ID   ATD22_SCHPO             Reviewed;        1201 AA.
AC   Q9C0W2; O13617;
DT   13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 118.
DE   RecName: Full=ATPase with bromodomain protein abo2 {ECO:0000312|PomBase:SPBP22H7.05c};
DE            EC=3.6.1.- {ECO:0000250|UniProtKB:O14114};
DE   AltName: Full=ATPase family AAA domain-containing protein abo2 {ECO:0000305};
DE            Short=AAA-ATPase {ECO:0000305};
GN   Name=abo2 {ECO:0000312|PomBase:SPBP22H7.05c};
GN   ORFNames=pi026, SPBP22H7.05c {ECO:0000312|PomBase:SPBP22H7.05c};
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=10620777;
RX   DOI=10.1002/(sici)1097-0061(20000115)16:1<71::aid-yea505>3.0.co;2-5;
RA   Machida M., Yamazaki S., Kunihiro S., Tanaka T., Kushida N., Jinno K.,
RA   Haikawa Y., Yamazaki J., Yamamoto S., Sekine M., Oguchi A., Nagai Y.,
RA   Sakai M., Aoki K., Ogura K., Kudoh Y., Kikuchi H., Zhang M.Q., Yanagida M.;
RT   "A 38 kb segment containing the cdc2 gene from the left arm of fission
RT   yeast chromosome II: sequence analysis and characterization of the genomic
RT   DNA and cDNAs encoded on the segment.";
RL   Yeast 16:71-80(2000).
RN   [2]
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   [3]
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   [4]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=26582768; DOI=10.15252/embr.201540476;
RA   Gal C., Murton H.E., Subramanian L., Whale A.J., Moore K.M.,
RA   Paszkiewicz K., Codlin S., Baehler J., Creamer K.M., Partridge J.F.,
RA   Allshire R.C., Kent N.A., Whitehall S.K.;
RT   "Abo1, a conserved bromodomain AAA-ATPase, maintains global nucleosome
RT   occupancy and organisation.";
RL   EMBO Rep. 17:79-93(2016).
CC   -!- FUNCTION: Probable ATPase which may play a role in nucleosome
CC       organization. {ECO:0000269|PubMed:26582768}.
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;
CC         Evidence={ECO:0000250|UniProtKB:O14114};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13066;
CC         Evidence={ECO:0000250|UniProtKB:O14114};
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16823372}.
CC   -!- DISRUPTION PHENOTYPE: Double knockout with abo1 results in lethality.
CC       {ECO:0000269|PubMed:26582768}.
CC   -!- SIMILARITY: Belongs to the AAA ATPase family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAA21405.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AB004535; BAA21405.1; ALT_INIT; Genomic_DNA.
DR   EMBL; CU329671; CAC37373.1; -; Genomic_DNA.
DR   RefSeq; NP_595602.1; NM_001021497.2.
DR   AlphaFoldDB; Q9C0W2; -.
DR   SMR; Q9C0W2; -.
DR   BioGRID; 277800; 34.
DR   STRING; 4896.SPBP22H7.05c.1; -.
DR   iPTMnet; Q9C0W2; -.
DR   PaxDb; Q9C0W2; -.
DR   PRIDE; Q9C0W2; -.
DR   EnsemblFungi; SPBP22H7.05c.1; SPBP22H7.05c.1:pep; SPBP22H7.05c.
DR   GeneID; 2541287; -.
DR   KEGG; spo:SPBP22H7.05c; -.
DR   PomBase; SPBP22H7.05c; -.
DR   VEuPathDB; FungiDB:SPBP22H7.05c; -.
DR   eggNOG; KOG0732; Eukaryota.
DR   HOGENOM; CLU_000536_6_3_1; -.
DR   InParanoid; Q9C0W2; -.
DR   OMA; RSRYKKF; -.
DR   PhylomeDB; Q9C0W2; -.
DR   PRO; PR:Q9C0W2; -.
DR   Proteomes; UP000002485; Chromosome II.
DR   GO; GO:0000785; C:chromatin; ISM:PomBase.
DR   GO; GO:0005634; C:nucleus; HDA:PomBase.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; ISM:PomBase.
DR   GO; GO:0003682; F:chromatin binding; IBA:GO_Central.
DR   GO; GO:0042393; F:histone binding; IBA:GO_Central.
DR   GO; GO:0006338; P:chromatin remodeling; ISM:PomBase.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:PomBase.
DR   Gene3D; 3.40.50.300; -; 2.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR041569; AAA_lid_3.
DR   InterPro; IPR045199; ATAD2-like.
DR   InterPro; IPR003959; ATPase_AAA_core.
DR   InterPro; IPR003960; ATPase_AAA_CS.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR23069; PTHR23069; 1.
DR   Pfam; PF00004; AAA; 2.
DR   Pfam; PF17862; AAA_lid_3; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF52540; SSF52540; 2.
DR   PROSITE; PS00674; AAA; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Bromodomain; Hydrolase; Nucleotide-binding; Nucleus;
KW   Reference proteome.
FT   CHAIN           1..1201
FT                   /note="ATPase with bromodomain protein abo2"
FT                   /id="PRO_0000310283"
FT   DOMAIN          969..1000
FT                   /note="Bromo"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00035"
FT   REGION          1..223
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          305..324
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        25..42
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        67..101
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        127..141
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        149..167
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        209..223
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         413..420
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   1201 AA;  137385 MW;  FEB8D759048697B4 CRC64;
     MRRRARSIRF SSDDNEDNEE DDDYYSNAHS EKSEDHSNHI KVSHFDPSSY KQKLVSVRET
     QRNRKFSSLQ KHLNTETPSF SVSIENPSKP SAAFNDASLG KKSTEHQIDG IRNGSSNLQM
     EGNDKELDTD NNEDESTTFK DEEDDLISPK SYLTSSKTFS YPKAPTESTN GDYLDEDYVD
     GQSDPESSNA SDSDFADSPD DLTKVRSPIP SRRGRRKRKM RGPILPVKKN LRVKKAMSPL
     RAERNSPDFR RKLRSRDNRP NYHLFDYYNE IASSPNPSTT KITYNPPKLP MKDFATLPIG
     YQSTCDSDET SELSSTSSEQ TSDVEGLNAY NNLGASSDIE NAPSSQLHFG HIDEKTIRST
     DPFANRENLD FNSIGGLEDI ILQLKEMVML PLLYPEVFLH LHITPPRGVL FHGPPGTGKT
     LMARVLAANC STKNQKISFF LRKGSDCLSK WVGEAERQLR LLFEEARRVQ PSIIFFDEID
     GLAPIRSSKQ EQTHSSIVST LLALMDGLDT RGQVVVIGAT NRPNDLDPAL RRPGRFDREF
     YFPLPNKQAR MKILEINSLH FSPKIPESYL LHLAESTSGY GGADLKALCT EAALNAVRRT
     FPQIYTSSDK FLIDLNEISV SICDFVVASE KIAVSTRRSD VKPNIPITDS HKILFKKSIE
     VITSKIRRLL KLDVYLPTVE SLQKLPAEEL MRQKEINSLK TTMSFRPRLL ITDIYGYGCT
     YLSKVLFSML DGIHVQSLDI SELLMDTTTS PRSLLTKIFS EARKNAPSII FINNVEKWPS
     LFSHSFLSMF LLLLDSISPL EPVMLLGFAN TNQEKLSSTV RSWFPSHRSE YHDLSFPDYS
     SRYSFFHYLL KRISFLPIHQ KSAEAASVDI LPKVLPVSKT SDLTDKVNRR QRKNDKKIKN
     KIQVKLSSIL EMLRSRYKKF KKPIIDLNDI YIDESNERVV KGKSKDNFEY FLSGNTVTRK
     KDNACFKMMN FEEIERRLWS GRYCTPKEFL RDIKMIKQDA ILSGDVNLKH KAKEMFAHAE
     LNVDELIDAK LLYDCCQVSK REKAYKQLKQ KKLNNAKDAH EMQESKNEET FVRNDVAQED
     NFIELSSNEV RNVSNDEHKH TLFHGQSLTH NNLIAVTPPS RTGVEHKEEN KKYDNVNIQK
     TLAKCAEEFA EHTNFNKVEL LDFVYSKLSS TIWENREEHD LLKIVRDVRQ TFFRSLEDMG
     V