ID   SPT16_EMENI             Reviewed;        1019 AA.
AC   Q5B2X8; C8VEW4;
DT   11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   16-NOV-2011, sequence version 2.
DT   25-MAY-2022, entry version 99.
DE   RecName: Full=FACT complex subunit spt16;
DE   AltName: Full=Facilitates chromatin transcription complex subunit spt16;
GN   Name=spt16; ORFNames=AN5102;
OS   Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS   M139) (Aspergillus nidulans).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Nidulantes.
OX   NCBI_TaxID=227321;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX   PubMed=16372000; DOI=10.1038/nature04341;
RA   Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA   Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA   Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA   Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA   Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA   Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA   Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA   Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA   Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT   "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT   fumigatus and A. oryzae.";
RL   Nature 438:1105-1115(2005).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX   PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA   Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA   Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA   Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA   Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA   Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA   Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA   Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA   van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA   Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA   Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA   Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA   Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA   Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA   van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA   Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA   Oliver S.G., Turner G.;
RT   "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT   effort.";
RL   Fungal Genet. Biol. 46:S2-13(2009).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=EAA62283.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AACD01000088; EAA62283.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; BN001305; CBF80864.1; -; Genomic_DNA.
DR   RefSeq; XP_662706.1; XM_657614.1.
DR   AlphaFoldDB; Q5B2X8; -.
DR   SMR; Q5B2X8; -.
DR   STRING; 162425.CADANIAP00003086; -.
DR   PRIDE; Q5B2X8; -.
DR   EnsemblFungi; CBF80864; CBF80864; ANIA_05102.
DR   EnsemblFungi; EAA62283; EAA62283; AN5102.2.
DR   GeneID; 2871397; -.
DR   KEGG; ani:AN5102.2; -.
DR   VEuPathDB; FungiDB:AN5102; -.
DR   eggNOG; KOG1189; Eukaryota.
DR   HOGENOM; CLU_004627_1_0_1; -.
DR   InParanoid; Q5B2X8; -.
DR   OMA; HQFFLDG; -.
DR   OrthoDB; 145488at2759; -.
DR   Proteomes; UP000000560; Chromosome V.
DR   Proteomes; UP000005890; Unassembled WGS sequence.
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_0000245185"
FT   REGION          443..498
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          755..774
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          936..1019
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          477..501
FT                   /evidence="ECO:0000255"
FT   COILED          625..651
FT                   /evidence="ECO:0000255"
FT   COILED          775..798
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        444..459
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        468..498
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        939..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;  115311 MW;  2BE134B5998A2314 CRC64;
     MGDEIVIDKT AFFNRLSSFY AAWKADKRST NSVFGGAGSI IILMGKTDEA NSYQKNNAIH
     FWLLGYEFPA TLFVFTPEVM YVVTTAKKAK HLEPLKGGKI PVEILVTTKD QEEKTRLFEK
     CVDIIKSAGN KVGILPRDTT TGPFVEDWKR VYGKISGDVE EVDISPALSA ACFSVKDTDE
     LVSIRNASRA CSGLMSDYFV DEMSRLLDEE KQMTHKALSM RIDAKIDDAK FFNKLAKLPS
     EFDPQQIDWA YGPVIQSGGK YDLKLTAVSD DNNLEPGIII AGFGIRYKTY SSIIGRTYLV
     DPTKSQEANY SLLLSVHEAV LKEARDGVVA KELYNKAIGI VRARKPELES HFVKNVGAGI
     GIELRDSNMI LNGKNTRVLK SGMTFSITVG LVDVEEPSVK DKKKNVYSMM ITDTVRVGEQ
     GPHVFTKDAG IDMDSVSFYF GDEEEPQKPA KEKKETKSSA IASRNVTRTK LRAERPTQVN
     EGAEARRREH QKELAAKKTK EGLDRFAGTT GDDNGVTQKK FKRFESYKRD NQLPAKVKDL
     TVYVDHKAST VIVPVMGRPV PFHINTIKNA SKSDEGEYAY LRINFLSPGQ GVGRKDDQPF
     EDLSAHFLRN LTLRSKDNDR FAQVAQDITE LRKNALRREQ EKKEMEDVVE QDKLVEIRNR
     RPVKLPDVYL RPPLDGKRVP GEVEIHQNGL RYVSPFRNEH VDVLFSNVKH LFFQPCAHEL
     IVLIHVHLKT PIMIGKRKTR DIQFYREATE MQFDETGNRR RKHRYGDEEE FEAEQEERRR
     RAALDREFKA FAEKIADAGK DEGVDVDIPF REIGFTGVPN RSNVLIQPTT DALVQLTEPP
     FLVISLNEIE IAHLERVQFG LKNFDLVFVF KDFHRAPVHI NTIPVENLEG VKDWLDSVDI
     AYTEGPLNLN WTTIMKTVVS DPYGFFADGG WSFLAAESDS EDGSDEEEES AFELSESELA
     ADESSEEDSD YDDDASADDD FSADEDESGE DWDELEHQAK KKDRESGLDD EDRGKKRKR