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Database: UniProt
Entry: OLA1_CHICK
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ID   OLA1_CHICK              Reviewed;         396 AA.
AC   Q5ZM25;
DT   25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   24-JAN-2024, entry version 124.
DE   RecName: Full=Obg-like ATPase 1 {ECO:0000255|HAMAP-Rule:MF_03167};
GN   Name=OLA1 {ECO:0000255|HAMAP-Rule:MF_03167}; ORFNames=RCJMB04_3f20;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=CB; TISSUE=Bursa of Fabricius;
RX   PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA   Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA   Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA   Hayashizaki Y., Buerstedde J.-M.;
RT   "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT   function analysis.";
RL   Genome Biol. 6:R6.1-R6.9(2005).
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; AJ719559; CAG31218.1; -; mRNA.
DR   RefSeq; NP_001026425.1; NM_001031254.2.
DR   AlphaFoldDB; Q5ZM25; -.
DR   SMR; Q5ZM25; -.
DR   STRING; 9031.ENSGALP00000045498; -.
DR   PaxDb; 9031-ENSGALP00000015171; -.
DR   Ensembl; ENSGALT00000140082; ENSGALP00000078312; ENSGALG00000009325.
DR   Ensembl; ENSGALT00010064860.1; ENSGALP00010039644.1; ENSGALG00010026724.1.
DR   Ensembl; ENSGALT00015039222; ENSGALP00015022789; ENSGALG00015016056.
DR   GeneID; 424144; -.
DR   KEGG; gga:424144; -.
DR   CTD; 29789; -.
DR   VEuPathDB; HostDB:geneid_424144; -.
DR   eggNOG; KOG1491; Eukaryota.
DR   GeneTree; ENSGT00390000000673; -.
DR   HOGENOM; CLU_018395_1_0_1; -.
DR   InParanoid; Q5ZM25; -.
DR   PhylomeDB; Q5ZM25; -.
DR   TreeFam; TF300774; -.
DR   Reactome; R-GGA-114608; Platelet degranulation.
DR   PRO; PR:Q5ZM25; -.
DR   Proteomes; UP000000539; Chromosome 7.
DR   Bgee; ENSGALG00000009325; Expressed in skeletal muscle tissue and 13 other cell types or tissues.
DR   ExpressionAtlas; Q5ZM25; baseline and differential.
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; 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   CDD; cd04867; TGS_YchF_OLA1; 1.
DR   CDD; cd01900; YchF; 1.
DR   Gene3D; 3.10.20.30; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 1.10.150.300; TGS-like domain; 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   NCBIfam; TIGR00092; redox-regulated ATPase YchF; 1.
DR   PANTHER; PTHR23305; OBG GTPASE FAMILY; 1.
DR   PANTHER; PTHR23305:SF11; OBG-LIKE ATPASE 1; 1.
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; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF81271; TGS-like; 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_0000354699"
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;  44779 MW;  C4C86360DFBF8A40 CRC64;
     MAPKKAGDGV KAHPIIGRFG TSLKIGIVGL PNVGKSTFFN VLTKSQAAAE NFPFCTIDPN
     ESRVPVPDDR FDFLCQYHKP PSKIPAFLNV VDIAGLVKGA HTGQGLGNSF LSHINACDGI
     FHLMRAFEDD DITHVEGSVD PVRDIEIIHE ELRLKDEELI TQSIDKLEKV AVRGGDKKLK
     PEYDVMCKIK TWVIDEKKAV RFYHDWNDKE IDVLNKHLFF TSKPMIYLVN LSEKDYIRKK
     NKWLIKIKEW VDKHDPGALV IPFSGALELK LQDMSAEEKQ KYLEENMTQS ALPKIIKAGY
     AALQLEYFFT AGPDEVRAWT IRKGTKAPQA AGKIHTDFEK GFIMAEVMKY EDFKEGGSEA
     AVKAAGKYRQ QGRNYIVEDG DIIFFKFNTP QQPKKK
//
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