ID G0SDN1_CHATD Unreviewed; 1029 AA.
AC G0SDN1;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 75.
DE RecName: Full=FACT complex subunit {ECO:0000256|RuleBase:RU367052};
GN ORFNames=CTHT_0052370 {ECO:0000313|EMBL:EGS18632.1};
OS Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719)
OS (Thermochaetoides thermophila).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Chaetomiaceae; Thermochaetoides.
OX NCBI_TaxID=759272 {ECO:0000313|EMBL:EGS18632.1, ECO:0000313|Proteomes:UP000008066};
RN [1] {ECO:0000313|EMBL:EGS18632.1, ECO:0000313|Proteomes:UP000008066}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 1495 / CBS 144.50 / IMI 039719
RC {ECO:0000313|Proteomes:UP000008066};
RX PubMed=21784248; DOI=10.1016/j.cell.2011.06.039;
RA Amlacher S., Sarges P., Flemming D., van Noort V., Kunze R., Devos D.P.,
RA Arumugam M., Bork P., Hurt E.;
RT "Insight into structure and assembly of the nuclear pore complex by
RT utilizing the genome of a eukaryotic thermophile.";
RL Cell 146:277-289(2011).
RN [2] {ECO:0007829|PDB:4KHA, ECO:0007829|PDB:4KHB}
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 651-945 IN COMPLEX WITH CALCIUM.
RX PubMed=23698368; DOI=10.1038/nature12242;
RA Hondele M., Stuwe T., Hassler M., Halbach F., Bowman A., Zhang E.T.,
RA Nijmeijer B., Kotthoff C., Rybin V., Amlacher S., Hurt E., Ladurner A.G.;
RT "Structural basis of histone H2A-H2B recognition by the essential chaperone
RT FACT.";
RL Nature 499:111-114(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:RU367052}.
CC -!- SUBUNIT: Component of the FACT complex.
CC {ECO:0000256|RuleBase:RU367052}.
CC -!- INTERACTION:
CC G0SDN1; G0SHK5: CTHT_0070340; NbExp=3; IntAct=EBI-16058507, EBI-16058545;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|RuleBase:RU367052}.
CC Chromosome {ECO:0000256|RuleBase:RU367052}.
CC -!- SIMILARITY: Belongs to the peptidase M24 family. SPT16 subfamily.
CC {ECO:0000256|ARBA:ARBA00010779, ECO:0000256|RuleBase:RU367052}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; GL988045; EGS18632.1; -; Genomic_DNA.
DR RefSeq; XP_006695577.1; XM_006695514.1.
DR PDB; 4KHA; X-ray; 2.35 A; A=652-945.
DR PDB; 4KHB; X-ray; 2.40 A; A/C/E/G=521-647.
DR PDB; 4KHO; X-ray; 2.00 A; A/B=651-945.
DR PDBsum; 4KHA; -.
DR PDBsum; 4KHB; -.
DR PDBsum; 4KHO; -.
DR AlphaFoldDB; G0SDN1; -.
DR SMR; G0SDN1; -.
DR DIP; DIP-60189N; -.
DR IntAct; G0SDN1; 4.
DR STRING; 759272.G0SDN1; -.
DR GeneID; 18259275; -.
DR KEGG; cthr:CTHT_0052370; -.
DR eggNOG; KOG1189; Eukaryota.
DR HOGENOM; CLU_004627_1_0_1; -.
DR OMA; YHINTIP; -.
DR OrthoDB; 169847at2759; -.
DR Proteomes; UP000008066; Unassembled WGS sequence.
DR GO; GO:0035101; C:FACT complex; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-UniRule.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR CDD; cd01091; CDC68-like; 1.
DR Gene3D; 2.30.29.150; -; 1.
DR Gene3D; 3.90.230.10; Creatinase/methionine aminopeptidase superfamily; 1.
DR Gene3D; 3.40.350.10; Creatinase/prolidase N-terminal domain; 1.
DR Gene3D; 2.30.29.210; FACT complex subunit Spt16p/Cdc68p; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR InterPro; IPR029149; Creatin/AminoP/Spt16_NTD.
DR InterPro; IPR036005; Creatinase/aminopeptidase-like.
DR InterPro; IPR029148; FACT-Spt16_Nlobe.
DR InterPro; IPR013953; FACT_Spt16.
DR InterPro; IPR000994; Pept_M24.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR013719; RTT106/SPT16-like_middle_dom.
DR InterPro; IPR040258; Spt16.
DR InterPro; IPR048969; SPT16_C.
DR InterPro; IPR033825; Spt16_M24.
DR PANTHER; PTHR13980; CDC68 RELATED; 1.
DR PANTHER; PTHR13980:SF15; FACT COMPLEX SUBUNIT SPT16; 1.
DR Pfam; PF14826; FACT-Spt16_Nlob; 1.
DR Pfam; PF00557; Peptidase_M24; 1.
DR Pfam; PF08512; Rttp106-like_middle; 1.
DR Pfam; PF08644; SPT16; 1.
DR Pfam; PF21091; SPT16_C; 1.
DR SMART; SM01285; FACT-Spt16_Nlob; 1.
DR SMART; SM01287; Rtt106; 1.
DR SMART; SM01286; SPT16; 1.
DR SUPFAM; SSF55920; Creatinase/aminopeptidase; 1.
PE 1: Evidence at protein level;
KW 3D-structure {ECO:0007829|PDB:4KHA, ECO:0007829|PDB:4KHB};
KW Calcium {ECO:0007829|PDB:4KHO};
KW Chromosome {ECO:0000256|ARBA:ARBA00022454, ECO:0000256|RuleBase:RU367052};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW DNA damage {ECO:0000256|ARBA:ARBA00022763, ECO:0000256|RuleBase:RU367052};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204, ECO:0000256|RuleBase:RU367052};
KW DNA replication {ECO:0000256|ARBA:ARBA00022705,
KW ECO:0000256|RuleBase:RU367052}; Metal-binding {ECO:0007829|PDB:4KHO};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|RuleBase:RU367052};
KW Reference proteome {ECO:0000313|Proteomes:UP000008066};
KW Transcription {ECO:0000256|ARBA:ARBA00023163,
KW ECO:0000256|RuleBase:RU367052};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015,
KW ECO:0000256|RuleBase:RU367052}.
FT DOMAIN 6..167
FT /note="FACT complex subunit Spt16 N-terminal lobe"
FT /evidence="ECO:0000259|SMART:SM01285"
FT DOMAIN 547..697
FT /note="FACT complex subunit Spt16"
FT /evidence="ECO:0000259|SMART:SM01286"
FT DOMAIN 821..911
FT /note="Histone chaperone RTT106/FACT complex subunit SPT16-
FT like middle"
FT /evidence="ECO:0000259|SMART:SM01287"
FT REGION 446..504
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 943..1029
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 626..656
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 446..464
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 479..504
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 946..1001
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1002..1029
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 780
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0007829|PDB:4KHO"
FT BINDING 783
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0007829|PDB:4KHO"
SQ SEQUENCE 1029 AA; 117280 MW; 5F7DB60886762EB7 CRC64;
MADIKIDSKL FQERISHFIS AWKADKRSGD ALFGGVSSIV ILMGKVDEEP EFYKNNAMHF
WLLGYEFPTT LMLFTLDTLY IITTQKKAKY LDQIKGGRFP VEVLVRGKDN AENEKTFIKI
ADMIKAAGNK VGVLTKDTSK GPFIDEWKKI FAERCKGVEE VDIALALSAG AFSIKDETEL
RAMRTSSKAC VALLTPYFLD EMSSILDQDK KISHASLADK VMNKLEDEKF WKTVELPNRG
KLPSDFDPEQ LDWILGPIVQ SGGKFDLKWQ TDSDDEPLHP GIIIAAMGLR YKSYCSQIAR
TFMVDPNKSQ ESNYRVLLAV HNLILKEIRD GVVVKDVYNK AYNLIKTKKP ELEKHFLKNV
GYGIGLESKD STLILSAKNT RTLKDGMTLC IVTGFSDIPN PDPQGKKDKV YSLVLTDTIR
VTTGEPVVFT GEAPSDMDAT SFFFKDEEEA QPTPKKEKKD PRVGAVATRN ITSTRLRSER
NTAPDEDAEK RRREHQKELA AKKQKEGLLK YADATAGQNG VEVKKFKRFE SYKRDNQLPP
KVRDMGIVID QKNNTIVLPI MGRPVPFHIN TIKNASKSDE GEWSFLRINF LSPGQGVGRK
DDQPFEDASA HFVRSLTFRS TDGDRYAEIA NQISNLKREA VKREQEKKDL EDVVEQDKLI
EIRNRRPAVL DNVYIRPALE GKRVPGKVEI HQNGIRYQSP LSTTQRVDVL FSNIRHLFFQ
PCQNEMIVII HLHLKDPILF GKKKTKDVQF YREAIDIQFD ETGNRKRKYR YGDEDEFEAE
QEERRRKAEL DRLFKSFAEK IAEAGRNEGI EVDMPIRDLG FNGVPNRSNV VIYPTTECLI
QITEPPFLVI TLEDVEWAHL ERVQFGLKNF DLVFVFKDFT RPVVHINTIP VESLEDVKEF
LDSSDIPFSE GPLNLNWSVI MKTVTANPHQ FFLDGGWGFL QNDSDASDAS EEEEDEDSAF
EISESELEAA SESSEEDSDY EDASEEESDA PPSEDDEGES WDELERKARK RDRESGLDDD
DRGGKKRRR
//
