GPN1_DICDI
ID GPN1_DICDI Reviewed; 396 AA.
AC Q54C25;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=GPN-loop GTPase 1 {ECO:0000250|UniProtKB:Q9HCN4};
DE EC=3.6.5.- {ECO:0000250|UniProtKB:Q9HCN4};
DE AltName: Full=XPA-binding protein 1 homolog {ECO:0000250|UniProtKB:Q9HCN4};
GN Name=gpn1 {ECO:0000312|dictyBase:DDB_G0293220};
GN Synonyms=xab1 {ECO:0000250|UniProtKB:Q9HCN4}; ORFNames=DDB_G0293220;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
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:0000250|UniProtKB:Q9HCN4}.
CC -!- SUBUNIT: Heterodimer with gpn3. Binds to RNA polymerase II (RNAPII).
CC {ECO:0000250|UniProtKB:Q9HCN4}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9HCN4}. Nucleus
CC {ECO:0000250|UniProtKB:Q9HCN4}. Note=Shuttles between the nucleus and
CC the cytoplasm. {ECO:0000250|UniProtKB:Q9HCN4}.
CC -!- SIMILARITY: Belongs to the GPN-loop GTPase family. {ECO:0000305}.
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; AAFI02000200; EAL60809.1; -; Genomic_DNA.
DR RefSeq; XP_629241.1; XM_629239.1.
DR AlphaFoldDB; Q54C25; -.
DR SMR; Q54C25; -.
DR STRING; 44689.DDB0233477; -.
DR PaxDb; Q54C25; -.
DR EnsemblProtists; EAL60809; EAL60809; DDB_G0293220.
DR GeneID; 8629123; -.
DR KEGG; ddi:DDB_G0293220; -.
DR dictyBase; DDB_G0293220; gpn1.
DR eggNOG; KOG1532; Eukaryota.
DR HOGENOM; CLU_037460_1_3_1; -.
DR InParanoid; Q54C25; -.
DR OMA; MIIVFNK; -.
DR PhylomeDB; Q54C25; -.
DR PRO; PR:Q54C25; -.
DR Proteomes; UP000002195; Chromosome 6.
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; IBA:GO_Central.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR004130; Gpn.
DR InterPro; IPR030230; Gpn1/Npa3/XAB1.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR21231; PTHR21231; 1.
DR PANTHER; PTHR21231:SF8; PTHR21231:SF8; 1.
DR Pfam; PF03029; ATP_bind_1; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 3: Inferred from homology;
KW Coiled coil; Cytoplasm; GTP-binding; Hydrolase; Nucleotide-binding;
KW Nucleus; Reference proteome.
FT CHAIN 1..396
FT /note="GPN-loop GTPase 1"
FT /id="PRO_0000330935"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 325..396
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 284..387
FT /evidence="ECO:0000255"
FT MOTIF 101..103
FT /note="Gly-Pro-Asn (GPN)-loop; involved in dimer interface"
FT /evidence="ECO:0000250|UniProtKB:Q9UYR9"
FT COMPBIAS 325..346
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 347..377
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 44..49
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q9UYR9"
FT BINDING 204..207
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q9UYR9"
FT SITE 103
FT /note="Stabilizes the phosphate intermediate; shared with
FT dimeric partner"
FT /evidence="ECO:0000250|UniProtKB:Q9UYR9"
SQ SEQUENCE 396 AA; 45457 MW; 8CC9893A71620483 CRC64;
MSETTATSTT TTKTTDKDNV NNNNNNENKE EKQPINIIVL GMAGSGKTTL LQRIRAHLYE
NKIPGYIINL DPAVSKLPYT PNIDIRDTVN YKEVMKQFNL GPNGGIVTSL NLFSTKFDKV
LEIVEKRSSS LDYIILDTPG QIEVFTWSAS GTIITELMAS SFPTVLVYVV DTPRTVDPTT
FMSNMLYACS IMYKSKLPMV VAFNKIDITN HRFAEEWMSD FDSFQDALTN DPTYMGNLTR
SLSLVLEEFY STLQSVGVSA VDGSGIDEFF EKIGLAAQDY HKYYKADLEK IKKQKSDKEQ
AEANKNWEKL KRDLEESKGA KVEYDFKKEK KRENQEKTKN IYDDEEDDYR DDRDMEDSGE
YESYEDEQEE GDYENEEERL EDQRAYESLM SSIKKI
