ID A0A0S4JL98_BODSA Unreviewed; 596 AA.
AC A0A0S4JL98;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Translation initiation factor eIF2B subunit beta {ECO:0000256|ARBA:ARBA00044122};
DE AltName: Full=eIF2B GDP-GTP exchange factor subunit beta {ECO:0000256|ARBA:ARBA00044228};
GN ORFNames=BSAL_29225 {ECO:0000313|EMBL:CUG90908.1};
OS Bodo saltans (Flagellated protozoan).
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Eubodonida; Bodonidae; Bodo.
OX NCBI_TaxID=75058 {ECO:0000313|EMBL:CUG90908.1, ECO:0000313|Proteomes:UP000051952};
RN [1] {ECO:0000313|Proteomes:UP000051952}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Lake Konstanz {ECO:0000313|Proteomes:UP000051952};
RG Pathogen Informatics;
RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000256|ARBA:ARBA00004514}.
CC -!- SIMILARITY: Belongs to the eIF-2B alpha/beta/delta subunits family.
CC {ECO:0000256|ARBA:ARBA00007251, ECO:0000256|RuleBase:RU003814}.
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DR EMBL; CYKH01001874; CUG90908.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S4JL98; -.
DR VEuPathDB; TriTrypDB:BSAL_29225; -.
DR OMA; NNEDAHL; -.
DR OrthoDB; 169494at2759; -.
DR Proteomes; UP000051952; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-KW.
DR InterPro; IPR000649; IF-2B-related.
DR InterPro; IPR042529; IF_2B-like_C.
DR InterPro; IPR037171; NagB/RpiA_transferase-like.
DR PANTHER; PTHR45859; TRANSLATION INITIATION FACTOR EIF-2B SUBUNIT BETA; 1.
DR PANTHER; PTHR45859:SF1; TRANSLATION INITIATION FACTOR EIF-2B SUBUNIT BETA; 1.
DR Pfam; PF01008; IF-2B; 1.
DR SUPFAM; SSF100950; NagB/RpiA/CoA transferase-like; 1.
PE 3: Inferred from homology;
KW Initiation factor {ECO:0000313|EMBL:CUG90908.1};
KW Protein biosynthesis {ECO:0000313|EMBL:CUG90908.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000051952}.
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 177..227
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 243..316
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 188..204
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 210..227
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 243..292
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 596 AA; 65354 MW; 82AD8441EE094652 CRC64;
MEFSTVRSYA SGGGGGVAKK SRSGATEGLG GEQYATKVKD NIEAYLAKLR KGKFVVREYQ
SQSIAAAREC AGILRAVVEL YHEAETQPQS KSVQSLLHDA PAIEVTTEQV STILRHVTRA
GSAMQRGPYF KLLLTNVTRR VLSILRQAAA ESVGSESELE AIAKIIIDDA RATLGSSVDE
SEVEEDSSFE VVQQATPPKE VQSGSSDDGS DDDDNNRHGD HSDDDDVQME TSAIATNNFL
KVEAAQQQKQ QREQQQQKPK GMKRTTFSLA DDSSSSAQKS KPMALGGLTR QQSSDNDDHH
GHEHQPSSLL SDFMVSTPPK NVLPRAPSIL GEVDVLKEKT YAVRFEEFIQ RSIDGIRSFE
GELAYVTQEL CKRAARQLHP LDTVITIGSS HSTLNFLLKA TEDYAKLGTM FKVIVLEGRP
LRGAHRLADA LRERGVEVRV LPDSSAFAVM STCTKVVIGV ENVLANGGLL APIGTHPLCI
AAQHFSVPVM VVTMTLKMTP YYPSDTRCTS LVKISRTRSE ELPWSTFAFP GDVLAMDEWA
AMDVDPKLQP IDVTNPLMEY VPPHLVSVFA TNEGEYTVPQ IHRIVRDNYN NEDAHL
//
