(data stored in ACNUC6288 zone)

SWISSPROT: Q6BMC2_DEBHA

ID   Q6BMC2_DEBHA            Unreviewed;       152 AA.
AC   Q6BMC2;
DT   16-AUG-2004, integrated into UniProtKB/TrEMBL.
DT   16-AUG-2004, sequence version 1.
DT   08-MAY-2019, entry version 97.
DE   SubName: Full=DEHA2F06666p {ECO:0000313|EMBL:CAG88981.1};
GN   OrderedLocusNames=DEHA2F06666g {ECO:0000313|EMBL:CAG88981.1};
OS   Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / JCM 1990 / NBRC
OS   0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX   NCBI_TaxID=284592 {ECO:0000313|EMBL:CAG88981.1, ECO:0000313|Proteomes:UP000000599};
RN   [1] {ECO:0000313|EMBL:CAG88981.1, ECO:0000313|Proteomes:UP000000599}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 36239 / CBS 767 / JCM 1990 / NBRC 0083 / IGC 2968
RC   {ECO:0000313|Proteomes:UP000000599};
RX   PubMed=15229592; DOI=10.1038/nature02579;
RG   Genolevures;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S.,
RA   Lafontaine I., de Montigny J., Marck C., Neuveglise C., Talla E.,
RA   Goffard N., Frangeul L., Aigle M., Anthouard V., Babour A., Barbe V.,
RA   Barnay S., Blanchin S., Beckerich J.M., Beyne E., Bleykasten C.,
RA   Boisrame A., Boyer J., Cattolico L., Confanioleri F., de Daruvar A.,
RA   Despons L., Fabre E., Fairhead C., Ferry-Dumazet H., Groppi A.,
RA   Hantraye F., Hennequin C., Jauniaux N., Joyet P., Kachouri R.,
RA   Kerrest A., Koszul R., Lemaire M., Lesur I., Ma L., Muller H.,
RA   Nicaud J.M., Nikolski M., Oztas S., Ozier-Kalogeropoulos O.,
RA   Pellenz S., Potier S., Richard G.F., Straub M.L., Suleau A.,
RA   Swennene D., Tekaia F., Wesolowski-Louvel M., Westhof E., Wirth B.,
RA   Zeniou-Meyer M., Zivanovic I., Bolotin-Fukuhara M., Thierry A.,
RA   Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J.,
RA   Wincker P., Souciet J.L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
CC   -!- FUNCTION: Seems to be required for maximal rate of protein
CC       biosynthesis. Enhances ribosome dissociation into subunits and
CC       stabilizes the binding of the initiator Met-tRNA(I) to 40 S
CC       ribosomal subunits. {ECO:0000256|RuleBase:RU004365}.
CC   -!- SIMILARITY: Belongs to the eIF-1A family.
CC       {ECO:0000256|RuleBase:RU004364}.
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DR   EMBL; CR382138; CAG88981.1; -; Genomic_DNA.
DR   RefSeq; XP_460649.1; XM_460649.1.
DR   STRING; 4959.XP_460649.1; -.
DR   EnsemblFungi; CAG88981; CAG88981; DEHA2F06666g.
DR   GeneID; 2904117; -.
DR   KEGG; dha:DEHA2F06666g; -.
DR   HOGENOM; HOG000223675; -.
DR   InParanoid; Q6BMC2; -.
DR   KO; K03236; -.
DR   OMA; CTFEFGD; -.
DR   OrthoDB; 1426335at2759; -.
DR   Proteomes; UP000000599; Chromosome F.
DR   GO; GO:0010494; C:cytoplasmic stress granule; IEA:EnsemblFungi.
DR   GO; GO:0016282; C:eukaryotic 43S preinitiation complex; IEA:EnsemblFungi.
DR   GO; GO:0033290; C:eukaryotic 48S preinitiation complex; IEA:EnsemblFungi.
DR   GO; GO:0003725; F:double-stranded RNA binding; IEA:EnsemblFungi.
DR   GO; GO:0019901; F:protein kinase binding; IEA:EnsemblFungi.
DR   GO; GO:0043024; F:ribosomal small subunit binding; IEA:EnsemblFungi.
DR   GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0031369; F:translation initiation factor binding; IEA:EnsemblFungi.
DR   GO; GO:0001732; P:formation of cytoplasmic translation initiation complex; IEA:EnsemblFungi.
DR   GO; GO:0001731; P:formation of translation preinitiation complex; IEA:EnsemblFungi.
DR   CDD; cd05793; S1_IF1A; 1.
DR   HAMAP; MF_00216; aIF_1A; 1.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR006196; RNA-binding_domain_S1_IF1.
DR   InterPro; IPR001253; TIF_eIF-1A.
DR   InterPro; IPR018104; TIF_eIF-1A_CS.
DR   PANTHER; PTHR21668; PTHR21668; 1.
DR   Pfam; PF01176; eIF-1a; 1.
DR   ProDom; PD005579; TIF_eIF-1A; 1.
DR   SMART; SM00652; eIF1a; 1.
DR   SUPFAM; SSF50249; SSF50249; 1.
DR   TIGRFAMs; TIGR00523; eIF-1A; 1.
DR   PROSITE; PS01262; IF1A; 1.
DR   PROSITE; PS50832; S1_IF1_TYPE; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q6BMC2.
DR   SWISS-2DPAGE; Q6BMC2.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000599};
KW   Initiation factor {ECO:0000256|PROSITE-ProRule:PRU00181,
KW   ECO:0000256|RuleBase:RU004365};
KW   Protein biosynthesis {ECO:0000256|PROSITE-ProRule:PRU00181,
KW   ECO:0000256|RuleBase:RU004365};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000599}.
FT   DOMAIN       23     97       S1-like. {ECO:0000259|PROSITE:PS50832}.
SQ   SEQUENCE   152 AA;  17206 MW;  944883C0FB4378D8 CRC64;
     MGKTGKGKGG KNRRRGKNDN GGQKRELIYK DEGQEYAQIT KMLGNGRIEV SCFDGEKRMG
     HIRGKLRKKV WMSQGDIILV SLRDFQDDQC DVIHKYNSDE ARTLKNVGEL PENAKINETD
     TFGADEDEDV NFEFGAEDSD EEEGEDLDID DI
//

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