POB3_ASHGO
ID POB3_ASHGO Reviewed; 542 AA.
AC Q756X6;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=FACT complex subunit POB3;
DE AltName: Full=Facilitates chromatin transcription complex subunit POB3;
GN Name=POB3; OrderedLocusNames=AER138C;
OS Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS (Yeast) (Eremothecium gossypii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX NCBI_TaxID=284811;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=15001715; DOI=10.1126/science.1095781;
RA Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA Gaffney T.D., Philippsen P.;
RT "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT cerevisiae genome.";
RL Science 304:304-307(2004).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=23749448; DOI=10.1534/g3.112.002881;
RA Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT loci, numerous translocations, lack of transposons, and distinct gene
RT duplications.";
RL G3 (Bethesda) 3:1225-1239(2013).
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; AE016818; AAS52821.1; -; Genomic_DNA.
DR RefSeq; NP_984997.1; NM_210351.1.
DR AlphaFoldDB; Q756X6; -.
DR SMR; Q756X6; -.
DR STRING; 33169.AAS52821; -.
DR EnsemblFungi; AAS52821; AAS52821; AGOS_AER138C.
DR GeneID; 4621203; -.
DR KEGG; ago:AGOS_AER138C; -.
DR eggNOG; KOG0526; Eukaryota.
DR HOGENOM; CLU_017374_3_0_1; -.
DR InParanoid; Q756X6; -.
DR OMA; SKQPGKC; -.
DR Proteomes; UP000000591; Chromosome V.
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..542
FT /note="FACT complex subunit POB3"
FT /id="PRO_0000245199"
FT REGION 458..542
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 483..520
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 528..542
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 542 AA; 61420 MW; B7090D9652E30B6A CRC64;
MSTDFDRIYY NQSKVSGRFR LGEGGLGWKA SATGGSAAMQ NNEPILLTAD ELASVQWSRG
CRGYELKINT KNKGVVQLDG FSQEDFTLLK NDLQRRFNVQ LEHKDHSLRG WNWGTTDLTR
NELIFSLNGK PTFEIPYSHI SNTNLTSKNE VALEFDLQKD GYNPAGDELV EMRLYVPGVV
TQEDRHSSPA EDADVDMEKD NKEEKSIAEA FYEELRAKAE IGEVSGDAII SFQDVFFTTP
RGRYDIDIYK NSIRLRGKTY EYKLQHRQIQ RIFSLPKADD IHHLMVLSIE PPLRQGQTTY
PYLVLQFQKD EETEVQLNVE DDEFERLYKD KLKKQYDAKT HVVLSHVLKG LTDTRVVVPG
EYKSKHEQCA VSCSFKANEG HLYPLDNAFM FLTKPTLYIP FQDVSSVNIS RAGQATTSSR
TFDLEVVLRS NRGSTTFANI SKEEQQILES FLKSKNVRVK NEEKETQQRL QTALGSDSED
EDVNMGSAAE DDESVDEDFQ AESEDDDVAE EFDSDAGVSE SETEAADGAD TEDRPSKKAK
LA
