ID F8MFQ9_NEUT8 Unreviewed; 399 AA.
AC F8MFQ9;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE RecName: Full=GPN-loop GTPase {ECO:0000256|RuleBase:RU365059};
DE EC=3.6.5.- {ECO:0000256|RuleBase:RU365059};
GN ORFNames=NEUTE1DRAFT_79233 {ECO:0000313|EMBL:EGO59285.1};
OS Neurospora tetrasperma (strain FGSC 2508 / ATCC MYA-4615 / P0657).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX NCBI_TaxID=510951 {ECO:0000313|EMBL:EGO59285.1};
RN [1] {ECO:0000313|EMBL:EGO59285.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=FGSC 2508 {ECO:0000313|EMBL:EGO59285.1};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Ellison C.E., Stajich J.E., Jacobson D.J., Lindquist E., Lapidus A.,
RA Foster B., Aerts A., Riley R., Grigoriev I.V., Taylor J.W.;
RT "Massive changes in genome architecture accompany the transition to self-
RT fertility in the filamentous fungus Neurospora tetrasperma.";
RL Submitted (APR-2011) 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}.
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DR EMBL; GL891303; EGO59285.1; -; Genomic_DNA.
DR RefSeq; XP_009849535.1; XM_009851233.1.
DR AlphaFoldDB; F8MFQ9; -.
DR GeneID; 20830175; -.
DR KEGG; nte:NEUTE1DRAFT79233; -.
DR VEuPathDB; FungiDB:NEUTE1DRAFT_79233; -.
DR HOGENOM; CLU_037460_1_2_1; -.
DR OrthoDB; 5475185at2759; -.
DR Proteomes; UP000008065; 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}.
FT REGION 318..369
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 348..363
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 399 AA; 43782 MW; AE32BF731C506161 CRC64;
MASTSASSAA KADQPVAIVC VGMAGSGKTT FMQQINAHLH GKKEPPYVIN LDPAVTHSPF
ESNIDIRDSV NYKEVMKQYN LGPNGGILTS LNLFATKVDQ VLGLLEKRTA PKPDDPTHTP
IKHILVDTPG QIEVFVWSAS GQILLESLAS SFPTVIAYII DTPRTSSTST FMSNMLYACS
ILYKTKLPMI LVFNKSDVKD PAFAKEWMTD YDAFQAALQE DETNNAFGGA EGSGDGMGSG
SGYMGSLLNS MSLMLEEFYA HLNVVGVSSL YGTGIDEFFA AVQEKAEEFK RDYQPELERR
REEREENKKK ARERELNKMM KGMSMGDAAG DVTVGDVNDK EAPEPLSTDE ESSDEEYGDD
PNDEYDREGL QARYAAAMQG EDDSVLADAS FAKYLHSQR
//
