SPT6_ASPOR
ID SPT6_ASPOR Reviewed; 1422 AA.
AC Q2U561;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Transcription elongation factor spt6;
DE AltName: Full=Chromatin elongation factor spt6;
GN Name=spt6; ORFNames=AO090020000058;
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: 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; AP007167; BAE63304.1; -; Genomic_DNA.
DR RefSeq; XP_001824437.1; XM_001824385.2.
DR AlphaFoldDB; Q2U561; -.
DR SMR; Q2U561; -.
DR STRING; 510516.Q2U561; -.
DR PRIDE; Q2U561; -.
DR EnsemblFungi; BAE63304; BAE63304; AO090020000058.
DR GeneID; 5996523; -.
DR KEGG; aor:AO090020000058; -.
DR VEuPathDB; FungiDB:AO090020000058; -.
DR HOGENOM; CLU_001680_0_1_1; -.
DR OMA; LCNGFKT; -.
DR Proteomes; UP000006564; Chromosome 6.
DR GO; GO:0000791; C:euchromatin; IEA:EnsemblFungi.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005721; C:pericentric heterochromatin; IEA:EnsemblFungi.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0042393; F:histone binding; IEA:EnsemblFungi.
DR GO; GO:0031491; F:nucleosome binding; IEA:EnsemblFungi.
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; IEA:EnsemblFungi.
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: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; IEA:EnsemblFungi.
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 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; 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; PF14633; SH2_2; 1.
DR Pfam; PF14632; SPT6_acidic; 1.
DR Pfam; PF14639; YqgF; 1.
DR PIRSF; PIRSF036947; Spt6; 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..1422
FT /note="Transcription elongation factor spt6"
FT /id="PRO_0000238570"
FT DOMAIN 1114..1183
FT /note="S1 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00180"
FT DOMAIN 1231..1331
FT /note="SH2"
FT REGION 1..164
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1185..1221
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 10..27
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 43..57
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 73..94
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 121..139
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1196..1217
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1422 AA; 163737 MW; 8C2D99BCE86C7719 CRC64;
MSARDLVEGE AMLDDEENEE ELADDYDGEG EAHQGAGTAN PYDSSEEDDD DDDDEEAARA
VREGFIVDED EELEDRAERR REKRKRRREE REREDEHLDE EDLELIGELN PSLQAPVAAE
SKFKRLKRGH KDRDLRQPSQ GIDDIFNSDE EEEAAGDYGR HGHRRHMHDE MDDFIEEDVF
SDEELQRERE DLEIARPAKK GMTGLGATDA AGLDENALED MRAAFGDGNE YLFALEMEDQ
EEEQEEDEEK HLDLKDVFEP SQLAEKMLTE EDNQIRLLDE PERHQIARKP YRNVVLTEEQ
FREEAAWISN LMLLKKRIEP ELREPFQRSV AKVLEFLVTD DWEVPFIFQH RKDYMIHAVK
APVEGAGEDG DASQYTVRAE KLLNMTDLWD IFDHDLKFKA LVEKRNTIQK TYDNLQSLFN
VSDSVVEEML PAAVTMEELQ DVQDYIHFQY ASQLRDMTLM NSDVNGETHR RKASSKTFFE
RVRNGKAYGL VRAFGITADA FAQNALKEGR RQYTEDPAER PEEMADGFVD NDFSNASHVI
KAAKSLFAEE IVMSPKMRKV IRQAYYMNGA VDCFRTEKGL RRIDEQHPYY EFKYLRNQQL
SDIARRPELY LRMLKAEEEG LVEVKVRFEN FDQFRQRLYP DIESDNYSEI ADGWNRSRRD
VLDMALGKLE RLINRSVKEN IRQECENHVA KECRETFSQR LDQAPYKPKG MVLGTVPRVL
ALSTGSGVVG REPIHWAYIE EDGRVLENGK FVDLSIGDRD RNIPDGKDVE AFVELVDRRR
PDVIGVSGMS PETRRLYKLL AEVVDKKDLR GAPYTDDHDE EISDRLEVII VNDEVARLYQ
HSERAKKDHP SFAPLTHYCV ALAKYLQSPL KEYASLGRDI VSIQFKPGQQ LVTQELLLKQ
LETALVDMVN LVGVDINEAV TDSSTANLLP YVCGLGPRKA AHLLKIVNMN GGVVNNRVEL
LGVNAQYPAM GVKVWNNCAS FLYIDFENVD PDADPLDNTR VHPEDYDIAR KMAADALELD
EEDIKAETDE NGTGAIVRKL FREEAQDRVN DLILEEYAEQ LEKNLNQRKR ATLETIRAEL
QQPYEELRKQ YVFLSTDDIF TMLTGETSDT LAEGMVVPIS IKRVSDDHID GKLDCGIDAL
VPESELTDRY DIPVRALYSP HQTVSAKILF LNRKNFTCNV SLREEQVSRP VSNTQDRLRG
EWDERQEQQD RESLQEKTQS GGRTMRVIKH PLFRPFNSTQ AEEFLGSQSR GDVVIRPSSK
GHDHLAVTWK VADGIFQHID VLELDKENEF SVGRTLKVGG RYTYSDLDDL IFNHVKAMAK
KVDEMMLHEK YQDGTKDATY SWLETYTKAN PKRSAYAFCI DPKHAGYFFL CFKAGENARL
HSWPVKVIPQ GYELQRNPYP DMRALCNGFK LLFTNMQAGK RR
