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Database: UniProt
Entry: S9VTU9_SCHCR
LinkDB: S9VTU9_SCHCR
Original site: S9VTU9_SCHCR 
ID   S9VTU9_SCHCR            Unreviewed;       109 AA.
AC   S9VTU9;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   31-JUL-2019, entry version 27.
DE   SubName: Full=Ribosomal protein A4 {ECO:0000313|EMBL:EPY49599.1};
GN   ORFNames=SPOG_01483 {ECO:0000313|EMBL:EPY49599.1};
OS   Schizosaccharomyces cryophilus (strain OY26 / ATCC MYA-4695 / CBS
OS   11777 / NBRC 106824 / NRRL Y48691) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales;
OC   Schizosaccharomycetaceae; Schizosaccharomyces.
OX   NCBI_TaxID=653667 {ECO:0000313|EMBL:EPY49599.1, ECO:0000313|Proteomes:UP000015464};
RN   [1] {ECO:0000313|EMBL:EPY49599.1, ECO:0000313|Proteomes:UP000015464}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OY26 / ATCC MYA-4695 / CBS 11777 / NBRC 106824 / NRRL Y48691
RC   {ECO:0000313|Proteomes:UP000015464};
RX   PubMed=21511999; DOI=10.1126/science.1203357;
RA   Rhind N., Chen Z., Yassour M., Thompson D.A., Haas B.J., Habib N.,
RA   Wapinski I., Roy S., Lin M.F., Heiman D.I., Young S.K., Furuya K.,
RA   Guo Y., Pidoux A., Chen H.M., Robbertse B., Goldberg J.M., Aoki K.,
RA   Bayne E.H., Berlin A.M., Desjardins C.A., Dobbs E., Dukaj L., Fan L.,
RA   FitzGerald M.G., French C., Gujja S., Hansen K., Keifenheim D.,
RA   Levin J.Z., Mosher R.A., Mueller C.A., Pfiffner J., Priest M.,
RA   Russ C., Smialowska A., Swoboda P., Sykes S.M., Vaughn M.,
RA   Vengrova S., Yoder R., Zeng Q., Allshire R., Baulcombe D.,
RA   Birren B.W., Brown W., Ekwall K., Kellis M., Leatherwood J., Levin H.,
RA   Margalit H., Martienssen R., Nieduszynski C.A., Spatafora J.W.,
RA   Friedman N., Dalgaard J.Z., Baumann P., Niki H., Regev A., Nusbaum C.;
RT   "Comparative functional genomics of the fission yeasts.";
RL   Science 332:930-936(2011).
CC   -!- SIMILARITY: Belongs to the eukaryotic ribosomal protein P1/P2
CC       family. {ECO:0000256|SAAS:SAAS01033820}.
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DR   EMBL; KE546995; EPY49599.1; -; Genomic_DNA.
DR   RefSeq; XP_013025624.1; XM_013170170.1.
DR   STRING; 866546.EPY49599; -.
DR   EnsemblFungi; EPY49599; EPY49599; SPOG_01483.
DR   GeneID; 25035811; -.
DR   OMA; EYIYAAM; -.
DR   OrthoDB; 1805852at2759; -.
DR   Proteomes; UP000015464; Unassembled WGS sequence.
DR   GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW.
DR   GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR   GO; GO:0006414; P:translational elongation; IEA:InterPro.
DR   Gene3D; 1.10.10.1410; -; 1.
DR   HAMAP; MF_01478; Ribosomal_L12_arch; 1.
DR   InterPro; IPR038716; P1/P2_N_sf.
DR   InterPro; IPR027534; Ribosomal_L12.
DR   InterPro; IPR001859; T.cruzi_P2-like.
DR   PRINTS; PR00456; RIBOSOMALP2.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000015464};
KW   Reference proteome {ECO:0000313|Proteomes:UP000015464};
KW   Ribonucleoprotein {ECO:0000256|SAAS:SAAS01033817};
KW   Ribosomal protein {ECO:0000256|SAAS:SAAS01033821,
KW   ECO:0000313|EMBL:EPY49599.1}.
FT   REGION       67    109       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   COILED       32     52       {ECO:0000256|SAM:Coils}.
FT   COMPBIAS     93    109       Acidic. {ECO:0000256|SAM:MobiDB-lite}.
SQ   SEQUENCE   109 AA;  11052 MW;  BCB4AA68910786A7 CRC64;
     MKYLAAYLLL TVGGKQSPSA SDVETVLSTV GIEAEKERVE CLLKELEGKN LEELIAAGNE
     KLATVPSGGG AAAAAPAAGA PGASATEEAK PEAPAEEESD EDMGFGLFD
//
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