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Database: UniProt
Entry: Q6CRK7
LinkDB: Q6CRK7
Original site: Q6CRK7 
ID   Q6CRK7_KLULA            Unreviewed;       237 AA.
AC   Q6CRK7;
DT   16-AUG-2004, integrated into UniProtKB/TrEMBL.
DT   16-AUG-2004, sequence version 1.
DT   07-APR-2021, entry version 119.
DE   SubName: Full=KLLA0D08305p {ECO:0000313|EMBL:CAH00528.1};
GN   ORFNames=KLLA0_D08305g {ECO:0000313|EMBL:CAH00528.1};
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 {ECO:0000313|Proteomes:UP000000598};
RN   [1] {ECO:0000313|EMBL:CAH00528.1, ECO:0000313|Proteomes:UP000000598}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 /
RC   WM37 {ECO:0000313|Proteomes:UP000000598};
RX   PubMed=15229592; DOI=10.1038/nature02579;
RG   Genolevures;
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., Straub M.L.,
RA   Suleau A., Swennene D., Tekaia F., Wesolowski-Louvel M., Westhof E.,
RA   Wirth B., 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).
RN   [2] {ECO:0007829|PDB:3J80, ECO:0007829|PDB:3J81}
RP   STRUCTURE BY ELECTRON MICROSCOPY (3.75 ANGSTROMS).
RX   PubMed=25417110; DOI=10.1016/j.cell.2014.10.001;
RA   Hussain T., Llacer J.L., Fernandez I.S., Munoz A., Martin-Marcos P.,
RA   Savva C.G., Lorsch J.R., Hinnebusch A.G., Ramakrishnan V.;
RT   "Structural changes enable start codon recognition by the eukaryotic
RT   translation initiation complex.";
RL   Cell 159:597-607(2014).
RN   [3] {ECO:0007829|PDB:3JAM, ECO:0007829|PDB:3JAP}
RP   STRUCTURE BY ELECTRON MICROSCOPY (3.46 ANGSTROMS).
RX   PubMed=26212456; DOI=10.1016/j.molcel.2015.06.033;
RA   Llacer J.L., Hussain T., Marler L., Aitken C.E., Thakur A., Lorsch J.R.,
RA   Hinnebusch A.G., Ramakrishnan V.;
RT   "Conformational differences between open and closed states of the
RT   eukaryotic translation initiation complex.";
RL   Mol. Cell 59:399-412(2015).
RN   [4] {ECO:0007829|PDB:5IT7, ECO:0007829|PDB:5IT9}
RP   STRUCTURE BY ELECTRON MICROSCOPY (3.60 ANGSTROMS) OF 3-225.
RX   PubMed=27159451; DOI=10.7554/eLife.13567;
RA   Murray J., Savva C.G., Shin B.S., Dever T.E., Ramakrishnan V.,
RA   Fernandez I.S.;
RT   "Structural characterization of ribosome recruitment and translocation by
RT   type IV IRES.";
RL   Elife 5:0-0(2016).
RN   [5] {ECO:0007829|PDB:6FYX, ECO:0007829|PDB:6FYY}
RP   STRUCTURE BY ELECTRON MICROSCOPY (3.05 ANGSTROMS).
RX   PubMed=30475211; DOI=10.7554/eLife.39273;
RA   Llacer J.L., Hussain T., Saini A.K., Nanda J.S., Kaur S., Gordiyenko Y.,
RA   Kumar R., Hinnebusch A.G., Lorsch J.R., Ramakrishnan V.;
RT   "Translational initiation factor eIF5 replaces eIF1 on the 40S ribosomal
RT   subunit to promote start-codon recognition.";
RL   Elife 7:0-0(2018).
RN   [6] {ECO:0007829|PDB:6GSM, ECO:0007829|PDB:6GSN}
RP   STRUCTURE BY ELECTRON MICROSCOPY (5.75 ANGSTROMS) OF 3-225.
RA   Llacer J.L., Hussain T., Gordiyenko Y., Ramakrishnan V.;
RT   "Towards a model of eIF3 on the 40S subunit interface in eukaryotic
RT   translation initiation.";
RL   Submitted (JUN-2018) to the PDB data bank.
RN   [7] {ECO:0007829|PDB:6UZ7}
RP   STRUCTURE BY ELECTRON MICROSCOPY (3.60 ANGSTROMS).
RX   PubMed=31900355; DOI=10.1073/pnas.1916436117;
RA   Huang B.Y., Fernandez I.S.;
RT   "Long-range interdomain communications in eIF5B regulate GTP hydrolysis and
RT   translation initiation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 117:1429-1437(2020).
CC   -!- SIMILARITY: Belongs to the universal ribosomal protein uS3 family.
CC       {ECO:0000256|ARBA:ARBA00010761, ECO:0000256|RuleBase:RU003624}.
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DR   EMBL; CR382124; CAH00528.1; -; Genomic_DNA.
DR   RefSeq; XP_453432.1; XM_453432.1.
DR   PDB; 3J80; EM; 3.75 A; D=1-237.
DR   PDB; 3J81; EM; 4.00 A; D=1-237.
DR   PDB; 3JAM; EM; 3.46 A; D=1-237.
DR   PDB; 3JAP; EM; 4.90 A; D=1-237.
DR   PDB; 3JAQ; EM; 6.00 A; D=1-237.
DR   PDB; 5IT7; EM; 3.60 A; D=3-225.
DR   PDB; 5IT9; EM; 3.80 A; D=3-225.
DR   PDB; 6FYX; EM; 3.05 A; D=1-237.
DR   PDB; 6FYY; EM; 3.05 A; D=1-237.
DR   PDB; 6GSM; EM; 5.15 A; D=3-225.
DR   PDB; 6GSN; EM; 5.75 A; D=3-225.
DR   PDB; 6UZ7; EM; 3.60 A; D=1-237.
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   SMR; Q6CRK7; -.
DR   STRING; 28985.XP_453432.1; -.
DR   EnsemblFungi; CAH00528; CAH00528; KLLA0_D08305g.
DR   GeneID; 2893244; -.
DR   KEGG; kla:KLLA0_D08305g; -.
DR   eggNOG; KOG3181; Eukaryota.
DR   HOGENOM; CLU_058591_2_1_1; -.
DR   InParanoid; Q6CRK7; -.
DR   OMA; MLPHDPE; -.
DR   Proteomes; UP000000598; Chromosome D.
DR   GO; GO:0022627; C:cytosolic small ribosomal subunit; IEA:EnsemblFungi.
DR   GO; GO:0030688; C:preribosome, small subunit precursor; IEA:EnsemblFungi.
DR   GO; GO:0003906; F:DNA-(apurinic or apyrimidinic site) endonuclease activity; IEA:EnsemblFungi.
DR   GO; GO:0034236; F:protein kinase A catalytic subunit binding; IEA:EnsemblFungi.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003735; F:structural constituent of ribosome; IEA:EnsemblFungi.
DR   GO; GO:0000056; P:ribosomal small subunit export from nucleus; IEA:EnsemblFungi.
DR   GO; GO:0006407; P:rRNA export from nucleus; IEA:EnsemblFungi.
DR   GO; GO:0006412; P:translation; IEA:InterPro.
DR   Gene3D; 3.30.1140.32; -; 1.
DR   Gene3D; 3.30.300.20; -; 1.
DR   InterPro; IPR015946; KH_dom-like_a/b.
DR   InterPro; IPR004044; KH_dom_type_2.
DR   InterPro; IPR009019; KH_sf_prok-type.
DR   InterPro; IPR001351; Ribosomal_S3_C.
DR   InterPro; IPR036419; Ribosomal_S3_C_sf.
DR   InterPro; IPR018280; Ribosomal_S3_CS.
DR   InterPro; IPR005703; Ribosomal_S3_euk/arc.
DR   Pfam; PF07650; KH_2; 1.
DR   Pfam; PF00189; Ribosomal_S3_C; 1.
DR   SUPFAM; SSF54814; SSF54814; 1.
DR   SUPFAM; SSF54821; SSF54821; 1.
DR   TIGRFAMs; TIGR01008; uS3_euk_arch; 1.
DR   PROSITE; PS50823; KH_TYPE_2; 1.
DR   PROSITE; PS00548; RIBOSOMAL_S3; 1.
PE   1: Evidence at protein level;
KW   3D-structure {ECO:0007829|PDB:3J80, ECO:0007829|PDB:3J81};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000598};
KW   Ribonucleoprotein {ECO:0000256|ARBA:ARBA00023274,
KW   ECO:0000256|RuleBase:RU003624};
KW   Ribosomal protein {ECO:0000256|ARBA:ARBA00022980,
KW   ECO:0000256|RuleBase:RU003624};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|PROSITE-
KW   ProRule:PRU00118}.
FT   DOMAIN          21..92
FT                   /note="KH type-2"
FT                   /evidence="ECO:0000259|PROSITE:PS50823"
FT   REGION          213..237
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        213..230
FT                   /note="Polyampholyte"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   237 AA;  26258 MW;  24976B64CD88150C CRC64;
     MVAIISKKRK LVADGVFYAE LNEFFTRELA EEGYSGVEVR VTPTKTEIII RATKVQDVVG
     ENGRRINELT LLIEKRFKYK RGTIALYAER VHDRGLSAVA QAESMKFKLL NGLAIRRAAY
     GVVRYVMESG AKGCEVVISG KLRAARAKSM KFADGFLIHS GQPVNDFIET ATRHVLLRQG
     VLGIKVKIMK DPSRNTSGPK ALPDAVTIIE PKEEEPVLEP SVKDYRPTEP VEAAESA
//
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