POB3_CRYNJ
ID POB3_CRYNJ Reviewed; 588 AA.
AC P0CR74; Q55IM8; Q5KD17;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 54.
DE RecName: Full=FACT complex subunit POB3;
DE AltName: Full=Facilitates chromatin transcription complex subunit POB3;
GN Name=POB3; OrderedLocusNames=CNH02980;
OS Cryptococcus neoformans var. neoformans serotype D (strain JEC21 / ATCC
OS MYA-565) (Filobasidiella neoformans).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Tremellales; Cryptococcaceae; Cryptococcus;
OC Cryptococcus neoformans species complex.
OX NCBI_TaxID=214684;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JEC21 / ATCC MYA-565;
RX PubMed=15653466; DOI=10.1126/science.1103773;
RA Loftus B.J., Fung E., Roncaglia P., Rowley D., Amedeo P., Bruno D.,
RA Vamathevan J., Miranda M., Anderson I.J., Fraser J.A., Allen J.E.,
RA Bosdet I.E., Brent M.R., Chiu R., Doering T.L., Donlin M.J., D'Souza C.A.,
RA Fox D.S., Grinberg V., Fu J., Fukushima M., Haas B.J., Huang J.C.,
RA Janbon G., Jones S.J.M., Koo H.L., Krzywinski M.I., Kwon-Chung K.J.,
RA Lengeler K.B., Maiti R., Marra M.A., Marra R.E., Mathewson C.A.,
RA Mitchell T.G., Pertea M., Riggs F.R., Salzberg S.L., Schein J.E.,
RA Shvartsbeyn A., Shin H., Shumway M., Specht C.A., Suh B.B., Tenney A.,
RA Utterback T.R., Wickes B.L., Wortman J.R., Wye N.H., Kronstad J.W.,
RA Lodge J.K., Heitman J., Davis R.W., Fraser C.M., Hyman R.W.;
RT "The genome of the basidiomycetous yeast and human pathogen Cryptococcus
RT neoformans.";
RL Science 307:1321-1324(2005).
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; AE017348; AAW45161.1; -; Genomic_DNA.
DR RefSeq; XP_572468.1; XM_572468.1.
DR AlphaFoldDB; P0CR74; -.
DR SMR; P0CR74; -.
DR STRING; 5207.AAW45161; -.
DR PaxDb; P0CR74; -.
DR EnsemblFungi; AAW45161; AAW45161; CNH02980.
DR GeneID; 3259295; -.
DR KEGG; cne:CNH02980; -.
DR VEuPathDB; FungiDB:CNH02980; -.
DR eggNOG; KOG0526; Eukaryota.
DR HOGENOM; CLU_017374_3_0_1; -.
DR InParanoid; P0CR74; -.
DR OMA; SKQPGKC; -.
DR OrthoDB; 915055at2759; -.
DR Proteomes; UP000002149; Chromosome 8.
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..588
FT /note="FACT complex subunit POB3"
FT /id="PRO_0000245204"
FT REGION 185..205
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 469..588
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 469..485
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 486..509
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 510..541
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 548..588
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 588 AA; 65466 MW; A1442DBAED4DE4E3 CRC64;
MSTVTFENIF HGDSADLGKL RFNPVGFGWK AYQSEDNNPT TYNGSDIRHA TWFRVARHFQ
LRLGMRNSEK PRISFDGFKR DDLDKIKRTL QEYFNITLET RDTSLKGWNW GEAQVKGSDL
VFQVQGKTAF DVPLSQVANS NIAGKYEVAL EFNPPSNYKF DPKDLNKRPP DEMVEMRFYI
PGKSMKKAGS DAGSGGEETE LDEEGNEVSA ADAFHSLIKE KADIGAVVGD SIVVFEDCLI
LTPRGRFSIE VYADSIRLVG KSTDHRVPFT SIHRIFLLPK LDDLHVQLVL GLDPPIRQGA
TRYPFLVAQW PKDEVVNAEL NLTDEELAQY PDLEKTYEAT TFQVVSRVLK ALTGKKVTPP
GSLRNAQGLN GIRANVKAVQ GELYFLEKGL IFISKQPILI DFSKTDSISF SRVGGGVASA
RTFDMRVVSK TGGADHVFSA INKQEVGPIS SFLQSKNIRL KNEMEEAIVD IDEPFSDDDE
EMESPSEDER PSKAKNDKSK TKPVKKAADD DEDESDDEDF EDESSDGGSP SESDSDDDSG
MASDASDPMM EELRKKTQAK RTKAKETSGS GSEDEKPKKK KAKKDDDE
