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Database: UniProt
Entry: Q6CNI7
LinkDB: Q6CNI7
Original site: Q6CNI7 
ID   Q6CNI7_KLULA            Unreviewed;       326 AA.
AC   Q6CNI7;
DT   16-AUG-2004, integrated into UniProtKB/TrEMBL.
DT   16-AUG-2004, sequence version 1.
DT   07-APR-2021, entry version 121.
DE   SubName: Full=KLLA0E12277p {ECO:0000313|EMBL:CAG99589.1};
GN   ORFNames=KLLA0_E12277g {ECO:0000313|EMBL:CAG99589.1};
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:CAG99589.1, 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 3-326.
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 3-326.
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).
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DR   EMBL; CR382125; CAG99589.1; -; Genomic_DNA.
DR   RefSeq; XP_454502.1; XM_454502.1.
DR   PDB; 3J80; EM; 3.75 A; g=1-326.
DR   PDB; 3J81; EM; 4.00 A; g=1-326.
DR   PDB; 3JAM; EM; 3.46 A; g=1-326.
DR   PDB; 3JAP; EM; 4.90 A; g=1-326.
DR   PDB; 3JAQ; EM; 6.00 A; g=1-326.
DR   PDB; 5IT7; EM; 3.60 A; g=3-326.
DR   PDB; 5IT9; EM; 3.80 A; g=3-326.
DR   PDB; 6FYX; EM; 3.05 A; g=1-326.
DR   PDB; 6FYY; EM; 3.05 A; g=1-326.
DR   PDB; 6GSM; EM; 5.15 A; g=3-326.
DR   PDB; 6GSN; EM; 5.75 A; g=3-326.
DR   PDB; 6UZ7; EM; 3.60 A; g=1-326.
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; Q6CNI7; -.
DR   STRING; 28985.XP_454502.1; -.
DR   EnsemblFungi; CAG99589; CAG99589; KLLA0_E12277g.
DR   GeneID; 2893986; -.
DR   KEGG; kla:KLLA0_E12277g; -.
DR   eggNOG; KOG0279; Eukaryota.
DR   HOGENOM; CLU_000288_57_7_1; -.
DR   InParanoid; Q6CNI7; -.
DR   OMA; CKAMLWD; -.
DR   Proteomes; UP000000598; Chromosome E.
DR   GO; GO:0022627; C:cytosolic small ribosomal subunit; IEA:EnsemblFungi.
DR   GO; GO:0001965; F:G-protein alpha-subunit binding; IEA:EnsemblFungi.
DR   GO; GO:0005092; F:GDP-dissociation inhibitor activity; IEA:EnsemblFungi.
DR   GO; GO:0005080; F:protein kinase C binding; IEA:EnsemblFungi.
DR   GO; GO:0043022; F:ribosome binding; IEA:EnsemblFungi.
DR   GO; GO:0000747; P:conjugation with cellular fusion; IEA:EnsemblFungi.
DR   GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IEA:EnsemblFungi.
DR   GO; GO:0001403; P:invasive growth in response to glucose limitation; IEA:EnsemblFungi.
DR   GO; GO:0061157; P:mRNA destabilization; IEA:EnsemblFungi.
DR   GO; GO:1902660; P:negative regulation of glucose mediated signaling pathway; IEA:EnsemblFungi.
DR   GO; GO:2001125; P:negative regulation of translational frameshifting; IEA:EnsemblFungi.
DR   GO; GO:0031954; P:positive regulation of protein autophosphorylation; IEA:EnsemblFungi.
DR   GO; GO:0008104; P:protein localization; IEA:EnsemblFungi.
DR   GO; GO:0080135; P:regulation of cellular response to stress; IEA:EnsemblFungi.
DR   GO; GO:0032995; P:regulation of fungal-type cell wall biogenesis; IEA:EnsemblFungi.
DR   GO; GO:0010389; P:regulation of G2/M transition of mitotic cell cycle; IEA:EnsemblFungi.
DR   Gene3D; 2.130.10.10; -; 1.
DR   InterPro; IPR020472; G-protein_beta_WD-40_rep.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   InterPro; IPR001680; WD40_repeat.
DR   InterPro; IPR019775; WD40_repeat_CS.
DR   InterPro; IPR017986; WD40_repeat_dom.
DR   InterPro; IPR036322; WD40_repeat_dom_sf.
DR   Pfam; PF00400; WD40; 5.
DR   PRINTS; PR00320; GPROTEINBRPT.
DR   SMART; SM00320; WD40; 7.
DR   SUPFAM; SSF50978; SSF50978; 1.
DR   PROSITE; PS00678; WD_REPEATS_1; 3.
DR   PROSITE; PS50082; WD_REPEATS_2; 5.
DR   PROSITE; PS50294; WD_REPEATS_REGION; 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   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   WD repeat {ECO:0000256|ARBA:ARBA00022574, ECO:0000256|PROSITE-
KW   ProRule:PRU00221}.
FT   DOMAIN          14..326
FT                   /note="WD_REPEATS_REGION"
FT                   /evidence="ECO:0000259|PROSITE:PS50294"
FT   REPEAT          14..56
FT                   /note="WD"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT   REPEAT          62..103
FT                   /note="WD"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT   REPEAT          104..136
FT                   /note="WD"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT   REPEAT          199..240
FT                   /note="WD"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT   REPEAT          289..326
FT                   /note="WD"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
SQ   SEQUENCE   326 AA;  35794 MW;  BEA3298E4EE6352B CRC64;
     MSSSNIMLVL RGTLEGHNGW VTSLSTSAAQ PNLLVSGSRD KTLISWRLTE NEQQFGVPVR
     SYKGHSHIVQ DVVVSADGNY AVSASWDKTL RLWNLATGNS EARFVGHTGD VLSVAIDANS
     SKIISASRDK TIRVWNTVGD CAYVLLGHTD WVTKVRVAPK NLEDGEVDDG RITFVSAGMD
     KIVRSWSLNE DSYRIEADFI GHNNYINVVQ PSPDGSLAAS AGKDGQIYVW NLKHKSAFMN
     FDAKDEVFAL AFSPSRFWLT AATASGIKIY DLENEVLIDE LKPEFAGYTK AQDPHAVSLA
     WSADGQTLFA GYTDNVIRVW QVMTAN
//
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