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 27-MAR-2024, entry version 119.
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 / BCRC 20586 / JCM 3761 / NBRC 0622 /
OS NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Nakaseomyces.
OX NCBI_TaxID=284593;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138;
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; 284593.Q6FWT4; -.
DR EnsemblFungi; CAGL0C03047g-T; CAGL0C03047g-T-p1; 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; YHINTIP; -.
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:0140713; F:histone chaperone activity; IEA:EnsemblFungi.
DR GO; GO:0031491; F:nucleosome binding; IEA:EnsemblFungi.
DR GO; GO:0140719; P:constitutive heterochromatin formation; IEA:EnsemblFungi.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
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; 2.30.29.150; -; 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 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 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
//
