ID   AFG2_SCHPO              Reviewed;         809 AA.
AC   O60058;
DT   13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   03-AUG-2022, entry version 135.
DE   RecName: Full=ATPase family gene 2 protein {ECO:0000250|UniProtKB:P32794};
DE            EC=3.6.4.10 {ECO:0000250|UniProtKB:P32794};
GN   Name=afg2; ORFNames=SPBC56F2.07c;
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).
CC   -!- FUNCTION: ATP-dependent chaperone which uses the energy provided by ATP
CC       hydrolysis to generate mechanical force to disassemble protein
CC       complexes. Plays an essential role in the cytoplasmic maturation steps
CC       of pre-60S ribosomal particles by promoting the release of shuttling
CC       protein rlp24 from the pre-ribosomal particles. This step facilitates
CC       the subsequent release of other shuttling proteins such as nog1 and
CC       allows the transition of the pre-ribosomal particles to later
CC       maturation forms that bind SPCC550.15c/REI1.
CC       {ECO:0000250|UniProtKB:P32794}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.10;
CC         Evidence={ECO:0000250|UniProtKB:P32794};
CC   -!- SUBUNIT: Homohexamer; ATP binding induces oligomerization. Forms a
CC       ring-shaped particle of about 12 nm diameter, that displays 6-fold
CC       radial symmetry. Associates with cytoplasmic pre-60S ribosomal
CC       particles. {ECO:0000250|UniProtKB:P32794}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}.
CC   -!- DOMAIN: The first ATP-binding region binds ATP with low affinity
CC       whereas the second ATP-binding region binds ATP with high affinity.
CC       {ECO:0000250|UniProtKB:P32794}.
CC   -!- SIMILARITY: Belongs to the AAA ATPase family. AFG2 subfamily.
CC       {ECO:0000305}.
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DR   EMBL; CU329671; CAA18886.1; -; Genomic_DNA.
DR   PIR; T40537; T40537.
DR   RefSeq; NP_596710.1; NM_001022635.2.
DR   AlphaFoldDB; O60058; -.
DR   SMR; O60058; -.
DR   BioGRID; 277064; 9.
DR   IntAct; O60058; 2.
DR   STRING; 4896.SPBC56F2.07c.1; -.
DR   MaxQB; O60058; -.
DR   PaxDb; O60058; -.
DR   PRIDE; O60058; -.
DR   EnsemblFungi; SPBC56F2.07c.1; SPBC56F2.07c.1:pep; SPBC56F2.07c.
DR   GeneID; 2540537; -.
DR   KEGG; spo:SPBC56F2.07c; -.
DR   PomBase; SPBC56F2.07c; -.
DR   VEuPathDB; FungiDB:SPBC56F2.07c; -.
DR   eggNOG; KOG0730; Eukaryota.
DR   HOGENOM; CLU_000688_12_3_1; -.
DR   InParanoid; O60058; -.
DR   OMA; HITSWAN; -.
DR   PhylomeDB; O60058; -.
DR   PRO; PR:O60058; -.
DR   Proteomes; UP000002485; Chromosome II.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; HDA:PomBase.
DR   GO; GO:0005524; F:ATP binding; ISM:PomBase.
DR   GO; GO:0016887; F:ATP hydrolysis activity; ISM:PomBase.
DR   GO; GO:0042273; P:ribosomal large subunit biogenesis; ISO:PomBase.
DR   Gene3D; 3.40.50.300; -; 2.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR041569; AAA_lid_3.
DR   InterPro; IPR003959; ATPase_AAA_core.
DR   InterPro; IPR003960; ATPase_AAA_CS.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   Pfam; PF00004; AAA; 2.
DR   Pfam; PF17862; AAA_lid_3; 2.
DR   SMART; SM00382; AAA; 2.
DR   SUPFAM; SSF52540; SSF52540; 2.
DR   PROSITE; PS00674; AAA; 2.
PE   3: Inferred from homology;
KW   ATP-binding; Chaperone; Cytoplasm; Hydrolase; Nucleotide-binding;
KW   Reference proteome; Repeat.
FT   CHAIN           1..809
FT                   /note="ATPase family gene 2 protein"
FT                   /id="PRO_0000310282"
FT   REGION          169..199
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        169..188
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         320..327
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P32794"
FT   BINDING         589..596
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P32794"
SQ   SEQUENCE   809 AA;  88472 MW;  C32BED83A7F876B8 CRC64;
     MSVAIKFTVK INDGSLRRQQ TRHVFLSPAA LNRLKLSPSQ VIYLKHKGGE AVGITQSVKG
     NGIGPFEILI SPLLAKWANL KAFQRVNISQ YVHPLKEAEG IKIVASLSSN NEPIPESLIR
     KELLEIRYLH PGMIVMGESP MNMAKSGSKN LSSENMATEI FEINSGLSAQ SGTEVGSSQS
     SPSVNESEPK ATEDLDELSP GSYKVKEIHI RSPSNLIEAI SDMSLDEPRI YKFTAASSME
     IETPDLLKLP HEDRTQSAYN QGSEETQNFD GPPSAVTFSS IGGLQAQIAQ IRDIVELPFQ
     NPELFKFFNI MPPRGVLLYG PPGTGKTMVM RAVAAEANAQ VFTIDGPSVV GKYLGETESR
     LRKIFEDARA HQPSIIFIDE IDALAPKRTE DVSEAESRAV ATLLTLLDGM ANAGKVVVIA
     ATNRPNSIDE ALRRPGRLEK EIEIGIPDKS ARLDIIKLLL SGVPNEINDA QLEDLASRTH
     AYVGADLAAV VREAALRAIK RTISLQKDTS GLDIFGAVQM DDLEFALSSV RQSAMREFMM
     ESPNVHWSDI GGQEEVKQKL KESVEWPLTH GETFSRLGVR PPKGVLLYGP PGCSKTITAK
     AIATETGLNF IAVKGPELFD KFVGESERAV RQVFQKARQA SPSVIFFDEI DALTANRGED
     NSSDRVVAAL LNELDGIEAL RNVLVLAATN RPDMIDPALM RPGRLDRLLY VGPPNFEARK
     QIVKIQAEKM KFAEDVDLDL IAEKTEGCSG AEVVALCQEA GLIAMHEDLE AKEICQAHFK
     TALLALRKAI TRDMLEYYAS FSESVTSIS