ID   SPT6_NEUCR              Reviewed;        1402 AA.
AC   Q8NIV6; Q7S2H2;
DT   30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   03-AUG-2022, entry version 123.
DE   RecName: Full=Transcription elongation factor spt-6;
DE   AltName: Full=Chromatin elongation factor spt-6;
GN   Name=spt-6; ORFNames=NCU04611;
OS   Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS   FGSC 987).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX   NCBI_TaxID=367110;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX   PubMed=12712197; DOI=10.1038/nature01554;
RA   Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA   Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA   Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA   Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA   Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA   Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA   Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA   Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA   Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA   Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA   DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA   Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA   Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA   Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT   "The genome sequence of the filamentous fungus Neurospora crassa.";
RL   Nature 422:859-868(2003).
CC   -!- FUNCTION: Plays a role in maintenance of chromatin structure during RNA
CC       polymerase II transcription elongation thereby repressing transcription
CC       initiation from cryptic promoters. Mediates the reassembly of
CC       nucleosomes onto the promoters of at least a selected set of genes
CC       during repression; the nucleosome reassembly is essential for
CC       transcriptional repression (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the SPT6 family. {ECO:0000305}.
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DR   EMBL; AL807374; CAD37051.1; -; Genomic_DNA.
DR   EMBL; CM002240; EAA29618.1; -; Genomic_DNA.
DR   RefSeq; XP_958854.1; XM_953761.2.
DR   AlphaFoldDB; Q8NIV6; -.
DR   SMR; Q8NIV6; -.
DR   STRING; 5141.EFNCRP00000005865; -.
DR   PRIDE; Q8NIV6; -.
DR   EnsemblFungi; EAA29618; EAA29618; NCU04611.
DR   GeneID; 3875001; -.
DR   KEGG; ncr:NCU04611; -.
DR   HOGENOM; CLU_001680_0_1_1; -.
DR   InParanoid; Q8NIV6; -.
DR   Proteomes; UP000001805; Chromosome 2, Linkage Group V.
DR   GO; GO:0000791; C:euchromatin; IEA:EnsemblFungi.
DR   GO; GO:0005721; C:pericentric heterochromatin; IEA:EnsemblFungi.
DR   GO; GO:0008023; C:transcription elongation factor complex; IBA:GO_Central.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0042393; F:histone binding; IBA:GO_Central.
DR   GO; GO:0031491; F:nucleosome binding; IBA:GO_Central.
DR   GO; GO:0001073; F:transcription antitermination factor activity, DNA binding; IEA:EnsemblFungi.
DR   GO; GO:0000433; P:carbon catabolite repression of transcription from RNA polymerase II promoter by glucose; IEA:EnsemblFungi.
DR   GO; GO:0140673; P:co-transcriptional chromatin reassembly; IEA:EnsemblFungi.
DR   GO; GO:0042789; P:mRNA transcription by RNA polymerase II; IBA:GO_Central.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IEA:EnsemblFungi.
DR   GO; GO:0006334; P:nucleosome assembly; IEA:EnsemblFungi.
DR   GO; GO:0034728; P:nucleosome organization; IBA:GO_Central.
DR   GO; GO:0016973; P:poly(A)+ mRNA export from nucleus; IEA:EnsemblFungi.
DR   GO; GO:0032968; P:positive regulation of transcription elongation from RNA polymerase II promoter; IBA:GO_Central.
DR   GO; GO:0071931; P:positive regulation of transcription involved in G1/S transition of mitotic cell cycle; IEA:EnsemblFungi.
DR   GO; GO:0000414; P:regulation of histone H3-K36 methylation; IEA:EnsemblFungi.
DR   GO; GO:0031440; P:regulation of mRNA 3'-end processing; IEA:EnsemblFungi.
DR   GO; GO:0043618; P:regulation of transcription from RNA polymerase II promoter in response to stress; IEA:EnsemblFungi.
DR   GO; GO:0001178; P:regulation of transcriptional start site selection at RNA polymerase II promoter; IEA:EnsemblFungi.
DR   GO; GO:0006368; P:transcription elongation from RNA polymerase II promoter; IBA:GO_Central.
DR   CDD; cd09928; SH2_Cterm_SPT6_like; 1.
DR   CDD; cd09918; SH2_Nterm_SPT6_like; 1.
DR   Gene3D; 1.10.10.2740; -; 1.
DR   Gene3D; 1.10.10.650; -; 1.
DR   Gene3D; 1.10.3500.10; -; 1.
DR   Gene3D; 2.40.50.140; -; 1.
DR   Gene3D; 3.30.420.140; -; 1.
DR   Gene3D; 3.30.505.10; -; 2.
DR   InterPro; IPR041692; HHH_9.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR012337; RNaseH-like_sf.
DR   InterPro; IPR010994; RuvA_2-like.
DR   InterPro; IPR022967; S1_dom.
DR   InterPro; IPR003029; S1_domain.
DR   InterPro; IPR036860; SH2_dom_sf.
DR   InterPro; IPR028083; Spt6_acidic_N_dom.
DR   InterPro; IPR042066; Spt6_death-like.
DR   InterPro; IPR032706; Spt6_HHH.
DR   InterPro; IPR028088; Spt6_HTH_DNA-bd_dom.
DR   InterPro; IPR035420; Spt6_SH2.
DR   InterPro; IPR035018; Spt6_SH2_C.
DR   InterPro; IPR035019; Spt6_SH2_N.
DR   InterPro; IPR028231; Spt6_YqgF.
DR   InterPro; IPR023323; Tex-like_dom_sf.
DR   InterPro; IPR023319; Tex-like_HTH_dom_sf.
DR   InterPro; IPR017072; TF_Spt6.
DR   InterPro; IPR037027; YqgF/RNaseH-like_dom_sf.
DR   PANTHER; PTHR10145; PTHR10145; 1.
DR   Pfam; PF14635; HHH_7; 1.
DR   Pfam; PF17674; HHH_9; 1.
DR   Pfam; PF14641; HTH_44; 1.
DR   Pfam; PF00575; S1; 1.
DR   Pfam; PF14633; SH2_2; 1.
DR   Pfam; PF14632; SPT6_acidic; 1.
DR   Pfam; PF14639; YqgF; 1.
DR   PIRSF; PIRSF036947; Spt6; 1.
DR   SMART; SM00316; S1; 1.
DR   SUPFAM; SSF47781; SSF47781; 2.
DR   SUPFAM; SSF50249; SSF50249; 1.
DR   SUPFAM; SSF53098; SSF53098; 1.
DR   SUPFAM; SSF55550; SSF55550; 1.
DR   PROSITE; PS50126; S1; 1.
PE   3: Inferred from homology;
KW   Nucleus; Reference proteome; SH2 domain; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..1402
FT                   /note="Transcription elongation factor spt-6"
FT                   /id="PRO_0000238578"
FT   DOMAIN          1094..1161
FT                   /note="S1 motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00180"
FT   DOMAIN          1209..1306
FT                   /note="SH2"
FT   REGION          1..199
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        11..26
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        74..92
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        105..162
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        173..199
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        117
FT                   /note="Q -> QQTKFK (in Ref. 1; EAA29618)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1402 AA;  162802 MW;  CAC376F846172974 CRC64;
     MSNSMRDLID GEAELDDEED DESFDEEAGD RPRRRPNIDD SSEEEEDDED EEEARKIREG
     FIVDEDEEDE AEDSDARERR RRKKRRRERE EEEQLDEEDL DLIGEAIPEW ERKPQPQRLK
     RGHRDDHRPT ERRGLAEIFS DEDEEHDDRG YGRPSGRAQA DEFDDFIEDD YPEDDEERRH
     REEDEEVARP KDRGLNIDTT GLDKDALEDM DAIFGNGEDY EWALQLEEEQ EHAERTKEDI
     ELQDVFEPSQ LKEKLLTDED NRIRFNDEPE RFQLDRKAFK NLQMTSDQFK EEARWISNLM
     LPSKNLSSEL HGPFNKAVGK VLEFFVIDGV EVPYVFQHRR DYLIHAKKMR NPNRRDDPDA
     PEYTVDAEKL LTQDDLWKVL DLDIRFRSFL EKRNALEQTY DKLKEKTRDD ILEEMIRQAQ
     SIEELQDLQD YLNFQYSAEL KDLAANDNSA QREIKRAGGR TAQFERIRRS NAYKFVQALG
     ITPDRLAKNI LRESSKVTSE DDSRLPDDLA DTLVDADFPT GELVINAARQ MLAEEMFASP
     RMRKHFRKNF YGMGIVSCRR TDKGLRKIDE ANPYYEVKYL KNMSIADLAV RPELFLKMMK
     AEEEGLIEIK VSLENDREFR QQLFSDFASE NFSELADKWN AERQKVIDLA FDKLVKVIVK
     GVKDSLRTAC QDELLKTCRE LYFKRLDQAP YKPKGMVIGT TPRVLTLSNG MGDPNREPVS
     WVSMDEDGRI LEHGTFTNLA RDESQREALA ELVRRRQPDV IGISGFSADT HRLIKDVEGL
     VSEKGLVGPE YDDPETNEYR SDLLEVIVIN DEVARLYKDS PRAVADHPSL NPMTRYCIAL
     ARYMQNPMKE YAALGKDVTS LQIHPYQQYL PQAKLLKHLE TAMVDMVNLV GVDINVAMQD
     ANTAHLLPYV AGLGPRKAQL LIKGINKNGG VVTSRDELVG DPERHKLPVL GPRVWNNCAS
     FLFIEYEPTN PESDPLDNTR IHPEDYDLAR KVAADALGLD EEDVKAETDE NGAGAIVRKL
     FKDDEQDKVN ELILEEYAEQ LEREYQQRKR ATLETIRAEL QVPYEELRKK FESLTVDQVF
     TMLTGENRDS LCEGMIVAAN VRVVKDDFAI VKLDCGIEGR IESHDVSYRH SIKDVLHVGQ
     VVQAKLIDLN RKEFVSKLSM RDEEMRRPFR RHFDHGRDQW DYRKEDEDRE ELREKDKSTG
     RAQRVVNHPL FKPFNSTQAE EYLGSQPSGE VVIRPSSKGN DHLAVTWKVA DGVFQHVDVL
     ELQKENEFAV GRVLRVGKYT YQDLDELIVD HVKAMAKKVD ELMQCDKFQK GSRNETEKWL
     TTYMDANPNR STYAFCIDTK HPGYFFLCFK ASRNSRVNAW PVRVIPHAFE LMKSQYPDVR
     ALCNGFKLRY QSEMLKQQSG GR