ID   SPT16_YARLI             Reviewed;        1003 AA.
AC   Q6C931;
DT   11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   03-AUG-2022, entry version 108.
DE   RecName: Full=FACT complex subunit SPT16;
DE   AltName: Full=Facilitates chromatin transcription complex subunit SPT16;
GN   Name=SPT16; OrderedLocusNames=YALI0D14652g;
OS   Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Dipodascaceae; Yarrowia.
OX   NCBI_TaxID=284591;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CLIB 122 / E 150;
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; CR382130; CAG81019.1; -; Genomic_DNA.
DR   RefSeq; XP_502831.1; XM_502831.1.
DR   AlphaFoldDB; Q6C931; -.
DR   SMR; Q6C931; -.
DR   STRING; 4952.CAG81019; -.
DR   EnsemblFungi; CAG81019; CAG81019; YALI0_D14652g.
DR   GeneID; 2911323; -.
DR   KEGG; yli:YALI0D14652g; -.
DR   VEuPathDB; FungiDB:YALI0_D14652g; -.
DR   HOGENOM; CLU_004627_1_0_1; -.
DR   InParanoid; Q6C931; -.
DR   OMA; HQFFLDG; -.
DR   Proteomes; UP000001300; Chromosome D.
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   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..1003
FT                   /note="FACT complex subunit SPT16"
FT                   /id="PRO_0000245190"
FT   REGION          436..486
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          930..1003
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          428..460
FT                   /evidence="ECO:0000255"
FT   COILED          622..648
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        436..451
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        465..486
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        932..990
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1003 AA;  113416 MW;  1404E18F4B59773F CRC64;
     MEVKISESAF NTRVEKLQGA LNTHKDAFGG ADSVLLLIGK GGDDNPYIKT AVAQNWLLGY
     EFFSTALLVT PKRVIFVTNS SKAVHLEGLK KDDKVEVWVR PKEGGKEVME KLAKVAKEAG
     NKLGVVVKDK FRGPIVDEFE AALKDSGIEK VDIEVGLSHL LEAKDDDEIK SIRVASRAST
     AYLTKFFTDQ MLGIVDEERR LSHSKFSEQI ENKLQDEGFF AQNQVKLGSD FHQTNLEWCY
     MPIIQSGGKY DLRPSAVSDD ANLHGGTIVC TLGTRYKGYC SNVGRTFMIN PTKAQEQNYE
     VLVGLREKVF DSIKVGAKAC DVYNAAVSYI KSKAPKLEAH LLKTIGWSIG IDFRDAKFLL
     NAKCQREIVD GSTFDVSLGF QNLTNSAATD PKNKTYSLAL VDTVRVTRAG VAVLTDSAPV
     ALSEVTYFFE DDDEDAEKEK KKKEQAKKEK KQQQAAATVS SITRTKLRHE ARAEDNNDQK
     RKDDQKALHE KLNKAGLERF KNTEGALNGE EKVVIKKFES YKRDTQLPQN LLKDLRVHVD
     TRSQSIILPI NGRPVPFHIN TYKSGSKTDE GDYVYIRLNL SSPGQIAGSK KDAPQVFEDP
     DAQFLRSITF RSRHVEHMND VFKQIQDLKK ASTKKEAEKK EMEDVVAQDS LVEVRARRPL
     KLDAVFVRPA PDGKRVAGTL EIHQNGLRYV SPIRSDHKID VLFDNIKHLF FQPTEGELIV
     CIHAHLKNPI LIGKKKTWDV QFYREASDMA FDETGNRKRK YRYGDEDELE AEQEERRRRL
     QLDKEFKAFS EKISEASDRK VDVDTPFREL GFHGVPFRSN VLLQPSADCL VQLIDTPFSV
     ITLGEIELAH LERVQFGLKN FDLVFVYKDF NRPVTHINSI PVDQLDAVKD WLNEVEIPYS
     EGPVNLNWGS IMKTVVADPQ EFFTSGGWSF LDLESDDEDQ EEEESEFEVS DDEPEDEDED
     SEEFASEDDS EGDFDSEEES GEDWDELEKQ AAAEDGEPPR KKR