ID A4HZ00_LEIIN Unreviewed; 603 AA.
AC A4HZ00; A0A2K4YT59; A0A381MJ53;
DT 01-MAY-2007, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2007, sequence version 1.
DT 27-MAR-2024, entry version 81.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:CAM67541.1};
GN ORFNames=LINJ_20_1680 {ECO:0000313|EMBL:CAM67541.1};
OS Leishmania infantum.
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Leishmaniinae; Leishmania.
OX NCBI_TaxID=5671 {ECO:0000313|EMBL:CAM67541.1, ECO:0000313|Proteomes:UP000008153};
RN [1] {ECO:0000313|EMBL:CAM67541.1, ECO:0000313|Proteomes:UP000008153}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JPCM5 {ECO:0000313|EMBL:CAM67541.1,
RC ECO:0000313|Proteomes:UP000008153};
RX PubMed=17572675; DOI=10.1038/ng2053;
RA Peacock C.S., Seeger K., Harris D., Murphy L., Ruiz J.C., Quail M.A.,
RA Peters N., Adlem E., Tivey A., Aslett M., Kerhornou A., Ivens A.,
RA Fraser A., Rajandream M.A., Carver T., Norbertczak H., Chillingworth T.,
RA Hance Z., Jagels K., Moule S., Ormond D., Rutter S., Squares R.,
RA Whitehead S., Rabbinowitsch E., Arrowsmith C., White B., Thurston S.,
RA Bringaud F., Baldauf S.L., Faulconbridge A., Jeffares D., Depledge D.P.,
RA Oyola S.O., Hilley J.D., Brito L.O., Tosi L.R., Barrell B., Cruz A.K.,
RA Mottram J.C., Smith D.F., Berriman M.;
RT "Comparative genomic analysis of three Leishmania species that cause
RT diverse human disease.";
RL Nat. Genet. 39:839-847(2007).
RN [2] {ECO:0000313|EMBL:CAM67541.1, ECO:0000313|Proteomes:UP000008153}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JPCM5 {ECO:0000313|EMBL:CAM67541.1,
RC ECO:0000313|Proteomes:UP000008153};
RX PubMed=22038252; DOI=10.1101/gr.122945.111;
RA Rogers M.B., Hilley J.D., Dickens N.J., Wilkes J., Bates P.A.,
RA Depledge D.P., Harris D., Her Y., Herzyk P., Imamura H., Otto T.D.,
RA Sanders M., Seeger K., Dujardin J.C., Berriman M., Smith D.F.,
RA Hertz-Fowler C., Mottram J.C.;
RT "Chromosome and gene copy number variation allow major structural change
RT between species and strains of Leishmania.";
RL Genome Res. 21:2129-2142(2011).
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}.
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DR EMBL; FR796452; CAM67541.1; -; Genomic_DNA.
DR RefSeq; XP_001465291.1; XM_001465254.1.
DR AlphaFoldDB; A4HZ00; -.
DR SMR; A4HZ00; -.
DR STRING; 5671.A4HZ00; -.
DR GeneID; 5068709; -.
DR KEGG; lif:LINJ_20_1680; -.
DR VEuPathDB; TriTrypDB:LINF_200021600; -.
DR eggNOG; KOG2187; Eukaryota.
DR InParanoid; A4HZ00; -.
DR OMA; LHYRVIR; -.
DR OrthoDB; 120922at2759; -.
DR Proteomes; UP000008153; Chromosome 20.
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; IPR030391; MeTrfase_TrmA_CS.
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:SF2; TRNA (URACIL-5-)-METHYLTRANSFERASE HOMOLOG A; 1.
DR Pfam; PF05958; tRNA_U5-meth_tr; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS51687; SAM_MT_RNA_M5U; 1.
DR PROSITE; PS01231; TRMA_2; 1.
PE 3: Inferred from homology;
KW Methyltransferase {ECO:0000256|PROSITE-ProRule:PRU01024};
KW Reference proteome {ECO:0000313|Proteomes:UP000008153};
KW S-adenosyl-L-methionine {ECO:0000256|PROSITE-ProRule:PRU01024};
KW Transferase {ECO:0000256|PROSITE-ProRule:PRU01024}.
FT ACT_SITE 511
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 381
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 431
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 483
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
SQ SEQUENCE 603 AA; 65268 MW; 6474BF9BC5B6E07E CRC64;
MSVSLPPPST EEHGAVQLHE HSNANLLKID THDTYSTVGT IKKLIVKALP AEQREAPPQP
LLKGLIRINK NPKNAYLFMA FKTPEDRAAA SAVLQTISHR GRPWTETSVS PRDLELTHKG
GVKRRRDGDD GDGSSKLTQY EHLHMEEQLN RKKRHCLNVM RRILPAGVYG YAAFQDRFAG
ILTSPVTEGY RNHVNLSFGF CADGSTPALG FQQGSLVEGT AAVLPATLPD KDIVTMNSAA
KVVAAALMDM CMEFRDVAKG GLDVFNKVKA SGFWRKLQVR HNVKGEVMMD VEADAASTTA
DVWAAVRQRL VEVFACEEMR VKLVAATGLS TAAVVSLQCH THTGISSLPL DVPREVLYGA
PTLTEYLAGL CFELSPTAFF QVNTPGMETM MMKVAEVAEL SAGTTLLDLC SGTGTIGLTL
SKHVKRVIGI ELVESAVANA RRNAQQNGIT NTEFHCGRVE HLLPSVISGL PAEDRGDIVV
ILDPPRAGVN STVLRWIRGM ETIRRVVYIS CEQKALERDC PGLTKPSTKA YRGTPFEVTA
AFAVDLFPHT HHVEMVAVLT RRPESAAGPA SESAPAPKPA PVSAERAAEE EETVADANGG
CVE
//
