OLA1_YEAST
ID OLA1_YEAST Reviewed; 394 AA.
AC P38219; D6VQ27;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 03-AUG-2022, entry version 188.
DE RecName: Full=Obg-like ATPase 1 {ECO:0000255|HAMAP-Rule:MF_03167};
GN Name=OLA1 {ECO:0000255|HAMAP-Rule:MF_03167}; OrderedLocusNames=YBR025C;
GN ORFNames=YBR0309;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8091864; DOI=10.1002/yea.320100010;
RA Smits P.H.M., de Haan M., Maat C., Grivell L.A.;
RT "The complete sequence of a 33 kb fragment on the right arm of chromosome
RT II from Saccharomyces cerevisiae reveals 16 open reading frames, including
RT ten new open reading frames, five previously identified genes and a
RT homologue of the SCO1 gene.";
RL Yeast 10:S75-S80(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7813418; DOI=10.1002/j.1460-2075.1994.tb06923.x;
RA Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C.,
RA Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M.,
RA Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M.,
RA Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H.,
RA Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D.,
RA Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N.,
RA Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J.,
RA Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C.,
RA Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P.,
RA Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y.,
RA Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F.,
RA Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E.,
RA Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M.,
RA Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B.,
RA Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L.,
RA Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M.,
RA Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S.,
RA Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K.,
RA Mewes H.-W., Kleine K.;
RT "Complete DNA sequence of yeast chromosome II.";
RL EMBO J. 13:5795-5809(1994).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP PROTEIN SEQUENCE OF 99-125 AND 144-153, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RA Bienvenut W.V., Peters C.;
RL Submitted (JUN-2005) to UniProtKB.
RN [5]
RP INDUCTION.
RX PubMed=9712873; DOI=10.1074/jbc.273.35.22480;
RA Godon C., Lagniel G., Lee J., Buhler J.-M., Kieffer S., Perrot M.,
RA Boucherie H., Toledano M.B., Labarre J.;
RT "The H2O2 stimulon in Saccharomyces cerevisiae.";
RL J. Biol. Chem. 273:22480-22489(1998).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RX PubMed=10684247; DOI=10.1083/jcb.148.4.635;
RA Rout M.P., Aitchison J.D., Suprapto A., Hjertaas K., Zhao Y., Chait B.T.;
RT "The yeast nuclear pore complex: composition, architecture, and transport
RT mechanism.";
RL J. Cell Biol. 148:635-651(2000).
RN [7]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [8]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND INTERACTION WITH RPT6.
RX PubMed=16284124; DOI=10.1074/mcp.m500303-mcp200;
RA Guerrero C., Tagwerker C., Kaiser P., Huang L.;
RT "An integrated mass spectrometry-based proteomic approach: quantitative
RT analysis of tandem affinity-purified in vivo cross-linked protein complexes
RT (QTAX) to decipher the 26 S proteasome-interacting network.";
RL Mol. Cell. Proteomics 5:366-378(2006).
RN [10]
RP FUNCTION, AND ATPASE ACTIVITY.
RX PubMed=17430889; DOI=10.1074/jbc.m700541200;
RA Koller-Eichhorn R., Marquardt T., Gail R., Wittinghofer A., Kostrewa D.,
RA Kutay U., Kambach C.;
RT "Human OLA1 defines an ATPase subfamily in the Obg family of GTP-binding
RT proteins.";
RL J. Biol. Chem. 282:19928-19937(2007).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-89, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-116 AND SER-119, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
RN [13]
RP INDUCTION.
RX PubMed=22842922; DOI=10.1038/ncb2549;
RA Tkach J.M., Yimit A., Lee A.Y., Riffle M., Costanzo M., Jaschob D.,
RA Hendry J.A., Ou J., Moffat J., Boone C., Davis T.N., Nislow C., Brown G.W.;
RT "Dissecting DNA damage response pathways by analysing protein localization
RT and abundance changes during DNA replication stress.";
RL Nat. Cell Biol. 14:966-976(2012).
RN [14]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-98, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22106047; DOI=10.1002/pmic.201100166;
RA Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.;
RT "Sites of ubiquitin attachment in Saccharomyces cerevisiae.";
RL Proteomics 12:236-240(2012).
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, ECO:0000269|PubMed:17430889}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC -!- SUBUNIT: Monomer (By similarity). Interacts with the 26S proteasome
CC subunit RPT6. {ECO:0000255|HAMAP-Rule:MF_03167,
CC ECO:0000269|PubMed:16284124}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03167,
CC ECO:0000269|PubMed:10684247, ECO:0000269|PubMed:14562095}.
CC -!- INDUCTION: By hydrogen peroxide and during DNA replication stress.
CC {ECO:0000269|PubMed:22842922, ECO:0000269|PubMed:9712873}.
CC -!- MISCELLANEOUS: Present with 36803 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
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; X76078; CAA53682.1; -; Genomic_DNA.
DR EMBL; Z35894; CAA84967.1; -; Genomic_DNA.
DR EMBL; BK006936; DAA07147.1; -; Genomic_DNA.
DR PIR; S45881; S45881.
DR RefSeq; NP_009581.1; NM_001178373.1.
DR AlphaFoldDB; P38219; -.
DR SMR; P38219; -.
DR BioGRID; 32728; 174.
DR DIP; DIP-4893N; -.
DR IntAct; P38219; 52.
DR MINT; P38219; -.
DR STRING; 4932.YBR025C; -.
DR CarbonylDB; P38219; -.
DR iPTMnet; P38219; -.
DR MaxQB; P38219; -.
DR PaxDb; P38219; -.
DR PRIDE; P38219; -.
DR EnsemblFungi; YBR025C_mRNA; YBR025C; YBR025C.
DR GeneID; 852313; -.
DR KEGG; sce:YBR025C; -.
DR SGD; S000000229; OLA1.
DR VEuPathDB; FungiDB:YBR025C; -.
DR eggNOG; KOG1491; Eukaryota.
DR GeneTree; ENSGT00390000000673; -.
DR HOGENOM; CLU_018395_1_2_1; -.
DR InParanoid; P38219; -.
DR OMA; VLRCFDN; -.
DR BioCyc; YEAST:G3O-29005-MON; -.
DR Reactome; R-SCE-114608; Platelet degranulation.
DR PRO; PR:P38219; -.
DR Proteomes; UP000002311; Chromosome II.
DR RNAct; P38219; protein.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IDA:SGD.
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 1: Evidence at protein level;
KW ATP-binding; Cytoplasm; Direct protein sequencing; Hydrolase;
KW Isopeptide bond; Magnesium; Metal-binding; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Ubl conjugation.
FT CHAIN 1..394
FT /note="Obg-like ATPase 1"
FT /id="PRO_0000122462"
FT DOMAIN 21..285
FT /note="OBG-type G"
FT DOMAIN 306..389
FT /note="TGS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01228"
FT BINDING 30..35
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03167"
FT BINDING 34
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 55
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 233
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03167"
FT MOD_RES 89
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 116
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 119
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT CROSSLNK 98
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
SQ SEQUENCE 394 AA; 44174 MW; 4D3E59931A155BCB CRC64;
MPPKKQVEEK KVLLGRPGNN LKAGIVGLAN VGKSTFFQAI TRCPLGNPAN YPFATIDPEE
ARVIVPSPRF DKLCEIYKKT ASEVPAHLTV YDIAGLTKGA SAGEGLGNAF LSHIRSVDSI
YQVVRCFDDA EIIHVEGDVD PVRDLEIINQ ELRLKDIEFA QKALEGAEKI AKRGGQSLEV
KQKKEEMDLI TKIIKLLESG QRVANHSWTS KEVEIINSMF LLTAKPCIYL INLSERDYIR
KKNKHLLRIK EWVDKYSPGD LIIPFSVSLE ERLSHMSPED AEEELKKLQT ISALPKIITT
MRQKLDLISF FTCGPDEVRE WTIRRGTKAP QAAGVIHNDL MNTFILAQVM KCEDVFEYKD
DSAIKAAGKL MQKGKDYVVE DGDIIYFRAG AGKN
