位置:首页 > 蛋白库 > GSP1_ENCCU
GSP1_ENCCU
ID   GSP1_ENCCU              Reviewed;         214 AA.
AC   Q8SS11;
DT   01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   03-AUG-2022, entry version 121.
DE   RecName: Full=GTP-binding nuclear protein GSP1;
DE   AltName: Full=GTPase Ran homolog;
GN   Name=GSP1; OrderedLocusNames=ECU04_1560;
OS   Encephalitozoon cuniculi (strain GB-M1) (Microsporidian parasite).
OC   Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Unikaryonidae;
OC   Encephalitozoon.
OX   NCBI_TaxID=284813;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GB-M1;
RX   PubMed=11719806; DOI=10.1038/35106579;
RA   Katinka M.D., Duprat S., Cornillot E., Metenier G., Thomarat F.,
RA   Prensier G., Barbe V., Peyretaillade E., Brottier P., Wincker P.,
RA   Delbac F., El Alaoui H., Peyret P., Saurin W., Gouy M., Weissenbach J.,
RA   Vivares C.P.;
RT   "Genome sequence and gene compaction of the eukaryote parasite
RT   Encephalitozoon cuniculi.";
RL   Nature 414:450-453(2001).
RN   [2]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], DEVELOPMENTAL
RP   STAGE, AND SUBCELLULAR LOCATION.
RX   PubMed=16691553; DOI=10.1002/pmic.200500796;
RA   Brosson D., Kuhn L., Delbac F., Garin J., Vivares C.P., Texier C.;
RT   "Proteomic analysis of the eukaryotic parasite Encephalitozoon cuniculi
RT   (microsporidia): a reference map for proteins expressed in late sporogonial
RT   stages.";
RL   Proteomics 6:3625-3635(2006).
RN   [3]
RP   X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) IN COMPLEX WITH GDP.
RG   Seattle structural genomics center for infectious disease (SSGCID);
RT   "Crystal structure of a nuclear GTP-binding protein from Encephalitozoon
RT   cuniculi bound to GDP-MG2+.";
RL   Submitted (FEB-2012) to the PDB data bank.
CC   -!- FUNCTION: GTP-binding protein involved in nucleocytoplasmic transport.
CC       Required for the import of protein into the nucleus and also for RNA
CC       export (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Found in a nuclear export complex with RanGTP, exportin and
CC       pre-miRNA (By similarity). {ECO:0000250|UniProtKB:P62825}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- DEVELOPMENTAL STAGE: Expressed in late sporogonial stages.
CC       {ECO:0000269|PubMed:16691553}.
CC   -!- SIMILARITY: Belongs to the small GTPase superfamily. Ran family.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AL590444; CAD25345.1; -; Genomic_DNA.
DR   RefSeq; NP_584841.1; NM_001041191.1.
DR   PDB; 4DJT; X-ray; 1.80 A; A/B=1-214.
DR   PDBsum; 4DJT; -.
DR   AlphaFoldDB; Q8SS11; -.
DR   SMR; Q8SS11; -.
DR   STRING; 284813.Q8SS11; -.
DR   GeneID; 858989; -.
DR   KEGG; ecu:ECU04_1560; -.
DR   VEuPathDB; MicrosporidiaDB:ECU04_1560; -.
DR   HOGENOM; CLU_041217_10_6_1; -.
DR   InParanoid; Q8SS11; -.
DR   OMA; IRFNIWD; -.
DR   OrthoDB; 1083175at2759; -.
DR   Proteomes; UP000000819; Chromosome IV.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR   GO; GO:0006913; P:nucleocytoplasmic transport; IEA:InterPro.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR002041; Ran_GTPase.
DR   InterPro; IPR005225; Small_GTP-bd_dom.
DR   InterPro; IPR001806; Small_GTPase.
DR   PANTHER; PTHR24071; PTHR24071; 1.
DR   Pfam; PF00071; Ras; 1.
DR   SMART; SM00174; RHO; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR00231; small_GTP; 1.
PE   1: Evidence at protein level;
KW   3D-structure; GTP-binding; Nucleotide-binding; Nucleus; Protein transport;
KW   Reference proteome; Transport.
FT   CHAIN           1..214
FT                   /note="GTP-binding nuclear protein GSP1"
FT                   /id="PRO_0000382910"
FT   BINDING         17..22
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0007744|PDB:4DJT"
FT   BINDING         66
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P62825"
FT   BINDING         121..124
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0007744|PDB:4DJT"
FT   BINDING         151..153
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0007744|PDB:4DJT"
FT   STRAND          7..13
FT                   /evidence="ECO:0007829|PDB:4DJT"
FT   HELIX           20..24
FT                   /evidence="ECO:0007829|PDB:4DJT"
FT   STRAND          35..37
FT                   /evidence="ECO:0007829|PDB:4DJT"
FT   TURN            38..41
FT                   /evidence="ECO:0007829|PDB:4DJT"
FT   STRAND          42..51
FT                   /evidence="ECO:0007829|PDB:4DJT"
FT   STRAND          56..64
FT                   /evidence="ECO:0007829|PDB:4DJT"
FT   HELIX           67..69
FT                   /evidence="ECO:0007829|PDB:4DJT"
FT   HELIX           75..78
FT                   /evidence="ECO:0007829|PDB:4DJT"
FT   STRAND          82..89
FT                   /evidence="ECO:0007829|PDB:4DJT"
FT   HELIX           93..97
FT                   /evidence="ECO:0007829|PDB:4DJT"
FT   HELIX           99..110
FT                   /evidence="ECO:0007829|PDB:4DJT"
FT   STRAND          112..114
FT                   /evidence="ECO:0007829|PDB:4DJT"
FT   STRAND          116..121
FT                   /evidence="ECO:0007829|PDB:4DJT"
FT   HELIX           133..139
FT                   /evidence="ECO:0007829|PDB:4DJT"
FT   TURN            140..142
FT                   /evidence="ECO:0007829|PDB:4DJT"
FT   STRAND          146..151
FT                   /evidence="ECO:0007829|PDB:4DJT"
FT   TURN            152..155
FT                   /evidence="ECO:0007829|PDB:4DJT"
FT   TURN            157..159
FT                   /evidence="ECO:0007829|PDB:4DJT"
FT   HELIX           160..170
FT                   /evidence="ECO:0007829|PDB:4DJT"
FT   TURN            201..204
FT                   /evidence="ECO:0007829|PDB:4DJT"
SQ   SEQUENCE   214 AA;  24364 MW;  27FD8429479467C7 CRC64;
     MERRELTYKI CLIGDGGVGK TTYINRVLDG RFEKNYNATV GAVNHPVTFL DDQGNVIKFN
     VWDTAGQEKK AVLKDVYYIG ASGAIFFFDV TSRITCQNLA RWVKEFQAVV GNEAPIVVCA
     NKIDIKNRQK ISKKLVMEVL KGKNYEYFEI SAKTAHNFGL PFLHLARIFT GRPDLIFVSN
     VNLEPTEVNY DYHSPEESKY IDYMEQASKM APEE
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024