GNL3_DICDI
ID GNL3_DICDI Reviewed; 615 AA.
AC Q54KS4;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Guanine nucleotide-binding protein-like 3 homolog;
GN Name=gnl3; ORFNames=DDB_G0287147;
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 -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- DOMAIN: In contrast to other GTP-binding proteins, this family is
CC characterized by a circular permutation of the GTPase motifs described
CC by a G4-G1-G3 pattern.
CC -!- SIMILARITY: Belongs to the TRAFAC class YlqF/YawG GTPase family.
CC {ECO:0000255|PROSITE-ProRule:PRU01058}.
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DR EMBL; AAFI02000098; EAL63848.1; -; Genomic_DNA.
DR RefSeq; XP_637356.1; XM_632264.1.
DR AlphaFoldDB; Q54KS4; -.
DR SMR; Q54KS4; -.
DR BioGRID; 1250981; 1.
DR STRING; 44689.DDB0266396; -.
DR PaxDb; Q54KS4; -.
DR EnsemblProtists; EAL63848; EAL63848; DDB_G0287147.
DR GeneID; 8625978; -.
DR KEGG; ddi:DDB_G0287147; -.
DR dictyBase; DDB_G0287147; gnl3.
DR eggNOG; KOG2484; Eukaryota.
DR HOGENOM; CLU_011106_5_3_1; -.
DR InParanoid; Q54KS4; -.
DR OMA; FKLDGLW; -.
DR PhylomeDB; Q54KS4; -.
DR Reactome; R-DDI-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR PRO; PR:Q54KS4; -.
DR Proteomes; UP000002195; Chromosome 4.
DR GO; GO:0005730; C:nucleolus; IBA:GO_Central.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR Gene3D; 1.10.1580.10; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR030378; G_CP_dom.
DR InterPro; IPR014813; Gnl3_N_dom.
DR InterPro; IPR006073; GTP-bd.
DR InterPro; IPR023179; GTP-bd_ortho_bundle_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF08701; GN3L_Grn1; 1.
DR Pfam; PF01926; MMR_HSR1; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS51721; G_CP; 1.
PE 3: Inferred from homology;
KW Coiled coil; GTP-binding; Nucleotide-binding; Nucleus; Reference proteome.
FT CHAIN 1..615
FT /note="Guanine nucleotide-binding protein-like 3 homolog"
FT /id="PRO_0000327660"
FT DOMAIN 135..321
FT /note="CP-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01058"
FT REGION 1..126
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 460..615
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 53..105
FT /evidence="ECO:0000255"
FT COILED 473..556
FT /evidence="ECO:0000255"
FT COMPBIAS 8..34
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 59..110
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 466..517
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 522..563
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 585..615
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 183..186
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT BINDING 270..277
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT BINDING 314..317
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
SQ SEQUENCE 615 AA; 70789 MW; 72A491928587B0F4 CRC64;
MGKQTASKRQ SLHHKHKVLK KVAEHHRKVK RFAKQHPELN KSRKDPGIPN LWPFKEDMLN
KIEQQKQKAS EEKKNKKEKR RLEQMAEARR DIASMAADAK RRESEFQERQ QLKQQQKQQG
KFEKEGKDSS LKQFYREVKK VIEAGDVILQ VLDARDPMGC RCLEIEKMIL ERYTNKKIVL
ILNKIDLVPR ENVLMWLKYL RNFYPTLAFK CSTQQQKRNL GQQGGIQPEL ASNDMLNSTE
SLGAEQLLQL LKNYSRSLNI KTSVTVGIIG YPNVGKSSLI NSLKRTRSVG VGATPGFTKF
AQEVHLDKNV KLLDSPGIVP IKGNVDENII LRNVVKLEKV LDPIAPVDAI LSRCSQKQIL
DIYEIAQYQS TTDFLTQVAA KRKKIVKGGI ADLRSTAISV IRDWTGGKIP FYTQPPKVLV
KSTLLSQFSD ELNIDQSDLI STVSNQNTSF ASLKYLEPKQ QELDNSLFDD DDEEDEEEME
DEDEDDDEEE EEEMEDEEDE EDEEDEEDED EMEEDSDSEA LLKYQQQKQV VKATAKQVAQ
IKSKSQNLKD ENDQFNPQSN KQLKKQNKKL KKKFGIVSTS SKQVQDDDDE DDDDEQEEID
QDDEDDEDID EDEAF
