ID E4ZM46_LEPMJ Unreviewed; 440 AA.
AC E4ZM46;
DT 08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT 08-FEB-2011, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE RecName: Full=GPN-loop GTPase {ECO:0000256|RuleBase:RU365059};
DE EC=3.6.5.- {ECO:0000256|RuleBase:RU365059};
GN ORFNames=LEMA_P051010.1 {ECO:0000313|EMBL:CBX92395.1};
OS Leptosphaeria maculans (strain JN3 / isolate v23.1.3 / race Av1-4-5-6-7-8)
OS (Blackleg fungus) (Phoma lingam).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Leptosphaeriaceae;
OC Plenodomus; Plenodomus lingam/Leptosphaeria maculans species complex.
OX NCBI_TaxID=985895 {ECO:0000313|Proteomes:UP000002668};
RN [1] {ECO:0000313|Proteomes:UP000002668}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JN3 / isolate v23.1.3 / race Av1-4-5-6-7-8
RC {ECO:0000313|Proteomes:UP000002668};
RX PubMed=21326234; DOI=10.1038/ncomms1189;
RA Rouxel T., Grandaubert J., Hane J.K., Hoede C., van de Wouw A.P.,
RA Couloux A., Dominguez V., Anthouard V., Bally P., Bourras S.,
RA Cozijnsen A.J., Ciuffetti L.M., Degrave A., Dilmaghani A., Duret L.,
RA Fudal I., Goodwin S.B., Gout L., Glaser N., Linglin J., Kema G.H.J.,
RA Lapalu N., Lawrence C.B., May K., Meyer M., Ollivier B., Poulain J.,
RA Schoch C.L., Simon A., Spatafora J.W., Stachowiak A., Turgeon B.G.,
RA Tyler B.M., Vincent D., Weissenbach J., Amselem J., Quesneville H.,
RA Oliver R.P., Wincker P., Balesdent M.-H., Howlett B.J.;
RT "Effector diversification within compartments of the Leptosphaeria maculans
RT genome affected by Repeat-Induced Point mutations.";
RL Nat. Commun. 2:202-202(2011).
CC -!- FUNCTION: Small GTPase required for proper nuclear import of RNA
CC polymerase II (RNAPII). May act at an RNAP assembly step prior to
CC nuclear import. {ECO:0000256|RuleBase:RU365059}.
CC -!- SUBUNIT: Binds to RNA polymerase II. {ECO:0000256|RuleBase:RU365059}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|RuleBase:RU365059}.
CC Nucleus {ECO:0000256|RuleBase:RU365059}.
CC -!- SIMILARITY: Belongs to the GPN-loop GTPase family.
CC {ECO:0000256|ARBA:ARBA00005290, ECO:0000256|RuleBase:RU365059}.
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DR EMBL; FP929094; CBX92395.1; -; Genomic_DNA.
DR RefSeq; XP_003835760.1; XM_003835712.1.
DR AlphaFoldDB; E4ZM46; -.
DR STRING; 985895.E4ZM46; -.
DR EnsemblFungi; CBX92395; CBX92395; LEMA_P051010.1.
DR GeneID; 13287125; -.
DR eggNOG; KOG1532; Eukaryota.
DR HOGENOM; CLU_037460_1_2_1; -.
DR InParanoid; E4ZM46; -.
DR OMA; MIIVFNK; -.
DR OrthoDB; 5475185at2759; -.
DR Proteomes; UP000002668; Genome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:EnsemblFungi.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IEA:EnsemblFungi.
DR GO; GO:0007064; P:mitotic sister chromatid cohesion; IEA:EnsemblFungi.
DR GO; GO:0006606; P:protein import into nucleus; IEA:EnsemblFungi.
DR CDD; cd17870; GPN1; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR004130; Gpn.
DR InterPro; IPR030230; Gpn1/Npa3/XAB1.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR21231:SF8; GPN-LOOP GTPASE 1; 1.
DR PANTHER; PTHR21231; XPA-BINDING PROTEIN 1-RELATED; 1.
DR Pfam; PF03029; ATP_bind_1; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|RuleBase:RU365059};
KW GTP-binding {ECO:0000256|RuleBase:RU365059};
KW Hydrolase {ECO:0000256|RuleBase:RU365059};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU365059};
KW Reference proteome {ECO:0000313|Proteomes:UP000002668}.
FT REGION 333..429
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 333..358
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 379..403
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 404..426
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 440 AA; 48791 MW; 6A8E96FDDAD44398 CRC64;
MSAAQAAEGS SASASKPPVA IVCVGMAGSG KTTFMQRLVS HLYTHPDPTQ SEPSVSKVAP
TPPYIINLDP AVHHVPFTPN IDIRDSVNYK EVMKQFNLGP NGGILTSLNL FSTKIDQVIA
LLEKRTQPPA PVQQPEQTTV EFMTNSGKEK QPAPVQQQQV KHILVDTPGQ IEVFVWSASG
EILLSSLAST FPTVIAYIID TPRTTSTSTF MSNMLYACSI LYKTKLPMIL VFNKTDAQDA
QFAKEWMTDF EAFQAALRNE EEGGTFGGEG VGAGSGYMGS LLNSMSLVLE EFYKHLSVVG
VSAMTGDGMD EFFRGVNEKA EEFERDYKPE LERRRAERER EKQATRQREL DKLMKDMKVG
GAGNKPTTRS RKDDPETVSD AEDTGDDHQD EDLDYEDELD SDDPEQGLQQ RYRDTIRDHS
TKAPDEDMSF ARYVQAAKFN
//
