ID   NOG1_KLULA              Reviewed;         643 AA.
AC   Q6CM00;
DT   27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   03-AUG-2022, entry version 100.
DE   RecName: Full=Nucleolar GTP-binding protein 1;
GN   Name=NOG1; OrderedLocusNames=KLLA0E24178g;
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: Involved in the biogenesis of the 60S ribosomal subunit.
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase
CC       superfamily. OBG GTPase family. NOG subfamily. {ECO:0000255|PROSITE-
CC       ProRule:PRU01047}.
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DR   EMBL; CR382125; CAH00126.1; -; Genomic_DNA.
DR   RefSeq; XP_455039.1; XM_455039.1.
DR   AlphaFoldDB; Q6CM00; -.
DR   SMR; Q6CM00; -.
DR   STRING; 28985.XP_455039.1; -.
DR   EnsemblFungi; CAH00126; CAH00126; KLLA0_E24135g.
DR   GeneID; 2894337; -.
DR   KEGG; kla:KLLA0_E24135g; -.
DR   eggNOG; KOG1490; Eukaryota.
DR   HOGENOM; CLU_011784_4_1_1; -.
DR   InParanoid; Q6CM00; -.
DR   OMA; EWKNDVM; -.
DR   Proteomes; UP000000598; Chromosome E.
DR   GO; GO:0005737; C:cytoplasm; IEA:EnsemblFungi.
DR   GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR   GO; GO:0030687; C:preribosome, large subunit precursor; IEA:EnsemblFungi.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:1902626; P:assembly of large subunit precursor of preribosome; IEA:EnsemblFungi.
DR   GO; GO:0042273; P:ribosomal large subunit biogenesis; IEA:EnsemblFungi.
DR   GO; GO:0000054; P:ribosomal subunit export from nucleus; IEA:EnsemblFungi.
DR   GO; GO:0006364; P:rRNA processing; IEA:EnsemblFungi.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR031167; G_OBG.
DR   InterPro; IPR006073; GTP-bd.
DR   InterPro; IPR024926; NOG1.
DR   InterPro; IPR041623; NOG1_N.
DR   InterPro; IPR010674; NOG1_Rossman_fold_dom.
DR   InterPro; IPR012973; NOG_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR005225; Small_GTP-bd_dom.
DR   Pfam; PF06858; NOG1; 1.
DR   Pfam; PF17835; NOG1_N; 1.
DR   Pfam; PF08155; NOGCT; 1.
DR   PIRSF; PIRSF038919; NOG1; 1.
DR   PRINTS; PR00326; GTP1OBG.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR00231; small_GTP; 1.
DR   PROSITE; PS51710; G_OBG; 1.
PE   3: Inferred from homology;
KW   GTP-binding; Nucleotide-binding; Nucleus; Reference proteome;
KW   Ribosome biogenesis.
FT   CHAIN           1..643
FT                   /note="Nucleolar GTP-binding protein 1"
FT                   /id="PRO_0000195033"
FT   DOMAIN          168..340
FT                   /note="OBG-type G"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01047"
FT   REGION          568..643
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        593..624
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         174..181
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01047"
FT   BINDING         220..224
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01047"
FT   BINDING         288..291
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01047"
SQ   SEQUENCE   643 AA;  73937 MW;  3F95A3726F9AC47F CRC64;
     MQLSWKDIPT VAPANDLLDI VLNRTQRKTP TVIRPGFNIT RIRAFYMRKV KFTGEGFVEK
     FDDILKGFPN INDVHPFHRD LMDTLYEKNH FKVSLAAVSR AKTLVEQVER DYTRLLKFGQ
     SLFQCKQLKR AALGRMATIV KKLKDPLVYL EQVRQHLGRM PSIDPNTRTL LICGYPNVGK
     SSFLRCITKA DVEVQPYAFT TKSLYVGHFD YKYLRFQAID TPGILDRPTD EMNNVEMQSI
     YAIAHLRSTV MYFMDLSEQC GFSIEAQVKL FHSIKPLFAN KSVMVVINKT DIIKPEDLDE
     ERKKLLDTVL EVPGVEIMTT SCHEEDNVMA VRNKACEKLL ASRIENKLKS QARITNVLNK
     IHVAQPQKRD DGIDRTPYIP EAIAKMKKYD PEDPNRRKLA KEIEIENGGA GVYNVNLKDK
     YLLEDDEWKN DVMPEILDGK NVYDFLDPEI AIKLQALEEE EERLESEGFY ESDEEETYEG
     FDADEISEIR EKAEWIRDRQ KKMINASRNR KALKNRGTMP RSKLAKTYGD MEKHMSSLGH
     DMTALQDKQR VAAEKNRYEQ TGADVVYGDQ EDSAPAGKLR QTDRLTDGVA DGSMRSKAER
     MAKLERRERN RMARAGESDR HATASLPKHL FSGKRGVGKT DFR