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YEAD_SCHPO
ID   YEAD_SCHPO              Reviewed;         407 AA.
AC   O14078;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 137.
DE   RecName: Full=Obg-like ATPase homolog;
DE            Short=OLA1 homolog;
GN   ORFNames=SPAC2E11.13c, SPACUNK4.13c;
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).
CC   -!- FUNCTION: Hydrolyzes ATP, and can also hydrolyze GTP with lower
CC       efficiency. Has lower affinity for GTP (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase
CC       superfamily. OBG GTPase family. {ECO:0000255|PROSITE-ProRule:PRU01047}.
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DR   EMBL; CU329670; CAA20143.1; -; Genomic_DNA.
DR   PIR; T41708; T41708.
DR   RefSeq; NP_593965.1; NM_001019392.2.
DR   AlphaFoldDB; O14078; -.
DR   SMR; O14078; -.
DR   STRING; 4896.SPACUNK4.13c.1; -.
DR   MaxQB; O14078; -.
DR   PaxDb; O14078; -.
DR   EnsemblFungi; SPACUNK4.13c.1; SPACUNK4.13c.1:pep; SPACUNK4.13c.
DR   GeneID; 2542506; -.
DR   KEGG; spo:SPACUNK4.13c; -.
DR   PomBase; SPACUNK4.13c; -.
DR   VEuPathDB; FungiDB:SPACUNK4.13c; -.
DR   eggNOG; KOG1491; Eukaryota.
DR   HOGENOM; CLU_018395_1_2_1; -.
DR   InParanoid; O14078; -.
DR   OMA; VYLVNMD; -.
DR   PhylomeDB; O14078; -.
DR   PRO; PR:O14078; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005739; C:mitochondrion; ISO:PomBase.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
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   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   3: Inferred from homology;
KW   ATP-binding; GTP-binding; Nucleotide-binding; Reference proteome.
FT   CHAIN           1..407
FT                   /note="Obg-like ATPase homolog"
FT                   /id="PRO_0000122461"
FT   DOMAIN          46..301
FT                   /note="OBG-type G"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01047"
FT   DOMAIN          322..405
FT                   /note="TGS"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01228"
FT   BINDING         55..60
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01047"
FT   BINDING         249
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   407 AA;  45362 MW;  ACF6BF06AB5A9CA0 CRC64;
     MRGIVTRIVL STQKCLPSVN CTRRYYSKQK DISIVRQRLG RPGNHLKIGI VGMPNIGKST
     LFQILTKTNL GNPANYPFAT IDPVHAKAPV LDSQYELLCE IYQPKTRIPA QLTIYDTAGL
     TRNSSKGEGL GNAFLSNIRS VDALFQLVRA FPEAQVPHVE KSVDPVRDLQ IIQEELLLKD
     AEFLESYLKK EGRSPKTCAK ALDTARRALE VVLGKGRQIS KAEWNDEQIP ILNSLNLLTA
     KPVVYLVNMD QDDYLSDEQE ALKGIKEWVE KNSFGDQVIP LSVLFEEQLF MLTPEEAAQE
     CASLGKNSQL SEIICAGYSA LNLIHYFTAS EKIVQAWTIA DGSKAPDAAG IIHSDFKKKF
     VAGEVIKFSD FEKYKSVDAC KSVGKCKTKG KDYTVEPGDI IFWKIAR
 
 
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