ID   LSG1_MACFA              Reviewed;         653 AA.
AC   Q4R8L2;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2005, sequence version 1.
DT   03-AUG-2022, entry version 60.
DE   RecName: Full=Large subunit GTPase 1 homolog;
DE            EC=3.6.1.-;
GN   Name=LSG1; ORFNames=QtsA-12215;
OS   Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9541;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
RG   International consortium for macaque cDNA sequencing and analysis;
RT   "DNA sequences of macaque genes expressed in brain or testis and its
RT   evolutionary implications.";
RL   Submitted (JUN-2005) 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       Endoplasmic reticulum {ECO:0000250}. Note=Shuttles between the Cajal
CC       bodies in the nucleus and the endoplasmic reticulum. {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; AB168440; BAE00560.1; -; mRNA.
DR   AlphaFoldDB; Q4R8L2; -.
DR   SMR; Q4R8L2; -.
DR   STRING; 9541.XP_005545399.1; -.
DR   PRIDE; Q4R8L2; -.
DR   eggNOG; KOG1424; Eukaryota.
DR   Proteomes; UP000233100; Unplaced.
DR   GO; GO:0015030; C:Cajal body; ISS:UniProtKB.
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; IEA:InterPro.
DR   GO; GO:0051168; P:nuclear export; ISS:UniProtKB.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
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; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR45709; PTHR45709; 1.
DR   Pfam; PF01926; MMR_HSR1; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS51721; G_CP; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Endoplasmic reticulum; GTP-binding; Hydrolase;
KW   Nucleotide-binding; Nucleus; Phosphoprotein; Protein transport;
KW   Reference proteome; Transport.
FT   CHAIN           1..653
FT                   /note="Large subunit GTPase 1 homolog"
FT                   /id="PRO_0000324554"
FT   DOMAIN          164..445
FT                   /note="CP-type G"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01058"
FT   REGION          1..31
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          251..358
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          630..653
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        251..289
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        297..332
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        333..352
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        639..653
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         212..215
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255"
FT   BINDING         394..401
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255"
FT   BINDING         438..441
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         93
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H089"
FT   MOD_RES         97
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H089"
FT   MOD_RES         252
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H089"
SQ   SEQUENCE   653 AA;  74475 MW;  AD12EF3693471BFC CRC64;
     MGRRRAPAGG SLGRALMRHQ TQRSRSHRHT DSWLHTSELN DGYDWGRLNL QSVTEESSLD
     DFLATAELAG TEFVAEKLNI KFVPAEARTG LLSFEESQRI KKLHEENKQF LCIPRRPNWN
     KNTTPEELKQ AEKDNFLEWR RQLVRLEEEQ KLILTSFERN LDFWRQLWRV IERSDIVVQI
     VDARNPLLFR CEDLECYVKE IDASKENVIL INKADLLTAE QRSAWATYFE KEDVKVIFWS
     ALAGAIHLNG DSEEEANKDD RQSNTAEFEH SSFDEAEISH SETEHLPARD SPSLSENLTT
     DEDDSEYEDC PEEEEDDWQT CSEEDGPEEE DCGQDWKESS AADSEAQSRK TPQKRQLHNF
     SHLVSKQELL ELFKELHTGR KVKDGQLTIG TGWGYPNVGK SSTINTIMGN KKVSVSATPG
     HTKHFQTLYV EPGLCLCDCP GLVMPSFVST KAEMTCSGIL PIDQMRDHVP PVSLVCQNIP
     RHVLEATYGI NIIKPREDED PHRPPTSEEL LTAYGYMRGF MTAHGQPDQP RSARYILKDY
     VNGKLLYCHP PPGRDPVTFQ HQHQRLPENK TNGDEIKMRP GRNKKVKQIE NIVDKTFFHQ
     ENVRALTKGV QAVMGYKPGS GVVTAATVSS ENGAGKPWKK HGNRNKKEKS CRL