ID J4C7N4_THEOR Unreviewed; 343 AA.
AC J4C7N4;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 24-JAN-2024, entry version 44.
DE SubName: Full=Eukaryotic translation initiation factor 2 subunit alpha {ECO:0000313|EMBL:BAM39343.1};
GN ORFNames=TOT_010000801 {ECO:0000313|EMBL:BAM39343.1};
OS Theileria orientalis strain Shintoku.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Piroplasmida;
OC Theileriidae; Theileria.
OX NCBI_TaxID=869250 {ECO:0000313|EMBL:BAM39343.1, ECO:0000313|Proteomes:UP000003786};
RN [1] {ECO:0000313|EMBL:BAM39343.1, ECO:0000313|Proteomes:UP000003786}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Shintoku {ECO:0000313|EMBL:BAM39343.1,
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).
CC -!- SIMILARITY: Belongs to the eIF-2-alpha family.
CC {ECO:0000256|ARBA:ARBA00007223}.
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DR EMBL; AP011946; BAM39343.1; -; Genomic_DNA.
DR RefSeq; XP_009689644.1; XM_009691349.1.
DR AlphaFoldDB; J4C7N4; -.
DR STRING; 869250.J4C7N4; -.
DR EnsemblProtists; BAM39343; BAM39343; TOT_010000801.
DR GeneID; 20713674; -.
DR KEGG; tot:TOT_010000801; -.
DR VEuPathDB; PiroplasmaDB:TOT_010000801; -.
DR eggNOG; KOG2916; Eukaryota.
DR OrthoDB; 4371132at2759; -.
DR Proteomes; UP000003786; Chromosome 1.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-KW.
DR CDD; cd04452; S1_IF2_alpha; 1.
DR Gene3D; 3.30.70.1130; EIF_2_alpha; 1.
DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR003029; S1_domain.
DR InterPro; IPR044126; S1_IF2_alpha.
DR InterPro; IPR024055; TIF2_asu_C.
DR InterPro; IPR024054; TIF2_asu_middle_sf.
DR InterPro; IPR011488; TIF_2_asu.
DR PANTHER; PTHR10602; EUKARYOTIC TRANSLATION INITIATION FACTOR 2 SUBUNIT 1; 1.
DR PANTHER; PTHR10602:SF0; EUKARYOTIC TRANSLATION INITIATION FACTOR 2 SUBUNIT 1; 1.
DR Pfam; PF07541; EIF_2_alpha; 1.
DR Pfam; PF00575; S1; 1.
DR SMART; SM00316; S1; 1.
DR SUPFAM; SSF110993; eIF-2-alpha, C-terminal domain; 1.
DR SUPFAM; SSF116742; eIF2alpha middle domain-like; 1.
DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR PROSITE; PS50126; S1; 1.
PE 3: Inferred from homology;
KW Initiation factor {ECO:0000256|ARBA:ARBA00022540,
KW ECO:0000313|EMBL:BAM39343.1};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW Reference proteome {ECO:0000313|Proteomes:UP000003786}.
FT DOMAIN 23..94
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT REGION 298..343
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 305..324
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 343 AA; 39442 MW; 17DE73037C900E7D CRC64;
MPPVSKSNLG DCRFYERKFP EPEELVMVKV NRIEAQGVYV SLLEYDDREG LILLNELSKR
RYRSINKLVK IGRHEVVLVL RVDPVKGYID LSKRRVTPED IIKCEERFSK SKKVHQTVRH
IAQKHGVSVE ELNRACIWPL YKTYPHALDA LKEAAANKEN VFKNLTLSQE IVDSLLQDIQ
LRLVPQALKL RCSIDVWCFG PEGINAVKTS LTKAKEVDPQ VRKSSDQFSA FDKQLRISIR
LIAPPQYEII TSCFDKEAGL NTMNQTLEVI ETNIRSFIGG DFKQKCEVVV IGDDEKHLED
LLEQHESTDE EDEEEEEEED EGMGRVDESM LPPNEENLEE DSD
//
