ID   SPT16_USTMA             Reviewed;        1032 AA.
AC   Q4P2U5; A0A0D1DVT3;
DT   11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2005, sequence version 1.
DT   25-MAY-2022, entry version 100.
DE   RecName: Full=FACT complex subunit SPT16;
DE   AltName: Full=Facilitates chromatin transcription complex subunit SPT16;
GN   Name=SPT16; ORFNames=UMAG_05568;
OS   Ustilago maydis (strain 521 / FGSC 9021) (Corn smut fungus).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC   Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Ustilago.
OX   NCBI_TaxID=237631;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=521 / FGSC 9021;
RX   PubMed=17080091; DOI=10.1038/nature05248;
RA   Kaemper J., Kahmann R., Boelker M., Ma L.-J., Brefort T., Saville B.J.,
RA   Banuett F., Kronstad J.W., Gold S.E., Mueller O., Perlin M.H.,
RA   Woesten H.A.B., de Vries R., Ruiz-Herrera J., Reynaga-Pena C.G.,
RA   Snetselaar K., McCann M., Perez-Martin J., Feldbruegge M., Basse C.W.,
RA   Steinberg G., Ibeas J.I., Holloman W., Guzman P., Farman M.L.,
RA   Stajich J.E., Sentandreu R., Gonzalez-Prieto J.M., Kennell J.C., Molina L.,
RA   Schirawski J., Mendoza-Mendoza A., Greilinger D., Muench K., Roessel N.,
RA   Scherer M., Vranes M., Ladendorf O., Vincon V., Fuchs U., Sandrock B.,
RA   Meng S., Ho E.C.H., Cahill M.J., Boyce K.J., Klose J., Klosterman S.J.,
RA   Deelstra H.J., Ortiz-Castellanos L., Li W., Sanchez-Alonso P.,
RA   Schreier P.H., Haeuser-Hahn I., Vaupel M., Koopmann E., Friedrich G.,
RA   Voss H., Schlueter T., Margolis J., Platt D., Swimmer C., Gnirke A.,
RA   Chen F., Vysotskaia V., Mannhaupt G., Gueldener U., Muensterkoetter M.,
RA   Haase D., Oesterheld M., Mewes H.-W., Mauceli E.W., DeCaprio D., Wade C.M.,
RA   Butler J., Young S.K., Jaffe D.B., Calvo S.E., Nusbaum C., Galagan J.E.,
RA   Birren B.W.;
RT   "Insights from the genome of the biotrophic fungal plant pathogen Ustilago
RT   maydis.";
RL   Nature 444:97-101(2006).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=521 / FGSC 9021;
RA   Gueldener U., Muensterkoetter M., Walter M.C., Mannhaupt G., Kahmann R.;
RL   Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
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; CM003157; KIS66580.1; -; Genomic_DNA.
DR   RefSeq; XP_011391874.1; XM_011393572.1.
DR   AlphaFoldDB; Q4P2U5; -.
DR   SMR; Q4P2U5; -.
DR   STRING; 5270.UM05568P0; -.
DR   PRIDE; Q4P2U5; -.
DR   EnsemblFungi; KIS66580; KIS66580; UMAG_05568.
DR   GeneID; 23565423; -.
DR   KEGG; uma:UMAG_05568; -.
DR   VEuPathDB; FungiDB:UMAG_05568; -.
DR   eggNOG; KOG1189; Eukaryota.
DR   HOGENOM; CLU_004627_1_0_1; -.
DR   InParanoid; Q4P2U5; -.
DR   OMA; HQFFLDG; -.
DR   OrthoDB; 145488at2759; -.
DR   Proteomes; UP000000561; Chromosome 18.
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   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..1032
FT                   /note="FACT complex subunit SPT16"
FT                   /id="PRO_0000245189"
FT   REGION          443..485
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          936..1032
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          633..653
FT                   /evidence="ECO:0000255"
FT   COILED          778..803
FT                   /evidence="ECO:0000255"
FT   COILED          996..1017
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        953..998
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        999..1032
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1032 AA;  116222 MW;  1144EC811A7AB63C CRC64;
     MSEQIQIDTG AFQRRVNKLL SCWKDSSADF EQLNQVDSLL VVMGGQNDDL IYSKTTAIHS
     WLLGYEFPST VILFTKDSVT FVTSASKAVH LEPLKRSSTG FNLEILKRSK DEASNRALWD
     DLVSRIDAQG SKVGCLPKDK PIGKFADEWQ SVFEKAQSSK DFKMIDVSAS LSAVWATKDD
     DEIKAIRYAS KMSSAVMSGY FENEMSTILD EGKKVTHEQL SERIEGKLDD TKLWKRVKGL
     EGADLSLADW CYTPIVQSGG EYDLKTSAVS STKRLQGADG NGGVVIASMG IKYRNYCSNI
     GRTYLIDPHN SQQKMYAFLH EIQTQLADKH LRAGATCKEI YSKAVEIVRA KDEKLVASFV
     KNVGFGIGLE FRDSAYVLSA KNNRALQRDM VVNLSVGFQD LDDPNHKGEV YSLLLIDTLR
     INDNAPATFL TDRVRGTNDM SFFFKDDEEE EEEEERRSPA KPDGKVTPGG KVLRNKNRGA
     AHDDTAAEKM KLHQKELAKQ KQEDGLARFA GEDGEGNASN EKVFKKFESY KRENLLPTKV
     ADLKIMVDHR AQSIILPIYG YAVPFHINTL KNVSKSDEGE YTYLRLNFVT PGQIAGKKED
     VPFDDPDATF VRSMSYRSSD SSRFTELFRE ITELRKSATK REAEEKELAD VVEQDKLILT
     KSRAYTLPEV FPRPAMEGKR VPGDLTIHQN GLRFSSPLRP DQKIDLLFSN MKHLFFQPCD
     KELIVIVHIH LKSPIMIGKR KAKDIQFYRE ASDVQFDETG NRKRKYRSGD EDEIELEQEE
     RRRRSQLNKE FKVFAERIAE ASEGRVSVDV PYRELGFNGV PFRTNVLLQP TTDCLVHLTD
     PPFLVITLTD VEIVHLERVQ FGLQSFDMVF VFSDFSRAPM HVTSIPTTSL DDVKQWLDSV
     DICVTEGAVN LNWGAIMKTV NEDPYDFFAE GGWGFLQSGS DDGGSSESES GSEFGSEMDD
     GQEETDEDSD SGSDFGDSAE DESGSEGFED ESEEGEDWDE LERKAARADE KKRRQQGGSD
     DDEDSGKKGK RR