OLA1_RAT
ID OLA1_RAT Reviewed; 396 AA.
AC A0JPJ7;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 12-DEC-2006, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Obg-like ATPase 1 {ECO:0000255|HAMAP-Rule:MF_03167};
GN Name=Ola1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
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; BC127457; AAI27458.1; -; mRNA.
DR RefSeq; NP_001029099.1; NM_001033927.1.
DR AlphaFoldDB; A0JPJ7; -.
DR SMR; A0JPJ7; -.
DR BioGRID; 255376; 1.
DR IntAct; A0JPJ7; 1.
DR STRING; 10116.ENSRNOP00000026040; -.
DR iPTMnet; A0JPJ7; -.
DR PhosphoSitePlus; A0JPJ7; -.
DR SwissPalm; A0JPJ7; -.
DR jPOST; A0JPJ7; -.
DR PaxDb; A0JPJ7; -.
DR PeptideAtlas; A0JPJ7; -.
DR PRIDE; A0JPJ7; -.
DR Ensembl; ENSRNOT00000026040; ENSRNOP00000026040; ENSRNOG00000019047.
DR GeneID; 296488; -.
DR KEGG; rno:296488; -.
DR UCSC; RGD:1307982; rat.
DR CTD; 29789; -.
DR RGD; 1307982; Ola1.
DR eggNOG; KOG1491; Eukaryota.
DR GeneTree; ENSGT00390000000673; -.
DR HOGENOM; CLU_018395_1_0_1; -.
DR InParanoid; A0JPJ7; -.
DR OMA; VLRCFDN; -.
DR OrthoDB; 738371at2759; -.
DR PhylomeDB; A0JPJ7; -.
DR TreeFam; TF300774; -.
DR Reactome; R-RNO-114608; Platelet degranulation.
DR PRO; PR:A0JPJ7; -.
DR Proteomes; UP000002494; Chromosome 3.
DR Bgee; ENSRNOG00000019047; Expressed in Ammon's horn and 20 other tissues.
DR Genevisible; A0JPJ7; RN.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; ISO:RGD.
DR GO; GO:0016887; F:ATP hydrolysis activity; ISO:RGD.
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 GO; GO:0046034; P:ATP metabolic process; ISO:RGD.
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_0000354698"
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; 44535 MW; 8CB12363A744398E CRC64;
MPPKKGGDGL KPPPIIGRFG TSLKIGIVGL PNVGKSTFFN VLTNSQASAE NFPFCTIDPN
ESRVPVPDER FDFLCQCHKP ASKIPAFLNV VDIAGLVKGA HNGQGLGNAF LSHISACDGI
FHLTRAFEDD DITHVEGSVD PIRDIEIIHE ELQLKDEEMI GPIIDKLEKV AVRGGDKKLK
PEYDIMCKVK SWVIDQKKPV RFYHDWNDKE IEVLNKHLLL TSKPMVYLVN LSEKDYIRKK
NKWLIKIKEW VDKSDPGALV IPFSGALELK LQELSAEERQ KYLEANMTQS ALPKIIKAGF
AALQLEYFFT AGPDEVRAWT IRKGTKAPQA AGKIHTDFEK GFIMAEVMKY DDFKDEGSEN
AVKAAGKYRQ QGRNYIVEDG DIIFFKFNTP QQSKKK
