(data stored in ACNUC7421 zone)

SWISSPROT: Q758P1_ASHGO

ID   Q758P1_ASHGO            Unreviewed;       625 AA.
AC   Q758P1;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 2.
DT   11-DEC-2019, entry version 95.
DE   RecName: Full=Eukaryotic translation initiation factor 2A {ECO:0000256|PIRNR:PIRNR017222};
DE            Short=eIF-2A {ECO:0000256|PIRNR:PIRNR017222};
GN   ORFNames=AGOS_AEL286C {ECO:0000313|EMBL:AAS52398.2};
OS   Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS   (Yeast) (Eremothecium gossypii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX   NCBI_TaxID=284811 {ECO:0000313|EMBL:AAS52398.2, ECO:0000313|Proteomes:UP000000591};
RN   [1] {ECO:0000313|EMBL:AAS52398.2, ECO:0000313|Proteomes:UP000000591}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056
RC   {ECO:0000313|Proteomes:UP000000591};
RX   PubMed=15001715; DOI=10.1126/science.1095781;
RA   Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA   Mohr C., Pohlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA   Gaffney T.D., Philippsen P.;
RT   "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT   cerevisiae genome.";
RL   Science 304:304-307(2004).
RN   [2] {ECO:0000313|Proteomes:UP000000591}
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056
RC   {ECO:0000313|Proteomes:UP000000591};
RX   PubMed=23749448; DOI=10.1534/g3.112.002881;
RA   Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT   "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT   loci, numerous translocations, lack of transposons, and distinct gene
RT   duplications.";
RL   G3 (Bethesda) 3:1225-1239(2013).
CC   -!- FUNCTION: Functions in the early steps of protein synthesis of a small
CC       number of specific mRNAs. Acts by directing the binding of methionyl-
CC       tRNAi to 40S ribosomal subunits. In contrast to the eIF-2 complex, it
CC       binds methionyl-tRNAi to 40S subunits in a codon-dependent manner,
CC       whereas the eIF-2 complex binds methionyl-tRNAi to 40S subunits in a
CC       GTP-dependent manner. {ECO:0000256|PIRNR:PIRNR017222}.
CC   -!- SIMILARITY: Belongs to the WD repeat EIF2A family.
CC       {ECO:0000256|PIRNR:PIRNR017222}.
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DR   EMBL; AE016818; AAS52398.2; -; Genomic_DNA.
DR   RefSeq; NP_984574.2; NM_209927.2.
DR   STRING; 33169.AAS52398; -.
DR   EnsemblFungi; AAS52398; AAS52398; AGOS_AEL286C.
DR   GeneID; 4620754; -.
DR   KEGG; ago:AGOS_AEL286C; -.
DR   HOGENOM; HOG000193775; -.
DR   InParanoid; Q758P1; -.
DR   KO; K15026; -.
DR   OMA; TYLSTWE; -.
DR   Proteomes; UP000000591; Chromosome V.
DR   GO; GO:0022627; C:cytosolic small ribosomal subunit; IBA:GO_Central.
DR   GO; GO:0043022; F:ribosome binding; IBA:GO_Central.
DR   GO; GO:0003743; F:translation initiation factor activity; IBA:GO_Central.
DR   GO; GO:0000049; F:tRNA binding; IBA:GO_Central.
DR   Gene3D; 2.130.10.10; -; 1.
DR   InterPro; IPR011387; TIF2A.
DR   InterPro; IPR013979; TIF_beta_prop-like.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   InterPro; IPR036322; WD40_repeat_dom_sf.
DR   PANTHER; PTHR13227; PTHR13227; 1.
DR   Pfam; PF08662; eIF2A; 1.
DR   PIRSF; PIRSF017222; eIF2A; 1.
DR   SUPFAM; SSF50978; SSF50978; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q758P1.
DR   SWISS-2DPAGE; Q758P1.
KW   Initiation factor {ECO:0000256|PIRNR:PIRNR017222,
KW   ECO:0000256|SAAS:SAAS00150708};
KW   Protein biosynthesis {ECO:0000256|PIRNR:PIRNR017222,
KW   ECO:0000256|SAAS:SAAS00150703};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000591};
KW   Translation regulation {ECO:0000256|PIRNR:PIRNR017222}.
FT   DOMAIN          218..417
FT                   /note="eIF2A"
FT                   /evidence="ECO:0000259|Pfam:PF08662"
FT   REGION          464..577
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        464..479
FT                   /note="Polar"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        495..512
FT                   /note="Polar"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        528..544
FT                   /note="Polyampholyte"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        546..560
FT                   /note="Polar"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        562..577
FT                   /note="Polyampholyte"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   625 AA;  69660 MW;  91A7CFF70FCF83AE CRC64;
     MSFQLFARTP AGPQIFEAYP SFQQVESPEV SGFITSKTSP CGRFLAVSSE NGVRVFKNER
     FQELLLELAL KDVYDLEFSP GGSYLSTWER PHVDNEQHDN VKIWFLNEDE PSAEQPKFQY
     QAKTQNAWSL QFSKLDNYAL KRFGKELRIA KLDHSSPEFN FNQPYARLVP EGHLSTYLIS
     PAEHPTICTF SAEKEGKPAQ LTIYPITEGN IQKKIASKMF FKADSCQLKW NDLGNAVLCL
     AITDFDASNK SYYGENTLYL LSFQGVNGSL GGDSVRVPLG KEGPIHDFTW SPTSRQFGVI
     YGYMPATITF FDLKGNAVHS LAEQRKNTMI FSPSGRYILI AGFGNLQGAV EILDRHDKFK
     CFSKFDAANT STCKWSPGGE FILTATTSPR LRVDNGLKVW HVTGKLCFVN EYTELLEASW
     RNACKYRPKR PDSHVILNWD SSKVEAAKDP AIVPSQLEVH PSVSAYSLKN PNKKNGGSSV
     SKPVGAYKPP HARRAAASNT SSPKSSVPGM TFKPTKSVVP GMAPKETKSA AKNRKKRENT
     GIRKGPDSDG GSSNGTTPEP KEPPKVNKET SPEEKKIRSL LKKLRAIESL KMRQADGDKL
     EDTQILKIQT EQAVLQELDY LGWKP
//

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