ID   POB3_USTMA              Reviewed;         558 AA.
AC   Q4P647; A0A0D1DXS7;
DT   11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2005, sequence version 1.
DT   03-AUG-2022, entry version 95.
DE   RecName: Full=FACT complex subunit POB3;
DE   AltName: Full=Facilitates chromatin transcription complex subunit POB3;
GN   Name=POB3; ORFNames=UMAG_04416;
OS   Ustilago maydis (strain 521 / FGSC 9021) (Corn smut fungus).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC   Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Ustilago.
OX   NCBI_TaxID=237631;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=521 / FGSC 9021;
RX   PubMed=17080091; DOI=10.1038/nature05248;
RA   Kaemper J., Kahmann R., Boelker M., Ma L.-J., Brefort T., Saville B.J.,
RA   Banuett F., Kronstad J.W., Gold S.E., Mueller O., Perlin M.H.,
RA   Woesten H.A.B., de Vries R., Ruiz-Herrera J., Reynaga-Pena C.G.,
RA   Snetselaar K., McCann M., Perez-Martin J., Feldbruegge M., Basse C.W.,
RA   Steinberg G., Ibeas J.I., Holloman W., Guzman P., Farman M.L.,
RA   Stajich J.E., Sentandreu R., Gonzalez-Prieto J.M., Kennell J.C., Molina L.,
RA   Schirawski J., Mendoza-Mendoza A., Greilinger D., Muench K., Roessel N.,
RA   Scherer M., Vranes M., Ladendorf O., Vincon V., Fuchs U., Sandrock B.,
RA   Meng S., Ho E.C.H., Cahill M.J., Boyce K.J., Klose J., Klosterman S.J.,
RA   Deelstra H.J., Ortiz-Castellanos L., Li W., Sanchez-Alonso P.,
RA   Schreier P.H., Haeuser-Hahn I., Vaupel M., Koopmann E., Friedrich G.,
RA   Voss H., Schlueter T., Margolis J., Platt D., Swimmer C., Gnirke A.,
RA   Chen F., Vysotskaia V., Mannhaupt G., Gueldener U., Muensterkoetter M.,
RA   Haase D., Oesterheld M., Mewes H.-W., Mauceli E.W., DeCaprio D., Wade C.M.,
RA   Butler J., Young S.K., Jaffe D.B., Calvo S.E., Nusbaum C., Galagan J.E.,
RA   Birren B.W.;
RT   "Insights from the genome of the biotrophic fungal plant pathogen Ustilago
RT   maydis.";
RL   Nature 444:97-101(2006).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=521 / FGSC 9021;
RA   Gueldener U., Muensterkoetter M., Walter M.C., Mannhaupt G., Kahmann R.;
RL   Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
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|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   -!- 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; CM003153; KIS67315.1; -; Genomic_DNA.
DR   RefSeq; XP_011391110.1; XM_011392808.1.
DR   AlphaFoldDB; Q4P647; -.
DR   SMR; Q4P647; -.
DR   STRING; 5270.UM04416P0; -.
DR   EnsemblFungi; KIS67315; KIS67315; UMAG_04416.
DR   GeneID; 23564609; -.
DR   KEGG; uma:UMAG_04416; -.
DR   VEuPathDB; FungiDB:UMAG_04416; -.
DR   eggNOG; KOG0526; Eukaryota.
DR   HOGENOM; CLU_017374_3_0_1; -.
DR   InParanoid; Q4P647; -.
DR   OMA; SKQPGKC; -.
DR   OrthoDB; 915055at2759; -.
DR   Proteomes; UP000000561; Chromosome 14.
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..558
FT                   /note="FACT complex subunit POB3"
FT                   /id="PRO_0000245211"
FT   REGION          162..186
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          495..558
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        162..180
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        495..523
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   558 AA;  61933 MW;  B3FDA31A7D086EDB CRC64;
     MSSTTQWENI YHGLDTTPGK LRMSQGGLGW KPSVGEGSTI TIPADQMASF QWIRVARNYQ
     LAIYLNKDRD APSSAQTNPR RTNFDGFVRD DFDRLSSHIR QYFNKPLEAK EVSTRGWNWG
     QAKISNHDVQ FLVRDKLAFE LPLSHLANSN IAKTEVSMEF LNPEQQQPGA NTGTSDVNGT
     KSRRSKGDQL VEMRLYVPGQ AIKDDGSDAA SAQDDDVNNE ETAAEAFHEA LKSKADIGQV
     AGDSIVVFKE VLVLTPRGRY DIDVFSTFIR LRGKTYDYKI LYSSMNKLFL LPKADEIHVM
     LVIGLDPPIR QGQTRYPYLV LQFPREEEMD AELNLDEQTI QEKYDGKLKK RYEEPTFRIV
     TNIFKVLSGQ KVATPTDFES SSGQTSIKCN VKAADGNLYP LEKSLLWVSK QPVYVPYSEI
     HQAILSRVGG AVASSKTFDL RVATKSGTEH TFQSISREEL DRLKAWLADR KVRIKNEMAE
     ETGGLAAAAA AGLLSDDDDE EMGAAGGADE DEDSEEDADF AADSDSDGGS PSEASSDEGE
     GGGYDDEGDE RPKKKRKD