OLA1_BOVIN
ID OLA1_BOVIN Reviewed; 396 AA.
AC Q2HJ33;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Obg-like ATPase 1 {ECO:0000255|HAMAP-Rule:MF_03167};
GN Name=OLA1 {ECO:0000255|HAMAP-Rule:MF_03167};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Uterus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (FEB-2006) 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; BC113336; AAI13337.1; -; mRNA.
DR RefSeq; NP_001039510.1; NM_001046045.1.
DR AlphaFoldDB; Q2HJ33; -.
DR SMR; Q2HJ33; -.
DR STRING; 9913.ENSBTAP00000009160; -.
DR PaxDb; Q2HJ33; -.
DR PeptideAtlas; Q2HJ33; -.
DR PRIDE; Q2HJ33; -.
DR Ensembl; ENSBTAT00000009160; ENSBTAP00000009160; ENSBTAG00000006970.
DR GeneID; 509966; -.
DR KEGG; bta:509966; -.
DR CTD; 29789; -.
DR VEuPathDB; HostDB:ENSBTAG00000006970; -.
DR VGNC; VGNC:32416; OLA1.
DR eggNOG; KOG1491; Eukaryota.
DR GeneTree; ENSGT00390000000673; -.
DR HOGENOM; CLU_018395_1_0_1; -.
DR InParanoid; Q2HJ33; -.
DR OMA; VLRCFDN; -.
DR OrthoDB; 738371at2759; -.
DR TreeFam; TF300774; -.
DR Reactome; R-BTA-114608; Platelet degranulation.
DR Proteomes; UP000009136; Chromosome 2.
DR Bgee; ENSBTAG00000006970; Expressed in semimembranosus muscle and 104 other tissues.
DR ExpressionAtlas; Q2HJ33; baseline and differential.
DR GO; GO:0005813; C:centrosome; IEA:Ensembl.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
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; 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 GO; GO:0046034; P:ATP metabolic process; IEA:Ensembl.
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_0000354696"
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; 44744 MW; 8F2B9557BECBFF55 CRC64;
MPPKKGGDGI KPPPIIGRFG TSLKIGIVGL PNVGKSTFFN VLTNSQASAE NFPFCTIDPN
ESRVPVPDER FDFLCQYHKP ASKIPAFLNV VDIAGLVKGA HNGQGLGNAF LSHISACDGI
FHLTRAFEDD DITHVEGSVD PVRDIEIIHE ELQLKDEEMV GPIIDKLEKV AVRGGDKKLK
PEYDIMCKVK SWVIDQKKPV RFYHDWNDKE IEVLNKHLFL TSKPMVYLVN LSEKDYIRKK
NKWLIKIKEW VDKYDPGALV IPFSGALELR LQELSAEERQ KYLEANMTQS ALPKIIKAGF
AALQLEYFFT AGPDEVRAWT IRKGTKAPQA AGKIHTDFEK GFIMAEVMKY EDFKEEGSEN
AVKAAGKYRQ QGRNYIVEDG DIIFFKFNTP QQPKKK
