ID   SPT16_ASPFU             Reviewed;        1019 AA.
AC   Q4WJ02;
DT   11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2005, sequence version 1.
DT   25-MAY-2022, entry version 112.
DE   RecName: Full=FACT complex subunit spt16;
DE   AltName: Full=Facilitates chromatin transcription complex subunit spt16;
GN   Name=spt16; ORFNames=AFUA_1G07720;
OS   Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS   A1100) (Aspergillus fumigatus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=330879;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100;
RX   PubMed=16372009; DOI=10.1038/nature04332;
RA   Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA   Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P.,
RA   Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.,
RA   Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N.,
RA   Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA   Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E.,
RA   Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H.,
RA   Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A.,
RA   Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L.,
RA   Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D.,
RA   O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L.,
RA   Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U.,
RA   Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M.,
RA   Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C.,
RA   Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F.,
RA   Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R.,
RA   Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N.,
RA   Barrell B.G., Denning D.W.;
RT   "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT   Aspergillus fumigatus.";
RL   Nature 438:1151-1156(2005).
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; AAHF01000007; EAL88480.1; -; Genomic_DNA.
DR   RefSeq; XP_750518.1; XM_745425.1.
DR   AlphaFoldDB; Q4WJ02; -.
DR   SMR; Q4WJ02; -.
DR   STRING; 746128.CADAFUBP00000794; -.
DR   EnsemblFungi; EAL88480; EAL88480; AFUA_1G07720.
DR   GeneID; 3507777; -.
DR   KEGG; afm:AFUA_1G07720; -.
DR   VEuPathDB; FungiDB:Afu1g07720; -.
DR   eggNOG; KOG1189; Eukaryota.
DR   HOGENOM; CLU_004627_1_0_1; -.
DR   InParanoid; Q4WJ02; -.
DR   OMA; HQFFLDG; -.
DR   OrthoDB; 145488at2759; -.
DR   Proteomes; UP000002530; Chromosome 1.
DR   GO; GO:0035101; C:FACT complex; IBA:GO_Central.
DR   GO; GO:0031491; F:nucleosome binding; IBA:GO_Central.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR   GO; GO:0034724; P:DNA replication-independent chromatin organization; IBA:GO_Central.
DR   GO; GO:0032968; P:positive regulation of transcription elongation from RNA polymerase II promoter; IBA:GO_Central.
DR   GO; GO:0006368; P:transcription elongation from RNA polymerase II promoter; IBA:GO_Central.
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..1019
FT                   /note="FACT complex subunit spt16"
FT                   /id="PRO_0000245179"
FT   REGION          754..773
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          935..1019
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          476..500
FT                   /evidence="ECO:0000255"
FT   COILED          614..650
FT                   /evidence="ECO:0000255"
FT   COILED          774..797
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        938..992
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        993..1019
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1019 AA;  115210 MW;  85E47575BBE927E6 CRC64;
     MAEEIVIDKT LFFNRLSSFY AAWRADKRSS HPTFGGVGSI VILMGKTDEA STFQKNNAMH
     FWLLGYEFPA TLLVFTLEAV YVVTTAKKAK HLEPLRGGKI PVEILITTKD PEGKLRSFEK
     CIEVIRSAGN KVGVLPKDTT TGPFAEDWKR TFAMLSAEIE EVDISPALSA AFAVKDTDEL
     VSIRNASRAC SGLMSEYFVE EMSRLLDEEK QMTHKALSAR VDAKIDDAKF FNKLGKLPAE
     FDAQQIDWAY GPVIQSGGKY DLRLTAVSDN SNLEPGIIIA GFGIRYKTYS SMIARTYLVD
     PSKSQETNYA FLLALHEAVM RDVRDGTIAK DLYNKAINLI RTKKPELESH FVKSVGAGIG
     IELRDPNMVL NGKNSRTLKS GMTLSITVGL TDVEDPELKG SKSSTYSMII TDTVRVGENG
     PHVFTKDAGL DMDSVSFYFG DEEEPQKPIK EKKEAKTSAI ASRNITRTKL RAERPTQINE
     GAEARRREHQ KELAAKKTRE GLDRFAGTTG DDNGVTQKKF KRFESYKRDN QLPTKVRELT
     IYVDQKASTV IVPIMGRPVP FHINTIKNAS KSDEGEYAYL RINFLSPGQG VGRKDDQPFE
     DLSAHFLRNL TLRSKDNERL AQVAQDITEL RKNALRREQE KKEMEDVVEQ DKLIEIRNRR
     PVKLPDVYLR PPLDGKRVPG EVEIHQNGLR YMSPFRNEHV DVLFSNVKHL FFQPCAHELI
     VLIHVHLKTP IMIGKRKTRD VQFYREATEM QFDETGNRRR KHRYGDEEEF EAEQEERRRR
     AALDREFKAF AEKIADAGKD EGVDVDIPFR EIGFTGVPNR SNVLIQPTTD ALVQLTEPPF
     LVITLNEIEI AHLERVQFGL KNFDLVFVFK DFHRAPVHIN TIPVESLEGV KDWLDSVDIA
     FTEGPLNLNW TTIMKTVVSD PYGFFADGGW SFLAAESDSE DGSEEEEESA FELSESELAA
     ADESSEDDSE FDDDASAEAS DFSAEEESGE DWDELERKAK KKDREGGLDD EEHGKKRKR