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SPT16_CANGA
ID   SPT16_CANGA             Reviewed;        1027 AA.
AC   Q6FWT4;
DT   11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 112.
DE   RecName: Full=FACT complex subunit SPT16;
DE   AltName: Full=Facilitates chromatin transcription complex subunit SPT16;
GN   Name=SPT16; OrderedLocusNames=CAGL0C03047g;
OS   Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS   Y-65) (Yeast) (Torulopsis glabrata).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC   Nakaseomyces/Candida clade.
OX   NCBI_TaxID=284593;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
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; CR380949; CAG58216.1; -; Genomic_DNA.
DR   RefSeq; XP_445310.1; XM_445310.1.
DR   AlphaFoldDB; Q6FWT4; -.
DR   SMR; Q6FWT4; -.
DR   STRING; 5478.XP_445310.1; -.
DR   EnsemblFungi; CAG58216; CAG58216; CAGL0C03047g.
DR   GeneID; 2886759; -.
DR   KEGG; cgr:CAGL0C03047g; -.
DR   CGD; CAL0127194; CAGL0C03047g.
DR   VEuPathDB; FungiDB:CAGL0C03047g; -.
DR   eggNOG; KOG1189; Eukaryota.
DR   HOGENOM; CLU_004627_1_0_1; -.
DR   InParanoid; Q6FWT4; -.
DR   OMA; HQFFLDG; -.
DR   Proteomes; UP000002428; Chromosome C.
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..1027
FT                   /note="FACT complex subunit SPT16"
FT                   /id="PRO_0000245182"
FT   REGION          767..790
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          952..1027
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          8..28
FT                   /evidence="ECO:0000255"
FT   COILED          82..102
FT                   /evidence="ECO:0000255"
FT   COILED          208..233
FT                   /evidence="ECO:0000255"
FT   COILED          484..507
FT                   /evidence="ECO:0000255"
FT   COILED          637..658
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        772..790
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        955..1010
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1011..1027
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1027 AA;  117896 MW;  0FFCB8772A0ACED5 CRC64;
     MSELNIDAEA FKARVELLHG KYREFENEPN SMVFALGSSN PENPYQKTTA LHYWLMGYEF
     PATLIVFTPG KVVIITSGPK AKHLEKVVEL FKNNNNGVEL EIWQRNNKDV EHSQKLFKDI
     IELINTAGKT VGIPEKDVYE GKFMKEWKPI WDAAIKEHEF KLVDISAGLS STWEVKDDKE
     KAYISIASKC SDRFMNLLSD EMVRAVDDEL KITNSKLSDK IENKIDDLKF LKKITNDLSA
     MCPPNHKFTL DLLDWTYSPI IQSGNKFDLR VSAHSNNDQL HGNGCILASC GIRYNNYCSN
     TTRTFLIDPS EEMVNNYVFL LDLQKHIIEN ELKAGRTGKE VYESVVEFIK KVRPELAGNF
     TKNIGSLIGL EFRDSFFVLN SKNDKRKIQV GDCFNISFGF NALKDMKTNT NYALQLADTV
     ILNEDGPKIL TEYTKSKSQV SFYFNNDEVE KEKKPAASTK IPTNLDGNSK ILRSKLRGDA
     RGESQDAQKE QIRKENQRKL HEKLQKEGLL RFTAEDATTE GSETRQYFKK YESYVRESQI
     PNNVRDLRIH VDWRSQTIIV PIYGRPVPFH INSYKNGSKN EEGEYTYLRL NFHSPGSAGG
     ISKNVVELPY DDSPDNQFMR SITLRSKDGD RMSETFKQIT DLKKESTKRE QERKALADVV
     QQDKLIENKT GRTKRLDQIF VRPSPDTKRV PSTVFIHENG IRYQSPLRTD SRIDILFSNI
     KNLIFQSCKG ELIVIIHIHL KNPIMMGKKK IQDVQFYREA SDVSVDETGT GRRNQNKFRK
     YGDEDELEQE QEERRKRAML DKEFKYFADA IAEASNGLVS VESTFRDLGF QGVPNRSAVF
     CMPTTDCLVQ LIEPPFLVVN LEEIEVAILE RVQFGLKNFD LVFVYKDFKK PVTHINTIPI
     ESLDFLKQWL TDMDIPYAIS TINLKWSTIM QSLQEDPHQF FLDGGWSFLN ANSDEEGSDE
     SEEEISEYEA SEEEPEDESA YSDEDDYSED ISDGSYSGAD SEEEEGEDWD ELEKKAAKAD
     RTAGLRD
 
 
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