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Database: UniProt
Entry: A0A067BD31_SAPPC
LinkDB: A0A067BD31_SAPPC
Original site: A0A067BD31_SAPPC 
ID   A0A067BD31_SAPPC        Unreviewed;       235 AA.
AC   A0A067BD31;
DT   03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT   03-SEP-2014, sequence version 1.
DT   24-JAN-2024, entry version 34.
DE   RecName: Full=FACT complex subunit SSRP1 {ECO:0000256|RuleBase:RU364013};
GN   ORFNames=SPRG_18217 {ECO:0000313|EMBL:KDO16249.1};
OS   Saprolegnia parasitica (strain CBS 223.65).
OC   Eukaryota; Sar; Stramenopiles; Oomycota; Saprolegniales; Saprolegniaceae;
OC   Saprolegnia.
OX   NCBI_TaxID=695850 {ECO:0000313|EMBL:KDO16249.1, ECO:0000313|Proteomes:UP000030745};
RN   [1] {ECO:0000313|EMBL:KDO16249.1, ECO:0000313|Proteomes:UP000030745}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 223.65 {ECO:0000313|EMBL:KDO16249.1,
RC   ECO:0000313|Proteomes:UP000030745};
RX   PubMed=23785293;
RA   Jiang R.H., de Bruijn I., Haas B.J., Belmonte R., Lobach L., Christie J.,
RA   van den Ackerveken G., Bottin A., Bulone V., Diaz-Moreno S.M., Dumas B.,
RA   Fan L., Gaulin E., Govers F., Grenville-Briggs L.J., Horner N.R.,
RA   Levin J.Z., Mammella M., Meijer H.J., Morris P., Nusbaum C., Oome S.,
RA   Phillips A.J., van Rooyen D., Rzeszutek E., Saraiva M., Secombes C.J.,
RA   Seidl M.F., Snel B., Stassen J.H., Sykes S., Tripathy S., van den Berg H.,
RA   Vega-Arreguin J.C., Wawra S., Young S.K., Zeng Q., Dieguez-Uribeondo J.,
RA   Russ C., Tyler B.M., van West P.;
RT   "Distinctive expansion of potential virulence genes in the genome of the
RT   oomycete fish pathogen Saprolegnia parasitica.";
RL   PLoS Genet. 9:E1003272-E1003272(2013).
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. {ECO:0000256|RuleBase:RU364013}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|RuleBase:RU364013}.
CC       Chromosome {ECO:0000256|RuleBase:RU364013}.
CC   -!- SIMILARITY: Belongs to the SSRP1 family.
CC       {ECO:0000256|ARBA:ARBA00010060, ECO:0000256|RuleBase:RU364013}.
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DR   EMBL; KK584239; KDO16249.1; -; Genomic_DNA.
DR   RefSeq; XP_012213043.1; XM_012357653.1.
DR   AlphaFoldDB; A0A067BD31; -.
DR   STRING; 695850.A0A067BD31; -.
DR   EnsemblProtists; KDO16249; KDO16249; SPRG_18217.
DR   GeneID; 24139742; -.
DR   KEGG; spar:SPRG_18217; -.
DR   VEuPathDB; FungiDB:SPRG_18217; -.
DR   OrthoDB; 5488575at2759; -.
DR   Proteomes; UP000030745; Unassembled WGS sequence.
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:InterPro.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR   CDD; cd13231; PH2_SSRP1-like; 1.
DR   Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR013719; RTT106/SPT16-like_middle_dom.
DR   InterPro; IPR000969; SSRP1/POB3.
DR   PANTHER; PTHR45849; FACT COMPLEX SUBUNIT SSRP1; 1.
DR   PANTHER; PTHR45849:SF1; FACT COMPLEX SUBUNIT SSRP1; 1.
DR   Pfam; PF08512; Rttp106-like_middle; 1.
DR   PRINTS; PR00887; SSRCOGNITION.
DR   SMART; SM01287; Rtt106; 1.
DR   SUPFAM; SSF50729; PH domain-like; 1.
PE   3: Inferred from homology;
KW   Chromosome {ECO:0000256|ARBA:ARBA00022454, ECO:0000256|RuleBase:RU364013};
KW   DNA damage {ECO:0000256|ARBA:ARBA00022763, ECO:0000256|RuleBase:RU364013};
KW   DNA repair {ECO:0000256|ARBA:ARBA00023204, ECO:0000256|RuleBase:RU364013};
KW   DNA replication {ECO:0000256|ARBA:ARBA00022705,
KW   ECO:0000256|RuleBase:RU364013};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|RuleBase:RU364013};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030745};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163,
KW   ECO:0000256|RuleBase:RU364013};
KW   Transcription regulation {ECO:0000256|ARBA:ARBA00023015,
KW   ECO:0000256|RuleBase:RU364013}.
FT   DOMAIN          33..133
FT                   /note="Histone chaperone RTT106/FACT complex subunit SPT16-
FT                   like middle"
FT                   /evidence="ECO:0000259|SMART:SM01287"
FT   REGION          139..235
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        152..201
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   235 AA;  26137 MW;  DBCAAB66DA1CCFA5 CRC64;
     MSGALPQIVA TLFKFIIGKK VYTSGKFVTH SGDRAVKCAV KANSGVLFPL EKSFMFIHKP
     TTFIRYDDID YIEFQRYAGQ SGTSASRNFD LLVSCRAVGQ ELAHETLFSA IDRREFPELS
     QFLTSKKLKI RNLKETQATA PAKRGYEEMN EALGPEEGEV DEEEEEDSDF GPGAESDEDG
     SEDFSDESLS GNDEEEDEND DGEAKKTDKK KKDKKKDKKK AKKAKTSGGS DDEAE
//
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