ASF1_SCHPO
ID ASF1_SCHPO Reviewed; 262 AA.
AC O74515;
DT 06-DEC-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Histone chaperone cia1;
DE AltName: Full=Anti-silencing function protein 1;
GN Name=cia1; Synonyms=asf1; ORFNames=SPCC663.05c;
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 [GENOMIC DNA], AND FUNCTION.
RX PubMed=11856374; DOI=10.1046/j.1356-9597.2001.00493.x;
RA Umehara T., Chimura T., Ichikawa N., Horikoshi M.;
RT "Polyanionic stretch-deleted histone chaperone cia1/Asf1p is functional
RT both in vivo and in vitro.";
RL Genes Cells 7:59-73(2002).
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).
CC -!- FUNCTION: Histone chaperone that facilitates histone deposition and
CC histone exchange and removal during nucleosome assembly and
CC disassembly. {ECO:0000269|PubMed:11856374}.
CC -!- SUBUNIT: Interacts with histone H3 and histone H4. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16823372}.
CC -!- SIMILARITY: Belongs to the ASF1 family. {ECO:0000305}.
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DR EMBL; AB031397; BAB82475.1; -; Genomic_DNA.
DR EMBL; CU329672; CAA20365.1; -; Genomic_DNA.
DR PIR; T41536; T41536.
DR RefSeq; NP_588267.1; NM_001023257.2.
DR PDB; 2CU9; X-ray; 1.80 A; A=1-161.
DR PDB; 2DZE; X-ray; 1.80 A; A/B=1-161.
DR PDB; 2Z34; X-ray; 2.40 A; A/B=1-161.
DR PDB; 2Z3F; X-ray; 2.70 A; A/B/C/D/E/F/G/H=1-161.
DR PDBsum; 2CU9; -.
DR PDBsum; 2DZE; -.
DR PDBsum; 2Z34; -.
DR PDBsum; 2Z3F; -.
DR AlphaFoldDB; O74515; -.
DR SMR; O74515; -.
DR BioGRID; 276128; 74.
DR STRING; 4896.SPCC663.05c.1; -.
DR iPTMnet; O74515; -.
DR MaxQB; O74515; -.
DR PaxDb; O74515; -.
DR EnsemblFungi; SPCC663.05c.1; SPCC663.05c.1:pep; SPCC663.05c.
DR GeneID; 2539568; -.
DR KEGG; spo:SPCC663.05c; -.
DR PomBase; SPCC663.05c; cia1.
DR VEuPathDB; FungiDB:SPCC663.05c; -.
DR eggNOG; KOG3265; Eukaryota.
DR HOGENOM; CLU_060354_0_2_1; -.
DR InParanoid; O74515; -.
DR OMA; SYDEREF; -.
DR PhylomeDB; O74515; -.
DR EvolutionaryTrace; O74515; -.
DR PRO; PR:O74515; -.
DR Proteomes; UP000002485; Chromosome III.
DR GO; GO:0000785; C:chromatin; NAS:PomBase.
DR GO; GO:0005634; C:nucleus; IDA:PomBase.
DR GO; GO:0042393; F:histone binding; ISO:PomBase.
DR GO; GO:0030527; F:structural constituent of chromatin; IEA:InterPro.
DR GO; GO:0006325; P:chromatin organization; IMP:PomBase.
DR GO; GO:0006335; P:DNA replication-dependent chromatin assembly; IBA:GO_Central.
DR GO; GO:0006336; P:DNA replication-independent chromatin assembly; IBA:GO_Central.
DR GO; GO:0016573; P:histone acetylation; IEA:InterPro.
DR GO; GO:0006334; P:nucleosome assembly; IMP:PomBase.
DR GO; GO:0006337; P:nucleosome disassembly; IEA:InterPro.
DR Gene3D; 2.60.40.1490; -; 1.
DR IDEAL; IID50258; -.
DR InterPro; IPR006818; ASF1-like.
DR InterPro; IPR036747; ASF1-like_sf.
DR InterPro; IPR017282; Hist_deposition_Asf1.
DR PANTHER; PTHR12040; PTHR12040; 1.
DR Pfam; PF04729; ASF1_hist_chap; 1.
DR PIRSF; PIRSF037759; Histone_Asf1; 1.
DR SUPFAM; SSF101546; SSF101546; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Chaperone; Chromatin regulator; Coiled coil; Nucleus;
KW Reference proteome; Transcription; Transcription regulation.
FT CHAIN 1..262
FT /note="Histone chaperone cia1"
FT /id="PRO_0000089743"
FT REGION 157..262
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 173..196
FT /evidence="ECO:0000255"
FT COILED 223..253
FT /evidence="ECO:0000255"
FT COMPBIAS 169..245
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT STRAND 3..13
FT /evidence="ECO:0007829|PDB:2CU9"
FT STRAND 15..17
FT /evidence="ECO:0007829|PDB:2CU9"
FT STRAND 22..30
FT /evidence="ECO:0007829|PDB:2CU9"
FT STRAND 38..47
FT /evidence="ECO:0007829|PDB:2CU9"
FT HELIX 51..53
FT /evidence="ECO:0007829|PDB:2Z3F"
FT STRAND 54..62
FT /evidence="ECO:0007829|PDB:2CU9"
FT STRAND 67..76
FT /evidence="ECO:0007829|PDB:2CU9"
FT HELIX 81..83
FT /evidence="ECO:0007829|PDB:2CU9"
FT STRAND 84..86
FT /evidence="ECO:0007829|PDB:2Z3F"
FT HELIX 87..90
FT /evidence="ECO:0007829|PDB:2CU9"
FT STRAND 91..102
FT /evidence="ECO:0007829|PDB:2CU9"
FT STRAND 105..118
FT /evidence="ECO:0007829|PDB:2CU9"
FT HELIX 123..125
FT /evidence="ECO:0007829|PDB:2CU9"
FT HELIX 128..131
FT /evidence="ECO:0007829|PDB:2CU9"
FT HELIX 138..140
FT /evidence="ECO:0007829|PDB:2CU9"
FT STRAND 141..145
FT /evidence="ECO:0007829|PDB:2CU9"
FT STRAND 151..154
FT /evidence="ECO:0007829|PDB:2CU9"
SQ SEQUENCE 262 AA; 29431 MW; FA4E491BC8B49171 CRC64;
MSIVNILSVN VLNNPAKFSD PYKFEITFEC LEPLKSDLEW KLTYVGSATS QSYDQILDTL
LVGPIPIGIN KFVFEADPPN IDLLPQLSDV LGVTVILLSC AYEDNEFVRV GYYVNNEMEG
LNLQEMDDAE IKKVKVDISK VWRSILAEKP RVTRFNIQWD NPDFDDAPPV QPDADEEEEE
EEADEMEEEF DEEGEGDEEE EEEDDGDGDG EGDGDGEGEN DGKGSEEEEE EEIDIEEEEE
ESALANASAA EEKPEEKPET SQ
