ID A0A439D2I1_9PEZI Unreviewed; 401 AA.
AC A0A439D2I1;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 14.
DE RecName: Full=GPN-loop GTPase {ECO:0000256|RuleBase:RU365059};
DE EC=3.6.5.- {ECO:0000256|RuleBase:RU365059};
GN ORFNames=EKO27_g6643 {ECO:0000313|EMBL:RWA08451.1};
OS Xylaria grammica.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Xylariomycetidae; Xylariales; Xylariaceae; Xylaria.
OX NCBI_TaxID=363999 {ECO:0000313|EMBL:RWA08451.1, ECO:0000313|Proteomes:UP000286045};
RN [1] {ECO:0000313|EMBL:RWA08451.1, ECO:0000313|Proteomes:UP000286045}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IHI A82 {ECO:0000313|EMBL:RWA08451.1,
RC ECO:0000313|Proteomes:UP000286045};
RA Buettner E., Kellner H.;
RT "Draft genome sequence of Xylaria grammica IHI A82.";
RL Submitted (DEC-2018) 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:RWA08451.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; RYZI01000199; RWA08451.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A439D2I1; -.
DR STRING; 363999.A0A439D2I1; -.
DR Proteomes; UP000286045; 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:UP000286045}.
FT REGION 302..401
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 302..321
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 329..348
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 349..366
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 401 AA; 43822 MW; A1F2B0C7732A7743 CRC64;
MASEASASSS AAAAAAAAAA HQPVAIVCVG MAGSGKTTFM QRINAHLHAK KEPPYVINLD
PAVLNVPFES NIDIRDSVNY KEVMKQYNLG PNGGILTSLN LFATKVDQIL GLLEKRAAPD
PEKPDKKPIK NILVDTPGQI EVFVWSASGQ ILLESLASSF PTVIAYVIDT PRTASTSTFM
SNMLYACSIL YKTKLPMILV FNKTDVKDAS FAKEWMTDYD AFQEALAQDE AGNAFGGVEG
EGAGSGYMGS LLNSMSSMLE EFYAHLSVVG VSSMTGQGVD EFFAAVQEKA EEFKKDYLPE
LERKRKERDE QKRKMRQKEL DKMMNGMSMG EASSASGPKT VNNNDSDISS NDDEAEEDYA
DVDDEYDREG LQERYAAAME ANQDSTMDDA SFAKYLHSQR Q
//
