ID   SPT16_ASHGO             Reviewed;        1031 AA.
AC   Q756A7;
DT   11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2013, sequence version 2.
DT   03-AUG-2022, entry version 115.
DE   RecName: Full=FACT complex subunit SPT16;
DE   AltName: Full=Facilitates chromatin transcription complex subunit SPT16;
GN   Name=SPT16; OrderedLocusNames=AER360C;
OS   Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS   (Yeast) (Eremothecium gossypii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX   NCBI_TaxID=284811;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=15001715; DOI=10.1126/science.1095781;
RA   Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA   Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA   Gaffney T.D., Philippsen P.;
RT   "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT   cerevisiae genome.";
RL   Science 304:304-307(2004).
RN   [2]
RP   GENOME REANNOTATION, AND SEQUENCE REVISION TO 55 AND 1022-1023.
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=23749448; DOI=10.1534/g3.112.002881;
RA   Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT   "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT   loci, numerous translocations, lack of transposons, and distinct gene
RT   duplications.";
RL   G3 (Bethesda) 3:1225-1239(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 (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; AE016818; AAS53040.2; -; Genomic_DNA.
DR   RefSeq; NP_985216.2; NM_210570.2.
DR   PDB; 6A8M; X-ray; 1.70 A; A=2-460.
DR   PDBsum; 6A8M; -.
DR   AlphaFoldDB; Q756A7; -.
DR   SMR; Q756A7; -.
DR   STRING; 33169.AAS53040; -.
DR   PRIDE; Q756A7; -.
DR   EnsemblFungi; AAS53040; AAS53040; AGOS_AER360C.
DR   GeneID; 4621432; -.
DR   KEGG; ago:AGOS_AER360C; -.
DR   eggNOG; KOG1189; Eukaryota.
DR   HOGENOM; CLU_004627_1_0_1; -.
DR   InParanoid; Q756A7; -.
DR   OMA; HQFFLDG; -.
DR   Proteomes; UP000000591; Chromosome V.
DR   GO; GO:0035101; C:FACT complex; IBA:GO_Central.
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; IBA:GO_Central.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR   GO; GO:0034724; P:DNA replication-independent chromatin organization; IBA:GO_Central.
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:0032968; P:positive regulation of transcription elongation from RNA polymerase II promoter; IBA:GO_Central.
DR   GO; GO:0007063; P:regulation of sister chromatid cohesion; IEA:EnsemblFungi.
DR   GO; GO:0006368; P:transcription elongation from RNA polymerase II promoter; IBA:GO_Central.
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   1: Evidence at protein level;
KW   3D-structure; Chromosome; Coiled coil; DNA damage; DNA repair;
KW   DNA replication; Nucleus; Reference proteome; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..1031
FT                   /note="FACT complex subunit SPT16"
FT                   /id="PRO_0000245178"
FT   REGION          450..501
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          952..1031
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          478..499
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        450..464
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        471..501
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        957..1013
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1014..1031
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   HELIX           8..21
FT                   /evidence="ECO:0007829|PDB:6A8M"
FT   HELIX           22..24
FT                   /evidence="ECO:0007829|PDB:6A8M"
FT   STRAND          30..36
FT                   /evidence="ECO:0007829|PDB:6A8M"
FT   HELIX           47..56
FT                   /evidence="ECO:0007829|PDB:6A8M"
FT   STRAND          61..67
FT                   /evidence="ECO:0007829|PDB:6A8M"
FT   STRAND          69..76
FT                   /evidence="ECO:0007829|PDB:6A8M"
FT   HELIX           78..94
FT                   /evidence="ECO:0007829|PDB:6A8M"
FT   TURN            95..98
FT                   /evidence="ECO:0007829|PDB:6A8M"
FT   STRAND          100..105
FT                   /evidence="ECO:0007829|PDB:6A8M"
FT   HELIX           112..127
FT                   /evidence="ECO:0007829|PDB:6A8M"
FT   STRAND          129..133
FT                   /evidence="ECO:0007829|PDB:6A8M"
FT   HELIX           142..157
FT                   /evidence="ECO:0007829|PDB:6A8M"
FT   STRAND          161..164
FT                   /evidence="ECO:0007829|PDB:6A8M"
FT   HELIX           166..173
FT                   /evidence="ECO:0007829|PDB:6A8M"
FT   HELIX           178..207
FT                   /evidence="ECO:0007829|PDB:6A8M"
FT   HELIX           214..223
FT                   /evidence="ECO:0007829|PDB:6A8M"
FT   HELIX           224..226
FT                   /evidence="ECO:0007829|PDB:6A8M"
FT   HELIX           228..232
FT                   /evidence="ECO:0007829|PDB:6A8M"
FT   HELIX           235..238
FT                   /evidence="ECO:0007829|PDB:6A8M"
FT   HELIX           239..241
FT                   /evidence="ECO:0007829|PDB:6A8M"
FT   HELIX           250..252
FT                   /evidence="ECO:0007829|PDB:6A8M"
FT   STRAND          253..257
FT                   /evidence="ECO:0007829|PDB:6A8M"
FT   STRAND          260..262
FT                   /evidence="ECO:0007829|PDB:6A8M"
FT   STRAND          264..266
FT                   /evidence="ECO:0007829|PDB:6A8M"
FT   STRAND          277..279
FT                   /evidence="ECO:0007829|PDB:6A8M"
FT   STRAND          283..290
FT                   /evidence="ECO:0007829|PDB:6A8M"
FT   STRAND          292..294
FT                   /evidence="ECO:0007829|PDB:6A8M"
FT   STRAND          301..308
FT                   /evidence="ECO:0007829|PDB:6A8M"
FT   HELIX           311..329
FT                   /evidence="ECO:0007829|PDB:6A8M"
FT   HELIX           338..352
FT                   /evidence="ECO:0007829|PDB:6A8M"
FT   HELIX           354..356
FT                   /evidence="ECO:0007829|PDB:6A8M"
FT   TURN            357..359
FT                   /evidence="ECO:0007829|PDB:6A8M"
FT   STRAND          362..367
FT                   /evidence="ECO:0007829|PDB:6A8M"
FT   STRAND          369..373
FT                   /evidence="ECO:0007829|PDB:6A8M"
FT   STRAND          377..382
FT                   /evidence="ECO:0007829|PDB:6A8M"
FT   STRAND          393..404
FT                   /evidence="ECO:0007829|PDB:6A8M"
FT   TURN            406..408
FT                   /evidence="ECO:0007829|PDB:6A8M"
FT   STRAND          411..423
FT                   /evidence="ECO:0007829|PDB:6A8M"
FT   STRAND          426..429
FT                   /evidence="ECO:0007829|PDB:6A8M"
FT   HELIX           437..440
FT                   /evidence="ECO:0007829|PDB:6A8M"
SQ   SEQUENCE   1031 AA;  117773 MW;  6D9FD826D57C267B CRC64;
     MSEVIIDFST FENRLLALRD RFPSFDGSPS SLVFILGSAD EENPYQKTTI LHNWLLGYEF
     PTTLIAVFKE GCVVITSAAK TRYLEEGVAQ MNKKLENTFK IELWQSSKEP GHNLKLFEDL
     VERVREAGSA VGLATKDSYQ GKFITEWKGV WDTAVEKHGL NGVDVSLGLS SLWAVKDEKE
     QAYLQVSSRG SDKFMNLLSD ELVRAVDEEI KITDAKLSDN VENEIDKSRF LKKLSPELTP
     LCPKGEKFDV NYLDWAYSPI IQSGPKYDLR VSARSSETQL DGNGCILASC GIRYKNYCSN
     ISRTFLIDPS DEMTDNYDFL LLLQEEIINN LLRVGATPKQ IYDGAVNYIN SKKPELSAGF
     TKNVGSLMGL EFRDSQFVLN NKNDYRKVEN GDCFNISLGF NNLKDSKTGA SYALQLADTV
     QLTSGGPKVL TNYTKSRSQI SFYFNNEDDG TTKVKSEESK TASIPTKPDP KSKILRSKLR
     GESRAEDDEK EQIRKENQRK LHEKLQREGL LRFTDTDAAD KDQKPVVHFK KYESYVRETQ
     IPNTVRDLRI HVDWKNQTFI LPIYGRPVPF HINSYKNGSK NEEGEYTYIR LNFHSPGTGG
     VSKKTEELPY EDSPDHQFVR SLTLRSKDGD RMADIFKQIT ELKKESTKRE QERKVLADVV
     EQAKLVENRT GRTKRLDQIF VRPSPDTKRV PGTVFIHENG IRYQSPLRTD SRIDILFSNV
     KNLFFQPCKG ELIVIIHIHL KNPILMGKKK IQDVQFYREA SDMAVDETGN GRRNQMKFRR
     YGDEDELEQE QEERRKRAAL DKEFRYFAEA IAEASNGLVE VDHPFRDLGF QGVPSRSAVF
     CMPTRDCLIQ LVEPPFLVVN LSEVEICILE RVQFGLKNFD MVFVYKDFTK PVTHINTIPI
     EQLEFIKSWL TDVDIPYTVS TINLNWATIM KSLQDDPHQF FLDGGWSFLA TGSDDEMSGT
     SEEEVSEYEV SDEDPSDEEV DSEDDYSEGD NEEFSDEGSE DFSGEESEEG EDWDELEKKA
     AKADRGNRFA D