POB3_ASPOR
ID POB3_ASPOR Reviewed; 576 AA.
AC Q2USL9;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=FACT complex subunit pob3;
DE AltName: Full=Facilitates chromatin transcription complex subunit pob3;
GN Name=pob3; ORFNames=AO090005000376;
OS Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=510516;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 42149 / RIB 40;
RX PubMed=16372010; DOI=10.1038/nature04300;
RA Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K.,
RA Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H.,
RA Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.,
RA Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D.,
RA Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A.,
RA Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y.,
RA Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H.,
RA Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T.,
RA Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O.,
RA Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y.,
RA Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N.,
RA Kikuchi H.;
RT "Genome sequencing and analysis of Aspergillus oryzae.";
RL Nature 438:1157-1161(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|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; AP007151; BAE55446.1; -; Genomic_DNA.
DR RefSeq; XP_001817448.1; XM_001817396.2.
DR AlphaFoldDB; Q2USL9; -.
DR SMR; Q2USL9; -.
DR STRING; 510516.Q2USL9; -.
DR PRIDE; Q2USL9; -.
DR EnsemblFungi; BAE55446; BAE55446; AO090005000376.
DR VEuPathDB; FungiDB:AO090005000376; -.
DR HOGENOM; CLU_017374_3_0_1; -.
DR OMA; SKQPGKC; -.
DR Proteomes; UP000006564; Chromosome 1.
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..576
FT /note="FACT complex subunit pob3"
FT /id="PRO_0000245201"
FT REGION 153..172
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 193..213
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 490..576
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 492..506
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 507..524
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 546..562
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 576 AA; 64203 MW; 893B39AEF354D997 CRC64;
MESFDNIYLD LSKQPGKCKL AESGLGWKPS GEGETFTLDS SNVGAAQWSR AAKGFELKIL
SRSSGVIQLD GFDQEDFERL SKAFKIWYGI NVESREHALR GWNWGKAEFT KAELSFNVQN
RPAFEVPYSE ISNTNLAGKN EVAVELALNT DGADANAQPA GSTKNRGRKA ASGPDELVEM
RFYIPGTVMK TEKGIKEENG KEENGEEEEE GEEQNAANLF YEMLMEKAEI GDVAGDTFAT
FLDVLHLTPR GRFDIDMYES SFRLRGKTYD YKIQYSSIKK FFLLPKNDDT HTLIVLGLDP
PLRQGQTRYP FLVMQLKLDE EISLELNMTD ELMETRYKDK LEPRYEEPIH QVVTKIFRGL
SGKKVIMPSK DFVSHHGHSG VKCSIKANEG LLYFLDKSLI FVPKPATYIQ VENIAIITMS
RVGGAVSASR TFDITVSLKA GMGEHQFSNI NREEQQPLEE FFKAKNIRFK NEMSDDAGAL
LAAALDNDVM GSSDDEGVRA DRGSADEDEE SIDEDFQAES ESDVAEEYDS AHESSGSGSD
AEMNDASDGG GDDDDDDEDV DMSEEERPKK KSKVGK
