OLA1_CHICK
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 03-AUG-2022, entry version 118.
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.ENSGALP00000015171; -.
DR PaxDb; Q5ZM25; -.
DR Ensembl; ENSGALT00000015187; ENSGALP00000015171; ENSGALG00000009325.
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 OrthoDB; 738371at2759; -.
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 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 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_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
