ID   LSG1_DANRE              Reviewed;         640 AA.
AC   Q6NY89;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 97.
DE   RecName: Full=Large subunit GTPase 1 homolog;
DE            EC=3.6.1.-;
GN   Name=lsg1; ORFNames=zgc:76988;
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: GTPase required for the XPO1/CRM1-mediated nuclear export of
CC       the 60S ribosomal subunit. Probably acts by mediating the release of
CC       NMD3 from the 60S ribosomal subunit after export into the cytoplasm (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC   -!- DOMAIN: In contrast to other GTP-binding proteins, this family is
CC       characterized by a circular permutation of the GTPase motifs described
CC       by a G4-G1-G3 pattern.
CC   -!- SIMILARITY: Belongs to the TRAFAC class YlqF/YawG GTPase family. LSG1
CC       subfamily. {ECO:0000255|PROSITE-ProRule:PRU01058}.
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DR   EMBL; BC066695; AAH66695.1; -; mRNA.
DR   RefSeq; NP_997807.1; NM_212642.1.
DR   AlphaFoldDB; Q6NY89; -.
DR   SMR; Q6NY89; -.
DR   STRING; 7955.ENSDARP00000012550; -.
DR   PaxDb; Q6NY89; -.
DR   GeneID; 323464; -.
DR   KEGG; dre:323464; -.
DR   CTD; 55341; -.
DR   ZFIN; ZDB-GENE-030131-2184; lsg1.
DR   eggNOG; KOG1424; Eukaryota.
DR   InParanoid; Q6NY89; -.
DR   OrthoDB; 839833at2759; -.
DR   PhylomeDB; Q6NY89; -.
DR   PRO; PR:Q6NY89; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Unplaced.
DR   GO; GO:0015030; C:Cajal body; ISS:UniProtKB.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR   GO; GO:0005525; F:GTP binding; ISS:UniProtKB.
DR   GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR   GO; GO:0051168; P:nuclear export; ISS:UniProtKB.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   GO; GO:0000054; P:ribosomal subunit export from nucleus; IBA:GO_Central.
DR   Gene3D; 1.10.1580.10; -; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR030378; G_CP_dom.
DR   InterPro; IPR043358; GNL1-like.
DR   InterPro; IPR006073; GTP-bd.
DR   InterPro; IPR023179; GTP-bd_ortho_bundle_sf.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR45709; PTHR45709; 1.
DR   Pfam; PF01926; MMR_HSR1; 1.
DR   PRINTS; PR00326; GTP1OBG.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS51721; G_CP; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; GTP-binding; Hydrolase; Nucleotide-binding; Nucleus;
KW   Protein transport; Reference proteome; Transport.
FT   CHAIN           1..640
FT                   /note="Large subunit GTPase 1 homolog"
FT                   /id="PRO_0000324558"
FT   DOMAIN          165..426
FT                   /note="CP-type G"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01058"
FT   REGION          251..341
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          602..640
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        268..290
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        291..308
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         213..216
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255"
FT   BINDING         375..382
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255"
FT   BINDING         419..422
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   640 AA;  72897 MW;  D595E0836131565A CRC64;
     MGKKKTRGEG SGLGRALIKE RLNAGRGYRR NDTWLHTSEL NDGYDWGRLN LQSVTEQSSL
     DDFLATAELA GTEFVAEKLN IKFVPAEARA GLLSSEESRR LKKLHEENKQ LLRIPRRPPW
     DESTSPEVLQ QTEKDSFLTW RRDLARLEEE QKLILTPFER NLDFWRQLWR VIERSDVVVQ
     IVDARNPLLF RCPDLEKYVK EVSVHKVNML LLNKADLLTR EQRRAWARYF QKEGIRAVFW
     SALAEAQRLE AEERGEDAMD QEDQSDTEEE TASKNATDHH EENSSSPNEE KDENEQDEEE
     EGEDERICVD ESEWQTCSEE SGDEDHAEEN PESTATSSFY NSSRLLRKNE LLEMFKSVHS
     GPTCKDGQIT VGLVGYPNVG KSSTINTIFR NKKVSVSATP GHTKHFQTLF VEPGLCLCDC
     PGLVMPSFVS TKAEMICSGI LPIDQMRDHV PAISLVCQNI PRNVLEGTYG INIIRPREDE
     DPDRPPTYEE LLMAYGYMRG FMTAHGQPDQ SRSARYVLKD YVSGKLLYCH PPPHINPEDF
     QPQHAKFAMR ITGAEQIDGS GGKPSKVKRI ENTVDKQFFH QANVRALTKG VQMVMGYKPG
     SGPVEAGKAN TEQQAGKPWK KHGNRNKKEK VRRLNKHLDA