SPT6_ASHGO
ID SPT6_ASHGO Reviewed; 1432 AA.
AC Q75EP8;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2013, sequence version 2.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Transcription elongation factor SPT6;
DE AltName: Full=Chromatin elongation factor SPT6;
GN Name=SPT6; OrderedLocusNames=AAR031W;
OS Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS (Yeast) (Eremothecium gossypii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX NCBI_TaxID=284811;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=15001715; DOI=10.1126/science.1095781;
RA Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA Gaffney T.D., Philippsen P.;
RT "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT cerevisiae genome.";
RL Science 304:304-307(2004).
RN [2]
RP GENOME REANNOTATION, AND SEQUENCE REVISION TO 262 AND 1302.
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=23749448; DOI=10.1534/g3.112.002881;
RA Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT loci, numerous translocations, lack of transposons, and distinct gene
RT duplications.";
RL G3 (Bethesda) 3:1225-1239(2013).
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; AE016814; AAS50396.2; -; Genomic_DNA.
DR RefSeq; NP_982572.2; NM_207925.2.
DR AlphaFoldDB; Q75EP8; -.
DR SMR; Q75EP8; -.
DR STRING; 33169.AAS50396; -.
DR EnsemblFungi; AAS50396; AAS50396; AGOS_AAR031W.
DR GeneID; 4618537; -.
DR KEGG; ago:AGOS_AAR031W; -.
DR eggNOG; KOG1856; Eukaryota.
DR HOGENOM; CLU_001680_0_1_1; -.
DR InParanoid; Q75EP8; -.
DR OMA; LCNGFKT; -.
DR Proteomes; UP000000591; Chromosome I.
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; -; 2.
DR Gene3D; 3.30.420.140; -; 1.
DR Gene3D; 3.30.505.10; -; 2.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR010994; RuvA_2-like.
DR InterPro; IPR000980; SH2.
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; IPR006641; YqgF/RNaseH-like_dom.
DR InterPro; IPR037027; YqgF/RNaseH-like_dom_sf.
DR PANTHER; PTHR10145; PTHR10145; 1.
DR Pfam; PF14635; HHH_7; 1.
DR Pfam; PF14641; HTH_44; 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; SM00252; SH2; 1.
DR SMART; SM00732; YqgFc; 1.
DR SUPFAM; SSF47781; SSF47781; 1.
DR SUPFAM; SSF53098; SSF53098; 1.
DR SUPFAM; SSF55550; SSF55550; 1.
DR PROSITE; PS50001; SH2; 1.
PE 3: Inferred from homology;
KW Nucleus; Reference proteome; SH2 domain; Transcription;
KW Transcription regulation.
FT CHAIN 1..1432
FT /note="Transcription elongation factor SPT6"
FT /id="PRO_0000238568"
FT DOMAIN 1232..1329
FT /note="SH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00191"
FT REGION 1..215
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 8..24
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 25..51
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 52..74
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 84..150
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 160..178
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 193..208
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1432 AA; 166707 MW; 68BB80552D246416 CRC64;
MSSEGLASAR ELEERDLGAT RDTEEIPSDE EEGEDVFDSS EEDEDLDEDE EEARKVKEGF
IVSDDEEDDS SVKQRRRRKH KRRPRHEEDD GKLSEDDLDL LMENAGVKRT TRPETDATKG
RFKRLKRAGS PDESEGQQDT DGRHENRLED FFSEEEDEEH LGGTENRRLR TGGKDVLDEL
DDFIEEDEFS DEDEATRQQR RKLKEQRSKQ SVQITGLSSD KIDEMYDIFG DGHDYDWALA
VENEDDLENL DEYQQEEDDD ETSDQKAKKK KITLQDIYDM QDLKKNLMTE EDMVIRRSDI
PERYQELRAG LKNYGQLTPE DQLLEQNWIS DKIAVDKNFD ATYDISEFRE AVGDAVRFIS
KENLEVSFIY AYRRNYISSR DKNGFILSED DLWDIVFYDI EFHSIIYKRD YVKKFYEQLG
IRDSLVDDYF NDESMTELNS LQDIYNYLEF RYAHEINDAL LADSSSKTKK HLKNSSYEKF
KSSSLYQAVK DVGITAEQIG ENIGAETQIH PVVDHPNLKP SESISQILDA ASADLQVFAK
NHKLAWDTVQ KYFAAEIGNN PKVRQKIRND FYKYYIVDVV LTTKGRKEIQ RSSPYEDIKY
AINRTPGHFR SAPDVFLRML EAESLHLMNI KIHMSSQEQY CEHLFQIALE TTNTSEIAIE
WNNFRRNAFY QALEKIFEDI AQEIKDELKK TSQKLVANSV RHRFMSKLDQ APFIPNPREP
KIPRVLTITC GQGRFGLDAI IAVLLNRKGD FVKDFKIVQN PFDRDQPQAF EAVLDNIIQE
AQPNVIGING PNPKTQKLFK KIQEVIQKKQ IVDNRGHNIP VIFVEDEIAI RYQSSERGAQ
EFPNKPTLVK YCIALARYIH SPLLEYTNLS EEELQSLLIH PHQSLLPRHI FKRALETSFV
DIVNLVGVEV NKANDNPYYA KALQYIAGLG KRKAIDFLES LQRLNEPLLA RQQLITHDIL
HKTIFMNSAG FLYISWNEKN QRYEDLEHDH LDSTRIHPED YHLATKVAAD ALEYDPDAIR
EKEEQGAMSE FIELLRDDPD RRMKLESLNL EEYADELERS TGQRKLNNLN TIVLELLEGF
EELRNDFHPL QGDEIFTSLT GETDKTFFKG SIIPVRVERF KHNDIICISN SQVECIVNAQ
RHLGVQLKRP ASDIYEVGKT YPAKIIFIDY ENISAEVSLL DHDVKHQYIP VDYSKDPTIW
NLKQELEDVE EEKKISMAEA RAKRTHRVIN HPYYFPFNGK QAEDYLRSKE RGEFIIRQSS
RGDDHLAITW KLDKDLFQHV DILELDKENP LALGKTLIVD NNKYNDLDHV IVEYLQNKIK
LLNEITSNEK FKKGTKKEVV KFIEDYSNVN PNRSVYYLSF NYEHPGWFYL MFKINAQSKL
CTWNVKLTHN GFSLADYNYP TVIQLCNGFK TLLKSSSRAR TQEASGSGYY GY
