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Database: UniProt
Entry: M0M442_HALMO
LinkDB: M0M442_HALMO
Original site: M0M442_HALMO 
ID   M0M442_HALMO            Unreviewed;       266 AA.
AC   M0M442;
DT   03-APR-2013, integrated into UniProtKB/TrEMBL.
DT   03-APR-2013, sequence version 1.
DT   24-JAN-2024, entry version 36.
DE   SubName: Full=Translation initiation factor IF-2 subunit alpha {ECO:0000313|EMBL:EMA40466.1};
GN   ORFNames=C448_13996 {ECO:0000313|EMBL:EMA40466.1};
OS   Halococcus morrhuae DSM 1307.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC   Halococcaceae; Halococcus.
OX   NCBI_TaxID=931277 {ECO:0000313|EMBL:EMA40466.1, ECO:0000313|Proteomes:UP000011568};
RN   [1] {ECO:0000313|EMBL:EMA40466.1, ECO:0000313|Proteomes:UP000011568}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 1307 {ECO:0000313|EMBL:EMA40466.1,
RC   ECO:0000313|Proteomes:UP000011568};
RX   PubMed=25393412; DOI=10.1371/journal.pgen.1004784;
RA   Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I., Wu D.,
RA   Madern D., Eisen J.A., Darling A.E., Facciotti M.T.;
RT   "Phylogenetically driven sequencing of extremely halophilic archaea reveals
RT   strategies for static and dynamic osmo-response.";
RL   PLoS Genet. 10:E1004784-E1004784(2014).
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:EMA40466.1}.
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DR   EMBL; AOMC01000152; EMA40466.1; -; Genomic_DNA.
DR   RefSeq; WP_004055618.1; NZ_AOMC01000152.1.
DR   AlphaFoldDB; M0M442; -.
DR   STRING; 931277.C448_13996; -.
DR   GeneID; 71762792; -.
DR   PATRIC; fig|931277.6.peg.2750; -.
DR   eggNOG; arCOG04107; Archaea.
DR   OrthoDB; 84794at2157; -.
DR   Proteomes; UP000011568; 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:EMA40466.1};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW   Reference proteome {ECO:0000313|Proteomes:UP000011568}.
FT   DOMAIN          10..81
FT                   /note="S1 motif"
FT                   /evidence="ECO:0000259|PROSITE:PS50126"
FT   REGION          243..266
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   266 AA;  29354 MW;  B8FF3CECAEAD9C1A CRC64;
     MKYSGWPDPS ELVVGKVDEI ADFGVFVDLS EYEDKRGLVH ISEVASGWIK NVRDHVSVGQ
     TVVAKVLDVD EGSQQIDLSL KDVNDHQRSE KVREWKSEQK ADNWMTIAFG EEISDEQYAT
     VANEFLAAFG SLYDGFEEAA IHGTEALTDT DLSDEEIDAI VQTARENVSV PYVTVSGYVD
     LESPDSAGVD VIRDALHAAE GNGDLPEEVD LDVTYVGSPE YRIRVQAPDY KIAERELEAS
     ADRAAANIGD HGGTAEFHRE RRSDDE
//
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