ID   NOG2_CRYNV              Reviewed;         693 AA.
AC   P0CS94; Q8J0Y9; Q8J109;
DT   06-FEB-2013, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2013, sequence version 1.
DT   03-AUG-2022, entry version 29.
DE   RecName: Full=Nucleolar GTP-binding protein 2;
GN   Name=NOG2;
OS   Cryptococcus neoformans var. grubii (Filobasidiella neoformans var.
OS   grubii).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC   Tremellales; Cryptococcaceae; Cryptococcus;
OC   Cryptococcus neoformans species complex.
OX   NCBI_TaxID=178876;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=125.91;
RX   PubMed=12455690; DOI=10.1128/ec.1.5.704-718.2002;
RA   Lengeler K.B., Fox D.S., Fraser J.A., Allen A., Forrester K.,
RA   Dietrich F.S., Heitman J.;
RT   "Mating-type locus of Cryptococcus neoformans: a step in the evolution of
RT   sex chromosomes.";
RL   Eukaryot. Cell 1:704-718(2002).
RN   [2]
RP   SEQUENCE REVISION.
RA   Dietrich F.S.;
RL   Submitted (DEC-2004) to the EMBL/GenBank/DDBJ databases.
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   -!- MISCELLANEOUS: The C.neoformans mating-type locus is unique, spans >100
CC       kb, and contains more than 20 genes. MAT-encoded products include
CC       homologs of regulators of sexual development in other fungi, pheromone
CC       and pheromone receptors, divergent components of a MAP kinase cascade,
CC       and other proteins with no obvious function in mating.
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; AF542528; AAN75146.2; -; Genomic_DNA.
DR   AlphaFoldDB; P0CS94; -.
DR   SMR; P0CS94; -.
DR   PRIDE; P0CS94; -.
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   Gene3D; 1.10.1580.10; -; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR030378; G_CP_dom.
DR   InterPro; IPR006073; GTP-bd.
DR   InterPro; IPR023179; GTP-bd_ortho_bundle_sf.
DR   InterPro; IPR024929; NOG2.
DR   InterPro; IPR012971; NOG2_N_dom.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR11089:SF9; PTHR11089:SF9; 1.
DR   Pfam; PF01926; MMR_HSR1; 1.
DR   Pfam; PF08153; NGP1NT; 1.
DR   PRINTS; PR00326; GTP1OBG.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS51721; G_CP; 1.
PE   3: Inferred from homology;
KW   GTP-binding; Nucleotide-binding; Nucleus; Ribosome biogenesis.
FT   CHAIN           1..693
FT                   /note="Nucleolar GTP-binding protein 2"
FT                   /id="PRO_0000215811"
FT   DOMAIN          198..359
FT                   /note="CP-type G"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01058"
FT   REGION          1..27
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          144..164
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          461..500
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          541..693
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..15
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        481..500
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        541..586
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        594..617
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        618..642
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        643..660
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        661..693
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         308..315
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255"
FT   BINDING         352..356
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   693 AA;  77644 MW;  3DFDC9EF1BE61119 CRC64;
     MGKGKNHDRK ANPGFGKVKS KTGTSTGEFT LKRVKGENFY RDAKSASRVK MLNGGKAVRD
     RDGKIVEAAA FQKGEKEAEP GRVKPDRRWF GNTRVISQSA LDHFRTALKE QKADPYSVLL
     KRNKLPMGFG SRKNRKQRPH IVETEPFGNT FGPKAQRKRP RLDIGKGNGT ADLADIYHPT
     TSTAREPIYA KGTSRRIWGE LYKVLDSSDV VIHVLDARDP LGTRCKPVVE YLRKEKAHKH
     LVYVLNKVDL VPTWVTARWV KHLSLSAPTI AFHASINNSF GKGSLIQLLR QFSVLHSDKK
     QISVGFIGYP NTGKSSIINT LKKKKVCTVA PIPGETKVWQ YITLMRRIYL IDCPGIVPVS
     AKDSDTDTVL KGVVRVENLA TPAEHIPALL ERVRPEYLER TYGLEHVEGG WHGEEGATFV
     LTAIAKKSGK LLKGGEPDQE AAAKMVLNDW IRGKVPFFVA PPTKPESGAD AHVSSATTEK
     VQEQEQKELA EEKETKEMLE EQERSLGKVL GIKRVKGVEQ PISKIVTMTK FLGDDARRYV
     EEEEVDVDDV DKEMAEEDED EDEDDDDDVE ESGEDQEEEE LAWDDVFPEE AAGVDAADGE
     EVEEDDEEEE GDEDDEDVPS AKQLGKRKAI DSDEEEQTAI KAKRMTTNKQ KASNFYTHAN
     VKNRNRDRKV PKNPGKRSRG DDEPTGKKAK KRR