ID   NOG2_NEUCR              Reviewed;         619 AA.
AC   Q7SHR8;
DT   27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2003, sequence version 1.
DT   03-AUG-2022, entry version 106.
DE   RecName: Full=Nucleolar GTP-binding protein 2;
GN   Name=nog-2; ORFNames=NCU02546;
OS   Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS   FGSC 987).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX   NCBI_TaxID=367110;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX   PubMed=12712197; DOI=10.1038/nature01554;
RA   Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA   Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA   Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA   Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA   Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA   Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA   Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA   Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA   Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA   Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA   DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA   Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA   Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA   Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT   "The genome sequence of the filamentous fungus Neurospora crassa.";
RL   Nature 422:859-868(2003).
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; CM002236; EAA36441.1; -; Genomic_DNA.
DR   RefSeq; XP_965677.1; XM_960584.2.
DR   AlphaFoldDB; Q7SHR8; -.
DR   SMR; Q7SHR8; -.
DR   STRING; 5141.EFNCRP00000002015; -.
DR   EnsemblFungi; EAA36441; EAA36441; NCU02546.
DR   GeneID; 3881827; -.
DR   KEGG; ncr:NCU02546; -.
DR   VEuPathDB; FungiDB:NCU02546; -.
DR   HOGENOM; CLU_011106_4_0_1; -.
DR   InParanoid; Q7SHR8; -.
DR   Proteomes; UP000001805; Chromosome 1, Linkage Group I.
DR   GO; GO:0005730; C:nucleolus; IBA:GO_Central.
DR   GO; GO:0005654; C:nucleoplasm; IEA:EnsemblFungi.
DR   GO; GO:0030687; C:preribosome, large subunit precursor; IEA:EnsemblFungi.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0070180; F:large ribosomal subunit rRNA binding; IEA:EnsemblFungi.
DR   GO; GO:2000200; P:regulation of ribosomal subunit export from nucleus; IEA:EnsemblFungi.
DR   GO; GO:0000055; P:ribosomal large subunit export from nucleus; IEA:EnsemblFungi.
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; Reference proteome;
KW   Ribosome biogenesis.
FT   CHAIN           1..619
FT                   /note="Nucleolar GTP-binding protein 2"
FT                   /id="PRO_0000215813"
FT   DOMAIN          222..383
FT                   /note="CP-type G"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01058"
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          473..619
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..20
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        476..511
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        532..546
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        562..602
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         332..339
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255"
FT   BINDING         376..380
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   619 AA;  69144 MW;  9BACFA70DA0A8914 CRC64;
     MGTGKKEKSR IQRQGKVTGD PKVKGENFYR SAKKIKALNV LKEGKAIRNK EGKVVKAASY
     QSRDVPTAVI EPNRRWFNNT RVISQDTLTS FREAIAEKDK DPYSVLLKSN KLPMSLIRDG
     PKDALKKHQA KMTIESEPFS QTFGPKAQRK RPKLSFNTIG DLTEHSEKSM DTYQARLEEI
     KLLSGASGYG GGLADDDVQE EDFSVATAKE AIFTKGQSKR IWNELYKVID SSDVILHVID
     ARDPLGTRCR HVEKYLATEA PHKHLIFVLN KIDLVPSKTA AAWIRVLQKD HPTCAMRSSI
     KNPFGRGSLI DLLRQFSILH KDRKQISVGL VGYPNVGKSS IINALRGKPV AKVAPIPGET
     KVWQYVTLMR RIYLIDCPGI VPPNQNDTPQ DLLLRGVVRV ENVDNPEQYI PAVLNKVKPH
     HMERTYELKG WKDHIHFLEM LARKGGRLLK GGEPDVDGVA KMVLNDFMRG KIPWFTPAPE
     KEEGETDTME GREGRYGEMS KKRKRDEDDS APATTPASAG EDAKEEDPEN FAGFDSDSDS
     EVEEAAEEKG EEKSTAEDMI PLDASSDEEE DGEEEGSDVE DDEEGSDLDI EGASELEESE
     SEAEAAPAPP PKKQRRSRK