OLA1_SCHPO
ID OLA1_SCHPO Reviewed; 392 AA.
AC O13998;
DT 16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Obg-like ATPase 1 {ECO:0000255|HAMAP-Rule:MF_03167};
GN ORFNames=SPAC27E2.03c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
RN [3]
RP FUNCTION.
RX PubMed=22624651; DOI=10.1186/gb-2012-13-5-r36;
RA Navarro F.J., Nurse P.;
RT "A systematic screen reveals new elements acting at the G2/M cell cycle
RT control.";
RL Genome Biol. 13:R36.1-R36.10(2012).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
RG New York structural genomix research consortium (NYSGXRC);
RT "Structure of the s. pombe ychf GTP-binding protein.";
RL Submitted (JAN-2005) to the PDB data bank.
CC -!- FUNCTION: Hydrolyzes ATP, and can also hydrolyze GTP with lower
CC efficiency. Has lower affinity for GTP (By similarity). Negatively
CC regulates the G2/M transition in the cell cycle. {ECO:0000255|HAMAP-
CC Rule:MF_03167, ECO:0000269|PubMed:22624651}.
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 ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000255|HAMAP-Rule:MF_03167,
CC ECO:0000269|PubMed:16823372}.
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; CU329670; CAB11677.1; -; Genomic_DNA.
DR PIR; T38450; T38450.
DR RefSeq; NP_594403.1; NM_001019834.2.
DR PDB; 1NI3; X-ray; 2.80 A; A=1-392.
DR PDBsum; 1NI3; -.
DR AlphaFoldDB; O13998; -.
DR SMR; O13998; -.
DR BioGRID; 277939; 11.
DR STRING; 4896.SPAC27E2.03c.1; -.
DR iPTMnet; O13998; -.
DR MaxQB; O13998; -.
DR PaxDb; O13998; -.
DR PRIDE; O13998; -.
DR EnsemblFungi; SPAC27E2.03c.1; SPAC27E2.03c.1:pep; SPAC27E2.03c.
DR PomBase; SPAC27E2.03c; -.
DR VEuPathDB; FungiDB:SPAC27E2.03c; -.
DR eggNOG; KOG1491; Eukaryota.
DR HOGENOM; CLU_018395_1_2_1; -.
DR InParanoid; O13998; -.
DR OMA; VLRCFDN; -.
DR PhylomeDB; O13998; -.
DR Reactome; R-SPO-114608; Platelet degranulation.
DR EvolutionaryTrace; O13998; -.
DR PRO; PR:O13998; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; ISO:PomBase.
DR GO; GO:0005525; F:GTP binding; NAS:PomBase.
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 3D-structure; ATP-binding; Cytoplasm; Hydrolase; Magnesium; Metal-binding;
KW Nucleotide-binding; Nucleus; Reference proteome.
FT CHAIN 1..392
FT /note="Obg-like ATPase 1"
FT /id="PRO_0000356254"
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 STRAND 15..19
FT /evidence="ECO:0007829|PDB:1NI3"
FT STRAND 22..27
FT /evidence="ECO:0007829|PDB:1NI3"
FT STRAND 29..32
FT /evidence="ECO:0007829|PDB:1NI3"
FT HELIX 33..42
FT /evidence="ECO:0007829|PDB:1NI3"
FT TURN 44..46
FT /evidence="ECO:0007829|PDB:1NI3"
FT STRAND 60..65
FT /evidence="ECO:0007829|PDB:1NI3"
FT HELIX 68..77
FT /evidence="ECO:0007829|PDB:1NI3"
FT STRAND 80..83
FT /evidence="ECO:0007829|PDB:1NI3"
FT STRAND 85..90
FT /evidence="ECO:0007829|PDB:1NI3"
FT HELIX 93..95
FT /evidence="ECO:0007829|PDB:1NI3"
FT STRAND 101..105
FT /evidence="ECO:0007829|PDB:1NI3"
FT HELIX 107..113
FT /evidence="ECO:0007829|PDB:1NI3"
FT STRAND 117..124
FT /evidence="ECO:0007829|PDB:1NI3"
FT STRAND 135..138
FT /evidence="ECO:0007829|PDB:1NI3"
FT HELIX 140..168
FT /evidence="ECO:0007829|PDB:1NI3"
FT STRAND 176..178
FT /evidence="ECO:0007829|PDB:1NI3"
FT HELIX 179..197
FT /evidence="ECO:0007829|PDB:1NI3"
FT HELIX 203..205
FT /evidence="ECO:0007829|PDB:1NI3"
FT HELIX 210..217
FT /evidence="ECO:0007829|PDB:1NI3"
FT HELIX 222..224
FT /evidence="ECO:0007829|PDB:1NI3"
FT STRAND 227..232
FT /evidence="ECO:0007829|PDB:1NI3"
FT HELIX 235..238
FT /evidence="ECO:0007829|PDB:1NI3"
FT TURN 239..241
FT /evidence="ECO:0007829|PDB:1NI3"
FT HELIX 246..254
FT /evidence="ECO:0007829|PDB:1NI3"
FT STRAND 262..265
FT /evidence="ECO:0007829|PDB:1NI3"
FT HELIX 267..273
FT /evidence="ECO:0007829|PDB:1NI3"
FT HELIX 278..287
FT /evidence="ECO:0007829|PDB:1NI3"
FT HELIX 294..304
FT /evidence="ECO:0007829|PDB:1NI3"
FT STRAND 307..312
FT /evidence="ECO:0007829|PDB:1NI3"
FT STRAND 315..324
FT /evidence="ECO:0007829|PDB:1NI3"
FT HELIX 329..336
FT /evidence="ECO:0007829|PDB:1NI3"
FT HELIX 338..342
FT /evidence="ECO:0007829|PDB:1NI3"
FT STRAND 345..350
FT /evidence="ECO:0007829|PDB:1NI3"
FT HELIX 352..358
FT /evidence="ECO:0007829|PDB:1NI3"
FT HELIX 361..366
FT /evidence="ECO:0007829|PDB:1NI3"
FT STRAND 372..374
FT /evidence="ECO:0007829|PDB:1NI3"
FT STRAND 384..386
FT /evidence="ECO:0007829|PDB:1NI3"
SQ SEQUENCE 392 AA; 44333 MW; AEBBAF47DA1BC5F8 CRC64;
MPPKKQQEVV KVQWGRPGNN LKTGIVGMPN VGKSTFFRAI TKSVLGNPAN YPYATIDPEE
AKVAVPDERF DWLCEAYKPK SRVPAFLTVF DIAGLTKGAS TGVGLGNAFL SHVRAVDAIY
QVVRAFDDAE IIHVEGDVDP IRDLSIIVDE LLIKDAEFVE KHLEGLRKIT SRGANTLEMK
AKKEEQAIIE KVYQYLTETK QPIRKGDWSN REVEIINSLY LLTAKPVIYL VNMSERDFLR
QKNKYLPKIK KWIDENSPGD TLIPMSVAFE ERLTNFTEEE AIEECKKLNT KSMLPKIIVT
GYNALNLINY FTCGEDEVRS WTIRKGTKAP QAAGVIHTDF EKAFVVGEIM HYQDLFDYKT
ENACRAAGKY LTKGKEYVME SGDIAHWKAG KR
