LSG1_SCHPO
ID LSG1_SCHPO Reviewed; 616 AA.
AC Q10190;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Large subunit GTPase 1;
DE EC=3.6.1.-;
GN Name=lsg1; ORFNames=SPAC3F10.16c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
CC -!- FUNCTION: GTPase required for the nuclear export of the 60S ribosomal
CC subunit. Acts by mediating the release of nmd3 from the 60S ribosomal
CC subunit after export into the cytoplasm (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {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; CU329670; CAA93314.1; -; Genomic_DNA.
DR PIR; T38717; T38717.
DR RefSeq; NP_593948.1; NM_001019375.2.
DR AlphaFoldDB; Q10190; -.
DR SMR; Q10190; -.
DR BioGRID; 277954; 1.
DR STRING; 4896.SPAC3F10.16c.1; -.
DR iPTMnet; Q10190; -.
DR MaxQB; Q10190; -.
DR PaxDb; Q10190; -.
DR EnsemblFungi; SPAC3F10.16c.1; SPAC3F10.16c.1:pep; SPAC3F10.16c.
DR GeneID; 2541449; -.
DR KEGG; spo:SPAC3F10.16c; -.
DR PomBase; SPAC3F10.16c; -.
DR VEuPathDB; FungiDB:SPAC3F10.16c; -.
DR eggNOG; KOG1424; Eukaryota.
DR HOGENOM; CLU_011072_5_0_1; -.
DR InParanoid; Q10190; -.
DR OMA; VNKADMM; -.
DR PhylomeDB; Q10190; -.
DR PRO; PR:Q10190; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005525; F:GTP binding; NAS:PomBase.
DR GO; GO:0003924; F:GTPase activity; ISM:PomBase.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0000027; P:ribosomal large subunit assembly; ISO:PomBase.
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 SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS51721; G_CP; 1.
PE 3: Inferred from homology;
KW Cytoplasm; GTP-binding; Hydrolase; Nucleotide-binding; Protein transport;
KW Reference proteome; Transport.
FT CHAIN 1..616
FT /note="Large subunit GTPase 1"
FT /id="PRO_0000122453"
FT DOMAIN 161..359
FT /note="CP-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01058"
FT REGION 247..269
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 552..574
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 587..616
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 209..212
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT BINDING 308..315
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT BINDING 352..355
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
SQ SEQUENCE 616 AA; 69675 MW; F02A2996AF06FB68 CRC64;
MVLPKSKNQI GLGRAIQSDF TKNRRNRKGG LKHIVDSDPK AHRAALRSVT HETDLDEFLN
TAELGEVEFI AEKQNVTVIQ NPEQNPFLLS KEEAARSKQK QEKNKDRLTI PRRPHWDQTT
TAVELDRMER ESFLNWRRNL AQLQDVEGFI VTPFERNLEI WRQLWRVIER SDVVVQIVDA
RNPLFFRSAH LEQYVKEVGP SKKNFLLVNK ADMLTEEQRN YWSSYFNENN IPFLFFSARM
AAEANERGED LETYESTSSN EIPESLQADE NDVHSSRIAT LKVLEGIFEK FASTLPDGKT
KMTFGLVGYP NVGKSSTINA LVGSKKVSVS STPGKTKHFQ TINLSEKVSL LDCPGLVFPS
FATTQADLVL DGVLPIDQLR EYTGPSALMA ERIPKEVLET LYTIRIRIKP IEEGGTGVPS
AQEVLFPFAR SRGFMRAHHG TPDDSRAARI LLKDYVNGKL LYVHPPPNYP NSGSEFNKEH
HQKIVSATSD SITEKLQRTA ISDNTLSAES QLVDDEYFQE NPHVRPMVKG TAVAMQGPVY
KGRNTMQPFQ RRLNDDASPK YPMNAQGKPL SRRKARQLTA LELGVSPEAL SSATSKKHNK
KNKRSKQRSG VVIDDY
