AG94; -.
DR   VEuPathDB; VectorBase:SSCA004751; -.
DR   OMA; DQMLPLW; -.
DR   OrthoDB; 120922at2759; -.
DR   Proteomes; UP000616769; Unassembled WGS sequence.
DR   GO; GO:0008173; F:RNA methyltransferase activity; IEA:InterPro.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   GO; GO:0006396; P:RNA processing; IEA:InterPro.
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   InterPro; IPR025714; Methyltranfer_dom.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   InterPro; IPR045850; TRM2_met.
DR   InterPro; IPR010280; U5_MeTrfase_fam.
DR   PANTHER; PTHR45904; TRNA (URACIL-5-)-METHYLTRANSFERASE; 1.
DR   PANTHER; PTHR45904:SF1; TRNA (URACIL-5-)-METHYLTRANSFERASE HOMOLOG B; 1.
DR   Pfam; PF13847; Methyltransf_31; 1.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR   PROSITE; PS51687; SAM_MT_RNA_M5U; 1.
PE   3: Inferred from homology;
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|PROSITE-
KW   ProRule:PRU01024};
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}.
FT   DOMAIN          249..316
FT                   /note="Methyltransferase"
FT                   /evidence="ECO:0000259|Pfam:PF13847"
FT   ACT_SITE        357
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         229
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         279
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         329
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
SQ   SEQUENCE   408 AA;  46847 MW;  D3B8C7A02ECB9B7E CRC64;
     MPLYPIPYGQ QIKIKSIRSK NILQSFGEKL KNLNQSIRFN SHHLPCPLEP LRPSPSIDSY
     RNKDEFSVWP GFDDNPKTVG FFVGKPSAND RVICVEPDKI IISKQSHLDL AKKFQNYLRE
     VSPYDVCQNY GLGGHWRRFH VRSNLRNEHM VTAIMHPQDL NETELAEEMK RFRSYFVDNS
     LISSLYFHTS RHTRSTHTNE PYFHLAGNET ITESLFDRNF IISPSSFFQI NTTAAEILYR
     VIMTEMKLTK RTTVLDLCCG TGVLSVLVAD QVRKVIGIDS SRSAIEDAKR NADLNSVKNA
     NFIVGTIEEE LPKLLQENYL KEPVIAVVNP SRQGLHPSVI DVLKRISYIE RLVYVSCKPE
     GDAMRNFVQL CQRSKQCATS FWPINAIPVD MFPQTEHCEL IITFERFG
//
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