ID J4C353_THEOR Unreviewed; 368 AA.
AC J4C353;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE SubName: Full=Methionine-tRNA ligase {ECO:0000313|EMBL:BAM39841.1};
GN ORFNames=TOT_020000112 {ECO:0000313|EMBL:BAM39841.1};
OS Theileria orientalis strain Shintoku.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Piroplasmida;
OC Theileriidae; Theileria.
OX NCBI_TaxID=869250 {ECO:0000313|EMBL:BAM39841.1, ECO:0000313|Proteomes:UP000003786};
RN [1] {ECO:0000313|EMBL:BAM39841.1, ECO:0000313|Proteomes:UP000003786}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Shintoku {ECO:0000313|EMBL:BAM39841.1,
RC ECO:0000313|Proteomes:UP000003786};
RX PubMed=22951932;
RA Hayashida K., Hara Y., Abe T., Yamasaki C., Toyoda A., Kosuge T.,
RA Suzuki Y., Sato Y., Kawashima S., Katayama T., Wakaguri H., Inoue N.,
RA Homma K., Tada-Umezaki M., Yagi Y., Fujii Y., Habara T., Kanehisa M.,
RA Watanabe H., Ito K., Gojobori T., Sugawara H., Imanishi T., Weir W.,
RA Gardner M., Pain A., Shiels B., Hattori M., Nene V., Sugimoto C.;
RT "Comparative genome analysis of three eukaryotic parasites with differing
RT abilities to transform leukocytes reveals key mediators of Theileria-
RT induced leukocyte transformation.";
RL MBio 3:e00204-e00212(2012).
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DR EMBL; AP011947; BAM39841.1; -; Genomic_DNA.
DR RefSeq; XP_009690142.1; XM_009691847.1.
DR AlphaFoldDB; J4C353; -.
DR STRING; 869250.J4C353; -.
DR EnsemblProtists; BAM39841; BAM39841; TOT_020000112.
DR GeneID; 20714294; -.
DR KEGG; tot:TOT_020000112; -.
DR VEuPathDB; PiroplasmaDB:TOT_020000112; -.
DR eggNOG; KOG2241; Eukaryota.
DR OrthoDB; 1341752at2759; -.
DR Proteomes; UP000003786; Chromosome 2.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-UniRule.
DR CDD; cd10289; GST_C_AaRS_like; 1.
DR CDD; cd02799; tRNA_bind_EMAP-II_like; 1.
DR Gene3D; 1.20.1050.10; -; 1.
DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR InterPro; IPR010987; Glutathione-S-Trfase_C-like.
DR InterPro; IPR036282; Glutathione-S-Trfase_C_sf.
DR InterPro; IPR004046; GST_C.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR002547; tRNA-bd_dom.
DR PANTHER; PTHR11586:SF46; AMINOACYL TRNA SYNTHASE COMPLEX-INTERACTING MULTIFUNCTIONAL PROTEIN 1; 1.
DR PANTHER; PTHR11586; TRNA-AMINOACYLATION COFACTOR ARC1 FAMILY MEMBER; 1.
DR Pfam; PF00043; GST_C; 1.
DR Pfam; PF01588; tRNA_bind; 1.
DR SUPFAM; SSF47616; GST C-terminal domain-like; 1.
DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR PROSITE; PS50405; GST_CTER; 1.
DR PROSITE; PS50886; TRBD; 1.
PE 4: Predicted;
KW Ligase {ECO:0000313|EMBL:BAM39841.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000003786};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|PROSITE-
KW ProRule:PRU00209};
KW tRNA-binding {ECO:0000256|ARBA:ARBA00022555, ECO:0000256|PROSITE-
KW ProRule:PRU00209}.
FT DOMAIN 48..188
FT /note="GST C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50405"
FT DOMAIN 223..325
FT /note="TRNA-binding"
FT /evidence="ECO:0000259|PROSITE:PS50886"
FT REGION 186..219
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 368 AA; 41791 MW; F328318D05AC38AC CRC64;
MIELVVYSDS QESQIVKLLL KYLNLNDVSL TLSTNKDEEL FLKLPGETEP VKHFPLMLER
LLKSSPHGSL LLPTDPELKA TMDSFVDFGF KHGFNVLDVD SLRMLDNYLL NETFFSGPTI
SLADVVLFVS VTYWTSRSKS KERMEVPNLM RWFDHLQHLP EFASCFEEFK VIQLFDEKLV
MTEPKKGKPR AAYHPSEKAE KKKEKKEKPK VEKPPVETRP YDDVTRLNVV VGLVKSIRKH
EDADKLYCLK IDVGSEVRSI CSGLVDFLMP DQILDKKVCV LANLPKKNLR GEESNGMVLC
VSNSDKSSVE LLEPPVDAPV GERVYWEGYS GEADEQLSSK KGKDTFAMVQ KDLNCKENVG
FYKVSGAE
//
