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Database: UniProt
Entry: W7AE19_9APIC
LinkDB: W7AE19_9APIC
Original site: W7AE19_9APIC 
ID   W7AE19_9APIC            Unreviewed;       498 AA.
AC   W7AE19;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   24-JAN-2024, entry version 38.
DE   RecName: Full=FACT complex subunit SSRP1 {ECO:0000256|RuleBase:RU364013};
GN   ORFNames=C922_00376 {ECO:0000313|EMBL:EUD69513.1};
OS   Plasmodium inui San Antonio 1.
OC   Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC   Plasmodiidae; Plasmodium; Plasmodium (Plasmodium).
OX   NCBI_TaxID=1237626 {ECO:0000313|EMBL:EUD69513.1, ECO:0000313|Proteomes:UP000030640};
RN   [1] {ECO:0000313|EMBL:EUD69513.1, ECO:0000313|Proteomes:UP000030640}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=San Antonio 1 {ECO:0000313|EMBL:EUD69513.1,
RC   ECO:0000313|Proteomes:UP000030640};
RG   The Broad Institute Genome Sequencing Platform;
RG   The Broad Institute Genome Sequencing Center for Infectious Disease;
RA   Neafsey D., Cheeseman I., Volkman S., Adams J., Walker B., Young S.K.,
RA   Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA   Arachchi H.M., Berlin A.M., Chapman S.B., Dewar J., Goldberg J., Griggs A.,
RA   Gujja S., Hansen M., Howarth C., Imamovic A., Larimer J., McCowan C.,
RA   Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T.,
RA   Sisk P., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Plasmodium inui San Antonio 1.";
RL   Submitted (FEB-2013) 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. {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; KI965460; EUD69513.1; -; Genomic_DNA.
DR   RefSeq; XP_008814215.1; XM_008815993.1.
DR   AlphaFoldDB; W7AE19; -.
DR   EnsemblProtists; EUD69513; EUD69513; C922_00376.
DR   GeneID; 20035650; -.
DR   VEuPathDB; PlasmoDB:C922_00376; -.
DR   OrthoDB; 5488575at2759; -.
DR   Proteomes; UP000030640; 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; cd13230; PH1_SSRP1-like; 1.
DR   CDD; cd13231; PH2_SSRP1-like; 1.
DR   Gene3D; 2.30.29.150; -; 1.
DR   Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 2.
DR   Gene3D; 2.30.29.220; Structure-specific recognition protein (SSRP1); 1.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR013719; RTT106/SPT16-like_middle_dom.
DR   InterPro; IPR048993; SSRP1-like_PH1.
DR   InterPro; IPR000969; SSRP1/POB3.
DR   InterPro; IPR035417; SSRP1/POB3_N.
DR   InterPro; IPR024954; SSRP1_DD.
DR   InterPro; IPR038167; SSRP1_sf.
DR   PANTHER; PTHR45849; FACT COMPLEX SUBUNIT SSRP1; 1.
DR   PANTHER; PTHR45849:SF1; FACT COMPLEX SUBUNIT SSRP1; 1.
DR   Pfam; PF21103; PH1_SSRP1-like; 1.
DR   Pfam; PF17292; POB3_N; 1.
DR   Pfam; PF08512; Rttp106-like_middle; 1.
DR   Pfam; PF03531; SSrecog; 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   Transcription {ECO:0000256|ARBA:ARBA00023163,
KW   ECO:0000256|RuleBase:RU364013};
KW   Transcription regulation {ECO:0000256|ARBA:ARBA00023015,
KW   ECO:0000256|RuleBase:RU364013}.
FT   DOMAIN          349..441
FT                   /note="Histone chaperone RTT106/FACT complex subunit SPT16-
FT                   like middle"
FT                   /evidence="ECO:0000259|SMART:SM01287"
FT   REGION          445..498
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        455..498
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   498 AA;  57900 MW;  515D64EBB36B9377 CRC64;
     MGDNAGSSGS NPVISIGNIR GFGGCDLGSF RMSNEFLGWK NKKTNNVYQY KYSDISEAEW
     IKTSYNNNRL HLKFSEKKDN LIIFFDGFPD RNTSEITQHF QKYFNLRLVS RKLATRGWNW
     GEFKLENSNI TFDIDNKYAF SIPTNSISQL NVQIKTDIAM ELKNEENKRT NEDFLSEIRF
     CYPHENDENQ NFQNFKNDLL EKVNIGDSKS ECIASLTNIP LLVPRGRYEI EMYTKSFKLH
     GKSYDFTIQY TNINKMLLVP KSNSNQYVLI FSLNNKMKQG QTEYPFILIQ LNNDDDMELD
     INASEEDLKK YKLEKSLSGK ASDVVTRLFT ALVKKNAIIP GDYRTAKNEH GITCSYRAAS
     GQLYPLNKYF LFIVKPVILI SFDDIVTLSF QRTGNINQHR FFSLIIKHKR GMSYEYTNID
     KNEYLPLLEF LKSKNIHIQD DSNVADKKQD FGDELSESDE EEYVADEDDD DEDDYVAEDE
     EDDDDDDEEE EEEEDDDK
//
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