GPN3_CRYNB
ID GPN3_CRYNB Reviewed; 287 AA.
AC P0CN95; Q55YA6; Q5KLN2;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 42.
DE RecName: Full=GPN-loop GTPase 3 {ECO:0000250|UniProtKB:Q06543};
GN OrderedLocusNames=CNBB1090;
OS Cryptococcus neoformans var. neoformans serotype D (strain B-3501A)
OS (Filobasidiella neoformans).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Tremellales; Cryptococcaceae; Cryptococcus;
OC Cryptococcus neoformans species complex.
OX NCBI_TaxID=283643;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B-3501A;
RX PubMed=15653466; DOI=10.1126/science.1103773;
RA Loftus B.J., Fung E., Roncaglia P., Rowley D., Amedeo P., Bruno D.,
RA Vamathevan J., Miranda M., Anderson I.J., Fraser J.A., Allen J.E.,
RA Bosdet I.E., Brent M.R., Chiu R., Doering T.L., Donlin M.J., D'Souza C.A.,
RA Fox D.S., Grinberg V., Fu J., Fukushima M., Haas B.J., Huang J.C.,
RA Janbon G., Jones S.J.M., Koo H.L., Krzywinski M.I., Kwon-Chung K.J.,
RA Lengeler K.B., Maiti R., Marra M.A., Marra R.E., Mathewson C.A.,
RA Mitchell T.G., Pertea M., Riggs F.R., Salzberg S.L., Schein J.E.,
RA Shvartsbeyn A., Shin H., Shumway M., Specht C.A., Suh B.B., Tenney A.,
RA Utterback T.R., Wickes B.L., Wortman J.R., Wye N.H., Kronstad J.W.,
RA Lodge J.K., Heitman J., Davis R.W., Fraser C.M., Hyman R.W.;
RT "The genome of the basidiomycetous yeast and human pathogen Cryptococcus
RT neoformans.";
RL Science 307:1321-1324(2005).
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; AAEY01000007; EAL22660.1; -; Genomic_DNA.
DR RefSeq; XP_777307.1; XM_772214.1.
DR AlphaFoldDB; P0CN95; -.
DR SMR; P0CN95; -.
DR EnsemblFungi; EAL22660; EAL22660; CNBB1090.
DR GeneID; 4934199; -.
DR KEGG; cnb:CNBB1090; -.
DR VEuPathDB; FungiDB:CNBB1090; -.
DR HOGENOM; CLU_037460_0_0_1; -.
DR Proteomes; UP000001435; Chromosome 2.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0007064; P:mitotic sister chromatid cohesion; IEA:EnsemblFungi.
DR GO; GO:0006606; P:protein import into nucleus; IEA:EnsemblFungi.
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.
FT CHAIN 1..287
FT /note="GPN-loop GTPase 3"
FT /id="PRO_0000410102"
FT MOTIF 69..71
FT /note="Gly-Pro-Asn (GPN)-loop; involved in dimer interface"
FT /evidence="ECO:0000250|UniProtKB:Q9UYR9"
FT BINDING 12..17
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q9UYR9"
FT BINDING 172..175
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q9UYR9"
FT SITE 71
FT /note="Stabilizes the phosphate intermediate; shared with
FT dimeric partner"
FT /evidence="ECO:0000250|UniProtKB:Q9UYR9"
SQ SEQUENCE 287 AA; 32331 MW; 1A1AD2166333D107 CRC64;
MRYAVLVTGP AGAGKSTFCA SLITHAQTIG RSVHLVNLDP AADKFEYEPT IDIRDLINLE
DVMEELEFGP NGGLIYCFEY LLNNLDWLED ELGAYEDDYL IIDCPGQIEL YTHVPLLPRL
ATFLSTSLNF RTSAVYLIDS QFMQDKSKFF AGVMSAMSCM LSLGISMLCL MSKMDLVKDK
KGRTKREVGR YLDPDPNLLL EDINQGTNSK FNQLNRAVVS LIEDQNIVSF LPLDVTSEDS
VNTVLSHIDN MMQYGEDEEP KVPKDMDDGE FVAPPRSYNI KLIVRDR