POB3_SCHPO
ID POB3_SCHPO Reviewed; 512 AA.
AC O94529;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=FACT complex subunit pob3 {ECO:0000305};
DE AltName: Full=Facilitates chromatin transcription complex subunit pob3;
GN Name=pob3 {ECO:0000312|PomBase:SPBC609.05};
GN ORFNames=SPBC609.05 {ECO:0000312|PomBase:SPBC609.05};
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 INTERACTION WITH ABO1, 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: Component of the FACT complex, a general chromatin factor
CC that acts to reorganize nucleosomes. The FACT complex is involved in
CC multiple processes that require DNA as a template such as mRNA
CC elongation, DNA replication and DNA repair. During transcription
CC elongation the FACT complex acts as a histone chaperone that both
CC destabilizes and restores nucleosomal structure. It facilitates the
CC passage of RNA polymerase II and transcription by promoting the
CC dissociation of one histone H2A-H2B dimer from the nucleosome, then
CC subsequently promotes the reestablishment of the nucleosome following
CC the passage of RNA polymerase II (By similarity).
CC {ECO:0000250|UniProtKB:Q04636}.
CC -!- SUBUNIT: Forms a stable heterodimer with spt16 (By similarity). The
CC spt16-pob3 dimer weakly associates with multiple molecules of nhp6 to
CC form the FACT complex (By similarity). Interacts with abo1
CC (PubMed:26582768). {ECO:0000250|UniProtKB:Q04636,
CC ECO:0000269|PubMed:26582768}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q04636}.
CC Chromosome {ECO:0000250|UniProtKB:Q04636}. Note=Colocalizes with RNA
CC polymerase II on chromatin. Recruited to actively transcribed loci.
CC {ECO:0000250|UniProtKB:Q04636}.
CC -!- DISRUPTION PHENOTYPE: Sensitive to methyl methanesulfonate (DNA
CC damaging agent). {ECO:0000269|PubMed:26582768}.
CC -!- MISCELLANEOUS: In contrast to the orthologous protein in animals and
CC plants, this protein does not contain a HMG box DNA-binding domain.
CC This function may instead be provided by the HMG box of the associated
CC nhp6 protein in the FACT complex of fungi.
CC -!- SIMILARITY: Belongs to the SSRP1 family. {ECO:0000305}.
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DR EMBL; CU329671; CAA22834.1; -; Genomic_DNA.
DR PIR; T40576; T40576.
DR RefSeq; NP_596315.1; NM_001022237.2.
DR AlphaFoldDB; O94529; -.
DR SMR; O94529; -.
DR BioGRID; 277603; 235.
DR STRING; 4896.SPBC609.05.1; -.
DR MaxQB; O94529; -.
DR PaxDb; O94529; -.
DR EnsemblFungi; SPBC609.05.1; SPBC609.05.1:pep; SPBC609.05.
DR GeneID; 2541088; -.
DR KEGG; spo:SPBC609.05; -.
DR PomBase; SPBC609.05; pob3.
DR VEuPathDB; FungiDB:SPBC609.05; -.
DR eggNOG; KOG0526; Eukaryota.
DR HOGENOM; CLU_017374_3_0_1; -.
DR InParanoid; O94529; -.
DR OMA; SKQPGKC; -.
DR PhylomeDB; O94529; -.
DR Reactome; R-SPO-674695; RNA Polymerase II Pre-transcription Events.
DR Reactome; R-SPO-6796648; TP53 Regulates Transcription of DNA Repair Genes.
DR Reactome; R-SPO-6804756; Regulation of TP53 Activity through Phosphorylation.
DR Reactome; R-SPO-75955; RNA Polymerase II Transcription Elongation.
DR PRO; PR:O94529; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0000791; C:euchromatin; EXP:PomBase.
DR GO; GO:0035101; C:FACT complex; IDA:PomBase.
DR GO; GO:0043596; C:nuclear replication fork; ISS:PomBase.
DR GO; GO:0005634; C:nucleus; IDA:PomBase.
DR GO; GO:0003677; F:DNA binding; ISM:PomBase.
DR GO; GO:0042393; F:histone binding; IBA:GO_Central.
DR GO; GO:0140713; F:histone chaperone activity; EXP:PomBase.
DR GO; GO:0031491; F:nucleosome binding; IBA:GO_Central.
DR GO; GO:0140673; P:co-transcriptional chromatin reassembly; TAS:PomBase.
DR GO; GO:0140719; P:constitutive heterochromatin assembly; IMP:PomBase.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR GO; GO:0006334; P:nucleosome assembly; ISO:PomBase.
DR GO; GO:0034728; P:nucleosome organization; IMP:PomBase.
DR Gene3D; 2.30.29.220; -; 1.
DR Gene3D; 2.30.29.30; -; 2.
DR InterPro; IPR013719; DUF1747.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR035417; POB3_N.
DR InterPro; IPR000969; SSrcognition.
DR InterPro; IPR024954; SSRP1_dom.
DR InterPro; IPR038167; SSRP1_sf.
DR Pfam; PF17292; POB3_N; 1.
DR Pfam; PF08512; Rtt106; 1.
DR Pfam; PF03531; SSrecog; 1.
DR PRINTS; PR00887; SSRCOGNITION.
DR SMART; SM01287; Rtt106; 1.
PE 1: Evidence at protein level;
KW Chromosome; DNA damage; DNA repair; DNA replication; Nucleus;
KW Reference proteome; Transcription; Transcription regulation.
FT CHAIN 1..512
FT /note="FACT complex subunit pob3"
FT /id="PRO_0000245210"
FT REGION 460..512
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 460..502
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 512 AA; 57457 MW; A9D3A487DAB2A5BC CRC64;
MAAKTVQYDN IYLNLSEKPG KLRIAPSGLG WKSPSLAEPF TLPISEIRRF CWSRFARGYE
LKIILKSKDP VSLDGFSQED LDDLINVIKQ NFDMGIEQKE FSIKGWNWGE ANFLGSELVF
DVNSRPAFEI PISAVTNTNL SGKNEVALEF STTDDKQIPS AQVDELVEMR LYVPGTTAKE
DAADGEEVEQ NAANLFYESL KERADIGQAA GDAIVSFSEI LLLTPRGRYD IDMYETCMRL
RGKTYDYKVE YSSINSLFLL PKPDEQHVVF VIGLEPPLRQ GQTRYPFLVT QFVRDEDMEV
DLNIEETVLK EKYADKVKAS YDQPAFEVVS QIFRGLTGRK VTTPAEFLSH EGHAAVKCSY
KANEGQLYCL DKSFLFIPKP TLLMNTSDIT RVTLSRVGMS VSAARTFDLT FTLRSGTSYQ
FSNINRVEQS ALVAFLESKQ IKIHNDLADE TQQTLLTSAL DDEDEEGDEE MEEALSEDED
FQAESESDVA EEYDENAESS DEEGASGAEG SE
