ID   SSRP1_CIOIN             Reviewed;         704 AA.
AC   Q4H2R2;
DT   11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   30-AUG-2005, sequence version 1.
DT   25-MAY-2022, entry version 86.
DE   RecName: Full=FACT complex subunit SSRP1;
DE   AltName: Full=Facilitates chromatin transcription complex subunit SSRP1;
DE   AltName: Full=Structure-specific recognition protein 1;
GN   Name=SSRP1; ORFNames=ciad093d18;
OS   Ciona intestinalis (Transparent sea squirt) (Ascidia intestinalis).
OC   Eukaryota; Metazoa; Chordata; Tunicata; Ascidiacea; Phlebobranchia;
OC   Cionidae; Ciona.
OX   NCBI_TaxID=7719;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Satou Y.;
RT   "Expressed genes in Ciona intestinalis.";
RL   Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
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 double-stranded
CC       DNA (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Component of the FACT complex, a stable heterodimer of SSRP1
CC       and SUPT16H. May also be a component of a CK2-SPT16-SSRP1 complex,
CC       composed of SSRP1, SUPT16H, CSNK2A1, CSNK2A2 and CSNK2B (By
CC       similarity). {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; AB210710; BAE06715.1; -; mRNA.
DR   RefSeq; NP_001071827.1; NM_001078359.1.
DR   AlphaFoldDB; Q4H2R2; -.
DR   SMR; Q4H2R2; -.
DR   STRING; 7719.NP_001071827.1; -.
DR   GeneID; 778769; -.
DR   KEGG; cin:778769; -.
DR   CTD; 6749; -.
DR   eggNOG; KOG0526; Eukaryota.
DR   InParanoid; Q4H2R2; -.
DR   OrthoDB; 915055at2759; -.
DR   Proteomes; UP000008144; Unassembled WGS sequence.
DR   GO; GO:0035101; C:FACT complex; IBA:GO_Central.
DR   GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0042393; F:histone binding; IBA:GO_Central.
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; IBA:GO_Central.
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   2: Evidence at transcript level;
KW   Chromosome; DNA damage; DNA repair; DNA replication; DNA-binding; Nucleus;
KW   Reference proteome; Transcription; Transcription regulation.
FT   CHAIN           1..704
FT                   /note="FACT complex subunit SSRP1"
FT                   /id="PRO_0000245192"
FT   DNA_BIND        554..622
FT                   /note="HMG box"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00267"
FT   REGION          460..562
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          618..704
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        468..493
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        519..547
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        643..679
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   704 AA;  81570 MW;  6B97EE6B55FCF397 CRC64;
     MTENGQFLDY KNVFQENRGA MHDGRLQLLK EKIVFKNNKT GKIDSIQQND LHSALWRRVA
     RDFELKFQMN SGQVFRFDGF KEMEFERLKD FVKNYYKIDL EHQELSGKGW NWGTTDFEGN
     EMMFQVGQKL SFEIPLNNVS QCTQNKDEVT MEFHQNDDSE LSLMEMRFFI PPSQDEMIDK
     VKDFHDNVMA KADVLQVKGT AICVFQDLQC LTPRGRYDIR MYPKFIQLHG KTFDYKITYT
     SILRLFLLPH KDQRQIFFVV SLDPPLKQGM TRYHFLILLF YKEDDLAVEL SLPDDEIEER
     FGGKLQKDMS GPMYEVVSRV MKHLVQRKIT VPGSFKGLNG VQSITCTYKA SSGFLFPLER
     GFMYVHKPPV HIRFDEIAYV NFARGTTKIN KSFDFEIETR SKNNFVFSNI ERDQYASLYD
     FVHNKQLKIK NIGKDGADFD LMVDSDEDAD VHDPYMERMK QEAAEREKQV DDDDDDESED
     DDFQPETNVA EVEEEYNSDV GSASSGASDE EEEDGEEEVE EKPKKRKKEK VMKERRQKET
     PGKVKRKKKD PNAPKRPQSA YFLWLNENRG RFKAENKGIS VTELTKLAGK EWKKIDPDEK
     QKFERMYQKS KVKFDAAMKE YKSQGGGRTS SSPAKKMKMK SPKPSKASSS MVSPSKFKSK
     EFITESDSLS SSDSDAEVKS KNSPPADEES ASESEAASEE EESD