ID   SPT16_ASPOR             Reviewed;        1042 AA.
AC   Q2UBF1;
DT   11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, 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=AO090012001024;
OS   Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=510516;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 42149 / RIB 40;
RX   PubMed=16372010; DOI=10.1038/nature04300;
RA   Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K.,
RA   Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H.,
RA   Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.,
RA   Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D.,
RA   Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A.,
RA   Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y.,
RA   Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H.,
RA   Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T.,
RA   Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O.,
RA   Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y.,
RA   Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N.,
RA   Kikuchi H.;
RT   "Genome sequencing and analysis of Aspergillus oryzae.";
RL   Nature 438:1157-1161(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; AP007161; BAE61114.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q2UBF1; -.
DR   SMR; Q2UBF1; -.
DR   STRING; 510516.Q2UBF1; -.
DR   EnsemblFungi; BAE61114; BAE61114; AO090012001024.
DR   HOGENOM; CLU_004627_1_0_1; -.
DR   OMA; HQFFLDG; -.
DR   Proteomes; UP000006564; Chromosome 4.
DR   GO; GO:0035101; C:FACT complex; IEA:InterPro.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
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; 2.
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..1042
FT                   /note="FACT complex subunit spt16"
FT                   /id="PRO_0000245180"
FT   REGION          464..519
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          776..795
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          958..1042
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          498..522
FT                   /evidence="ECO:0000255"
FT   COILED          636..672
FT                   /evidence="ECO:0000255"
FT   COILED          796..819
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        465..480
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        489..519
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        962..1015
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1016..1042
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1042 AA;  117534 MW;  9DF5F02560039887 CRC64;
     MAEEIVIDKS AFFNRLSSFF AAWKADKRPG HAVFGGVGSI VILMGKTDEA NSFQKNNAMH
     FWLLGYEFPA TLMVFTTDMM YVVTTAKKGE DWPNTDSAYL SANTGLLNVA KHLEPLKGGK
     IPVEILVTSK DPDEKSRSFE KCLEVIKNAG KRVGVLPKDT AAGPFAEDWK RAFANITQDV
     EEVDISPALS SAAFSVKDTD ELVAIRNASR ACSGLMSEYF VDEMSRLLDE EKQMTHKALS
     MRIDAKIDDA KFFKKLAKLP AEFDPQQIDW AYGPVIQSGG KYDLRLTATS DNSHLQAGII
     VAGFGIRYKT YSSIIARTYL VDPSKSQEAN YAFLLNLHDT VMKDVRDGTM AKDLFNKAIG
     LVRAKKPELE SHFVKSVGAG IGIELRDSNM VLNGKNNKIL KSGMTLSITV GLTDVEELES
     KDKNTAVYSM IITDTVRVGE NGPHIFTKDA GIDMDSVSFY FGDEEEPQKP AKEKKEVKSN
     AMTSRNVTRT KLRAERPTQV NEGAEARRRE HQKELATKKT KEGLDRFAGT TGDDNGVTQK
     KFKRFESYKR DNQLPTKVKD LTIYVDHKAS TVIVPIMGRP VPFHINTIKN ASKSDEGEYA
     YLRINFLSPG QGVGRKDDQP FEDISAHFLR NLTLRSKDNE RLAQVAQDIT ELRKNALRRE
     QEKKEMEDVV EQDKLVEIRN RRPVRLPDVY LRPPLDGKRV PGEVEIHQNG LRYMSPFRNE
     HVDVLFSNVK HLFFQPCAHE LIVLIHVHLK TPIMIGKRKT RDVQFYREAT EMQFDETGNR
     RRKHRYGDEE EFEAEQEERR RRAALDREFK AFAEKIADAG KDEGVDVDIP FREIGFTGVP
     NRSNVLIQPT TDALVQLTEP PFLVITLNEI EIAHLERVQF GLKNFDLVFV FKDFHRPPVH
     VNTIPVESLE GVKDWLDSVD IAFTEGPLNL NWTTIMKTVV SDPYGFFADG GWSFLAAESD
     SEGGASDEEE SAFELSESEL AAADESSEDD SEFDDDASAE ASEDFSADED SGEDWDELER
     KAKKKDRESG LDDEERGKKR KR