ID   LSG1_BOVIN              Reviewed;         652 AA.
AC   Q2YDM7;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   20-DEC-2005, sequence version 1.
DT   03-AUG-2022, entry version 91.
DE   RecName: Full=Large subunit GTPase 1 homolog;
DE            EC=3.6.1.-;
GN   Name=LSG1;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Crossbred X Angus; TISSUE=Liver;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (NOV-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; BC110150; AAI10151.1; -; mRNA.
DR   RefSeq; NP_001039375.1; NM_001045910.2.
DR   AlphaFoldDB; Q2YDM7; -.
DR   SMR; Q2YDM7; -.
DR   STRING; 9913.ENSBTAP00000011134; -.
DR   PaxDb; Q2YDM7; -.
DR   PRIDE; Q2YDM7; -.
DR   GeneID; 505082; -.
DR   KEGG; bta:505082; -.
DR   CTD; 55341; -.
DR   eggNOG; KOG1424; Eukaryota.
DR   InParanoid; Q2YDM7; -.
DR   OrthoDB; 839833at2759; -.
DR   Proteomes; UP000009136; 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; 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   PRINTS; PR00326; GTP1OBG.
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..652
FT                   /note="Large subunit GTPase 1 homolog"
FT                   /id="PRO_0000324552"
FT   DOMAIN          164..438
FT                   /note="CP-type G"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01058"
FT   REGION          288..347
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          625..652
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        293..317
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        324..338
FT                   /note="Basic and acidic 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         387..394
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255"
FT   BINDING         431..434
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         252
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H089"
SQ   SEQUENCE   652 AA;  74249 MW;  55D46ECBADB3F470 CRC64;
     MGRRRAPEGG TLGRALIRQQ VQRSRSHRHT DSWLHTSELN DGYDWGRLNL QSVTEQSSLD
     DFLATAELAG TEFVAEKLNI KFVPPEARTG LLSFEENQRI KKLHEENKQF LCIPRRPKWD
     QKTSPEELKQ AEKDNFLEWR RQLVWLEEEQ NLILTPFERN LDFWRQLWRV IERSDIVVQI
     VDARNPLLFR CEDLECYVKT IDDNKENVIL INKADLLTAE QRSAWAEFFK KENVKVIFWS
     ALAEAIKLMG NSKGDVNGDT GEAITAEFEN SSCDEAEILH KETEHLSLGE AASSEEDESE
     YEDCQEEEED WQTCLEDSSS SDEEACGQDC KEGHTVDSEA QGRNTPQKRQ IHNFSHLVSK
     QELLEVFKQL HSGKKVKDGQ LTVGLVGYPN VGKSSTINTI LGNKKVSVSA TPGHTKHFQT
     LYVEPGLCLC DCPGLVMPSF VSTKAEMICS GILPIDQMRD HVPPVSLVCQ NIPRHVLEAT
     YGIDIIKPRE DEDPRRPPTS EELLTAYGCM RGFMTAHGQP DQPRSARYIL KDYVNGKLLY
     CHPPPGRDPV TFQYQHQRLL EKKVNGGEIK LQVVRNKKVY QIENVVDKAF FHQENVRALT
     KGVQAVMGYK PGSGLVTAAA VSSERGAGKP WKKHGNRNKK EKSRRLYKHL DM