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Database: UniProt
Entry: R9P428_PSEHS
LinkDB: R9P428_PSEHS
Original site: R9P428_PSEHS 
ID   R9P428_PSEHS            Unreviewed;       537 AA.
AC   R9P428;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   24-JAN-2024, entry version 36.
DE   RecName: Full=FACT complex subunit POB3 {ECO:0000256|RuleBase:RU364013};
GN   ORFNames=PHSY_003586 {ECO:0000313|EMBL:GAC96007.1};
OS   Pseudozyma hubeiensis (strain SY62) (Yeast).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC   Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Pseudozyma.
OX   NCBI_TaxID=1305764 {ECO:0000313|EMBL:GAC96007.1, ECO:0000313|Proteomes:UP000014071};
RN   [1] {ECO:0000313|Proteomes:UP000014071}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SY62 {ECO:0000313|Proteomes:UP000014071};
RX   PubMed=23814110; DOI=10.1128/genomea.00409-13;
RA   Konishi M., Hatada Y., Horiuchi J.;
RT   "Draft genome sequence of the basidiomycetous yeast-like fungus Pseudozyma
RT   hubeiensis SY62, which produces an abundant amount of the biosurfactant
RT   mannosylerythritol lipids.";
RL   Genome Announc. 1:E0040913-E0040913(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. {ECO:0000256|ARBA:ARBA00025370,
CC       ECO:0000256|RuleBase:RU364013}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|RuleBase:RU364013}.
CC       Chromosome {ECO:0000256|RuleBase:RU364013}.
CC   -!- SIMILARITY: Belongs to the SSRP1 family.
CC       {ECO:0000256|ARBA:ARBA00010060, ECO:0000256|RuleBase:RU364013}.
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DR   EMBL; DF238800; GAC96007.1; -; Genomic_DNA.
DR   RefSeq; XP_012189594.1; XM_012334204.1.
DR   AlphaFoldDB; R9P428; -.
DR   STRING; 1305764.R9P428; -.
DR   GeneID; 24108873; -.
DR   eggNOG; KOG0526; Eukaryota.
DR   HOGENOM; CLU_017374_3_0_1; -.
DR   OrthoDB; 5488575at2759; -.
DR   Proteomes; UP000014071; Unassembled WGS sequence.
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   CDD; cd13230; PH1_SSRP1-like; 1.
DR   CDD; cd13231; PH2_SSRP1-like; 1.
DR   Gene3D; 2.30.29.150; -; 1.
DR   Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 2.
DR   Gene3D; 2.30.29.220; Structure-specific recognition protein (SSRP1); 1.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR013719; RTT106/SPT16-like_middle_dom.
DR   InterPro; IPR048993; SSRP1-like_PH1.
DR   InterPro; IPR000969; SSRP1/POB3.
DR   InterPro; IPR035417; SSRP1/POB3_N.
DR   InterPro; IPR024954; SSRP1_DD.
DR   InterPro; IPR038167; SSRP1_sf.
DR   PANTHER; PTHR45849; FACT COMPLEX SUBUNIT SSRP1; 1.
DR   PANTHER; PTHR45849:SF1; FACT COMPLEX SUBUNIT SSRP1; 1.
DR   Pfam; PF21103; PH1_SSRP1-like; 1.
DR   Pfam; PF17292; POB3_N; 1.
DR   Pfam; PF08512; Rttp106-like_middle; 1.
DR   Pfam; PF03531; SSrecog; 1.
DR   PRINTS; PR00887; SSRCOGNITION.
DR   SMART; SM01287; Rtt106; 1.
DR   SUPFAM; SSF50729; PH domain-like; 1.
PE   3: Inferred from homology;
KW   Chromosome {ECO:0000256|ARBA:ARBA00022454, ECO:0000256|RuleBase:RU364013};
KW   DNA damage {ECO:0000256|ARBA:ARBA00022763, ECO:0000256|RuleBase:RU364013};
KW   DNA repair {ECO:0000256|ARBA:ARBA00023204, ECO:0000256|RuleBase:RU364013};
KW   DNA replication {ECO:0000256|ARBA:ARBA00022705,
KW   ECO:0000256|RuleBase:RU364013};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|RuleBase:RU364013};
KW   Reference proteome {ECO:0000313|Proteomes:UP000014071};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163,
KW   ECO:0000256|RuleBase:RU364013};
KW   Transcription regulation {ECO:0000256|ARBA:ARBA00023015,
KW   ECO:0000256|RuleBase:RU364013}.
FT   DOMAIN          363..456
FT                   /note="Histone chaperone RTT106/FACT complex subunit SPT16-
FT                   like middle"
FT                   /evidence="ECO:0000259|SMART:SM01287"
FT   REGION          141..167
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          180..202
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          474..537
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        141..158
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        474..502
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   537 AA;  59382 MW;  FE0F4FC3C3496239 CRC64;
     MSQGGLGWKP SVGEGSTITI PADQMASFQW IRVARNYQLA ISLSKDRDAP SSAQPNPRRT
     NFDGFVRDDF DRLSSHLRQY FNKPLETKEV STRGWNWGQA KISNHDVQFL VRDKLAFELP
     LSHLANSNIA KTEVSMEFLN PEQQQPGANT GSSDANGSKS RRNKGDQLVE MRLYVPGQAT
     KDDASDAGSA AADGEDNNEE TAAEAFHEAL KSKADIGQVA GDSIVVFKEV LVLTPRGRYD
     IDVFNSFIRL RGKTYDYKIL YSSMNKLFLL PKADEIHVML VIGLDPPIRQ GQTRYPYLVL
     QFPREEEMDA ELNLDEQTIQ EKYDGKLKKR YEEPTFRIVT NIFKVLSGQK VATPTDFESS
     SGQTSIKCNV KAADGNLYPL EKSLLWVSKQ PVYVPYSEIH QAILSRVGGA VASSKTFDLR
     VATKSGTDHT FQSISREELD RLKAWLADRK VRIKNEMAEE TGGLAAAAAA GLLSDDDDEE
     MGAAGGADED EDSEEDADFA ADSDTDGGSP SEASSDEDGD AGYEDEGEER PKKKRKD
//
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