ID   OLA1_XENLA              Reviewed;         396 AA.
AC   Q7ZWM6;
DT   25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 103.
DE   RecName: Full=Obg-like ATPase 1 {ECO:0000255|HAMAP-Rule:MF_03167};
GN   Name=ola1;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
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       Nucleus {ECO:0000255|HAMAP-Rule:MF_03167}. Nucleus, nucleolus
CC       {ECO:0000255|HAMAP-Rule:MF_03167}. Note=Predominantly cytoplasmic,
CC       shuttles between the nucleus and the cytoplasm. {ECO:0000255|HAMAP-
CC       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}.
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DR   EMBL; BC046937; AAH46937.1; -; mRNA.
DR   RefSeq; NP_001079680.1; NM_001086211.1.
DR   AlphaFoldDB; Q7ZWM6; -.
DR   SMR; Q7ZWM6; -.
DR   MaxQB; Q7ZWM6; -.
DR   DNASU; 379367; -.
DR   GeneID; 379367; -.
DR   KEGG; xla:379367; -.
DR   CTD; 379367; -.
DR   Xenbase; XB-GENE-1015264; ola1.L.
DR   OrthoDB; 738371at2759; -.
DR   Proteomes; UP000186698; Chromosome 9_10L.
DR   Bgee; 379367; Expressed in spleen and 19 other tissues.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:UniProtKB-UniRule.
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   2: Evidence at transcript level;
KW   ATP-binding; Cytoplasm; Hydrolase; Magnesium; Metal-binding;
KW   Nucleotide-binding; Nucleus; Reference proteome.
FT   CHAIN           1..396
FT                   /note="Obg-like ATPase 1"
FT                   /id="PRO_0000354701"
FT   DOMAIN          23..283
FT                   /note="OBG-type G"
FT   DOMAIN          304..387
FT                   /note="TGS"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01228"
FT   MOTIF           267..274
FT                   /note="Nuclear export signal"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03167"
FT   BINDING         32..37
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03167"
FT   BINDING         36
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         56
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         231
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03167"
SQ   SEQUENCE   396 AA;  44950 MW;  0F8E673C0E941D7F CRC64;
     MPPKKADDGP KQHPIIGRFG TSLKIGIVGL PNIGKSTFFN VLTKSQAAAE NFPFCTINPN
     ESRVPVPDDR FEFLCEHHKP ASKVPAFLNV VDIAGLVKGA SAGQGLGNAF LSHISACDGI
     FHLMRAFDDD DIIHVEGNVN PVRDIEIIRE ELRLKDEEMI IAALDKLEKV AVRGGDKKLK
     PEYDIMCKVK TWVIDEKNHV RYYHDWNDKE IDVLNKYLFL TSKPMIYLIN LSEKDYIRKK
     NKWLIKIKEW VDKNDPGALV IPFSGVLELN LQDMSDEEKQ KYLEEKMTQS VLSKIIKTGY
     AALQLEYFFT AGPDEVRAWT IKKGTKAPQA AGKIHTDFEK GFIMAEVMKF DDFKEEGTEA
     SVKAAGKYRQ QGRNYTVEDG DIIFFKFNTP QQSKKK