GPN3_GIBZE
ID GPN3_GIBZE Reviewed; 301 AA.
AC Q4IQT8; A0A098D0B7; A0A0E0RM73; I1RA93;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2005, sequence version 1.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=GPN-loop GTPase 3 {ECO:0000250|UniProtKB:Q06543};
GN ORFNames=FGRRES_15740, FGSG_00420;
OS Gibberella zeae (strain ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084
OS / PH-1) (Wheat head blight fungus) (Fusarium graminearum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX NCBI_TaxID=229533;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1;
RX PubMed=17823352; DOI=10.1126/science.1143708;
RA Cuomo C.A., Gueldener U., Xu J.-R., Trail F., Turgeon B.G., Di Pietro A.,
RA Walton J.D., Ma L.-J., Baker S.E., Rep M., Adam G., Antoniw J., Baldwin T.,
RA Calvo S.E., Chang Y.-L., DeCaprio D., Gale L.R., Gnerre S., Goswami R.S.,
RA Hammond-Kosack K., Harris L.J., Hilburn K., Kennell J.C., Kroken S.,
RA Magnuson J.K., Mannhaupt G., Mauceli E.W., Mewes H.-W., Mitterbauer R.,
RA Muehlbauer G., Muensterkoetter M., Nelson D., O'Donnell K., Ouellet T.,
RA Qi W., Quesneville H., Roncero M.I.G., Seong K.-Y., Tetko I.V., Urban M.,
RA Waalwijk C., Ward T.J., Yao J., Birren B.W., Kistler H.C.;
RT "The Fusarium graminearum genome reveals a link between localized
RT polymorphism and pathogen specialization.";
RL Science 317:1400-1402(2007).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1;
RX PubMed=20237561; DOI=10.1038/nature08850;
RA Ma L.-J., van der Does H.C., Borkovich K.A., Coleman J.J., Daboussi M.-J.,
RA Di Pietro A., Dufresne M., Freitag M., Grabherr M., Henrissat B.,
RA Houterman P.M., Kang S., Shim W.-B., Woloshuk C., Xie X., Xu J.-R.,
RA Antoniw J., Baker S.E., Bluhm B.H., Breakspear A., Brown D.W.,
RA Butchko R.A.E., Chapman S., Coulson R., Coutinho P.M., Danchin E.G.J.,
RA Diener A., Gale L.R., Gardiner D.M., Goff S., Hammond-Kosack K.E.,
RA Hilburn K., Hua-Van A., Jonkers W., Kazan K., Kodira C.D., Koehrsen M.,
RA Kumar L., Lee Y.-H., Li L., Manners J.M., Miranda-Saavedra D.,
RA Mukherjee M., Park G., Park J., Park S.-Y., Proctor R.H., Regev A.,
RA Ruiz-Roldan M.C., Sain D., Sakthikumar S., Sykes S., Schwartz D.C.,
RA Turgeon B.G., Wapinski I., Yoder O., Young S., Zeng Q., Zhou S.,
RA Galagan J., Cuomo C.A., Kistler H.C., Rep M.;
RT "Comparative genomics reveals mobile pathogenicity chromosomes in
RT Fusarium.";
RL Nature 464:367-373(2010).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1;
RX PubMed=26198851; DOI=10.1186/s12864-015-1756-1;
RA King R., Urban M., Hammond-Kosack M.C.U., Hassani-Pak K.,
RA Hammond-Kosack K.E.;
RT "The completed genome sequence of the pathogenic ascomycete fungus Fusarium
RT graminearum.";
RL BMC Genomics 16:544-544(2015).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ESU05601.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; DS231663; ESU05601.1; ALT_SEQ; Genomic_DNA.
DR EMBL; HG970332; CEF72348.1; -; Genomic_DNA.
DR RefSeq; XP_011316086.1; XM_011317784.1.
DR AlphaFoldDB; Q4IQT8; -.
DR SMR; Q4IQT8; -.
DR STRING; 5518.FGSG_00420P0; -.
DR EnsemblFungi; ESU05601; ESU05601; FGSG_00420.
DR GeneID; 23547909; -.
DR KEGG; fgr:FGSG_00420; -.
DR VEuPathDB; FungiDB:FGRAMPH1_01G01091; -.
DR eggNOG; KOG1534; Eukaryota.
DR HOGENOM; CLU_037460_0_0_1; -.
DR InParanoid; Q4IQT8; -.
DR PHI-base; PHI:1618; -.
DR Proteomes; UP000070720; Chromosome 1.
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..301
FT /note="GPN-loop GTPase 3"
FT /id="PRO_0000255592"
FT REGION 212..232
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 301 AA; 33563 MW; 859BABD0D84F8E75 CRC64;
MSKFGAMVMG PAGAGKSTFC AALITHLNLN RRSAFYINLD PAAESFEHEP DLDIKELISL
KDAMEEVGLG PNGGLIYCFE FLMENLDWLT DALEGLTEEY LIIIDMPGQI ELYTHVPILP
ALVKFLSQPG SLDVRMAAVY LLEATFVVDR AKFFSGTLSA MSAMLMLEVP HINILSKMDL
VKGQVKKKDL KRFLTPDVGL LDDDPVEHTR RIAEGQDAED DESKAPDEKD QVMKGASFRR
LNRAVAGLIE SFSMINYHKL DVTNEDSVAA ILSYIDDCIQ FHEAQDPKEP HDDEETEEFE
G
