SSRP1_DROPS
ID SSRP1_DROPS Reviewed; 727 AA.
AC Q293F6;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 20-JAN-2009, sequence version 2.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=FACT complex subunit Ssrp1;
DE AltName: Full=Facilitates chromatin transcription complex subunit Ssrp1;
DE AltName: Full=Recombination signal sequence recognition protein;
DE AltName: Full=Single-strand recognition protein;
GN Name=Ssrp; ORFNames=GA18454;
OS Drosophila pseudoobscura pseudoobscura (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=46245;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MV2-25 / Tucson 14011-0121.94;
RX PubMed=15632085; DOI=10.1101/gr.3059305;
RA Richards S., Liu Y., Bettencourt B.R., Hradecky P., Letovsky S.,
RA Nielsen R., Thornton K., Hubisz M.J., Chen R., Meisel R.P., Couronne O.,
RA Hua S., Smith M.A., Zhang P., Liu J., Bussemaker H.J., van Batenburg M.F.,
RA Howells S.L., Scherer S.E., Sodergren E., Matthews B.B., Crosby M.A.,
RA Schroeder A.J., Ortiz-Barrientos D., Rives C.M., Metzker M.L., Muzny D.M.,
RA Scott G., Steffen D., Wheeler D.A., Worley K.C., Havlak P., Durbin K.J.,
RA Egan A., Gill R., Hume J., Morgan M.B., Miner G., Hamilton C., Huang Y.,
RA Waldron L., Verduzco D., Clerc-Blankenburg K.P., Dubchak I., Noor M.A.F.,
RA Anderson W., White K.P., Clark A.G., Schaeffer S.W., Gelbart W.M.,
RA Weinstock G.M., Gibbs R.A.;
RT "Comparative genome sequencing of Drosophila pseudoobscura: chromosomal,
RT gene, and cis-element evolution.";
RL Genome Res. 15:1-18(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. Binds specifically to single-stranded
CC DNA and RNA with highest affinity for nucleotides G and U. The FACT
CC complex is required for expression of Hox genes (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Component of the FACT complex, a stable heterodimer of
CC dre4/spt16 and Ssrp. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q05344}.
CC Chromosome {ECO:0000250|UniProtKB:Q05344}. Nucleus, nucleolus
CC {ECO:0000250|UniProtKB:Q05344}. Note=Colocalizes with RNA polymerase II
CC on chromatin. Recruited to actively transcribed loci.
CC {ECO:0000250|UniProtKB:Q05344}.
CC -!- SIMILARITY: Belongs to the SSRP1 family. {ECO:0000305}.
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DR EMBL; CM000071; EAL24655.2; -; Genomic_DNA.
DR RefSeq; XP_001357531.2; XM_001357495.3.
DR AlphaFoldDB; Q293F6; -.
DR SMR; Q293F6; -.
DR STRING; 7237.FBpp0277246; -.
DR EnsemblMetazoa; FBtr0278808; FBpp0277246; FBgn0078456.
DR GeneID; 4803391; -.
DR KEGG; dpo:Dpse_GA18454; -.
DR eggNOG; KOG0526; Eukaryota.
DR HOGENOM; CLU_017374_2_0_1; -.
DR InParanoid; Q293F6; -.
DR OMA; SKQPGKC; -.
DR Proteomes; UP000001819; Chromosome 3.
DR Bgee; FBgn0078456; Expressed in female reproductive system and 3 other tissues.
DR GO; GO:0005829; C:cytosol; IEA:EnsemblMetazoa.
DR GO; GO:0035101; C:FACT complex; IEA:EnsemblMetazoa.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0005705; C:polytene chromosome interband; IEA:EnsemblMetazoa.
DR GO; GO:0005703; C:polytene chromosome puff; IEA:EnsemblMetazoa.
DR GO; GO:0070087; F:chromo shadow domain binding; IEA:EnsemblMetazoa.
DR GO; GO:0031492; F:nucleosomal DNA binding; IEA:EnsemblMetazoa.
DR GO; GO:0046982; F:protein heterodimerization activity; IEA:EnsemblMetazoa.
DR GO; GO:0043621; F:protein self-association; IEA:EnsemblMetazoa.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR GO; GO:0001933; P:negative regulation of protein phosphorylation; IEA:EnsemblMetazoa.
DR GO; GO:0030707; P:ovarian follicle cell development; IEA:EnsemblMetazoa.
DR GO; GO:0030838; P:positive regulation of actin filament polymerization; IEA:EnsemblMetazoa.
DR GO; GO:1902275; P:regulation of chromatin organization; IEA:EnsemblMetazoa.
DR GO; GO:0051101; P:regulation of DNA binding; IEA:EnsemblMetazoa.
DR Gene3D; 1.10.30.10; -; 1.
DR Gene3D; 2.30.29.220; -; 1.
DR Gene3D; 2.30.29.30; -; 2.
DR InterPro; IPR013719; DUF1747.
DR InterPro; IPR009071; HMG_box_dom.
DR InterPro; IPR036910; HMG_box_dom_sf.
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; PF00505; HMG_box; 1.
DR Pfam; PF17292; POB3_N; 1.
DR Pfam; PF08512; Rtt106; 1.
DR Pfam; PF03531; SSrecog; 1.
DR PRINTS; PR00887; SSRCOGNITION.
DR SMART; SM00398; HMG; 1.
DR SMART; SM01287; Rtt106; 1.
DR SUPFAM; SSF47095; SSF47095; 1.
DR PROSITE; PS50118; HMG_BOX_2; 1.
PE 3: Inferred from homology;
KW Chromosome; DNA damage; DNA repair; DNA replication; DNA-binding; Nucleus;
KW Reference proteome; RNA-binding; Transcription; Transcription regulation.
FT CHAIN 1..727
FT /note="FACT complex subunit Ssrp1"
FT /id="PRO_0000245194"
FT DNA_BIND 556..622
FT /note="HMG box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00267"
FT REGION 458..565
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 596..727
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 464..483
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 491..509
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 533..557
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 596..618
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 634..649
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 663..707
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 709..727
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 727 AA; 81769 MW; F27099A2456BB7A9 CRC64;
MTDSLEYNDI NAEVRGVLSS GRLKLTDQNI IFKNNKTGKV EQISVDDIDL INSQKFVGTW
GLRVFTKSGA LHRFTGFRDS EHEKLGKFIK DAYSQEMVEK EMCVKGWNWG TARFMGSVLS
FDKDSKTIFE VPLSHVSQCV TGKNEVTLEY HQNDDAPVGL LEMRFHIPAV ESADDDPVEK
FHQNVMSKAS VISASGESIA IFREIQILTP RGRYDIKIFS TFFQLHGKTF DYKIPMDSVL
RLFMLPHKDS RQMFFVLSLD PPIKQGQTRY HYLVLLFAPD EETTIELPFS EAELRDKYEG
KLEKELSGPV YEVMGKVMKV LIGRKITGPG NFIGHSGTAA VGCSFKAAAG YLYPLERGFI
YIHKPPLHIR FEEISSVNFA RSGGSTRSFD FEVTLKNGTV HIFSSIEKEE YAKLFDFITQ
KKLHVSNMGK DKSGYKDVDF GDSDNENEPD AYLARLKAEA REKEEEDDDG DDSDEESTDE
DFKPNENESD VAEEYDSNVE DDSDDDSDAS GGGGDGGTDG STKKKHKEKK NEKKEKTHKE
KEKIKKPTKK KDTGKPKRGT SAFMLWLNDT RESIKRENPG IKVTEIAKKG GEMWKELKDK
SKWEEAANKD KIRYQEEMRN YKSGAGGGSE DEKGGTSKAT KKRKSEPSPS KKANTSGSGF
KSKEYISDDE STSDDQEKVK EIPKKKNKST AEDKDKNSKK SESEGGDSDD ASNASEDDDE
EEDEGSD
