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Database: UniProt
Entry: F9WUR0_TRYVY
LinkDB: F9WUR0_TRYVY
Original site: F9WUR0_TRYVY 
ID   F9WUR0_TRYVY            Unreviewed;       354 AA.
AC   F9WUR0;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   27-MAR-2024, entry version 43.
DE   SubName: Full=Methionyl-tRNA synthetase, putative {ECO:0000313|EMBL:CCD21309.1};
DE   Flags: Fragment;
GN   ORFNames=TvY486_0042210 {ECO:0000313|EMBL:CCD21309.1};
OS   Trypanosoma vivax (strain Y486).
OC   Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC   Trypanosomatida; Trypanosomatidae; Trypanosoma; Duttonella.
OX   NCBI_TaxID=1055687 {ECO:0000313|EMBL:CCD21309.1, ECO:0000313|Proteomes:UP000009027};
RN   [1] {ECO:0000313|EMBL:CCD21309.1, ECO:0000313|Proteomes:UP000009027}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Y486 {ECO:0000313|EMBL:CCD21309.1,
RC   ECO:0000313|Proteomes:UP000009027};
RX   PubMed=22331916; DOI=10.1073/pnas.1117313109;
RA   Jackson A.P., Berry A., Aslett M., Allison H.C., Burton P.,
RA   Vavrova-Anderson J., Brown R., Browne H., Corton N., Hauser H., Gamble J.,
RA   Gilderthorp R., Marcello L., McQuillan J., Otto T.D., Quail M.A.,
RA   Sanders M.J., van Tonder A., Ginger M.L., Field M.C., Barry J.D.,
RA   Hertz-Fowler C., Berriman M.;
RT   "Antigenic diversity is generated by distinct evolutionary mechanisms in
RT   African trypanosome species.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:3416-3421(2012).
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       {ECO:0000256|RuleBase:RU363039}.
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DR   EMBL; CAEX01007420; CCD21309.1; -; Genomic_DNA.
DR   AlphaFoldDB; F9WUR0; -.
DR   VEuPathDB; TriTrypDB:TvY486_0042210; -.
DR   OrthoDB; 166496at2759; -.
DR   Proteomes; UP000009027; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004825; F:methionine-tRNA ligase activity; IEA:InterPro.
DR   GO; GO:0006431; P:methionyl-tRNA aminoacylation; IEA:InterPro.
DR   Gene3D; 2.170.220.10; -; 1.
DR   Gene3D; 3.40.50.620; HUPs; 1.
DR   InterPro; IPR023457; Met-tRNA_synth_2.
DR   InterPro; IPR015413; Methionyl/Leucyl_tRNA_Synth.
DR   InterPro; IPR033911; MetRS_core.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   PANTHER; PTHR43326:SF1; METHIONINE--TRNA LIGASE, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR43326; METHIONYL-TRNA SYNTHETASE; 1.
DR   Pfam; PF09334; tRNA-synt_1g; 1.
DR   PRINTS; PR01041; TRNASYNTHMET.
DR   SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146,
KW   ECO:0000256|RuleBase:RU363039};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU363039};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|RuleBase:RU363039};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU363039};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917,
KW   ECO:0000256|RuleBase:RU363039};
KW   Reference proteome {ECO:0000313|Proteomes:UP000009027}.
FT   DOMAIN          4..296
FT                   /note="Methionyl/Leucyl tRNA synthetase"
FT                   /evidence="ECO:0000259|Pfam:PF09334"
FT   NON_TER         354
FT                   /evidence="ECO:0000313|EMBL:CCD21309.1"
SQ   SEQUENCE   354 AA;  40404 MW;  2E89ECB1D3483274 CRC64;
     MGFDVDYFIR TTSESHKAVV REVWSKLEAK GDIYLGRYEG WYSVSDESFL TAQSVVDGVD
     KDGNPCKVSL ESGHVVTWMA EDNYMFRLSA FRDRLLAWYN DNPGCIVPEF RRREVIRTVE
     KGLHDLSVSR RKETLHNWAI PVPGNSDHCI YVWLDALTNY YTASRVHVDG SGAEVRCVDD
     FRELERFPAD VHVIGKDILK FHAIYWPAFL MSVGLPLPKK IVAHGWWTKD RRKISKSLGN
     AFDPLEKGAE FGLDALKYFL LRESGFSDDG DYSDRNMIAR LNGELADTLG NLVMRCTSSK
     INTSREWPQP GTYTERDNLL VRLISDMPGT VDHYYGIPDL QKALATIFDV LRAI
//
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