ID   POB3_CANGA              Reviewed;         543 AA.
AC   Q6FKI2;
DT   11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 101.
DE   RecName: Full=FACT complex subunit POB3;
DE   AltName: Full=Facilitates chromatin transcription complex subunit POB3;
GN   Name=POB3; OrderedLocusNames=CAGL0L11352g;
OS   Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS   Y-65) (Yeast) (Torulopsis glabrata).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC   Nakaseomyces/Candida clade.
OX   NCBI_TaxID=284593;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
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|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; CR380958; CAG62236.1; -; Genomic_DNA.
DR   RefSeq; XP_449262.1; XM_449262.1.
DR   AlphaFoldDB; Q6FKI2; -.
DR   SMR; Q6FKI2; -.
DR   STRING; 5478.XP_449262.1; -.
DR   EnsemblFungi; CAG62236; CAG62236; CAGL0L11352g.
DR   GeneID; 2890961; -.
DR   KEGG; cgr:CAGL0L11352g; -.
DR   CGD; CAL0136134; CAGL0L11352g.
DR   VEuPathDB; FungiDB:CAGL0L11352g; -.
DR   eggNOG; KOG0526; Eukaryota.
DR   HOGENOM; CLU_017374_3_0_1; -.
DR   InParanoid; Q6FKI2; -.
DR   OMA; SKQPGKC; -.
DR   Proteomes; UP000002428; Chromosome L.
DR   GO; GO:0035101; C:FACT complex; IEA:EnsemblFungi.
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; IEA:EnsemblFungi.
DR   GO; GO:0031491; F:nucleosome binding; IEA:EnsemblFungi.
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..543
FT                   /note="FACT complex subunit POB3"
FT                   /id="PRO_0000245203"
FT   REGION          183..204
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          472..543
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        185..204
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        484..531
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   543 AA;  61452 MW;  6237DCC80879927D CRC64;
     MSTDFDRIFM NQSKFGGRFR IADSGLGWKV STSGGSASAQ NKAPFLLPAT ELSTVQWSRG
     CRGFELKINT KNQGVIQLEG FSEDDFNIIK GDFHRRFSIQ VEHKEHSLRG WNWGQTDLAR
     NEMVFALNGK PVFEIPYARI NNTNLTAKNE VAVEFNIQDD TYQPAGDEMV EMRFYLPGSV
     VVDEDQPAPK KEGEEEGEEA AETETKSLAE AFYEELKNKA DIGEIAGDAI VSFQDVFFTT
     PRGRYDIDIY ENSIRLRGKT YEYKLQHNQI QRIVSLPKAD DINHLVVLAM DPPLRQGQTT
     YPFLVLQFQK DEETEVQLNL SDQEYEEKYK DKLKKQYDSK THIVISHVLK GLTGRRVVVP
     GEYKSKYEQC AVSCSYKANE GYLYPLDNAF FFLTKPTLYI PFNDVSSVVI SRAGQTSTSS
     RTFDLEVILR SNRGSTIFGN ISKEEQQLLE NFLKSKNLRV KNEEKDAQVR LQSALGSDSD
     DEDVNMGSAG EDDESVDEDF HVSSGDDDDE VAEEFDSEAA SEGEDEDEDM DGSDRPTKKP
     KTE