SSRP1_DICDI
ID SSRP1_DICDI Reviewed; 527 AA.
AC Q54G78;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=FACT complex subunit SSRP1;
DE AltName: Full=Facilitates chromatin transcription complex subunit SSRP1;
DE AltName: Full=Structure-specific recognition protein;
GN Name=ssrp1; Synonyms=ssrp; ORFNames=DDB_G0290331;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(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 (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Forms a stable heterodimer with spt16. The spt16-ssrp1 dimer
CC associates with a HMG box DNA-binding domain protein, probably nhp6, to
CC form the FACT complex (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Chromosome {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the SSRP1 family. {ECO:0000305}.
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DR EMBL; AAFI02000162; EAL62292.1; -; Genomic_DNA.
DR RefSeq; XP_635805.1; XM_630713.1.
DR AlphaFoldDB; Q54G78; -.
DR SMR; Q54G78; -.
DR STRING; 44689.DDB0216434; -.
DR PaxDb; Q54G78; -.
DR EnsemblProtists; EAL62292; EAL62292; DDB_G0290331.
DR GeneID; 8627610; -.
DR KEGG; ddi:DDB_G0290331; -.
DR dictyBase; DDB_G0290331; ssrp1.
DR eggNOG; KOG0526; Eukaryota.
DR HOGENOM; CLU_017374_3_0_1; -.
DR InParanoid; Q54G78; -.
DR OMA; SKQPGKC; -.
DR PhylomeDB; Q54G78; -.
DR Reactome; R-DDI-674695; RNA Polymerase II Pre-transcription Events.
DR Reactome; R-DDI-6796648; TP53 Regulates Transcription of DNA Repair Genes.
DR Reactome; R-DDI-6804756; Regulation of TP53 Activity through Phosphorylation.
DR Reactome; R-DDI-75955; RNA Polymerase II Transcription Elongation.
DR PRO; PR:Q54G78; -.
DR Proteomes; UP000002195; Chromosome 5.
DR GO; GO:0035101; C:FACT complex; ISS:dictyBase.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0042393; F:histone binding; IDA:dictyBase.
DR GO; GO:0042802; F:identical protein binding; IPI:dictyBase.
DR GO; GO:0031491; F:nucleosome binding; IBA:GO_Central.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR GO; GO:1902275; P:regulation of chromatin organization; ISS:dictyBase.
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..527
FT /note="FACT complex subunit SSRP1"
FT /id="PRO_0000327488"
FT REGION 179..213
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 479..527
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 179..198
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 199..213
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 483..514
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 527 AA; 59642 MW; 4253B2D7DC62B890 CRC64;
MSSSSNPVSQ FNNISLGGRI SGTRGILKFT TNNITWKSEN GKIETVSSSD IKRANWARVT
PRIFQLILSI KGGATVKFDG FKEQDYEVVR KYLSDQYNVS PLEIIELSSK GCNWGEVKVN
GPMIQFTTDH GKVGFEFPIS EVSQSVIGAN NKNELTLEFH HDKAMDDDDE TMVEMRFFTP
IRPSKEGEEG GKEKKVGEDG EEDEEDEEDA EKEEEISALE QFQQTIMNKS DMVSNVGKSL
VVFSAIQFLT PRGRIDIEMY PTFLKLHGKT HDYKVPYESI SRLFQFFRPD QKHIFFIISL
DPPIRQGQTK YAHLVIQFQA EENIHLELNL TDELQQKFKD QLSPIMNGNA NALICKILKA
LTGKKITIPG NFQSDSGANS IKCSLKANEG YLYPLERCFF FVHKPPTYIK FEDISNIEFA
RYGAPSVRGG SNRTFDLSIN LKNSTSIQFV NIQREEYPSL FNFLKEKKLS ILNPVTTGPA
MIIDDDDSDD DDYEPSESGS ESDEGSASDE SEEESEEDKK AKKKQKK
