SPT6_EMENI
ID SPT6_EMENI Reviewed; 1417 AA.
AC Q5B7Q7; C8VHJ8;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 16-NOV-2011, sequence version 2.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Transcription elongation factor spt6;
DE AltName: Full=Chromatin elongation factor spt6;
GN Name=spt6; ORFNames=AN3423;
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: 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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EAA62900.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AACD01000056; EAA62900.1; ALT_SEQ; Genomic_DNA.
DR EMBL; BN001306; CBF82740.1; -; Genomic_DNA.
DR RefSeq; XP_661027.1; XM_655935.1.
DR AlphaFoldDB; Q5B7Q7; -.
DR SMR; Q5B7Q7; -.
DR STRING; 162425.CADANIAP00009616; -.
DR EnsemblFungi; CBF82740; CBF82740; ANIA_03423.
DR EnsemblFungi; EAA62900; EAA62900; AN3423.2.
DR GeneID; 2874464; -.
DR KEGG; ani:AN3423.2; -.
DR VEuPathDB; FungiDB:AN3423; -.
DR eggNOG; KOG1856; Eukaryota.
DR HOGENOM; CLU_001680_0_1_1; -.
DR InParanoid; Q5B7Q7; -.
DR OMA; LCNGFKT; -.
DR OrthoDB; 56990at2759; -.
DR Proteomes; UP000000560; Chromosome VI.
DR Proteomes; UP000005890; Unassembled WGS sequence.
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; 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; 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.
PE 3: Inferred from homology;
KW Nucleus; Reference proteome; SH2 domain; Transcription;
KW Transcription regulation.
FT CHAIN 1..1417
FT /note="Transcription elongation factor spt6"
FT /id="PRO_0000238575"
FT DOMAIN 1108..1177
FT /note="S1 motif"
FT DOMAIN 1226..1326
FT /note="SH2"
FT REGION 1..109
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 122..185
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1181..1215
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 10..28
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 41..55
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 72..92
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 122..136
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 151..168
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1183..1215
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1417 AA; 163079 MW; 85B1D0D2C2847034 CRC64;
MSARDFVEGE AMLDEEENEE ELVDDYGDGE ERLETGGNHY DSSEEDEDED DDEDAVRAVR
EGFIVDEDEE EEERAERRRE RRKRRREERE REDEHLDEED LELIGELNPG LQYAAAADSK
FKRLKRGHKD RDSRQPSQAI NDFFNSDEED EPAPDYGRHR RHPGDEMDDF IEEDVFSDDE
LQREREDLEV ARPRKTIGFG ATDTTGLDEN ALEDMRAAFG DGNEYDFALA MEEEEEQQEE
DVEKHLDLKD VFEPSQLAEK MLTEEDNQIR LIDEPERHQI ARKPYRNVVL SEDQFREEAA
WIANLMLLKK RLEPELREPF QRSVAKVLEF LVTDDWEVPF IFQHRKDYMI HTVKVPVNGA
SADDSSSQYT IKAEKLLNMT DLWDIFDYDL KFKALVEKRN TIQKTYDNIR SVFSVEDPIV
EEMLPIATTM EELQDIQDYL HFQYASQIRD LTLTNGDTNG EVQRRKALTR NFFERVRNSK
AYGLVRAFGI TADAFAQNAL KEGRRQYTED ASERPEDMAD GLVDNDFNNS SQVLKAAKGM
FAEEIVMSPK MRKVIRQAYY MNGAVDCFRT EKGLRRIDEQ HPYYEFKYLR DQQLSDIARS
PELFLRMLKA EEEGLIEVKV RFENFENFRK RLYPNIESDN YSELADSWNR LRREAVDLAL
GKLERVINRS VKENIRQECE NHVAKECREA FSQRLDQAPY KPKGMILGTV PRVLALSTGT
GIIGRAPIHW AYVEEDGRVL ENGKFTDLSL GDKDRGIADG KDLEALVELV NRRRPDVIGV
SGMSPETRRL YKLLTEIVDA KDLRGALYTD DRDEEVSDRL EVVIVNDEVA RLYQNSDRAK
KDHPSFAPLT HYCVGLAKYL QSPLKEYASL GRDIVSIQFK PGQQLVAQEL LLKQLETALV
DMVNLVGVDI NEAVSDPATA NLLPYVCGLG PRKAAHLLKI VNMTGGVVNS RFSLLGVGVQ
YPAMGVKVWN NSASFLYIDY ESADADSDPL DNTRVHPEDY DIARKMAADA LELDEEDIKA
ETDENGPGAI VRKLFREDAQ DRVNDLILEE YAEQLEKNLN QRKRATLETI RAELQQPYEE
LRKHFVFLST DDIFTMLTGE TAQTLAEGMV VPISIKSIRD DHIEGKLDCG VDALVGESEM
TDRYDIPVRA IYSLHQTVPA KVMFLNRKTF TCNVSLREEQ VSRPSRPAAD RAHAGEWDYR
QEEQDREALE AKTQDGGRTM RVIKHPLFRP FNSTQAVEFL GSQSRGDVVI RPSSKGPDHL
AVTWKVADGI FQHIDVLELD KENEFSVGRT LKVGGRFTYS DLDDLIFNHV KAMAKKVDEM
MLHEKYQEGS KDSTYQWLET YTKANPRRSA YAFCIDPKHA GYFFLCFKAG EHAQVHSWPV
KVIPQGYELQ RNPYPDMRAL CNGFKLLFTN MQSGKRR