NOG1_ENCCU
ID NOG1_ENCCU Reviewed; 528 AA.
AC Q8SVJ8;
DT 27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Nucleolar GTP-binding protein 1;
GN Name=NOG1; OrderedLocusNames=ECU05_0800;
OS Encephalitozoon cuniculi (strain GB-M1) (Microsporidian parasite).
OC Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Unikaryonidae;
OC Encephalitozoon.
OX NCBI_TaxID=284813;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GB-M1;
RX PubMed=11719806; DOI=10.1038/35106579;
RA Katinka M.D., Duprat S., Cornillot E., Metenier G., Thomarat F.,
RA Prensier G., Barbe V., Peyretaillade E., Brottier P., Wincker P.,
RA Delbac F., El Alaoui H., Peyret P., Saurin W., Gouy M., Weissenbach J.,
RA Vivares C.P.;
RT "Genome sequence and gene compaction of the eukaryote parasite
RT Encephalitozoon cuniculi.";
RL Nature 414:450-453(2001).
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; AL590445; CAD26599.1; -; Genomic_DNA.
DR RefSeq; NP_597422.1; NM_001041288.1.
DR AlphaFoldDB; Q8SVJ8; -.
DR SMR; Q8SVJ8; -.
DR STRING; 284813.Q8SVJ8; -.
DR PRIDE; Q8SVJ8; -.
DR GeneID; 859087; -.
DR KEGG; ecu:ECU05_0800; -.
DR VEuPathDB; MicrosporidiaDB:ECU05_0800; -.
DR HOGENOM; CLU_011784_5_1_1; -.
DR InParanoid; Q8SVJ8; -.
DR OMA; ISAYRCK; -.
DR OrthoDB; 678655at2759; -.
DR Proteomes; UP000000819; Chromosome V.
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; 3.40.50.300; -; 1.
DR InterPro; IPR031167; G_OBG.
DR InterPro; IPR006073; GTP-bd.
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 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..528
FT /note="Nucleolar GTP-binding protein 1"
FT /id="PRO_0000195032"
FT DOMAIN 168..335
FT /note="OBG-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01047"
FT REGION 470..528
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 470..490
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 504..519
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 287..290
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01047"
SQ SEQUENCE 528 AA; 61339 MW; E84804BA4EA5E9DE CRC64;
MKANFGYITP VPLNMELIDI SLSKTQKRTP TVIHPQYNIV KIRMFYMRKV KHAGNEFASR
LGTILTDFPR IEDIHPFYGD LINVLYDRDH YKLALGHVNA AKNGIEKVSK EFVKLLKFAD
SLYRCKQLKR AALGRMASAA KKLGKTLEYL EEVRMHMSRL PSIDLSGRTL LVCGFPNVGK
SSFVRKISRA DVEVQPYPFT TKSLYVGHFD YKYLQWQVID TPGILDQPLE NRNTIEMLSI
TALAHIKAVV LYFIDLSETC GYSVEEQMDL FNTLNPLLSS NMVIVLSKSD VLGLSGMEDK
KAIMSFLEGK KYMEMSCEKE ENIDAVKAMA CDLLLDERFE RKINSERLSE YINRITIVRP
KELREKAESF ICSREVTEIE NEQERYLIPE EYRYDIVPEI VDGKNVADFF DPDIEKKLKE
VEEEEEGLLP MYCKTYDVLS PEERALKEEV VAGIERRRII NRLREKKRLP DSWKHRSRNS
GGDIAVHVRR DSKTQVAQPP RLPSKKKARF DDKHYYDRKP KHLYRGRK