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GPN3_DEBHA
ID   GPN3_DEBHA              Reviewed;         274 AA.
AC   Q6BI59;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   16-DEC-2008, sequence version 2.
DT   03-AUG-2022, entry version 81.
DE   RecName: Full=GPN-loop GTPase 3 {ECO:0000250|UniProtKB:Q06543};
GN   OrderedLocusNames=DEHA2G13222g;
OS   Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990
OS   / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX   NCBI_TaxID=284592;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC 2968;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA   Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA   Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA   Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA   Weissenbach J., Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
CC   -!- FUNCTION: Small GTPase required for proper nuclear import of RNA
CC       polymerase II and III (RNAPII and RNAPIII). May act at an RNAP assembly
CC       step prior to nuclear import. {ECO:0000250|UniProtKB:Q06543}.
CC   -!- SUBUNIT: Heterodimers with GPN1 or GPN2. Binds to RNA polymerase II
CC       (RNAPII). {ECO:0000250|UniProtKB:Q06543}.
CC   -!- SIMILARITY: Belongs to the GPN-loop GTPase family. {ECO:0000305}.
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DR   EMBL; CR382139; CAG90598.2; -; Genomic_DNA.
DR   RefSeq; XP_462112.2; XM_462112.1.
DR   AlphaFoldDB; Q6BI59; -.
DR   SMR; Q6BI59; -.
DR   STRING; 4959.XP_462112.2; -.
DR   EnsemblFungi; CAG90598; CAG90598; DEHA2G13222g.
DR   GeneID; 2905026; -.
DR   KEGG; dha:DEHA2G13222g; -.
DR   VEuPathDB; FungiDB:DEHA2G13222g; -.
DR   eggNOG; KOG1534; Eukaryota.
DR   HOGENOM; CLU_037460_0_0_1; -.
DR   InParanoid; Q6BI59; -.
DR   OMA; CFEYLLQ; -.
DR   OrthoDB; 964931at2759; -.
DR   Proteomes; UP000000599; Chromosome G.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR004130; Gpn.
DR   InterPro; IPR030228; Gpn3.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR21231; PTHR21231; 1.
DR   PANTHER; PTHR21231:SF7; PTHR21231:SF7; 1.
DR   Pfam; PF03029; ATP_bind_1; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
PE   3: Inferred from homology;
KW   GTP-binding; Hydrolase; Nucleotide-binding; Reference proteome.
FT   CHAIN           1..274
FT                   /note="GPN-loop GTPase 3"
FT                   /id="PRO_0000255591"
FT   REGION          255..274
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           70..72
FT                   /note="Gly-Pro-Asn (GPN)-loop; involved in dimer interface"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UYR9"
FT   BINDING         13..18
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UYR9"
FT   BINDING         173..176
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UYR9"
FT   SITE            72
FT                   /note="Stabilizes the phosphate intermediate; shared with
FT                   dimeric partner"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UYR9"
SQ   SEQUENCE   274 AA;  30796 MW;  52320ACA361F8AA9 CRC64;
     MSRVGVLALG PAGVGKSTFC NSIITHMQSI GRRAHIVNLD PAAEPSEYEF TIDIRDLISL
     QDVMEEMDLG PNGALIYCFE FLMNNLDWLD EEIGDFNDEY LIFDCPGQIE LYTHIPVLPT
     IVRHLQTSLN FNLCATYLLE APFVIDRSKF FSGALSAMSA MILLELPHIN ILSKIDLIKN
     EVSKKELKKF LNPDPLLLNA SSDNESNPKF AKLNKAIANL VDDFGMVQFL PLDCNKDSDS
     VATILSYIDD VTQWSESQEP KEPVEEIEEE VDFE
 
 
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