ID A0A3A2ZKR8_9EURO Unreviewed; 394 AA.
AC A0A3A2ZKR8;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=GPN-loop GTPase {ECO:0000256|RuleBase:RU365059};
DE EC=3.6.5.- {ECO:0000256|RuleBase:RU365059};
GN ORFNames=PHISCL_04751 {ECO:0000313|EMBL:RJE22903.1};
OS Aspergillus sclerotialis.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Polypaecilum.
OX NCBI_TaxID=2070753 {ECO:0000313|EMBL:RJE22903.1, ECO:0000313|Proteomes:UP000266188};
RN [1] {ECO:0000313|Proteomes:UP000266188}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 366.77 {ECO:0000313|Proteomes:UP000266188};
RA Tafer H., Lopandic K.;
RL Submitted (FEB-2017) to the EMBL/GenBank/DDBJ databases.
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}.
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:RJE22903.1}.
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DR EMBL; MVGC01000145; RJE22903.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3A2ZKR8; -.
DR STRING; 2070753.A0A3A2ZKR8; -.
DR Proteomes; UP000266188; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
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:UP000266188}.
FT REGION 284..394
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 284..304
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 326..356
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 394 AA; 43910 MW; 509F2176E7D3E026 CRC64;
MAASPVSVVC VGMAGSGKTT FMQRINSYLH TKKTVPYVLN LDPAVHSVPF ESNIDIRDSI
NYKEVMRQYN LGPNGGILTS LNLFATKVDQ IISLLEKRAS PNPSNPSGKS IEHILVDTPG
QIEVFVWSAS GSIFLETLAS SFPTVIAYVI DTPRTSSTST FMSNMLYACS ILYKTKLPMI
LVFNKTDVQD AEFAKEWMTD FDAFQQALRE EEEGGSFGQE GGVGGSGYMS SLLNSMSLML
EEFYRHLNVV GVSSMTGDGI DEFFKAVEEK RQEFERDYKP ELERKKKERE EAKESNRELE
LGKLMKDMSV SGSTRSRHRE TEAETVSEAE EEEEARQKDE EFGLDDSDDD EAPTAADDEG
LSQRYQQAMA DSRAGPSDGD HSFARYLGAN RINR
//
