ID   GPN3_ASPFU              Reviewed;         293 AA.
AC   Q4WT40;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2005, sequence version 1.
DT   03-AUG-2022, entry version 96.
DE   RecName: Full=GPN-loop GTPase 3 {ECO:0000250|UniProtKB:Q06543};
GN   ORFNames=AFUA_1G10640;
OS   Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS   A1100) (Aspergillus fumigatus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=330879;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100;
RX   PubMed=16372009; DOI=10.1038/nature04332;
RA   Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA   Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P.,
RA   Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.,
RA   Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N.,
RA   Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA   Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E.,
RA   Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H.,
RA   Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A.,
RA   Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L.,
RA   Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D.,
RA   O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L.,
RA   Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U.,
RA   Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M.,
RA   Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C.,
RA   Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F.,
RA   Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R.,
RA   Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N.,
RA   Barrell B.G., Denning D.W.;
RT   "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT   Aspergillus fumigatus.";
RL   Nature 438:1151-1156(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; AAHF01000004; EAL90392.1; -; Genomic_DNA.
DR   RefSeq; XP_752430.1; XM_747337.1.
DR   AlphaFoldDB; Q4WT40; -.
DR   SMR; Q4WT40; -.
DR   STRING; 746128.CADAFUBP00000987; -.
DR   EnsemblFungi; EAL90392; EAL90392; AFUA_1G10640.
DR   GeneID; 3510541; -.
DR   KEGG; afm:AFUA_1G10640; -.
DR   VEuPathDB; FungiDB:Afu1g10640; -.
DR   eggNOG; KOG1534; Eukaryota.
DR   HOGENOM; CLU_037460_0_0_1; -.
DR   InParanoid; Q4WT40; -.
DR   OMA; CFEYLLQ; -.
DR   OrthoDB; 964931at2759; -.
DR   Proteomes; UP000002530; Chromosome 1.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
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; Reference proteome.
FT   CHAIN           1..293
FT                   /note="GPN-loop GTPase 3"
FT                   /id="PRO_0000255587"
FT   REGION          272..293
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         176..179
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   293 AA;  32888 MW;  811FB59EC95F724D CRC64;
     MSKFGVLVMG PAGAGKSTFC SALIQHLQTT RRSCFYVNLD PAAESFNYEP DLDIRELITL
     EDVMEEMELG PNGGLIYCFE FLLQNLDFLS QALDPLSEEY LIIFDMPGQI ELYTHIPLLP
     SLVQYLSRQG PLNINLCAAY LLESTFVIDK AKFFAGTLSA MSAMLMLEMP HVNILSKMDQ
     VRDMVSRKEL KRFVNVDVNL LQDEIGGAEE PVEGDPSSKD TLLSGRSFKR LNRAVGQLID
     DFSMVSFLKL DVQDEDSVAA VLSHIDDAIQ FHEAQEPREP NDEQDVDYED ADI