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POB3_KLULA
ID   POB3_KLULA              Reviewed;         555 AA.
AC   Q6CWD7;
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=KLLA0B04906g;
OS   Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS   NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX   NCBI_TaxID=284590;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
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; CR382122; CAH02145.1; -; Genomic_DNA.
DR   RefSeq; XP_451752.1; XM_451752.1.
DR   AlphaFoldDB; Q6CWD7; -.
DR   SMR; Q6CWD7; -.
DR   STRING; 28985.XP_451752.1; -.
DR   EnsemblFungi; CAH02145; CAH02145; KLLA0_B04906g.
DR   GeneID; 2897209; -.
DR   KEGG; kla:KLLA0_B04906g; -.
DR   eggNOG; KOG0526; Eukaryota.
DR   HOGENOM; CLU_017374_3_0_1; -.
DR   InParanoid; Q6CWD7; -.
DR   OMA; SKQPGKC; -.
DR   Proteomes; UP000000598; Chromosome B.
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: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: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..555
FT                   /note="FACT complex subunit POB3"
FT                   /id="PRO_0000245208"
FT   REGION          194..217
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          476..555
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        194..210
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        476..491
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        492..535
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        537..555
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   555 AA;  63344 MW;  5D469935115D53C5 CRC64;
     MSTDFDRIYY NQSKLGGRFR LAEGGLGWKA SATGGSASTQ NNEPLLLAAD EVSSVQWSRG
     CRGYELKIST KNKGLIQMDG FQQEDFNLLK NDFQRRFNMQ LEHREHSLRG WNWGKLDLAR
     NEMVFSLNGK PTFEIPYTHI NNTNLTAKNE IALEFDTQNE AYNPAGDELV EMRLYVPGTV
     EENEDQDQIM VKDEAEAEDG VKSEVKTEEG SEEPDVQEEK TLAEYFYEEL RSKADIGEIS
     GDAIISFQDL FFTTPRGRYD IDIYKNSIRL RGKTYEYKLQ HRQINRIFSL PKADDIHYLM
     VLSIDPPIRQ GQTSYPFLVL QFQKDEETEV QLNVEDDEFE KLYKDKLKKQ YDAKTHIVLS
     HVLKGLTGRR VIVPGEYKSK YDQCAVSCSY KVNEGHLYPL DNAFLFLTKP TLYIPFQDIA
     AVNISRAGQT STSARTFDLE VVMRANRGTT TFANISKEEQ QLLETFLRSK NLRVKNEDKE
     AEQRLQTAFG SDSDDDDVDI NMGSAGEDEE SVDEDFHASD EDDDVAEEFD SEASASDSEG
     ETSKSERPSK KAKLE
 
 
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