ID F2U7M9_SALR5 Unreviewed; 797 AA.
AC F2U7M9;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE RecName: Full=FACT complex subunit SSRP1 {ECO:0000256|RuleBase:RU364013};
GN ORFNames=PTSG_04053 {ECO:0000313|EMBL:EGD83446.1};
OS Salpingoeca rosetta (strain ATCC 50818 / BSB-021).
OC Eukaryota; Choanoflagellata; Craspedida; Salpingoecidae; Salpingoeca.
OX NCBI_TaxID=946362 {ECO:0000313|Proteomes:UP000007799};
RN [1] {ECO:0000313|Proteomes:UP000007799}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 50818 {ECO:0000313|Proteomes:UP000007799};
RA Russ C., Cuomo C., Burger G., Gray M.W., Holland P.W.H., King N.,
RA Lang F.B.F., Roger A.J., Ruiz-Trillo I., Young S.K., Zeng Q., Gargeya S.,
RA Alvarado L., Berlin A., Chapman S.B., Chen Z., Freedman E., Gellesch M.,
RA Goldberg J., Griggs A., Gujja S., Heilman E., Heiman D., Howarth C.,
RA Mehta T., Neiman D., Pearson M., Roberts A., Saif S., Shea T., Shenoy N.,
RA Sisk P., Stolte C., Sykes S., White J., Yandava C., Haas B., Nusbaum C.,
RA Birren B.;
RT "Annotation of Salpingoeca rosetta.";
RL Submitted (AUG-2009) 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; GL832963; EGD83446.1; -; Genomic_DNA.
DR RefSeq; XP_004994950.1; XM_004994893.1.
DR AlphaFoldDB; F2U7M9; -.
DR STRING; 946362.F2U7M9; -.
DR EnsemblProtists; EGD83446; EGD83446; PTSG_04053.
DR GeneID; 16075528; -.
DR KEGG; sre:PTSG_04053; -.
DR eggNOG; KOG0381; Eukaryota.
DR eggNOG; KOG0526; Eukaryota.
DR InParanoid; F2U7M9; -.
DR OMA; KQPGKCK; -.
DR OrthoDB; 5488575at2759; -.
DR Proteomes; UP000007799; 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:UniProtKB-UniRule.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR CDD; cd01390; HMG-box_NHP6-like; 1.
DR CDD; cd21994; HMG-box_SSRP1-like; 1.
DR CDD; cd13230; PH1_SSRP1-like; 1.
DR CDD; cd13231; PH2_SSRP1-like; 1.
DR Gene3D; 2.30.29.150; -; 1.
DR Gene3D; 1.10.30.10; High mobility group box domain; 2.
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; IPR009071; HMG_box_dom.
DR InterPro; IPR036910; HMG_box_dom_sf.
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; PF00505; HMG_box; 2.
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; SM00398; HMG; 2.
DR SMART; SM01287; Rtt106; 1.
DR SUPFAM; SSF47095; HMG-box; 2.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR PROSITE; PS50118; HMG_BOX_2; 2.
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 DNA-binding {ECO:0000256|PROSITE-ProRule:PRU00267};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|PROSITE-
KW ProRule:PRU00267}; Reference proteome {ECO:0000313|Proteomes:UP000007799};
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 577..645
FT /note="HMG box"
FT /evidence="ECO:0000259|PROSITE:PS50118"
FT DOMAIN 667..735
FT /note="HMG box"
FT /evidence="ECO:0000259|PROSITE:PS50118"
FT DNA_BIND 577..645
FT /note="HMG box"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00267"
FT DNA_BIND 667..735
FT /note="HMG box"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00267"
FT REGION 449..585
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 626..672
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 735..797
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 463..490
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 491..508
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 534..555
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 626..657
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 735..756
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 757..771
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 797 AA; 89955 MW; 1DC940582DE5529D CRC64;
MADEKLIVET PVFMIVRGAS CRGRMRCSPQ GLAFKREATD KTQTFYKSDM ASCETKRVAR
GHQLRIKLKS GGHATFEGFK SNDMNAMIDF FKKHYDLDIK IVELSLKGNN SGSARFHGNF
LVFDVDGKPA FEVPLNAVGN VTSQKYEASI DFIQDEDADD NEQRVESMRF LVIPDPESEQ
YAKTEEFVEN VKARASIAEY TSRAICTIGK LSFLVPRGRF DVELYPSFMQ LRGSTYDHRL
FYDYISHIYL LPRPDDGEYI VLAVDPPLRH GQTRYPHVLL QFTREHEGAD VVVNVTSDEV
RSSLSYLTES IPADQAEVTE TGPLASILSR LLKALTKRKI ITPGSFTSSE GFAAVNCTYK
ANRGTLYPLD RGFLFLHKPL LHISIVRNLR VTFDRVKESS SRDTKSFDMR LLHPERGEFE
FRGLGQDELQ PLIDFLRLKR VAIEGLDEAP AAAGDDDGFD SSEDEDHVVR PGDFDDGSSE
SDHSFAEDDV EESSMDSEED EQLQDELVED DMLGQAPAKK KRASKSRQSK QRDDDEEDDD
DDEDEDEDED EDDIIVEDKP VKSKKKTQKA SAAKRGPKKA KTAYALWSSS ARSKLKEQHP
DLSFGELSKK LGQAWQDLAD EDKAEWNEKA KEDRQRYLKE KKKFDAENPD AAKPAKKMRK
KKDPNAPKGA KSAYIYFSTE MREKIKEEKP DLTLGQISQE CGTLWRGLSD EEKKKYEKMA
AEDKKRYEAE MAEYKAKNDA DDDGDGDGDN AGSKKRSAKG TKSKAKKSKT SKAPAKGQST
LKFKSDEVVL SSESDDE
//
