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IF1A_SCHPO
ID   IF1A_SCHPO              Reviewed;         138 AA.
AC   P55877;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   15-JUL-1998, sequence version 2.
DT   25-MAY-2022, entry version 136.
DE   RecName: Full=Eukaryotic translation initiation factor 1A;
DE            Short=eIF-1A;
DE   AltName: Full=Eukaryotic translation initiation factor 4C;
DE            Short=eIF-4C;
GN   Name=tif11; ORFNames=SPBC25H2.07;
OS   Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC   Schizosaccharomyces.
OX   NCBI_TaxID=284812;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=11859360; DOI=10.1038/nature724;
RA   Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA   Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA   Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA   Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA   Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA   Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA   Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA   Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA   O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA   Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA   Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA   Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA   Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA   Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA   Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA   Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA   Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA   Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA   Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA   Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA   del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA   Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA   Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA   Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 3-138.
RA   Kawamukai M.;
RT   "S.pombe translation initiation factor eIF1A.";
RL   Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
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 ribosomal
CC       subunits (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the eIF-1A family. {ECO:0000305}.
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DR   EMBL; CU329671; CAB08783.1; -; Genomic_DNA.
DR   EMBL; AB000518; BAA19134.1; -; mRNA.
DR   PIR; T40002; T40002.
DR   RefSeq; NP_596359.1; NM_001022280.2.
DR   AlphaFoldDB; P55877; -.
DR   SMR; P55877; -.
DR   BioGRID; 277049; 3.
DR   STRING; 4896.SPBC25H2.07.1; -.
DR   MaxQB; P55877; -.
DR   PaxDb; P55877; -.
DR   EnsemblFungi; SPBC25H2.07.1; SPBC25H2.07.1:pep; SPBC25H2.07.
DR   GeneID; 2540521; -.
DR   KEGG; spo:SPBC25H2.07; -.
DR   PomBase; SPBC25H2.07; tif11.
DR   VEuPathDB; FungiDB:SPBC25H2.07; -.
DR   eggNOG; KOG3403; Eukaryota.
DR   HOGENOM; CLU_109098_2_0_1; -.
DR   InParanoid; P55877; -.
DR   OMA; KMEDQEY; -.
DR   PhylomeDB; P55877; -.
DR   Reactome; R-SPO-156827; L13a-mediated translational silencing of Ceruloplasmin expression.
DR   Reactome; R-SPO-72649; Translation initiation complex formation.
DR   Reactome; R-SPO-72689; Formation of a pool of free 40S subunits.
DR   Reactome; R-SPO-72695; Formation of the ternary complex, and subsequently, the 43S complex.
DR   Reactome; R-SPO-72702; Ribosomal scanning and start codon recognition.
DR   PRO; PR:P55877; -.
DR   Proteomes; UP000002485; Chromosome II.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; HDA:PomBase.
DR   GO; GO:0003725; F:double-stranded RNA binding; IDA:PomBase.
DR   GO; GO:0033592; F:RNA strand annealing activity; IDA:PomBase.
DR   GO; GO:0003743; F:translation initiation factor activity; ISO:PomBase.
DR   GO; GO:0002183; P:cytoplasmic translational initiation; ISO:PomBase.
DR   GO; GO:0006413; P:translational initiation; IBA:GO_Central.
DR   CDD; cd05793; S1_IF1A; 1.
DR   Gene3D; 2.40.50.140; -; 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   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   2: Evidence at transcript level;
KW   Initiation factor; Protein biosynthesis; Reference proteome.
FT   CHAIN           1..138
FT                   /note="Eukaryotic translation initiation factor 1A"
FT                   /id="PRO_0000145112"
FT   DOMAIN          22..96
FT                   /note="S1-like"
FT   REGION          1..28
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        13..28
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   138 AA;  15678 MW;  BF8C81EBFDC0FF85 CRC64;
     MPKNKGKGGK NRRRGKNENE NEKRELTYAE EGQMYAQVTK MLGNGRIEAA CFDGVKRLGH
     IRGKLRKKVW INQGDIILLS LREFQDEKGD VILKYTADEA RTLKNQGELP ETAKINETDT
     FGAEGEDDLD FEFDVDAI
 
 
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