ID   POB3_YARLI              Reviewed;         544 AA.
AC   Q6C7V4;
DT   11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   03-AUG-2022, entry version 100.
DE   RecName: Full=FACT complex subunit POB3;
DE   AltName: Full=Facilitates chromatin transcription complex subunit POB3;
GN   Name=POB3; OrderedLocusNames=YALI0D25058g;
OS   Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Dipodascaceae; Yarrowia.
OX   NCBI_TaxID=284591;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CLIB 122 / E 150;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA   Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA   Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA   Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA   Weissenbach J., Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
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). {ECO:0000250}.
CC   -!- SUBUNIT: Forms a stable heterodimer with SPT16. The SPT16-POB3 dimer
CC       weakly associates with multiple molecules of NHP6 to form the FACT
CC       complex (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Chromosome {ECO:0000250}.
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; CR382130; CAG81462.1; -; Genomic_DNA.
DR   RefSeq; XP_503258.1; XM_503258.1.
DR   AlphaFoldDB; Q6C7V4; -.
DR   SMR; Q6C7V4; -.
DR   STRING; 4952.CAG81462; -.
DR   PRIDE; Q6C7V4; -.
DR   EnsemblFungi; CAG81462; CAG81462; YALI0_D25058g.
DR   GeneID; 2910851; -.
DR   KEGG; yli:YALI0D25058g; -.
DR   VEuPathDB; FungiDB:YALI0_D25058g; -.
DR   HOGENOM; CLU_017374_3_0_1; -.
DR   InParanoid; Q6C7V4; -.
DR   OMA; SKQPGKC; -.
DR   Proteomes; UP000001300; Chromosome D.
DR   GO; GO:0035101; C:FACT complex; IBA:GO_Central.
DR   GO; GO:0031298; C:replication fork protection complex; IEA:EnsemblFungi.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0042393; F:histone binding; IBA:GO_Central.
DR   GO; GO:0031491; F:nucleosome binding; IBA:GO_Central.
DR   GO; GO:0140719; P:constitutive heterochromatin assembly; IEA:EnsemblFungi.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR   GO; GO:0034724; P:DNA replication-independent chromatin organization; IEA:EnsemblFungi.
DR   GO; GO:0006261; P:DNA-templated DNA replication; IEA:EnsemblFungi.
DR   GO; GO:0034728; P:nucleosome organization; IEA:EnsemblFungi.
DR   GO; GO:0045899; P:positive regulation of RNA polymerase II transcription preinitiation complex assembly; IEA:EnsemblFungi.
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   3: Inferred from homology;
KW   Chromosome; DNA damage; DNA repair; DNA replication; Nucleus;
KW   Reference proteome; Transcription; Transcription regulation.
FT   CHAIN           1..544
FT                   /note="FACT complex subunit POB3"
FT                   /id="PRO_0000245212"
FT   REGION          182..219
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          490..544
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        186..202
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        203..219
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        492..544
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   544 AA;  60958 MW;  1D36B7EA0A6663F5 CRC64;
     MSTTEFDGIY LNQSKAHGRL RMVETGLGWK AVQKTSMGGS KETKKDEPFL LGKEELLAAF
     WSRGSRGFEM KIQTKNRGAA NFDGFEQDNL EELKNVMKRN YGISVEQREH SVKGWNWGKT
     DFERSELVFS VANKPAFEIP YAEVANSNLV GKNEVALEFQ QPADGRAGDE LVEMRFYVPG
     VTSVEGDENP KKKQKTEKEG EEGKEGDDDA DADDESEEEV QSTAQIFYDT LKEKADIGAV
     AGTAVVSLSE IYLVIPRGRY DIDMYANFMR LRGKTYDYMV QYKHVQRLIV LPKPDDLHNI
     LVVQLDPPLR QGQTRYPFLV MQFLREAEIK VELNVDDAEF AEKYADKGLK QSYDESAHQV
     VGSIFRGLTG RKLTVPGSFK TVHGHAGVSC SLKASEGHLY PLERNFLFLS KPVFIPFAEI
     QDITLSRVGS SVTTSRTFDM TLKLRNAQGE YQFSNISKEE QEGLEAFIKS KGIRLKNDLA
     EEKALLAATL AEVDDDSDDG GEFRGSADED DESPDEDFHA ESDSEVAEEF DSNAESSSGE
     EDDE