OLA1_DROME
ID OLA1_DROME Reviewed; 397 AA.
AC Q8SWU7; Q8IRM4; Q9W317;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Obg-like ATPase 1 {ECO:0000255|HAMAP-Rule:MF_03167};
GN ORFNames=CG1354;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [2]
RP GENOME REANNOTATION, AND ALTERNATIVE SPLICING.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
RC STRAIN=Berkeley; TISSUE=Embryo;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-132, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RX PubMed=17372656; DOI=10.1039/b617545g;
RA Bodenmiller B., Mueller L.N., Pedrioli P.G.A., Pflieger D., Juenger M.A.,
RA Eng J.K., Aebersold R., Tao W.A.;
RT "An integrated chemical, mass spectrometric and computational strategy for
RT (quantitative) phosphoproteomics: application to Drosophila melanogaster
RT Kc167 cells.";
RL Mol. Biosyst. 3:275-286(2007).
CC -!- FUNCTION: Hydrolyzes ATP, and can also hydrolyze GTP with lower
CC efficiency. Has lower affinity for GTP. {ECO:0000255|HAMAP-
CC Rule:MF_03167}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_03167}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03167}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=A; Synonyms=C, D;
CC IsoId=Q8SWU7-1; Sequence=Displayed;
CC Name=B;
CC IsoId=Q8SWU7-2; Sequence=VSP_037204;
CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase
CC superfamily. OBG GTPase family. YchF/OLA1 subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_03167}.
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DR EMBL; AE014298; AAF46520.2; -; Genomic_DNA.
DR EMBL; AE014298; AAN09613.1; -; Genomic_DNA.
DR EMBL; AE014298; AAN09614.1; -; Genomic_DNA.
DR EMBL; AE014298; AAN09615.1; -; Genomic_DNA.
DR EMBL; AY095074; AAM11402.1; -; mRNA.
DR RefSeq; NP_001259389.1; NM_001272460.1. [Q8SWU7-1]
DR RefSeq; NP_572580.1; NM_132352.4. [Q8SWU7-1]
DR RefSeq; NP_727362.1; NM_167201.4. [Q8SWU7-1]
DR RefSeq; NP_727363.1; NM_167202.4. [Q8SWU7-1]
DR RefSeq; NP_727364.1; NM_167203.2. [Q8SWU7-2]
DR AlphaFoldDB; Q8SWU7; -.
DR SMR; Q8SWU7; -.
DR BioGRID; 58352; 5.
DR IntAct; Q8SWU7; 5.
DR STRING; 7227.FBpp0088408; -.
DR iPTMnet; Q8SWU7; -.
DR PaxDb; Q8SWU7; -.
DR PRIDE; Q8SWU7; -.
DR DNASU; 31914; -.
DR EnsemblMetazoa; FBtr0089383; FBpp0088408; FBgn0030151. [Q8SWU7-1]
DR EnsemblMetazoa; FBtr0089384; FBpp0088409; FBgn0030151. [Q8SWU7-1]
DR EnsemblMetazoa; FBtr0089385; FBpp0088410; FBgn0030151. [Q8SWU7-1]
DR EnsemblMetazoa; FBtr0089386; FBpp0088411; FBgn0030151. [Q8SWU7-2]
DR EnsemblMetazoa; FBtr0336922; FBpp0307859; FBgn0030151. [Q8SWU7-1]
DR GeneID; 31914; -.
DR KEGG; dme:Dmel_CG1354; -.
DR UCSC; CG1354-RA; d. melanogaster. [Q8SWU7-1]
DR UCSC; CG1354-RB; d. melanogaster.
DR FlyBase; FBgn0030151; CG1354.
DR VEuPathDB; VectorBase:FBgn0030151; -.
DR eggNOG; KOG1491; Eukaryota.
DR GeneTree; ENSGT00390000000673; -.
DR HOGENOM; CLU_018395_1_0_1; -.
DR InParanoid; Q8SWU7; -.
DR OMA; VLRCFDN; -.
DR PhylomeDB; Q8SWU7; -.
DR Reactome; R-DME-114608; Platelet degranulation.
DR BioGRID-ORCS; 31914; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 31914; -.
DR PRO; PR:Q8SWU7; -.
DR Proteomes; UP000000803; Chromosome X.
DR Bgee; FBgn0030151; Expressed in eye disc (Drosophila) and 40 other tissues.
DR ExpressionAtlas; Q8SWU7; baseline and differential.
DR Genevisible; Q8SWU7; DM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central.
DR GO; GO:0005525; F:GTP binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0043023; F:ribosomal large subunit binding; IEA:UniProtKB-UniRule.
DR GO; GO:0043022; F:ribosome binding; IEA:UniProtKB-UniRule.
DR CDD; cd04867; TGS_YchF_OLA1; 1.
DR CDD; cd01900; YchF; 1.
DR Gene3D; 1.10.150.300; -; 1.
DR Gene3D; 3.10.20.30; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_00944; YchF_OLA1_ATPase; 1.
DR InterPro; IPR004396; ATPase_YchF/OLA1.
DR InterPro; IPR012675; Beta-grasp_dom_sf.
DR InterPro; IPR031167; G_OBG.
DR InterPro; IPR006073; GTP-bd.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR004095; TGS.
DR InterPro; IPR012676; TGS-like.
DR InterPro; IPR023192; TGS-like_dom_sf.
DR InterPro; IPR013029; YchF_C.
DR InterPro; IPR041706; YchF_N.
DR Pfam; PF01926; MMR_HSR1; 1.
DR Pfam; PF06071; YchF-GTPase_C; 1.
DR PIRSF; PIRSF006641; CHP00092; 1.
DR PRINTS; PR00326; GTP1OBG.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF81271; SSF81271; 1.
DR TIGRFAMs; TIGR00092; TIGR00092; 1.
DR PROSITE; PS51710; G_OBG; 1.
DR PROSITE; PS51880; TGS; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Cytoplasm; Hydrolase; Magnesium;
KW Metal-binding; Nucleotide-binding; Phosphoprotein; Reference proteome.
FT CHAIN 1..397
FT /note="Obg-like ATPase 1"
FT /id="PRO_0000372847"
FT DOMAIN 22..281
FT /note="OBG-type G"
FT DOMAIN 302..385
FT /note="TGS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01228"
FT BINDING 31..36
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03167"
FT BINDING 35
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 55
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 229
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03167"
FT MOD_RES 132
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:17372656"
FT VAR_SEQ 1..61
FT /note="MPPKKHDEPERKPLIGRIGTNLRIGIVGVPNVGKSTFFNVLTQSAAPAENFP
FT FCTIKPNES -> MLPPMAFALPTR (in isoform B)"
FT /evidence="ECO:0000305"
FT /id="VSP_037204"
SQ SEQUENCE 397 AA; 44910 MW; C4FAB4A56F3C5C48 CRC64;
MPPKKHDEPE RKPLIGRIGT NLRIGIVGVP NVGKSTFFNV LTQSAAPAEN FPFCTIKPNE
SRVPVPDERF DYLVEYHKPA SVVPAYLNVV DIAGLVKGAA EGQGLGNDFL SHISACDAIF
HLCRAFEDPD VTHVEGEVDP VRDLEIISEE LRLKDEENLL KNLDKLEKVV ARGGDKKLKP
EYDSMLKIKD ILIDQKRHLR FEDWNAHDIE ALNKYLFLTS KPVIYLVNLS DKDFIRKKNK
WLPKIKEWID KNDPGALLIP FSGAFEHQLT EKDELERKAY ETETKCKSML EKIVVTGYKG
LQLEYFFTAG PDEVKAWTIQ KGTKAPQAAG RIHTDFEKGF IMAEVMHFED FKAEGSEANA
KAAGKYRQQG RNYTVEDGDI IFFKFNAGAG LKDAKKK
