ID   NOG2_SCHPO              Reviewed;         537 AA.
AC   O14236; Q9US70;
DT   27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 130.
DE   RecName: Full=Nucleolar GTP-binding protein 2;
GN   Name=nog2; ORFNames=SPAC6F6.03c;
OS   Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC   Schizosaccharomyces.
OX   NCBI_TaxID=284812;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=11859360; DOI=10.1038/nature724;
RA   Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA   Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA   Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA   Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA   Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA   Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA   Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA   Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA   O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA   Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA   Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA   Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA   Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA   Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA   Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA   Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA   Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA   Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA   Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA   Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA   del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA   Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA   Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA   Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 1-104, AND SUBCELLULAR
RP   LOCATION.
RC   STRAIN=ATCC 38364 / 968;
RX   PubMed=10759889; DOI=10.1046/j.1365-2443.2000.00317.x;
RA   Ding D.-Q., Tomita Y., Yamamoto A., Chikashige Y., Haraguchi T.,
RA   Hiraoka Y.;
RT   "Large-scale screening of intracellular protein localization in living
RT   fission yeast cells by the use of a GFP-fusion genomic DNA library.";
RL   Genes Cells 5:169-190(2000).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-186; THR-484 AND SER-487, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=18257517; DOI=10.1021/pr7006335;
RA   Wilson-Grady J.T., Villen J., Gygi S.P.;
RT   "Phosphoproteome analysis of fission yeast.";
RL   J. Proteome Res. 7:1088-1097(2008).
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:0000269|PubMed:10759889}.
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; CU329670; CAB11727.1; -; Genomic_DNA.
DR   EMBL; AB028005; BAA87309.1; -; Genomic_DNA.
DR   PIR; T39037; T39037.
DR   RefSeq; NP_593896.1; NM_001019326.2.
DR   AlphaFoldDB; O14236; -.
DR   SMR; O14236; -.
DR   BioGRID; 279226; 9.
DR   STRING; 4896.SPAC6F6.03c.1; -.
DR   iPTMnet; O14236; -.
DR   MaxQB; O14236; -.
DR   PaxDb; O14236; -.
DR   PRIDE; O14236; -.
DR   EnsemblFungi; SPAC6F6.03c.1; SPAC6F6.03c.1:pep; SPAC6F6.03c.
DR   GeneID; 2542777; -.
DR   KEGG; spo:SPAC6F6.03c; -.
DR   PomBase; SPAC6F6.03c; nog2.
DR   VEuPathDB; FungiDB:SPAC6F6.03c; -.
DR   eggNOG; KOG2423; Eukaryota.
DR   HOGENOM; CLU_011106_4_0_1; -.
DR   InParanoid; O14236; -.
DR   OMA; HKHKKFR; -.
DR   PhylomeDB; O14236; -.
DR   PRO; PR:O14236; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0072686; C:mitotic spindle; HDA:PomBase.
DR   GO; GO:0005730; C:nucleolus; ISO:PomBase.
DR   GO; GO:0005634; C:nucleus; HDA:PomBase.
DR   GO; GO:0005525; F:GTP binding; ISO:PomBase.
DR   GO; GO:0003924; F:GTPase activity; ISO:PomBase.
DR   GO; GO:0000055; P:ribosomal large subunit export from nucleus; ISO:PomBase.
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   1: Evidence at protein level;
KW   GTP-binding; Nucleotide-binding; Nucleus; Phosphoprotein;
KW   Reference proteome; Ribosome biogenesis.
FT   CHAIN           1..537
FT                   /note="Nucleolar GTP-binding protein 2"
FT                   /id="PRO_0000215815"
FT   DOMAIN          207..368
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          468..537
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        468..487
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        499..513
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         317..324
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255"
FT   BINDING         361..365
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         186
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
FT   MOD_RES         484
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
FT   MOD_RES         487
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
SQ   SEQUENCE   537 AA;  59914 MW;  425F4F38949AF964 CRC64;
     MGTYKKEKSR IGREGANEKK PGNLRVKGEN FYRNAKDVAR VNMYRGGKAK YNAAGELVRA
     AEFQSSEVPK ARIQPDRRWF NNTRVIAQPT LTQFREAMGQ KLNDPYQVLL RRNKLPMSLL
     QENTEIPKVR VLESEPFENT FGPKSQRKRP KISFDSVAEL AKESDEKQNA YEEKIEERIL
     ANPDESDDVM LAARDAIFSK GQSKRIWNEL YKVIDSSDVL IQVLDARDPV GTRCGTVERY
     LRNEASHKHM ILVLNKVDLV PTSVAAAWVK ILAKEYPTIA FHASINNSFG KGSLIQILRQ
     FASLHSDKKQ ISVGLIGFPN AGKSSIINTL RKKKVCNVAP IPGETKVWQY VALMKRIFLI
     DCPGIVPPSS NDSDAELLLK GVVRVENVSN PEAYIPTVLS RCKVKHLERT YEISGWNDST
     EFLAKLAKKG GRLLKGGEPD EASVAKMVLN DFMRGKIPWF IGPKGLSSSN DEINSSQKVA
     TQQTEGSDQD GEEAEEEWHG ISDDGKADES ESTKPVAEGS ASESTDESAV DDNKNRS