ID A0A3M2T0A7_9EURO Unreviewed; 312 AA.
AC A0A3M2T0A7;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE SubName: Full=Translation initiation factor 2 {ECO:0000313|EMBL:RMJ23223.1};
GN ORFNames=PHISP_05906 {ECO:0000313|EMBL:RMJ23223.1};
OS Aspergillus sp. HF37.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1960876 {ECO:0000313|EMBL:RMJ23223.1, ECO:0000313|Proteomes:UP000272442};
RN [1] {ECO:0000313|EMBL:RMJ23223.1, ECO:0000313|Proteomes:UP000272442}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HF37 {ECO:0000313|EMBL:RMJ23223.1,
RC ECO:0000313|Proteomes:UP000272442};
RA Tafer H., Lopandic K.;
RL Submitted (APR-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the eIF-2-alpha family.
CC {ECO:0000256|ARBA:ARBA00007223}.
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:RMJ23223.1}.
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DR EMBL; RAQS01000262; RMJ23223.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3M2T0A7; -.
DR STRING; 1960876.A0A3M2T0A7; -.
DR Proteomes; UP000272442; Unassembled WGS sequence.
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:RMJ23223.1};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW Reference proteome {ECO:0000313|Proteomes:UP000272442}.
FT DOMAIN 17..92
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT REGION 290..312
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 312 AA; 35565 MW; D5B1662A6E9BE459 CRC64;
MSLTNCRFYE EKYPEVDSYV MVNVKQIAEM GAYVKLLEYD NIDGMILLSE LSRRRIRSIQ
KLIRVGRNEI VIVLRVDKEK GKTVGYIDLS KRRVSPEDVV KCEERYNKSK AVHSIMRHVA
EATQTPLETL YQEIGWPLNR KYGHSHDAFK ISITNPDVWK EIEFPSDAVR KELMLYISKK
LTPSPTKVRA DIEVTCFGYD GIDAVKDALR TAEEANTDDS QIRVKLVAPP LYVLTSQCLD
KNLGLRMLED AIQRINKKIK ESGGGCIIKM VPKAVTDSDD AALQELMEKR ERENMEVSGD
ESQSESDEGV PE
//
