ID   NOG1_CANGA              Reviewed;         645 AA.
AC   Q6FRV0;
DT   27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 95.
DE   RecName: Full=Nucleolar GTP-binding protein 1;
GN   Name=NOG1; OrderedLocusNames=CAGL0H05709g;
OS   Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS   Y-65) (Yeast) (Torulopsis glabrata).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC   Nakaseomyces/Candida clade.
OX   NCBI_TaxID=284593;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
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; CR380954; CAG59977.1; -; Genomic_DNA.
DR   RefSeq; XP_447044.1; XM_447044.1.
DR   AlphaFoldDB; Q6FRV0; -.
DR   SMR; Q6FRV0; -.
DR   STRING; 5478.XP_447044.1; -.
DR   EnsemblFungi; CAG59977; CAG59977; CAGL0H05709g.
DR   GeneID; 2888702; -.
DR   KEGG; cgr:CAGL0H05709g; -.
DR   CGD; CAL0131474; CAGL0H05709g.
DR   VEuPathDB; FungiDB:CAGL0H05709g; -.
DR   eggNOG; KOG1490; Eukaryota.
DR   HOGENOM; CLU_011784_4_1_1; -.
DR   InParanoid; Q6FRV0; -.
DR   OMA; EWKNDVM; -.
DR   Proteomes; UP000002428; Chromosome H.
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   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   PROSITE; PS51710; G_OBG; 1.
PE   3: Inferred from homology;
KW   GTP-binding; Nucleotide-binding; Nucleus; Reference proteome;
KW   Ribosome biogenesis.
FT   CHAIN           1..645
FT                   /note="Nucleolar GTP-binding protein 1"
FT                   /id="PRO_0000195031"
FT   DOMAIN          168..340
FT                   /note="OBG-type G"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01047"
FT   REGION          567..645
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        567..581
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        595..626
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   645 AA;  74087 MW;  ABE5E55146DB1B8B CRC64;
     MQLSWKDIPT VAPANDMLDI VLNRTQRKTP TVIRPGFKIT RIRAFYMRKV KFTAEGFEEK
     FDDILKGFPN INDVHPFHRD LMDTLYEKNH YKISLAAVSR AKTLVEQVSR DYTRLLKFGQ
     SLFQCKQLKR AALGRMATIV KKLKDPLVYL EQVRQHLGRL PSIDPNTRTL LICGYPNVGK
     SSFLRCITKS DVEVQPYAFT TKSLYVGHFD YKYLRFQAID TPGILDRPTE EMNNIEMQSI
     YAIAHLRSCV MYFMDLSEQC GFSVEAQVKL FHSIKPLFAN KSVMVVINKT DIIRPEDLDE
     ERAKLLQTVT ELPGVEIMSA SCQLEDNVMN VRNKACEKLL ASRIENKLKS QARITNVLNK
     IHVAKPQARD DVERTPYIPE EFKKLKKYDP EDPERRLLAR DIEAENGGAG VFNINLKDKY
     ILDDDEWKND IMPEIMDGKN VYDFLDPDIA AKLQALEEEE ERLEKEGFYD SDEDESYGGF
     DQEEIDEIRE KADWIRNKQK KMIAEARNKK SLRNKAMMPR SKLVKSFGDM EKHMATLGHD
     MSSLQDKHRA AAEKSRYVET GADVVFGQND SMASGSNGGK LRQSDRLLDG VADGSMRSKA
     DRMAKLQRRQ RNRDARQGEA DRHATASLPK HLFSGKRGIG KSDFR