ATD2_SCHPO
ID ATD2_SCHPO Reviewed; 1190 AA.
AC O14114;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=ATPase histone chaperone abo1 {ECO:0000312|PomBase:SPAC31G5.19};
DE EC=3.6.1.- {ECO:0000269|PubMed:31848341};
DE AltName: Full=ATPase family AAA domain-containing protein abo1 {ECO:0000305};
DE Short=AAA-ATPase {ECO:0000305};
GN Name=abo1 {ECO:0000303|PubMed:26582768};
GN ORFNames=SPAC31G5.19 {ECO:0000312|PomBase:SPAC31G5.19};
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, INTERACTION WITH SPT16; POB3 AND HISTONE H3, SUBCELLULAR
RP LOCATION, 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).
RN [4]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=32269268; DOI=10.1038/s41598-020-63209-y;
RA Dong W., Oya E., Zahedi Y., Prasad P., Svensson J.P., Lennartsson A.,
RA Ekwall K., Durand-Dubief M.;
RT "Abo1 is required for the H3K9me2 to H3K9me3 transition in
RT heterochromatin.";
RL Sci. Rep. 10:6055-6055(2020).
RN [5]
RP FUNCTION.
RX PubMed=33658433; DOI=10.14348/molcells.2021.2242;
RA Kang Y., Cho C., Lee K.S., Song J.J., Lee J.Y.;
RT "Single-Molecule Imaging Reveals the Mechanism Underlying Histone Loading
RT of Schizosaccharomyces pombe AAA+ ATPase Abo1.";
RL Mol. Cells 44:79-87(2021).
RN [6] {ECO:0007744|PDB:6JPQ, ECO:0007744|PDB:6JPU, ECO:0007744|PDB:6JQ0}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.54 ANGSTROMS) OF MUTANT GLN-372 IN
RP COMPLEX WITH ATP, FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, INTERACTION WITH
RP HISTONES H3-H4, AND MUTAGENESIS OF TRP-345; GLU-372; GLU-385 AND GLU-900.
RX PubMed=31848341; DOI=10.1038/s41467-019-13743-9;
RA Cho C., Jang J., Kang Y., Watanabe H., Uchihashi T., Kim S.J., Kato K.,
RA Lee J.Y., Song J.J.;
RT "Structural basis of nucleosome assembly by the Abo1 AAA+ ATPase histone
RT chaperone.";
RL Nat. Commun. 10:5764-5764(2019).
CC -!- FUNCTION: ATPase histone chaperone which facilitates loading of histone
CC H3-H4 onto DNA in an ATP-dependent manner (PubMed:31848341,
CC PubMed:33658433). Plays a genome-wide role in nucleosome organization
CC and establishment of chromatin (PubMed:26582768, PubMed:31848341). Also
CC plays a role in heterochromatin assembly by stabilizing recruitment of
CC the histone methyltransferase clr4 to methylated histone H3, to promote
CC the transition from H3K9me2 to H3K9me3 (PubMed:32269268).
CC {ECO:0000269|PubMed:26582768, ECO:0000269|PubMed:31848341,
CC ECO:0000269|PubMed:32269268, ECO:0000269|PubMed:33658433}.
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:0000269|PubMed:31848341};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13066;
CC Evidence={ECO:0000269|PubMed:31848341};
CC -!- SUBUNIT: Homohexamer (PubMed:31848341). Interacts with the FACT complex
CC subunits spt16 and pob3 (PubMed:26582768). Interacts with histone H3-H4
CC (via N-terminus) (PubMed:31848341, PubMed:26582768).
CC {ECO:0000269|PubMed:26582768, ECO:0000269|PubMed:31848341}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16823372,
CC ECO:0000269|PubMed:26582768}. Chromosome {ECO:0000269|PubMed:26582768}.
CC -!- DISRUPTION PHENOTYPE: Abnormal nucleosome distribution
CC (PubMed:26582768). Decreases level of clr4 at the subtelomeric and
CC pericentromeric regions and at DSR (determinant of selective removal)
CC islands containing meiotic genes; decreases di- and tri-methylation of
CC histone H3 'Lys-9' at these regions (PubMed:32269268). Abnormal
CC heterochromatin formation at the pericentromeric outer and inner repeat
CC regions, the subtelomeric region, and the silenced mating-type locus
CC (PubMed:26582768, PubMed:32269268). Impairs centromere function; leads
CC to abnormal mitotic and meiotic chromosome segregation and sensitivity
CC to thiabendazole (spindle poison) (PubMed:26582768). Decreases
CC silencing of subtelomeric regions, including Tf2-type retrotransposons
CC (PubMed:26582768, PubMed:32269268). Decreases histone H3 and H2A
CC protein levels (PubMed:26582768). Abnormal transcription resulting in
CC increased levels of cryptic transcripts (PubMed:26582768). Increases
CC transcript levels of genes involved in the stress response
CC (PubMed:26582768). Sensitive to methyl methanesulfonate (DNA damaging
CC agent); double-knockout with nhp6, or triple-knockout with hht2 and
CC hhf2 exacerbates the effect (PubMed:26582768). Sensitive to heat and
CC cold; double-knockout with nhp6, clr3, clr4, or swi6, or triple-
CC knockout with hht2 and hhf2 exacerbates the effect (PubMed:26582768,
CC PubMed:32269268). Decreases cell viability and leads to slow cell
CC population growth with elongated cells; double-knockout with clr4 or
CC swi6 exacerbates the effect (PubMed:26582768, PubMed:32269268). Double
CC knockout with abo2 results in lethality (PubMed:26582768).
CC {ECO:0000269|PubMed:26582768, ECO:0000269|PubMed:32269268}.
CC -!- SIMILARITY: Belongs to the AAA ATPase family. {ECO:0000305}.
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DR EMBL; CU329670; CAB11703.1; -; Genomic_DNA.
DR PIR; T38636; T38636.
DR RefSeq; NP_594020.1; NM_001019446.2.
DR PDB; 6JPQ; EM; 4.44 A; A/B/C/D/E/F=1-1190.
DR PDB; 6JPU; EM; 4.27 A; A/B/C/D/E/F=1-1190.
DR PDB; 6JQ0; EM; 3.54 A; A/B/C/D/E/F=1-1190.
DR PDBsum; 6JPQ; -.
DR PDBsum; 6JPU; -.
DR PDBsum; 6JQ0; -.
DR AlphaFoldDB; O14114; -.
DR SMR; O14114; -.
DR BioGRID; 279517; 18.
DR STRING; 4896.SPAC31G5.19.1; -.
DR iPTMnet; O14114; -.
DR MaxQB; O14114; -.
DR PaxDb; O14114; -.
DR PRIDE; O14114; -.
DR EnsemblFungi; SPAC31G5.19.1; SPAC31G5.19.1:pep; SPAC31G5.19.
DR PomBase; SPAC31G5.19; -.
DR VEuPathDB; FungiDB:SPAC31G5.19; -.
DR eggNOG; KOG0732; Eukaryota.
DR HOGENOM; CLU_000536_6_3_1; -.
DR InParanoid; O14114; -.
DR OMA; KRAQEMY; -.
DR PhylomeDB; O14114; -.
DR PRO; PR:O14114; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0000785; C:chromatin; IDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0005524; F:ATP binding; ISM:PomBase.
DR GO; GO:0016887; F:ATP hydrolysis activity; IDA:UniProtKB.
DR GO; GO:0140665; F:ATP-dependent H3-H4 histone complex chaperone activity; IDA:UniProtKB.
DR GO; GO:0003682; F:chromatin binding; IBA:GO_Central.
DR GO; GO:0042393; F:histone binding; IDA:PomBase.
DR GO; GO:0006334; P:nucleosome assembly; IDA:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR Gene3D; 1.20.920.10; -; 1.
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; IPR036427; Bromodomain-like_sf.
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; 2.
DR SUPFAM; SSF47370; SSF47370; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR PROSITE; PS00674; AAA; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Bromodomain; Chaperone; Chromosome; Hydrolase;
KW Nucleotide-binding; Nucleus; Reference proteome.
FT CHAIN 1..1190
FT /note="ATPase histone chaperone abo1"
FT /id="PRO_0000310281"
FT DOMAIN 865..907
FT /note="Bromo"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00035"
FT REGION 1..185
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 204..253
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 12..27
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 62..83
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 84..102
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 128..150
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 171..185
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 309..314
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /evidence="ECO:0000269|PubMed:31848341,
FT ECO:0007744|PDB:6JQ0"
FT MUTAGEN 345
FT /note="W->A: Severely impairs histone deposition activity."
FT /evidence="ECO:0000269|PubMed:31848341"
FT MUTAGEN 372
FT /note="E->Q: Severely decreases ATPase activity and impairs
FT histone deposition activity."
FT /evidence="ECO:0000269|PubMed:31848341"
FT MUTAGEN 385
FT /note="E->A: Severely impairs histone deposition activity."
FT /evidence="ECO:0000269|PubMed:31848341"
FT MUTAGEN 900
FT /note="E->A: Severely impairs histone deposition activity."
FT /evidence="ECO:0000269|PubMed:31848341"
SQ SEQUENCE 1190 AA; 135351 MW; 44F5FE817DB188DC CRC64;
MKEEASEHGG SADETQELSP VSDSSDEMPN NAKRRRRSQS MIANKRIHQA FQEDEGDEDW
EEEEHKPKAK RRYNTRSNES FSEGDDEPFE VSESSALEDE LSDSEDSFIR SVRSKPKYKP
GTRRSTRLRN RRSQDEEESE EEHRPILRER TSRINYSVPL AFPPVDEMDG DPSSQVNQSR
SRKTHSELAI TKLLRQQVSS FMPYIDSSGS ESESDNTRIK KSSAKTIKAL TDPANSGGPP
DFGRIREKSD LADSDPLGVD SSLSFESVGG LDNYINQLKE MVMLPLLYPE IFQRFNMQPP
RGVLFHGPPG TGKTLMARAL AAACSSENKK VSFYMRKGAD CLSKWVGEAE RQLRLLFEEA
KSTQPSIIFF DEIDGLAPVR SSKQEQIHAS IVSTLLALMD GMESRGQVII IGATNRPDAV
DPALRRPGRF DREFYFPLPD RDARKKIIEI HTRNWDPPVP EWLCSMLAEK SKGYGGADLR
ALCTEAALNS IKRTYPQLYR STKRLQIDPK TIKVKVKDFV MSMKRMIPSS ERSSISPSKP
LSPELKPLLN EAFQDIEKTL QKLMPVASKL NPLEEVMYDD PKENDFEYQQ RLETFETLRI
YKPRFLICGR KGLGQTALGP AILQQYEGVH VQSFDMSTLL QDSTQSIETS IIHLFLEVRR
HTPSIIYIPD IDNWLNVLPL TAITTFSSML ERLDFSDQIL FLALSSSPLS ELHPQLREWF
SSKQSVYSLQ YPTRDSIIAF FQPILELIKA SPTELPGGIP RKRRVLPELP LAPDPPPFTS
QKITLKQTKQ ADMRLLNKLK IKLNALLGSL RARYRKFKKP LIDFNDIYCV DPETGHSYRS
REECHYEFVD DVVKQIGSDQ KFSMMSLEEI EKRTWDNCYC TPKQFVHDIK LILRDALQLE
DSETIKRAQE MYANVLLGVE DMEDDQFSQR CERMALREAE RRKLRHGKLQ KHLDETKADM
QFTSEKPSVD ESITEVDDAI KDGPPVLAET LTNSLMEDVG PENVDMDIED NEIFTNQSTM
SVPSMLVENE ESPKPDEYID QKDKVQSPLL NGKSPVGVPS EAALRVSTDV STNISSNGRA
DIPVDTLITS PADVPNNAPT DAHNITSADG HIENIEQEVV FPDLVFDEDR LTPLKQLLID
STTGFTVDQL LHLHSFLYQI IWNTKSEWNR NSVVDECERA VKEFMINALQ
