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POB3_DEBHA
ID   POB3_DEBHA              Reviewed;         540 AA.
AC   Q6BS60;
DT   11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   25-MAY-2022, entry version 96.
DE   RecName: Full=FACT complex subunit POB3;
DE   AltName: Full=Facilitates chromatin transcription complex subunit POB3;
GN   Name=POB3; OrderedLocusNames=DEHA2D11374g;
OS   Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990
OS   / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX   NCBI_TaxID=284592;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC 2968;
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; CR382136; CAG87121.1; -; Genomic_DNA.
DR   RefSeq; XP_458960.1; XM_458960.1.
DR   AlphaFoldDB; Q6BS60; -.
DR   SMR; Q6BS60; -.
DR   STRING; 4959.XP_458960.1; -.
DR   EnsemblFungi; CAG87121; CAG87121; DEHA2D11374g.
DR   GeneID; 2901144; -.
DR   KEGG; dha:DEHA2D11374g; -.
DR   VEuPathDB; FungiDB:DEHA2D11374g; -.
DR   eggNOG; KOG0526; Eukaryota.
DR   HOGENOM; CLU_017374_3_0_1; -.
DR   InParanoid; Q6BS60; -.
DR   OMA; SKQPGKC; -.
DR   OrthoDB; 915055at2759; -.
DR   Proteomes; UP000000599; Chromosome D.
DR   GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
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..540
FT                   /note="FACT complex subunit POB3"
FT                   /id="PRO_0000245205"
FT   REGION          475..540
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        477..520
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   540 AA;  61053 MW;  2067346B66EA3DAD CRC64;
     MVNTDFEKIH LNQSKNYGRM RIADSGLGWK ASVTNNASAS NNAPFLLPSE EILASQWSRG
     SRGYELRVQT KNKGVVMLDG FDVEDFANLK QELQRNFQVN LEHKEHSLRG WNWGKTDLAR
     NELVFQVNNK PDFEIPYSEI SNSNLTGKNE VAVEFNLDGA NSKAGDEMVE MRFYIPGTLE
     NETTPAVKNE ENGEVKEEET EEISAATVFY EQLKDKADIG QVAGEAIVSF SDVLFLTPRG
     RYDIDMYPTS LRLRGKTYDY KIQYNQIERI FSLPKPDEAH HLLVIQIDPP LRQGQTKYPF
     LVMQFAKEEE IELDLNVSEE EYNDKYKDRL KKSYDSQTHL VMSHCFKGLT ERRLVVPGSF
     QSRFLQPGIS CSLKASEGYL YPLDRCFLFV TKPTVYIPFS EISSITMSRT GAGGVSTSRT
     FDMDITLRGS NQSHNFGSIE REEQETIENY CLQKGLRIKN EEKLAKAMLA KAMNETADDD
     DDADVDMGSA GDDDDESADD DFNSGSDSDV AEEFDSDASV SDAEMSDSNQ EPPQKKPKNE
 
 
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