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RSSA_KLULA
ID   RSSA_KLULA              Reviewed;         254 AA.
AC   Q6CN12;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   25-MAY-2022, entry version 102.
DE   RecName: Full=40S ribosomal protein S0 {ECO:0000255|HAMAP-Rule:MF_03015};
GN   Name=RPS0 {ECO:0000255|HAMAP-Rule:MF_03015};
GN   OrderedLocusNames=KLLA0E16171g;
OS   Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS   NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX   NCBI_TaxID=284590;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA   Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA   Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA   Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA   Weissenbach J., Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
CC   -!- FUNCTION: Required for the assembly and/or stability of the 40S
CC       ribosomal subunit. Required for the processing of the 20S rRNA-
CC       precursor to mature 18S rRNA in a late step of the maturation of 40S
CC       ribosomal subunits. {ECO:0000255|HAMAP-Rule:MF_03015}.
CC   -!- SUBUNIT: Component of the small ribosomal subunit. Mature ribosomes
CC       consist of a small (40S) and a large (60S) subunit. The 40S subunit
CC       contains about 33 different proteins and 1 molecule of RNA (18S). The
CC       60S subunit contains about 49 different proteins and 3 molecules of RNA
CC       (25S, 5.8S and 5S). Interacts with RPS21. {ECO:0000255|HAMAP-
CC       Rule:MF_03015}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03015}.
CC   -!- SIMILARITY: Belongs to the universal ribosomal protein uS2 family.
CC       {ECO:0000255|HAMAP-Rule:MF_03015}.
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DR   EMBL; CR382125; CAG99764.1; -; Genomic_DNA.
DR   RefSeq; XP_454677.1; XM_454677.1.
DR   PDB; 3J80; EM; 3.75 A; A=1-254.
DR   PDB; 3J81; EM; 4.00 A; A=1-254.
DR   PDB; 3JAM; EM; 3.46 A; A=1-254.
DR   PDB; 3JAP; EM; 4.90 A; A=1-254.
DR   PDB; 3JAQ; EM; 6.00 A; A=1-254.
DR   PDB; 5IT7; EM; 3.60 A; A=2-207.
DR   PDB; 5IT9; EM; 3.80 A; A=2-207.
DR   PDB; 6FYX; EM; 3.05 A; A=1-254.
DR   PDB; 6FYY; EM; 3.05 A; A=1-254.
DR   PDB; 6GSM; EM; 5.15 A; A=2-209.
DR   PDB; 6GSN; EM; 5.75 A; A=2-220.
DR   PDB; 6UZ7; EM; 3.60 A; A=1-254.
DR   PDBsum; 3J80; -.
DR   PDBsum; 3J81; -.
DR   PDBsum; 3JAM; -.
DR   PDBsum; 3JAP; -.
DR   PDBsum; 3JAQ; -.
DR   PDBsum; 5IT7; -.
DR   PDBsum; 5IT9; -.
DR   PDBsum; 6FYX; -.
DR   PDBsum; 6FYY; -.
DR   PDBsum; 6GSM; -.
DR   PDBsum; 6GSN; -.
DR   PDBsum; 6UZ7; -.
DR   AlphaFoldDB; Q6CN12; -.
DR   SMR; Q6CN12; -.
DR   STRING; 28985.XP_454677.1; -.
DR   PRIDE; Q6CN12; -.
DR   EnsemblFungi; CAG99764; CAG99764; KLLA0_E16171g.
DR   GeneID; 2893732; -.
DR   KEGG; kla:KLLA0_E16171g; -.
DR   eggNOG; KOG0830; Eukaryota.
DR   HOGENOM; CLU_058171_2_0_1; -.
DR   InParanoid; Q6CN12; -.
DR   OMA; ENKMKRY; -.
DR   Proteomes; UP000000598; Chromosome E.
DR   GO; GO:0022627; C:cytosolic small ribosomal subunit; IEA:UniProtKB-UniRule.
DR   GO; GO:0003735; F:structural constituent of ribosome; IEA:UniProtKB-UniRule.
DR   GO; GO:0000028; P:ribosomal small subunit assembly; IEA:UniProtKB-UniRule.
DR   GO; GO:0006412; P:translation; IEA:UniProtKB-UniRule.
DR   CDD; cd01425; RPS2; 1.
DR   HAMAP; MF_03015; Ribosomal_S2_euk; 1.
DR   InterPro; IPR001865; Ribosomal_S2.
DR   InterPro; IPR018130; Ribosomal_S2_CS.
DR   InterPro; IPR027498; Ribosomal_S2_euk.
DR   InterPro; IPR005707; Ribosomal_S2_euk/arc.
DR   InterPro; IPR023591; Ribosomal_S2_flav_dom_sf.
DR   PANTHER; PTHR11489; PTHR11489; 1.
DR   Pfam; PF00318; Ribosomal_S2; 2.
DR   PRINTS; PR00395; RIBOSOMALS2.
DR   SUPFAM; SSF52313; SSF52313; 1.
DR   TIGRFAMs; TIGR01012; uS2_euk_arch; 1.
DR   PROSITE; PS00962; RIBOSOMAL_S2_1; 1.
DR   PROSITE; PS00963; RIBOSOMAL_S2_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Cytoplasm; Reference proteome;
KW   Ribonucleoprotein; Ribosomal protein.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03015"
FT   CHAIN           2..254
FT                   /note="40S ribosomal protein S0"
FT                   /id="PRO_0000371634"
FT   REGION          212..254
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        221..254
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03015"
FT   HELIX           11..20
FT                   /evidence="ECO:0007829|PDB:3JAM"
FT   TURN            21..24
FT                   /evidence="ECO:0007829|PDB:3JAM"
FT   STRAND          37..40
FT                   /evidence="ECO:0007829|PDB:3JAM"
FT   STRAND          46..48
FT                   /evidence="ECO:0007829|PDB:3JAM"
FT   HELIX           50..66
FT                   /evidence="ECO:0007829|PDB:3JAM"
FT   STRAND          67..69
FT                   /evidence="ECO:0007829|PDB:3JAM"
FT   HELIX           70..72
FT                   /evidence="ECO:0007829|PDB:3JAM"
FT   STRAND          73..77
FT                   /evidence="ECO:0007829|PDB:3JAM"
FT   HELIX           80..92
FT                   /evidence="ECO:0007829|PDB:3JAM"
FT   STRAND          96..100
FT                   /evidence="ECO:0007829|PDB:3JAM"
FT   STRAND          104..108
FT                   /evidence="ECO:0007829|PDB:3JAM"
FT   STRAND          119..124
FT                   /evidence="ECO:0007829|PDB:3JAM"
FT   TURN            126..128
FT                   /evidence="ECO:0007829|PDB:3JAM"
FT   HELIX           130..137
FT                   /evidence="ECO:0007829|PDB:3JAM"
FT   TURN            138..140
FT                   /evidence="ECO:0007829|PDB:3JAM"
FT   STRAND          143..145
FT                   /evidence="ECO:0007829|PDB:3JAM"
FT   STRAND          157..159
FT                   /evidence="ECO:0007829|PDB:3JAM"
FT   HELIX           168..185
FT                   /evidence="ECO:0007829|PDB:3JAM"
FT   STRAND          187..189
FT                   /evidence="ECO:0007829|PDB:3JAM"
FT   STRAND          191..193
FT                   /evidence="ECO:0007829|PDB:3JAM"
SQ   SEQUENCE   254 AA;  28238 MW;  BF62481CC047E9CC CRC64;
     MSLPSTFDLT SEDAQLLLAA RVHLGAKNVQ VHQEPYVYKA RPDGVNVINV GKTWEKIVLA
     ARIIAAIPNP EDVVAISSRT YGQRAVLKYA AHTGATPIAG RFTPGSFTNY ITRSFKEPRL
     VIVTDPRSDA QAIKESSYVN IPVIALTDLD SPSEYVDVAI PCNNRGKHSI GLIWYLLARE
     VLRLRGALPD RTQPWAIMPD LYFYRNPEEI EQQTAEEEAV ASGEQTEEAV DATEEQTEAA
     EWAEEGQAQE EEWN
 
 
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