ID A0A0F8VPI1_9EURO Unreviewed; 392 AA.
AC A0A0F8VPI1;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=GPN-loop GTPase {ECO:0000256|RuleBase:RU365059};
DE EC=3.6.5.- {ECO:0000256|RuleBase:RU365059};
GN ORFNames=ARAM_004570 {ECO:0000313|EMBL:KKK25086.1};
OS Aspergillus rambellii.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=308745 {ECO:0000313|EMBL:KKK25086.1, ECO:0000313|Proteomes:UP000034291};
RN [1] {ECO:0000313|EMBL:KKK25086.1, ECO:0000313|Proteomes:UP000034291}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SRRC1468 {ECO:0000313|EMBL:KKK25086.1,
RC ECO:0000313|Proteomes:UP000034291};
RA Moore G.G., Beltz S.B., Mack B.M.;
RT "Draft Genome Sequences of Two Closely-Related Aflatoxigenic Aspergillus
RT Species Obtained from the Cote d'Ivoire.";
RL Submitted (FEB-2015) 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:KKK25086.1}.
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DR EMBL; JZBS01000833; KKK25086.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0F8VPI1; -.
DR STRING; 308745.A0A0F8VPI1; -.
DR OrthoDB; 5475185at2759; -.
DR Proteomes; UP000034291; 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:UP000034291}.
FT REGION 280..392
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 280..299
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 350..392
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 392 AA; 43384 MW; 7884CFC8E8380123 CRC64;
MRFNIGSGKT TFMQRINSHL HSKKSPPYVL NLDPAVHSVP FESNIDIRDS INYKEVMKQY
NLGPNGGILT SLNLFATKVD QVIALLEKRT APNPSNPAAK PIEHILVDTP GQIEVFVWSA
SGSILLETLA SSFPTVIAYI IDTPRTSSTS TFMSNMLYAC SILYKTKLPM ILVFNKTDVQ
DAEFAKEWMS DFDAFQQALR EEEESGAFGT EGGAGGFGAG SGYMGSLLNS MSLMLEEFYR
HLNVVGVSSM TGDGIDEFFE AVEEKRQEFE RDYKPELERL KKEREEAKTT QREVELGKLM
KDMNLASSSR AQGADAAETV SEAEEEAEDN AARRGAFEES EDDSDEESSV PPAGDNQGLS
QRYQQALSDS TGMPSDQDLS FARYLRSSNI NQ
//
