SPT16_KLULA
ID SPT16_KLULA Reviewed; 1033 AA.
AC Q00976; Q6CKK9;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2004, sequence version 2.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=FACT complex subunit SPT16;
DE AltName: Full=Cell division control protein 68;
DE AltName: Full=Facilitates chromatin transcription complex subunit SPT16;
GN Name=SPT16; Synonyms=CDC68; OrderedLocusNames=KLLA0F09889g;
OS Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX NCBI_TaxID=284590;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9832518; DOI=10.1093/genetics/150.4.1393;
RA Evans D.R.H., Brewster N.K., Xu Q., Rowley A., Altheim B.A., Johnston G.C.,
RA Singer R.A.;
RT "The yeast protein complex containing cdc68 and pob3 mediates core-promoter
RT repression through the cdc68 N-terminal domain.";
RL Genetics 150:1393-1405(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
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}.
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DR EMBL; U48701; AAA97888.1; -; Genomic_DNA.
DR EMBL; CR382126; CAG98238.1; -; Genomic_DNA.
DR RefSeq; XP_455530.1; XM_455530.1.
DR AlphaFoldDB; Q00976; -.
DR SMR; Q00976; -.
DR STRING; 28985.XP_455530.1; -.
DR PRIDE; Q00976; -.
DR EnsemblFungi; CAG98238; CAG98238; KLLA0_F09889g.
DR GeneID; 2894946; -.
DR KEGG; kla:KLLA0_F09889g; -.
DR eggNOG; KOG1189; Eukaryota.
DR HOGENOM; CLU_004627_1_0_1; -.
DR InParanoid; Q00976; -.
DR OMA; HQFFLDG; -.
DR Proteomes; UP000000598; Chromosome F.
DR GO; GO:0035101; C:FACT complex; IEA:EnsemblFungi.
DR GO; GO:0031298; C:replication fork protection complex; IEA:EnsemblFungi.
DR GO; GO:0042393; F:histone binding; IEA:EnsemblFungi.
DR GO; GO:0031491; F:nucleosome binding; IEA:EnsemblFungi.
DR GO; GO:0140597; F:protein carrier chaperone; IEA:EnsemblFungi.
DR GO; GO:0140719; P:constitutive heterochromatin assembly; IEA:EnsemblFungi.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0034724; P:DNA replication-independent chromatin organization; IEA:EnsemblFungi.
DR GO; GO:0006261; P:DNA-templated DNA replication; IEA:EnsemblFungi.
DR GO; GO:0006334; P:nucleosome assembly; IEA:EnsemblFungi.
DR GO; GO:0045899; P:positive regulation of RNA polymerase II transcription preinitiation complex assembly; IEA:EnsemblFungi.
DR GO; GO:0007063; P:regulation of sister chromatid cohesion; IEA:EnsemblFungi.
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 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_0000089447"
FT REGION 454..474
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 776..795
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 953..1033
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 99..124
FT /evidence="ECO:0000255"
FT COILED 479..509
FT /evidence="ECO:0000255"
FT COILED 638..659
FT /evidence="ECO:0000255"
FT COMPBIAS 957..1016
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1017..1033
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 157..160
FT /note="THSL -> DAFF (in Ref. 1; AAA97888)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1033 AA; 117891 MW; FC88A1D61002AD7E CRC64;
MSDGGIEIDF QAFYDRFTKL GKAYSGFEGS PNSLLFVLGS TNEENPYQKT TILHNWLLGY
EFPATLIAFF KDKGVIITSS AKAKHLLPAV TKFEGSDYKL EIWQRNNKDA NHNKKLFEDL
IKLLSENGNT VGVPTKDSYQ GKLILEWKPL WEEAKKTHSL NVIDCSAGLS STWKGKDDKE
KAYLSVSSKG SDKFMDLMSN EIVNAVDEEL KISNSKLSDK IENKIDDSKF LKKLSSDLNP
LCPTDEKFDV NFLDWAYSPI VQSGSKFDLK VSARSNNDSL FGKGSILASC GIRYKNYCSN
ITRTFLIDPT DEMTDNYDFL LILQEKIIDD LLKVEADPTS IYEKTLEFIK EKKPELLSHF
TKNVGSLMGL EFRDSAGMIN AKPTAHKISE NCCYNISLGF GNLKDSKTGQ VYAVQLADTV
QLSSDGKPST LTKYTKARSQ ISFYFNNEEE NKAATVKSEK SKPPALPKPD GTSKILRSKL
RGESRADDEE KEQIRKENQR KLHERLQKEG LLRYSDADAV DGDEKPKHFF KKYESYVRET
QIPSNVRDLK IHVDWKSQTI ILPIYGRPVP FHINSYKNGS KNEEGEYTYL RLNFHSPGAG
GVGKKTEELP YEENPENQFV RSLTLRSKDG ARMSDVFKQI TDLKKESTKR EQERKALADV
VVQAKLVENK TGRTKRLDQI FVRPSPDTKR VPGTVFIHEN GIRYQSPLRT DSRIDILFSN
IKNLFFQSSK GELIVIIHVH LKNPILMGKK KIQDIQFYRE ASDMAVDETG NSRRNNMKFR
RYGDEDELEQ EQEERRKRAA LDKEFRYFAE AIAEASDGLL DVDSPFRDLG FQGVPSRSAV
FCMPTRDCLI QLVEPPFLVI NLNEVEICIL ERVQFGLKNF DMVFVYKDLT KPVSHINTVP
IEQLEFIKTW LTDVDIPYTV STINLNWSTI MKSLQDDPHQ FFLDGGWSFL ATGSDDERSD
ESEEEISEYE ASDEDPSDEE VYSEEEEDYS DDEKFSDEGS DDFADGSEDD EGDDWDDLEK
KAAKADRNSN YKE
