(data stored in ACNUC14238 zone)

SWISSPROT: POB3_EMENI

ID   POB3_EMENI              Reviewed;         575 AA.
AC   Q5AYE3; C8V1M2;
DT   11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   16-NOV-2011, sequence version 2.
DT   08-MAY-2019, entry version 84.
DE   RecName: Full=FACT complex subunit pob3;
DE   AltName: Full=Facilitates chromatin transcription complex subunit pob3;
GN   Name=pob3; ORFNames=AN6687;
OS   Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL
OS   194 / M139) (Aspergillus nidulans).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=227321;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX   PubMed=16372000; DOI=10.1038/nature04341;
RA   Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R.,
RA   Batzoglou S., Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J.,
RA   Kapitonov V., Jurka J., Scazzocchio C., Farman M.L., Butler J.,
RA   Purcell S., Harris S., Braus G.H., Draht O., Busch S., D'Enfert C.,
RA   Bouchier C., Goldman G.H., Bell-Pedersen D., Griffiths-Jones S.,
RA   Doonan J.H., Yu J., Vienken K., Pain A., Freitag M., Selker E.U.,
RA   Archer D.B., Penalva M.A., Oakley B.R., Momany M., Tanaka T.,
RA   Kumagai T., Asai K., Machida M., Nierman W.C., Denning D.W.,
RA   Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA   Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT   "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT   fumigatus and A. oryzae.";
RL   Nature 438:1105-1115(2005).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX   PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA   Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA   Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P.,
RA   von Dohren H., Doonan J., Driessen A.J., Durek P., Espeso E.,
RA   Fekete E., Flipphi M., Estrada C.G., Geysens S., Goldman G.,
RA   de Groot P.W., Hansen K., Harris S.D., Heinekamp T., Helmstaedt K.,
RA   Henrissat B., Hofmann G., Homan T., Horio T., Horiuchi H., James S.,
RA   Jones M., Karaffa L., Karanyi Z., Kato M., Keller N., Kelly D.E.,
RA   Kiel J.A., Kim J.M., van der Klei I.J., Klis F.M., Kovalchuk A.,
RA   Krasevec N., Kubicek C.P., Liu B., Maccabe A., Meyer V., Mirabito P.,
RA   Miskei M., Mos M., Mullins J., Nelson D.R., Nielsen J., Oakley B.R.,
RA   Osmani S.A., Pakula T., Paszewski A., Paulsen I., Pilsyk S., Pocsi I.,
RA   Punt P.J., Ram A.F., Ren Q., Robellet X., Robson G., Seiboth B.,
RA   van Solingen P., Specht T., Sun J., Taheri-Talesh N., Takeshita N.,
RA   Ussery D., vanKuyk P.A., Visser H., van de Vondervoort P.J.,
RA   de Vries R.P., Walton J., Xiang X., Xiong Y., Zeng A.P., Brandt B.W.,
RA   Cornell M.J., van den Hondel C.A., Visser J., Oliver S.G., Turner G.;
RT   "The 2008 update of the Aspergillus nidulans genome annotation: a
RT   community effort.";
RL   Fungal Genet. Biol. 46:S2-13(2009).
CC   -!- FUNCTION: Component of the FACT complex, a general chromatin
CC       factor that acts to reorganize nucleosomes. The FACT complex is
CC       involved in multiple processes that require DNA as a template such
CC       as mRNA elongation, DNA replication and DNA repair. During
CC       transcription elongation the FACT complex acts as a histone
CC       chaperone that both destabilizes and restores nucleosomal
CC       structure. It facilitates the passage of RNA polymerase II and
CC       transcription by promoting the dissociation of one histone H2A-H2B
CC       dimer from the nucleosome, then subsequently promotes the
CC       reestablishment of the nucleosome following the passage of RNA
CC       polymerase II (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Forms a stable heterodimer with spt16. The spt16-pob3
CC       dimer weakly associates with multiple molecules of nhp6 to form
CC       the FACT complex (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q04636}.
CC       Chromosome {ECO:0000250|UniProtKB:Q04636}. Note=Colocalizes with
CC       RNA polymerase II on chromatin. Recruited to actively transcribed
CC       loci. {ECO:0000250|UniProtKB:Q04636}.
CC   -!- MISCELLANEOUS: In contrast to the orthologous protein in animals
CC       and plants, this protein does not contain a HMG box DNA-binding
CC       domain. This function may instead be provided by the HMG box of
CC       the associated nhp6 protein in the FACT complex of fungi.
CC   -!- SIMILARITY: Belongs to the SSRP1 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=EAA57630.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
DR   EMBL; AACD01000111; EAA57630.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; BN001301; CBF71249.1; -; Genomic_DNA.
DR   RefSeq; XP_664291.1; XM_659199.1.
DR   SMR; Q5AYE3; -.
DR   STRING; 162425.CADANIAP00007472; -.
DR   EnsemblFungi; CBF71249; CBF71249; ANIA_06687.
DR   EnsemblFungi; EAA57630; EAA57630; AN6687.2.
DR   GeneID; 2870474; -.
DR   KEGG; ani:AN6687.2; -.
DR   HOGENOM; HOG000180790; -.
DR   InParanoid; Q5AYE3; -.
DR   KO; K09272; -.
DR   OMA; PRGRYDV; -.
DR   OrthoDB; 915055at2759; -.
DR   Proteomes; UP000000560; Chromosome I.
DR   Proteomes; UP000005890; Unassembled WGS sequence.
DR   GO; GO:0035101; C:FACT complex; IEA:EnsemblFungi.
DR   GO; GO:0000790; C:nuclear chromatin; 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 nucleosome organization; IEA:EnsemblFungi.
DR   GO; GO:0006261; P:DNA-dependent DNA replication; IEA:EnsemblFungi.
DR   GO; GO:0045899; P:positive regulation of RNA polymerase II transcriptional 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;
DR   PRODOM; Q5AYE3.
DR   SWISS-2DPAGE; Q5AYE3.
KW   Chromosome; Complete proteome; DNA damage; DNA repair;
KW   DNA replication; Nucleus; Reference proteome; Transcription;
KW   Transcription regulation.
FT   CHAIN         1    575       FACT complex subunit pob3.
FT                                /FTId=PRO_0000245206.
FT   COMPBIAS    474    560       Asp-rich.
SQ   SEQUENCE   575 AA;  63848 MW;  46E229B0094A204C CRC64;
     MESFDNIYLD LSNQPGKCKL AETGLGWRPS GGGDTFTLDS SNIGAAQWSR AAKGYELKIL
     SRSSGVIQLD GFDQEDFERL SKAFKIWYGI NVESREHALR GWNWGKAEFT KAELAFNVQN
     RPAFEVPYSE ISNTNLAGKN EVAVELSLSV DPNGSKPAGS TKNRGRKAAA GPDELVEMRF
     YIPGTAVKTE NGIKGENADE KNGGEGEENG EEQNAANLFY ELLMEKAEIG DVAGDTFATF
     LDVLHLTPRG RFDIDMYESS FRLRGKTYDY KIQYSSIKKF FLLPKNDDTH TLIVLGLEPP
     LRQGQTRYPF LVMQLKLDEE ISLELNMTEE LLETRYKDKL EPRYEEPIHQ VITKIFRGLS
     GKKVIMPSKD FVSHHGHSGV KCSIKANEGL LYFLDKSLIF VPKPATYIQM ENVAVVTMSR
     VGGAISASRT FDITVSLKAG MGEHQFSNIN REEQQPLEEF FKAKNIRIKN EMSDDTNALI
     AAALDNDDMM SSDEDGGGRP DRGSADEDEE SVDEDFQADS DSDVAEEYDS AHESSGSGSD
     AEMDDASDAG VDEDEDADAD MSEEERPKKK SKTGK
//

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