ID   OLA1_CAEEL              Reviewed;         395 AA.
AC   P91917;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   03-AUG-2022, entry version 148.
DE   RecName: Full=Obg-like ATPase 1 {ECO:0000255|HAMAP-Rule:MF_03167};
GN   Name=ola-1; Synonyms=tag-210; ORFNames=W08E3.3;
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2;
RX   PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RT   "Genome sequence of the nematode C. elegans: a platform for investigating
RT   biology.";
RL   Science 282:2012-2018(1998).
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   -!- 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}.
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; Z92773; CAB07131.1; -; Genomic_DNA.
DR   PIR; T26288; T26288.
DR   RefSeq; NP_001254006.1; NM_001267077.1.
DR   AlphaFoldDB; P91917; -.
DR   SMR; P91917; -.
DR   BioGRID; 38600; 8.
DR   DIP; DIP-26051N; -.
DR   IntAct; P91917; 1.
DR   STRING; 6239.W08E3.3a; -.
DR   EPD; P91917; -.
DR   PaxDb; P91917; -.
DR   PeptideAtlas; P91917; -.
DR   EnsemblMetazoa; W08E3.3a.1; W08E3.3a.1; WBGene00012344.
DR   EnsemblMetazoa; W08E3.3a.2; W08E3.3a.2; WBGene00012344.
DR   GeneID; 173205; -.
DR   KEGG; cel:CELE_W08E3.3; -.
DR   UCSC; W08E3.3; c. elegans.
DR   CTD; 173205; -.
DR   WormBase; W08E3.3a; CE14708; WBGene00012344; ola-1.
DR   eggNOG; KOG1491; Eukaryota.
DR   GeneTree; ENSGT00390000000673; -.
DR   HOGENOM; CLU_018395_1_0_1; -.
DR   InParanoid; P91917; -.
DR   OMA; VLRCFDN; -.
DR   OrthoDB; 738371at2759; -.
DR   PhylomeDB; P91917; -.
DR   Reactome; R-CEL-114608; Platelet degranulation.
DR   PRO; PR:P91917; -.
DR   Proteomes; UP000001940; Chromosome I.
DR   Bgee; WBGene00012344; Expressed in larva and 4 other tissues.
DR   ExpressionAtlas; P91917; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005783; C:endoplasmic reticulum; HDA:WormBase.
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   3: Inferred from homology;
KW   ATP-binding; Cytoplasm; Hydrolase; Magnesium; Metal-binding;
KW   Nucleotide-binding; Reference proteome.
FT   CHAIN           1..395
FT                   /note="Obg-like ATPase 1"
FT                   /id="PRO_0000122460"
FT   DOMAIN          22..280
FT                   /note="OBG-type G"
FT   DOMAIN          301..384
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         228
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03167"
SQ   SEQUENCE   395 AA;  44351 MW;  8B2728357A3283CC CRC64;
     MPPKKNVVEE KPALIGRLGT NLKVGILGLP NVGKSTFFNV LTKSEAQAEN FPFCTIDPNE
     SRVAVQDDRF DWLVNHYKPA SKVPAFLNVT DIAGLVKGAS EGQGLGNAFL SHVSACDALF
     HLCRAFDDDD VTHVEGEVDP VRDLEIISNE LFAKDLQFID GPLDKVEKLF TRANDKTKKI
     EYDTLVRVKK CLEEKKPVRQ ELWNEKEIEI LNKHLFLTAK PIVYLVNLSE KDYIRKKNKW
     LPKIKAWIDT NDAGAVLIPF SGAFELKLLD MPEDERQKYL KEQGVTSNLD KIVHTGYKAL
     QLEYFFTSGE DEVKAWTIQV GTPAPKAAGR IHTDFEKGFI MAEVMKVADL IELGDEAKCK
     AGGKYRQQGK TYIVQDGDVI FFKFNAGAGL QAKKK