ID   SPT16_DEBHA             Reviewed;        1033 AA.
AC   Q6BXE5;
DT   11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   16-DEC-2008, sequence version 2.
DT   25-MAY-2022, entry version 105.
DE   RecName: Full=FACT complex subunit SPT16;
DE   AltName: Full=Facilitates chromatin transcription complex subunit SPT16;
GN   Name=SPT16; OrderedLocusNames=DEHA2B03718g;
OS   Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990
OS   / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX   NCBI_TaxID=284592;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC 2968;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA   Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA   Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA   Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA   Weissenbach J., Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
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 (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Forms a stable heterodimer with POB3. The SPT16-POB3 dimer
CC       weakly associates with multiple molecules of NHP6 to form the FACT
CC       complex (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Chromosome {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the peptidase M24 family. SPT16 subfamily.
CC       {ECO:0000305}.
CC   -!- CAUTION: Although related to the peptidase M24 family, this protein
CC       lacks conserved active site residues suggesting that it may lack
CC       peptidase activity. {ECO:0000305}.
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; CR382134; CAG85117.2; -; Genomic_DNA.
DR   RefSeq; XP_457124.2; XM_457124.1.
DR   AlphaFoldDB; Q6BXE5; -.
DR   SMR; Q6BXE5; -.
DR   STRING; 4959.XP_457124.2; -.
DR   PRIDE; Q6BXE5; -.
DR   EnsemblFungi; CAG85117; CAG85117; DEHA2B03718g.
DR   GeneID; 2913232; -.
DR   KEGG; dha:DEHA2B03718g; -.
DR   VEuPathDB; FungiDB:DEHA2B03718g; -.
DR   eggNOG; KOG1189; Eukaryota.
DR   HOGENOM; CLU_004627_1_0_1; -.
DR   InParanoid; Q6BXE5; -.
DR   OMA; HQFFLDG; -.
DR   OrthoDB; 145488at2759; -.
DR   Proteomes; UP000000599; Chromosome B.
DR   GO; GO:0035101; C:FACT complex; IEA:InterPro.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR   CDD; cd01091; CDC68-like; 1.
DR   Gene3D; 2.30.29.30; -; 1.
DR   Gene3D; 3.40.350.10; -; 1.
DR   Gene3D; 3.90.230.10; -; 1.
DR   InterPro; IPR029149; Creatin/AminoP/Spt16_NTD.
DR   InterPro; IPR036005; Creatinase/aminopeptidase-like.
DR   InterPro; IPR013719; DUF1747.
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; IPR040258; Spt16.
DR   InterPro; IPR033825; Spt16_M24.
DR   PANTHER; PTHR13980; PTHR13980; 1.
DR   Pfam; PF14826; FACT-Spt16_Nlob; 1.
DR   Pfam; PF00557; Peptidase_M24; 1.
DR   Pfam; PF08512; Rtt106; 1.
DR   Pfam; PF08644; SPT16; 1.
DR   SMART; SM01285; FACT-Spt16_Nlob; 1.
DR   SMART; SM01287; Rtt106; 1.
DR   SMART; SM01286; SPT16; 1.
DR   SUPFAM; SSF55920; SSF55920; 1.
PE   3: Inferred from homology;
KW   Chromosome; Coiled coil; DNA damage; DNA repair; DNA replication; Nucleus;
KW   Reference proteome; Transcription; Transcription regulation.
FT   CHAIN           1..1033
FT                   /note="FACT complex subunit SPT16"
FT                   /id="PRO_0000245184"
FT   REGION          953..1033
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          103..128
FT                   /evidence="ECO:0000255"
FT   COILED          467..517
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        956..991
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1003..1017
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1018..1033
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1033 AA;  117433 MW;  EA51642754DCCE61 CRC64;
     MSEVKIDSNS FHKRLSLIQK NLTSIQDKQS CLLLLVGASD DENTYKKTTV LQTWLLGYEF
     VHTGIYITQD KCVFITSEGK AKYLTNLTSK PTENSSSVEI WPRYKDAEKN KETFKKLIEE
     LKKMSSREKP IGHIAKDQYR GKFIDEWNEV SADAGLSFSD CALLLSESME IKDSEEFANT
     KIASKSSTVL MDAFANEMMV VVDEEKKTSN SDLSEKIEDK IDSNKWYTKS ATGKKLLQSM
     KEFDPSLVDW CYSPIIQSGG EYDLKPSAQS TTKALVGDGV ILASLGLRYK SYCSNVARTF
     FIDPTPAMET NYDFLLKLQN HVTSTLLRDG TVASQVYQGA LDFIKSEKPD LVQHFTKNCG
     WLMGIEFRDS TFVLNSKNER KLQNGQIISL TLGFSNLTND KASNPKLKQY SLILTDTFKV
     SESEPILLTT YPKARSETSF YFKDDEPTAV KSENGGDKKL KSEKNIKTEK NLAANEANSK
     ILKSKLRHES SAADDSNNTE KIRQEIQSKL HEKRQHEGLA RFSKADATDA SDFKPVFKKY
     ESYVRESQIP SNVRDLKIHV DYKNQTIILP ICGRPVPFHI NSFKNGSQNE EGDFTYLRLN
     FNSPGAGGNV SRRAELPYED SPENSFLRSV TLRSRDHQRM VDVYKAIQDL KKDAVKREQE
     KKQMADVVSQ ANLVELKGSR VKKLDQVFIR PQPDTKKIGG VLQIHENGLR YQSSIRMDQK
     VDILFSNIKH LFFQSCKDEL IVIIHCHLKN PIMIGKKKTH DVQFYREASD MAFDETGGRK
     RRYRYGDEDE LQQEQEERRR KALLDKEFKA FAELISDSSS GMVDLDIPFR ELGFSGVPFR
     SSVLCMPTRD CLIQLIDPPY LVVTLEEIEI AHLERVQFGL KNFDLVFVFK DFNKSVVHIN
     TIPMELLEDV KSWLTDVDIP ISEGQMNLNW ATIMKTVQSD PYQFFADGGW SFLTGEGDSE
     EEDEEDEESE FEVSDPDPSD EDVESEAGSE DDYSSDASGS DASGGESEEE EEGEDWDEME
     RKAAREDKRL GAS