ID   OLA1_PONAB              Reviewed;         396 AA.
AC   Q5R821;
DT   25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 96.
DE   RecName: Full=Obg-like ATPase 1 {ECO:0000255|HAMAP-Rule:MF_03167};
GN   Name=OLA1 {ECO:0000255|HAMAP-Rule:MF_03167};
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) 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; CR859934; CAH92089.1; -; mRNA.
DR   RefSeq; NP_001127505.1; NM_001134033.1.
DR   AlphaFoldDB; Q5R821; -.
DR   SMR; Q5R821; -.
DR   STRING; 9601.ENSPPYP00000014451; -.
DR   GeneID; 100174581; -.
DR   KEGG; pon:100174581; -.
DR   CTD; 29789; -.
DR   eggNOG; KOG1491; Eukaryota.
DR   InParanoid; Q5R821; -.
DR   Proteomes; UP000001595; Unplaced.
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   Acetylation; 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_0000354697"
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"
FT   MOD_RES         294
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NTK5"
SQ   SEQUENCE   396 AA;  44697 MW;  F3839369AF7CD363 CRC64;
     MPPKKGGDGI KPPPIIGRFG TSLKIGIVGL PNVGKSTFFN VLTNSQASAE NFPFCTIDPN
     ESRVPVPDER FDSLCQYHKP ASKIPAFLNV VDIAGLVKGA HNGQGLGNAF LSHISACDGI
     FHLTRAFEDD DITHVEGSVD PIRDIEIIHE ELQLKDEEMI GPIIDKLEKV AVRGGDKKLK
     PEYDIMCKVK SWVIDQKKPV RFYHDWNDKE IEVLNKHLFL TSKPMVYLVN LSEKDYIRKK
     NKWLIKIKEW VDKYDPGALV IPFSGALELK LQELSAEERQ KYLEANMTQS ALPKIIKAGF
     AALQLEYFFT AGPEEVRAWT IRKGTKAPQA AGKIHTDFEK GFIMAEVMKY EDFKEEGSEN
     AVKAAGKYRQ QGRNYIVEDG DIIFFKFNTP QQPKKK