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Database: UniProt
Entry: A0A423WPS3_9PEZI
LinkDB: A0A423WPS3_9PEZI
Original site: A0A423WPS3_9PEZI 
ID   A0A423WPS3_9PEZI        Unreviewed;       349 AA.
AC   A0A423WPS3;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   22-FEB-2023, entry version 12.
DE   RecName: Full=GPN-loop GTPase 2 {ECO:0000256|RuleBase:RU365059};
GN   ORFNames=VSDG_00019 {ECO:0000313|EMBL:ROW05466.1};
OS   Valsa sordida.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Diaporthales; Valsaceae; Valsa.
OX   NCBI_TaxID=252740 {ECO:0000313|EMBL:ROW05466.1, ECO:0000313|Proteomes:UP000284375};
RN   [1] {ECO:0000313|EMBL:ROW05466.1, ECO:0000313|Proteomes:UP000284375}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YSFL {ECO:0000313|EMBL:ROW05466.1,
RC   ECO:0000313|Proteomes:UP000284375};
RA   Yin Z., Huang L.;
RT   "Host preference determinants of Valsa canker pathogens revealed by
RT   comparative genomics.";
RL   Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Small GTPase required for proper localization of RNA
CC       polymerase II and III (RNAPII and RNAPIII). May act at an RNAP assembly
CC       step prior to nuclear import. {ECO:0000256|RuleBase:RU365059}.
CC   -!- SUBUNIT: Binds to RNA polymerase II (RNAPII).
CC       {ECO:0000256|RuleBase:RU365059}.
CC   -!- SIMILARITY: Belongs to the GPN-loop GTPase family.
CC       {ECO:0000256|ARBA:ARBA00005290, ECO:0000256|RuleBase:RU365059}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:ROW05466.1}.
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DR   EMBL; LJZO01000001; ROW05466.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A423WPS3; -.
DR   STRING; 252740.A0A423WPS3; -.
DR   Proteomes; UP000284375; Unassembled WGS sequence.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   CDD; cd17871; GPN2; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR004130; Gpn.
DR   InterPro; IPR030231; Gpn2.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR21231:SF3; GPN-LOOP GTPASE 2; 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   GTP-binding {ECO:0000256|RuleBase:RU365059};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU365059};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU365059};
KW   Reference proteome {ECO:0000313|Proteomes:UP000284375}.
FT   REGION          297..349
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        297..313
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   349 AA;  39251 MW;  DE3B6BB0655A0619 CRC64;
     MPFAQLILGS PGAGKSTYCD GMHQFMGAIG RPCSVVNLDP ANDKTNYPCA LDIRDLITLE
     EVMGNDDLGP NGGVLYALEE LEHNFEWLEE GLKELGDDYI LFDCPGQVEL YTHHNSLRNI
     FFKLQKLGFR MVVLHLSDSF CLSQPSLYIS NILLALRAML QMDLPHINVL TKIDKVASYE
     SLPFNLDFYT EVQDLSYLLP SLEEESPALR SEKFRALNEA IANVVENFGL VRFEVLAVED
     KKSMMHLLKV IDRAGGYIFG STDGANDTVW QIAMRNEPSM LDVQDIQERW VDQKDAYDEA
     ERKAEEEQAK IREAQAEQNA PAGDGLDEFD GMPMPPSDLS VTVTRKKKT
//
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