ID A0A168DSR8_CORDF Unreviewed; 376 AA.
AC A0A168DSR8;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=GPN-loop GTPase {ECO:0000256|RuleBase:RU365059};
DE EC=3.6.5.- {ECO:0000256|RuleBase:RU365059};
GN ORFNames=LEL_08749 {ECO:0000313|EMBL:OAA72965.1};
OS Akanthomyces lecanii RCEF 1005.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Cordycipitaceae; Akanthomyces;
OC Cordyceps confragosa.
OX NCBI_TaxID=1081108 {ECO:0000313|EMBL:OAA72965.1, ECO:0000313|Proteomes:UP000076881};
RN [1] {ECO:0000313|EMBL:OAA72965.1, ECO:0000313|Proteomes:UP000076881}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RCEF 1005 {ECO:0000313|EMBL:OAA72965.1,
RC ECO:0000313|Proteomes:UP000076881};
RX PubMed=27071652; DOI=10.1093/gbe/evw082;
RA Shang Y., Xiao G., Zheng P., Cen K., Zhan S., Wang C.;
RT "Divergent and convergent evolution of fungal pathogenicity.";
RL Genome Biol. Evol. 8:1374-1387(2016).
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:OAA72965.1}.
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DR EMBL; AZHF01000007; OAA72965.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A168DSR8; -.
DR STRING; 1081108.A0A168DSR8; -.
DR OrthoDB; 5475185at2759; -.
DR Proteomes; UP000076881; 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:UP000076881}.
FT REGION 293..358
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 293..315
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 376 AA; 41634 MW; 6733610730BBBC91 CRC64;
MASESSSAAS ASPVAIVCVG MAGSGKTTFM QRINAHLHEK EDPPYVMNLD PAVMSVPFES
NIDIRDSVNY EEVMKQYNLG PNGGILTSLN LFATKVDQVV NLLEKRTKPD PENPQRPPVH
NILVDTPGQI EVFVWSASGT ILLESLASSF PTVIAYIIDT PRTSSTSTFM SNMLYACSIL
YKTKLPMILV FNKTDVKDAA FAKEWMTDFE AFQEALRKDE ESDALGGVEG GGHGGSGYMG
SLLNSMSLML EEFYSHLSMV AVSSRMGTGV DDFFAAVEEK RLEFLRDYQP ELERRRAERD
DQKKKSRDKE LDKMMQDMAV GQGEDNKEEE SSGDDEDSGD EAAKNSLQER YQAAMGDNED
SVLADASFAQ YLHKKR
//
