GPA_LEIDO
ID GPA_LEIDO Reviewed; 464 AA.
AC P43151;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Putative guanine nucleotide-binding protein subunit alpha;
OS Leishmania donovani.
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Leishmaniinae; Leishmania.
OX NCBI_TaxID=5661;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Heath S., Warbrick V.E., Procter J.;
RT "Characterisation and expression of a G-alpha protein gene from Leishmania
RT donovani.";
RL Submitted (OCT-1994) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP DOUBTS ON INTEGRITY OF SEQUENCE.
RA Bucher P.;
RL Unpublished observations (MAR-1996).
CC -!- FUNCTION: Guanine nucleotide-binding proteins (G proteins) are involved
CC as modulators or transducers in various transmembrane signaling
CC systems.
CC -!- SUBUNIT: G proteins are composed of 3 units; alpha, beta and gamma. The
CC alpha chain contains the guanine nucleotide binding site.
CC -!- SIMILARITY: In the N-terminal section; belongs to the G-alpha family.
CC {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the class-II
CC aminoacyl-tRNA synthetase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=Ref.2; Type=Miscellaneous discrepancy; Note=According to Ref.2, this sequence seems to be a hybrid that consists of parts of a G protein alpha subunit and a lysyl-tRNA synthetase.; Evidence={ECO:0000305};
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DR EMBL; L36832; AAA50285.1; -; mRNA.
DR AlphaFoldDB; P43151; -.
DR PRIDE; P43151; -.
DR VEuPathDB; TriTrypDB:LdBPK_150270.1; -.
DR VEuPathDB; TriTrypDB:LdCL_150007600; -.
DR VEuPathDB; TriTrypDB:LDHU3_15.0360; -.
DR GO; GO:0004812; F:aminoacyl-tRNA ligase activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0031683; F:G-protein beta/gamma-subunit complex binding; IEA:InterPro.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IEA:InterPro.
DR GO; GO:0006418; P:tRNA aminoacylation for protein translation; IEA:InterPro.
DR CDD; cd00066; G-alpha; 1.
DR Gene3D; 1.10.400.10; -; 1.
DR Gene3D; 2.40.50.140; -; 1.
DR Gene3D; 3.30.930.10; -; 1.
DR InterPro; IPR004364; Aa-tRNA-synt_II.
DR InterPro; IPR006195; aa-tRNA-synth_II.
DR InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR InterPro; IPR001019; Gprotein_alpha_su.
DR InterPro; IPR011025; GproteinA_insert.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF00503; G-alpha; 1.
DR Pfam; PF00152; tRNA-synt_2; 1.
DR PRINTS; PR00318; GPROTEINA.
DR SMART; SM00275; G_alpha; 1.
DR SUPFAM; SSF47895; SSF47895; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF55681; SSF55681; 1.
DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
DR PROSITE; PS51882; G_ALPHA; 1.
PE 2: Evidence at transcript level;
KW GTP-binding; Magnesium; Metal-binding; Nucleotide-binding; Transducer.
FT CHAIN 1..464
FT /note="Putative guanine nucleotide-binding protein subunit
FT alpha"
FT /id="PRO_0000203667"
FT DOMAIN 33..415
FT /note="G-alpha"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 36..49
FT /note="G1 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 212..220
FT /note="G2 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 235..244
FT /note="G3 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 306..313
FT /note="G4 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 382..387
FT /note="G5 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT BINDING 41..48
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 48
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 147..151
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 214..220
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 220
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 239..243
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 268..271
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 310..313
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
SQ SEQUENCE 464 AA; 51584 MW; 5ADF75B2F48C4DE9 CRC64;
MSRSTHASGH METVQVISAL TDYIDQSKFA EIHSKLKRGD GPGESGKSTI FQIIGIAGRP
SLSKSSEFSL KATEITLLST CYHMLPDDYF GLLPLSSASV NATSTLLSTA TISRPSFSVQ
TSSSTFANFL MSGTSWRSRR QRLKIVDVGG QRSQRRKLTA ELAQDIKALW ADPGIQNTFQ
RSSEFQLNDS AAYYFDSIDR ISQPLYLPSE NDVLRSRTKT TGIIETVFEI QNSTFRMVDV
GGQRELANAH TELNNPIVQR EEFVKQLRNR DKGDDESMEI DEGFVAALEH ALPPTGGWGL
GIDRLVMFLT SQSNIKEVLL FPAMKPEGKN AISYPPGTRC SMVRVFPCCS STLTFSFCFF
FSPFFMTVIL FVEAAAMKVR GGYSGTCLSV SPRFSNGGDV LWRTSETKRD KYNEKRHAAV
KTPAQRSFLE SGWNTASDVK CCSIRRFPYL PLPLSSSPFR FPPP
