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Database: UniProt
Entry: A0A2V0NWY2_9CHLO
LinkDB: A0A2V0NWY2_9CHLO
Original site: A0A2V0NWY2_9CHLO 
ID   A0A2V0NWY2_9CHLO        Unreviewed;       334 AA.
AC   A0A2V0NWY2;
DT   12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT   12-SEP-2018, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   SubName: Full=Eukaryotic translation initiation factor 2 subunit alpha {ECO:0000313|EMBL:GBF90073.1};
GN   ORFNames=Rsub_02781 {ECO:0000313|EMBL:GBF90073.1};
OS   Raphidocelis subcapitata.
OC   Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC   CS clade; Sphaeropleales; Selenastraceae; Raphidocelis.
OX   NCBI_TaxID=307507 {ECO:0000313|EMBL:GBF90073.1, ECO:0000313|Proteomes:UP000247498};
RN   [1] {ECO:0000313|EMBL:GBF90073.1, ECO:0000313|Proteomes:UP000247498}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NIES-35 {ECO:0000313|EMBL:GBF90073.1,
RC   ECO:0000313|Proteomes:UP000247498};
RX   PubMed=29795299; DOI=10.1038/s41598-018-26331-6;
RA   Suzuki S., Yamaguchi H., Nakajima N., Kawachi M.;
RT   "Raphidocelis subcapitata (=Pseudokirchneriella subcapitata) provides an
RT   insight into genome evolution and environmental adaptations in the
RT   Sphaeropleales.";
RL   Sci. Rep. 8:8058-8058(2018).
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:GBF90073.1}.
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DR   EMBL; BDRX01000014; GBF90073.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2V0NWY2; -.
DR   STRING; 307507.A0A2V0NWY2; -.
DR   InParanoid; A0A2V0NWY2; -.
DR   Proteomes; UP000247498; 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:GBF90073.1};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW   Reference proteome {ECO:0000313|Proteomes:UP000247498}.
FT   DOMAIN          18..89
FT                   /note="S1 motif"
FT                   /evidence="ECO:0000259|PROSITE:PS50126"
FT   REGION          299..334
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        299..317
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   334 AA;  37261 MW;  E2E7902DDCA08CFD CRC64;
     MSTHQDCRMY EPKYPEVDDV VYVQVKSIAE MGAYVSLLEY NGIEGMILLS ELSRRRIRSI
     TKLIKVGRQE PVMVLRVDKE KGYIDLSKRR VSPEDIGKCE ERFNKSKMVH SIMRHVAETT
     GQNLEELYKT IAWPLYRIFG HAFDAFKLMV ADDGAAIIAR LEEDHGGPME LLTPAVKDQL
     LKNIKRRMTP QPLKIRADVE MTCFAYDGIE RIKAAMRAGE ALSTEDCPVK MKLVAPPLYV
     LTTQSLDKQR GIDVLAAACD ACKGSIEGAK GKFTVKEAAR AVSERDDRLL AEKLEALEAA
     NKEVDGDDDH SSGSEEEGMG MEFDAEAGPA TLEV
//
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