ID A0A3B4HB77_9CICH Unreviewed; 315 AA.
AC A0A3B4HB77;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Eukaryotic translation initiation factor 2 subunit 1 {ECO:0000256|ARBA:ARBA00020950};
DE AltName: Full=Eukaryotic translation initiation factor 2 subunit alpha {ECO:0000256|ARBA:ARBA00033370};
GN Name=eif2s1 {ECO:0000313|RefSeq:XP_005731171.1,
GN ECO:0000313|RefSeq:XP_005731172.1};
OS Pundamilia nyererei.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Haplochromini; Pundamilia.
OX NCBI_TaxID=303518 {ECO:0000313|Ensembl:ENSPNYP00000030933.1, ECO:0000313|Proteomes:UP000261460};
RN [1] {ECO:0000313|Ensembl:ENSPNYP00000030933.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
RN [2] {ECO:0000313|RefSeq:XP_005731171.1, ECO:0000313|RefSeq:XP_005731172.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, Stress granule
CC {ECO:0000256|ARBA:ARBA00004210}.
CC -!- SIMILARITY: Belongs to the eIF-2-alpha family.
CC {ECO:0000256|ARBA:ARBA00007223}.
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DR RefSeq; XP_005731171.1; XM_005731114.1.
DR RefSeq; XP_005731172.1; XM_005731115.1.
DR AlphaFoldDB; A0A3B4HB77; -.
DR STRING; 303518.ENSPNYP00000030933; -.
DR Ensembl; ENSPNYT00000031682.1; ENSPNYP00000030933.1; ENSPNYG00000023310.1.
DR GeneID; 102213838; -.
DR CTD; 321564; -.
DR GeneTree; ENSGT00390000007015; -.
DR OrthoDB; 4371132at2759; -.
DR Proteomes; UP000261460; Unplaced.
DR Proteomes; UP000695023; Unplaced.
DR GO; GO:0010494; C:cytoplasmic stress granule; IEA:UniProtKB-SubCell.
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|RefSeq:XP_005731171.1};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW Reference proteome {ECO:0000313|Proteomes:UP000695023}.
FT DOMAIN 17..88
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT REGION 292..315
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 300..315
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 315 AA; 36039 MW; 3BAF2DAEB62409FE CRC64;
MPGLSCRFYQ HRFPEVEDVV MVNVRSIAEM GAYVSLLEYN NIEGMILLSE LSRRRIRSIN
KLIRIGRNEC VVVIRVDKEK GYIDLSKRRV SPEEAIKCED KFTKSKTVYS ILRHVAEVLE
YSKDEQLESL YQRTAWVFDE RYKRPGYGAY DVFKQAVSDP AILDGLDLTE EERNVLIDNI
NRRLTPQAVK IRADIEVACY GYEGIDAVKE ALRAGLGCST EAMPIKINLI APPRYVMTTT
TLERTEGLSV LNQAMAAIKE KIEEKRGVFN IQMEPKVVTD TDETELARQL ERLERENAEV
DGDDDAEEME AKAED
//
