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Database: UniProt
Entry: NOG2_KLULA
LinkDB: NOG2_KLULA
Original site: NOG2_KLULA 
ID   NOG2_KLULA              Reviewed;         513 AA.
AC   Q6CSP9;
DT   27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   27-MAR-2024, entry version 108.
DE   RecName: Full=Nucleolar GTP-binding protein 2;
GN   Name=NOG2; OrderedLocusNames=KLLA0C18843g;
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: GTPase that associates with pre-60S ribosomal subunits in the
CC       nucleolus and is required for their nuclear export and maturation.
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the TRAFAC class YlqF/YawG GTPase family. NOG2
CC       subfamily. {ECO:0000255|PROSITE-ProRule:PRU01058}.
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DR   EMBL; CR382123; CAH01891.1; -; Genomic_DNA.
DR   RefSeq; XP_453040.1; XM_453040.1.
DR   AlphaFoldDB; Q6CSP9; -.
DR   SMR; Q6CSP9; -.
DR   STRING; 284590.Q6CSP9; -.
DR   PaxDb; 284590-Q6CSP9; -.
DR   GeneID; 2892114; -.
DR   KEGG; kla:KLLA0_C18843g; -.
DR   eggNOG; KOG2423; Eukaryota.
DR   HOGENOM; CLU_011106_4_0_1; -.
DR   InParanoid; Q6CSP9; -.
DR   OMA; RTQGFNH; -.
DR   Proteomes; UP000000598; Chromosome C.
DR   GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0042254; P:ribosome biogenesis; IEA:UniProtKB-KW.
DR   CDD; cd01858; NGP_1; 1.
DR   Gene3D; 1.10.1580.10; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR030378; G_CP_dom.
DR   InterPro; IPR024929; GNL2_CP_dom.
DR   InterPro; IPR006073; GTP-bd.
DR   InterPro; IPR023179; GTP-bd_ortho_bundle_sf.
DR   InterPro; IPR012971; NOG2_N_dom.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR11089; GTP-BINDING PROTEIN-RELATED; 1.
DR   PANTHER; PTHR11089:SF9; NUCLEOLAR GTP-BINDING PROTEIN 2; 1.
DR   Pfam; PF01926; MMR_HSR1; 1.
DR   Pfam; PF08153; NGP1NT; 1.
DR   PRINTS; PR00326; GTP1OBG.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS51721; G_CP; 1.
PE   3: Inferred from homology;
KW   GTP-binding; Nucleotide-binding; Nucleus; Reference proteome;
KW   Ribosome biogenesis.
FT   CHAIN           1..513
FT                   /note="Nucleolar GTP-binding protein 2"
FT                   /id="PRO_0000215812"
FT   DOMAIN          211..372
FT                   /note="CP-type G"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01058"
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          459..513
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        465..488
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         321..328
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255"
FT   BINDING         365..369
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   513 AA;  58683 MW;  04A90C7694C0AAA0 CRC64;
     MGTGKKEKQR RIREGNTKDG NLRVKGENFY RDTKRVQFLN MYKGGRSVRN AKGDIIKAAP
     LQDTAAPTAR VAPDRRWFGN TRVISQDSLS HFREALGENK RDSYQVLLRR NKLPMSLLNE
     KDSAESPTAK ILETEPFEQT FGPKAQRKKP RIAASSLEEL ISSTSTDNKT FEEKQELDST
     LGLMGKQEEE DGWTQAAKEA IFHKGQSKRI WNELYKVIDS SDVVIHVLDA RDPLGTRCKS
     VTDYMTNETP HKHLIYVLNK CDLVPTWVAA AWVKHLSKER PTLAFHASIT NSFGKGSLIQ
     LLRQFSQLHK DRHQISVGFI GYPNTGKSSI INTLRKKKVC QVAPIPGETK VWQYITLMKR
     IFLIDCPGIV PPSSKDSEED ILFRGVVRVE HVSHPEQYIP GILKRCKRQH LERTYEISGW
     KDSVDFIEMI ARKQGRLLKG GEPDESGVSK QILNDFNRGK IPWFVPPPEK DKIEEKEPGD
     KKRPAEENQE DQEEEEKEQE EQEEPVSKKA KKE
//
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