ID   LSG1_CHICK              Reviewed;         653 AA.
AC   Q5ZJD3;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   03-AUG-2022, entry version 95.
DE   RecName: Full=Large subunit GTPase 1 homolog;
DE            EC=3.6.1.-;
GN   Name=LSG1; ORFNames=RCJMB04_19c19;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=CB; TISSUE=Bursa of Fabricius;
RX   PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA   Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA   Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA   Hayashizaki Y., Buerstedde J.-M.;
RT   "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT   function analysis.";
RL   Genome Biol. 6:R6.1-R6.9(2005).
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; AJ720501; CAG32160.1; -; mRNA.
DR   RefSeq; NP_001006549.1; NM_001006549.1.
DR   AlphaFoldDB; Q5ZJD3; -.
DR   SMR; Q5ZJD3; -.
DR   STRING; 9031.ENSGALP00000039544; -.
DR   PaxDb; Q5ZJD3; -.
DR   GeneID; 424897; -.
DR   KEGG; gga:424897; -.
DR   CTD; 55341; -.
DR   VEuPathDB; HostDB:geneid_424897; -.
DR   eggNOG; KOG1424; Eukaryota.
DR   InParanoid; Q5ZJD3; -.
DR   OrthoDB; 839833at2759; -.
DR   PhylomeDB; Q5ZJD3; -.
DR   PRO; PR:Q5ZJD3; -.
DR   Proteomes; UP000000539; 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; -; 2.
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; GTP-binding; Hydrolase; Nucleotide-binding; Nucleus;
KW   Protein transport; Reference proteome; Transport.
FT   CHAIN           1..653
FT                   /note="Large subunit GTPase 1 homolog"
FT                   /id="PRO_0000324557"
FT   DOMAIN          155..439
FT                   /note="CP-type G"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01058"
FT   REGION          1..47
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          248..323
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          621..653
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        252..273
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        274..292
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        293..316
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         203..206
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255"
FT   BINDING         388..395
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255"
FT   BINDING         432..435
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   653 AA;  73831 MW;  C48852D0D2334CAF CRC64;
     MGKKRGTGLG RSLQRQRGSE RRGASSWLHA SEVVGESGPE RRSAVEQSPL EEFLATAELA
     GTRFVAERLN IQFVSAQSRT GLLTAQEAQH VRQLHEENRQ FLRIPRRPYW DRTTSSEDLK
     QAERESFLEW RRQLAHLEEE KKLILTPFER NLEFWRQLWR VIERSDIVVQ IVDARNPLLF
     RCQDLESYVK EVSNDKENMI LINKADLLSE EQRAAWAQFF EKEGVKVVFW SALAECRRLS
     GEVKELDADS VADDLSDSEE ESSSQEEDVT AEDSAESTST GSALQTENQC LLSDDDSSDE
     YEDCEDEEED DWQTCSEDEG GDKVNAIAPK SMENRTDIVS MHHVVQEQNR NVKNFSHLVQ
     RNELLEIFKT LHSGPRVKDG EVNVGLVGYP NVGKSSTINT ILGDKKVSVS ATPGRTKHFQ
     TLYVEPGLCL CDCPGLVMPS FVSTKAEMIC SGILPIDQMR DHVPPISLVC QHIPRNILEA
     TYGINIIRPR EDEDPDRKPT AEELLTAYGY MRGFMTAHGQ PDQPRSARYV LKDYVSGKLL
     YCHPPPGIDP DGFQHQHERC PESRTVQASG PVKPKKNTKA KQIENVVDKS FFHQENVRAL
     MKGVRATMGY RPGSGLVSVP APSAGSVVGK PWKKHGNRNK KEKVRRITKH LEN