ID   SPT16_CRYNJ             Reviewed;        1035 AA.
AC   P0CQ22; Q55VJ3; Q5KKP5;
DT   28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT   28-JUN-2011, sequence version 1.
DT   25-MAY-2022, entry version 56.
DE   RecName: Full=FACT complex subunit SPT16;
DE   AltName: Full=Facilitates chromatin transcription complex subunit SPT16;
GN   Name=SPT16; OrderedLocusNames=CNC02310;
OS   Cryptococcus neoformans var. neoformans serotype D (strain JEC21 / ATCC
OS   MYA-565) (Filobasidiella neoformans).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC   Tremellales; Cryptococcaceae; Cryptococcus;
OC   Cryptococcus neoformans species complex.
OX   NCBI_TaxID=214684;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JEC21 / ATCC MYA-565;
RX   PubMed=15653466; DOI=10.1126/science.1103773;
RA   Loftus B.J., Fung E., Roncaglia P., Rowley D., Amedeo P., Bruno D.,
RA   Vamathevan J., Miranda M., Anderson I.J., Fraser J.A., Allen J.E.,
RA   Bosdet I.E., Brent M.R., Chiu R., Doering T.L., Donlin M.J., D'Souza C.A.,
RA   Fox D.S., Grinberg V., Fu J., Fukushima M., Haas B.J., Huang J.C.,
RA   Janbon G., Jones S.J.M., Koo H.L., Krzywinski M.I., Kwon-Chung K.J.,
RA   Lengeler K.B., Maiti R., Marra M.A., Marra R.E., Mathewson C.A.,
RA   Mitchell T.G., Pertea M., Riggs F.R., Salzberg S.L., Schein J.E.,
RA   Shvartsbeyn A., Shin H., Shumway M., Specht C.A., Suh B.B., Tenney A.,
RA   Utterback T.R., Wickes B.L., Wortman J.R., Wye N.H., Kronstad J.W.,
RA   Lodge J.K., Heitman J., Davis R.W., Fraser C.M., Hyman R.W.;
RT   "The genome of the basidiomycetous yeast and human pathogen Cryptococcus
RT   neoformans.";
RL   Science 307:1321-1324(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; AE017343; AAW42200.1; -; Genomic_DNA.
DR   RefSeq; XP_569507.1; XM_569507.1.
DR   AlphaFoldDB; P0CQ22; -.
DR   SMR; P0CQ22; -.
DR   STRING; 5207.AAW42200; -.
DR   PaxDb; P0CQ22; -.
DR   EnsemblFungi; AAW42200; AAW42200; CNC02310.
DR   GeneID; 3256484; -.
DR   KEGG; cne:CNC02310; -.
DR   VEuPathDB; FungiDB:CNC02310; -.
DR   eggNOG; KOG1189; Eukaryota.
DR   HOGENOM; CLU_004627_1_0_1; -.
DR   InParanoid; P0CQ22; -.
DR   OMA; HQFFLDG; -.
DR   OrthoDB; 145488at2759; -.
DR   Proteomes; UP000002149; Chromosome 3.
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..1035
FT                   /note="FACT complex subunit SPT16"
FT                   /id="PRO_0000245183"
FT   REGION          440..471
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          944..1035
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          637..657
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        949..982
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        999..1035
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1035 AA;  115812 MW;  8A2C2014A3816F3D CRC64;
     MSDIRLDSAT FFKRAAKIFD SWEKPSGDTQ ALEDINSIAI ILGDPNDEVA SYTKTTALQL
     WLLGYEFPST LMVFEKSPRK VTFVCGSSKA KLIRQLQPSD GIEIDVKVRS KDATAAKETM
     EEVVASLNGK FGSLPKDRPI GKLVDEWNSA VESKGDLEVV DVAIPISAVL AEKDGEELKT
     IITSAKLTST VMINYFKSKM ESIIDRGTKM SHEALAQLVE EKIGNEEKGP DMKLWNKNPS
     LGEIDFASSE FVYSPVIQSG GKYDLKVTAA SNNDNLKPGI ILANMGIRYK NYCSNMGRTF
     LISPSKKQET QYTTLLEVRK EALALLKTGA VASDVYNSVH QSLETKNATL ADSFLKNLGF
     ATGMEYRDSS FLLNAKNNRE LKENMVLVLT IGVADLPDAK NKGKTYSLLL SDTVKIGQNG
     AVVLTEGCTR LSDVVMDMEE EEEEDVKPQI DKKPKINNSP KKPRSSTVGG RVLNAKTRGA
     NREQATQTTA EKIKTNQQRL HAQLNADGVK RWEADAGGKN GAQQKVVKRY ESYRREEQLP
     RAVEDRRIYV DEQRQSVVLP INGYAVPYHI STIKNVTKTE ESNHMVLRIN FQSPGQIAGK
     KEDMPFEDPD ANFIRSVSFR SQDQRHMLKV YEAITALKKA AVKRETERKE LADVIEQEKL
     IEVKGRHPYV LKNVFPRPGP EGKKTDGNVE IHQNGIRFRP DGPASKIDIL FSNIKHLFFQ
     PSEKELIVII HVHLKAPIML GKKKTSDVQF YREVADMSFD ETGGKKRRAR YGDEDEIEQE
     QEDRKRRAEL DKLFHDFARR IETAAQAQQF ELEVDVPFRE LGFNGVPHKS IVALLPTTNC
     LIHISELPFT VITLSEVEIV HLERVQFGLK NFDMVFVLQD LKKPPVHINS IPVAHLDNVK
     EWLDSCDVPI SEGPVNLSWP AIMKTVNEDP HAFYAEGGWN FLTGSGSDDG SEESEEGSEF
     EGDSDVFDES SGSDEDSESA FEGDSDSASA ESLSDEGEDW DELERKAKRA DEKHRTDRGG
     DSDDDGKKKK KGSRR