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Database: UniProt
Entry: G3Q0Y4_GASAC
LinkDB: G3Q0Y4_GASAC
Original site: G3Q0Y4_GASAC 
ID   G3Q0Y4_GASAC            Unreviewed;       709 AA.
AC   G3Q0Y4;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   27-MAR-2024, entry version 67.
DE   RecName: Full=FACT complex subunit SSRP1 {ECO:0000256|ARBA:ARBA00016104, ECO:0000256|RuleBase:RU364013};
OS   Gasterosteus aculeatus (Three-spined stickleback).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Perciformes; Cottioidei; Gasterosteales; Gasterosteidae;
OC   Gasterosteus.
OX   NCBI_TaxID=69293 {ECO:0000313|Ensembl:ENSGACP00000023531.2, ECO:0000313|Proteomes:UP000007635};
RN   [1] {ECO:0000313|Ensembl:ENSGACP00000023531.2, ECO:0000313|Proteomes:UP000007635}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Lindblad-Toh K., Mauceli E., Grabherr M., Chang J.L., Lander E.S.;
RL   Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSGACP00000023531.2}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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|RuleBase:RU364013}.
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleolus
CC       {ECO:0000256|ARBA:ARBA00004604}. Nucleus
CC       {ECO:0000256|RuleBase:RU364013}. Chromosome
CC       {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   AlphaFoldDB; G3Q0Y4; -.
DR   STRING; 69293.ENSGACP00000023531; -.
DR   Ensembl; ENSGACT00000023577.2; ENSGACP00000023531.2; ENSGACG00000017801.2.
DR   eggNOG; KOG0526; Eukaryota.
DR   GeneTree; ENSGT00940000157117; -.
DR   InParanoid; G3Q0Y4; -.
DR   OMA; KQPGKCK; -.
DR   TreeFam; TF315228; -.
DR   Proteomes; UP000007635; Unassembled WGS sequence.
DR   Bgee; ENSGACG00000017801; Expressed in embryo and 12 other cell types or tissues.
DR   GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR   GO; GO:0051726; P:regulation of cell cycle; IEA:Ensembl.
DR   CDD; cd21994; HMG-box_SSRP1-like; 1.
DR   CDD; cd13230; PH1_SSRP1-like; 1.
DR   CDD; cd13231; PH2_SSRP1-like; 1.
DR   Gene3D; 2.30.29.150; -; 1.
DR   Gene3D; 1.10.30.10; High mobility group box domain; 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; IPR009071; HMG_box_dom.
DR   InterPro; IPR036910; HMG_box_dom_sf.
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; IPR048985; SSRP1_C.
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; PF00505; HMG_box; 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   Pfam; PF21092; SSRP1_C; 1.
DR   PRINTS; PR00887; SSRCOGNITION.
DR   SMART; SM00398; HMG; 1.
DR   SMART; SM01287; Rtt106; 1.
DR   SUPFAM; SSF47095; HMG-box; 1.
DR   SUPFAM; SSF50729; PH domain-like; 1.
DR   PROSITE; PS50118; HMG_BOX_2; 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   DNA-binding {ECO:0000256|PROSITE-ProRule:PRU00267};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|PROSITE-
KW   ProRule:PRU00267}; Reference proteome {ECO:0000313|Proteomes:UP000007635};
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          545..613
FT                   /note="HMG box"
FT                   /evidence="ECO:0000259|PROSITE:PS50118"
FT   DNA_BIND        545..613
FT                   /note="HMG box"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00267"
FT   REGION          459..551
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          602..709
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        470..495
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        520..535
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        633..692
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        693..709
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   709 AA;  80369 MW;  36E0A11EE277B9B9 CRC64;
     MGDTLEFSDI YQEVKGSWND GRLRFGKQSV VYKSSKTGKV DSIPAGDLNL AQWRRVCLGH
     GIKLGTGSGH IYKYDGFRDT DFEKISEFFK ANYKVELAEK DMCVKGWNWG TAKFSGPLLS
     FEVNESTAFE VPLANVSQCA TGKNEVTLEF HQNDDTEVSL MEVRFYVPPS QTDERQDPVE
     AFAENVLSKA DVIQATGDAV CIFKELQCLT PRGRYDIRIY PTFLHLHGKT FDYKIPYTTV
     LRLFLLPHKD QRQMFFVISL DPPIKQGQTR YHFLILLFSK EEDLTLTLNM SEDDVERRFE
     GKLSKNMSGS LYEMVSRVMK ALVNRKITVP GNFQGHSGAQ CITCSYKASS GLLYPLERGF
     IYVHKPPVHL RFEEISCVNF ARGTTTTRSF DFEVETKQGN QFTFSSIERE EYGKLFDFVN
     AKKLNIKNRG FKEGMKGKID EYSDSDEDQH DAYLERMKAE GKIREEGNDS EESDGESDES
     FNPGEEDDDI AEEYDSNASA SDSSDDGDDD DDSSKKKAPK VKVVKEKKER KPRREQKKQK
     DKGGPKRPMS AYMLWLNSSR ERIKSENPGI SITEISKKAG EMWRQLGKDD KEEWDIKAAE
     AKRQYDKAKQ EYKESGGGEA AAPAATSSSK NKKSGGVKEE KKRKSAGGDK EKERAAANDS
     FKSREFIETS EESSSDTDRK SKSKRKKESD DDEMEEEAVS TPASSEEES
//
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