ID   SSRP1_CATRO             Reviewed;         639 AA.
AC   Q39601;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   25-MAY-2022, entry version 94.
DE   RecName: Full=FACT complex subunit SSRP1;
DE   AltName: Full=Facilitates chromatin transcription complex subunit SSRP1;
DE   AltName: Full=Recombination signal sequence recognition protein 1;
GN   Name=SSRP1; Synonyms=HMG;
OS   Catharanthus roseus (Madagascar periwinkle) (Vinca rosea).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Gentianales; Apocynaceae; Rauvolfioideae; Vinceae;
OC   Catharanthinae; Catharanthus.
OX   NCBI_TaxID=4058;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=7665097; DOI=10.1016/0378-1119(95)00266-9;
RA   Hotz M., Lurz G., Schroeder J.;
RT   "A cDNA encoding a plant homologue to animal HMG box proteins involved in
RT   structure-specific recognition of DNA (SSRP family).";
RL   Gene 161:295-296(1995).
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 (Probable). {ECO:0000305}.
CC   -!- SUBUNIT: Component of the FACT complex, a stable heterodimer of SPT16
CC       and SSRP1. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00267}.
CC       Chromosome {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the SSRP1 family. {ECO:0000305}.
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DR   EMBL; Z28410; CAA82251.1; -; mRNA.
DR   PIR; S39242; S39242.
DR   AlphaFoldDB; Q39601; -.
DR   SMR; Q39601; -.
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:UniProtKB-KW.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
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   Transcription; Transcription regulation.
FT   CHAIN           1..639
FT                   /note="FACT complex subunit SSRP1"
FT                   /id="PRO_0000048611"
FT   DNA_BIND        555..623
FT                   /note="HMG box"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00267"
FT   REGION          469..559
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          612..639
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        476..508
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        510..546
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        620..639
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   639 AA;  71466 MW;  FB9A9093B60147FF CRC64;
     MADGHLFNNI TLGGRGGTNP GQLRVHSGGI LWKKQGGAKA VEVDKSDMVG LTWMKVPRSN
     QLGVRIKDGL FYKFTGFRDQ DVASLTSYLQ STCGITPEEK QLSVSGKNWG EVDLNGNMLT
     FLVGSKQAFE VSLADVAQTQ LQGKNDVMLE FMWMILLEQM RKNSLMEISF HVPNSNTQFV
     GDENRPPAQV FRDKIMSMAD VGAGGEDAVV TFEGIAILTP RGRYNVELHL SFLRLQGQAN
     DFKIQYSSVV RLFLLPKSNQ PHTFVVVTLD PPIRKGQTLY PHIVLQFETD YVVDSSLSIS
     EDLLSTKYKD KLEPTYKGLI HEVFTMILRG LSGAKVTRPG KFRSCQDGYA VKSSLKAEDG
     VLYPLEKSFF FLPKPPTLIL HEEIDYVEFE RHAAGGSNMH YFDLLIRLKT EQEHLFRNIQ
     RNEYHNLFDF ISSKGLKIMN LGADKAADAI TAVLQEDDDD AVDPHLERIK NEAGGDESDE
     EDEDFVADID DEGSPTDDSG EGESDGSDSG NEEIPTKKKP KKEASAPKVP LSRKKVGDDD
     NMKKKKQKKK KDPNAPKSIS AFMFFSQTER ENVKKDNPGI AFTDVGKVLG DRCNKCQLRK
     KHLLKQRLVA DKKRYTDEIS NYKNPQPMNV DSGNDSDSA