ID   SSRP1_VICFA             Reviewed;         642 AA.
AC   O04235;
DT   11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   02-JUN-2021, entry version 95.
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;
OS   Vicia faba (Broad bean) (Faba vulgaris).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; Hologalegina; IRL clade; Fabeae; Vicia.
OX   NCBI_TaxID=3906;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Minor; TISSUE=Cotyledon;
RA   Wohlfarth T.;
RL   Submitted (MAY-1996) 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 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; X97906; CAA66480.1; -; mRNA.
DR   PIR; T12113; T12113.
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..642
FT                   /note="FACT complex subunit SSRP1"
FT                   /id="PRO_0000245198"
FT   DNA_BIND        558..626
FT                   /note="HMG box"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00267"
FT   REGION          459..566
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          595..642
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        459..476
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        513..550
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        596..623
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        628..642
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   642 AA;  71358 MW;  4FD8C2A076BF3ACB CRC64;
     MTDGHLFNNI TLGXRGGTNP GQIKIYSGGI LWKRQGGGKT IDVDKTDIMG VTWMKVPKTN
     QLGVQIKDGL LYKFTGFRDQ DVVSLTNFFQ NTFGITVEEK QLSVTGRNWG EVDLNGNMLA
     FMVGSKQAFE VSLADVSQTN LQGKNDVILE FHVDDTTGAN EKDSLMEMSF HIPSSNTQFV
     GDENRPSAQV FRDKIMSMAD VGVGGEDAVV TFDGIAILTP RGRYSVELHL SFLRLQGQAN
     DFKIQYSSVV RLFLLPKSNQ PHTFVIISLD PPIRKGQTLY PHIVMQFETD TVVDSELAIS
     EDLYNSKYKD KLELSYKGLI HEVFTTVLRG LSGGKVTKPG NFRSCQDGYA VKSSLKAEDG
     ILYPLEKSFF FLPKPPTLIL HEEIDYVEFE RHAAGGSNMH YFDLLIRLKS EQEHLFRNIQ
     RNEYHNLYGF ISSKGLKIMN IADAQQAVGG VAKVLENDDD DAVDPHLERI RNEAGGDESD
     EEDSDFVIDK DDGGSPTDDS GADVSDASQS GGETEKPAKK EPKKDLSSKA SSSKKKSKDA
     DVDGVKKKQK KKKDPNAPKR ALSGFMFFSQ MERENLKKTN PGISFTDVGR VLGEKWKNLS
     AEEKEPYEAK AQADKKRYKD EISGYKNPQP MNVDSGNESD SA