SPT6_SCHPO
ID SPT6_SCHPO Reviewed; 1365 AA.
AC Q09915; Q9P7T3;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 29-AUG-2001, sequence version 2.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Transcription elongation factor spt6;
DE AltName: Full=Chromatin elongation factor spt6;
GN Name=spt6; ORFNames=SPAC1F7.01c, SPAC694.07c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-137; SER-143 AND SER-454, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=18257517; DOI=10.1021/pr7006335;
RA Wilson-Grady J.T., Villen J., Gygi S.P.;
RT "Phosphoproteome analysis of fission yeast.";
RL J. Proteome Res. 7:1088-1097(2008).
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:0000305}.
CC -!- SIMILARITY: Belongs to the SPT6 family. {ECO:0000305}.
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DR EMBL; CU329670; CAB71845.1; -; Genomic_DNA.
DR PIR; T38095; S62573.
DR PIR; T50252; T50252.
DR RefSeq; NP_594487.2; NM_001019916.2.
DR AlphaFoldDB; Q09915; -.
DR SMR; Q09915; -.
DR BioGRID; 278102; 13.
DR IntAct; Q09915; 1.
DR STRING; 4896.SPAC1F7.01c.1; -.
DR iPTMnet; Q09915; -.
DR MaxQB; Q09915; -.
DR PaxDb; Q09915; -.
DR PRIDE; Q09915; -.
DR EnsemblFungi; SPAC1F7.01c.1; SPAC1F7.01c.1:pep; SPAC1F7.01c.
DR GeneID; 2541605; -.
DR KEGG; spo:SPAC1F7.01c; -.
DR PomBase; SPAC1F7.01c; spt6.
DR VEuPathDB; FungiDB:SPAC1F7.01c; -.
DR eggNOG; KOG1856; Eukaryota.
DR HOGENOM; CLU_001680_0_1_1; -.
DR InParanoid; Q09915; -.
DR OMA; LCNGFKT; -.
DR PhylomeDB; Q09915; -.
DR Reactome; R-SPO-674695; RNA Polymerase II Pre-transcription Events.
DR Reactome; R-SPO-75955; RNA Polymerase II Transcription Elongation.
DR PRO; PR:Q09915; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0005721; C:pericentric heterochromatin; IDA:PomBase.
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:0140673; P:co-transcriptional chromatin reassembly; IMP:PomBase.
DR GO; GO:0042789; P:mRNA transcription by RNA polymerase II; IMP:PomBase.
DR GO; GO:0034728; P:nucleosome organization; IBA:GO_Central.
DR GO; GO:0032968; P:positive regulation of transcription elongation from RNA polymerase II promoter; IBA:GO_Central.
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; 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; 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; 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 SMART; SM00732; YqgFc; 1.
DR SUPFAM; SSF47781; SSF47781; 1.
DR SUPFAM; SSF50249; SSF50249; 1.
DR SUPFAM; SSF53098; SSF53098; 1.
DR SUPFAM; SSF55550; SSF55550; 1.
DR PROSITE; PS50126; S1; 1.
PE 1: Evidence at protein level;
KW Nucleus; Phosphoprotein; Reference proteome; SH2 domain; Transcription;
KW Transcription regulation.
FT CHAIN 1..1365
FT /note="Transcription elongation factor spt6"
FT /id="PRO_0000116440"
FT DOMAIN 1050..1118
FT /note="S1 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00180"
FT DOMAIN 1167..1262
FT /note="SH2"
FT REGION 1..165
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 181..202
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1124..1146
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..18
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 43..60
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 139..155
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 137
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 143
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 454
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 1365 AA; 157210 MW; 0E6DB64E25667A92 CRC64;
MSENEVVGSP TTNGDKNEDG YPAENGEGTN VDDNNNEEEK DGIPLDNDND ENDSSEESAT
DEEAERQVRE GFIVEDEEDE VPQEIRRKKK RKKHAESTAD QDMLDEEDLE LVMENTGQGS
RFSKLRRLKR GRDQEETLEN IFSEEEEEEE NEVDDEAPNR TQGHRAGVID EFADFIEQDE
FEDEERQEEK YETGPPIESV RPEALGISDD DYIQIYEVFG DGTDYAFALE DEDAEDELEE
SVSLKTIFEP SELKDKMLTE EDEIIRITDE PERMQLYMKR NIDCSEDEFR EQVAWIIDYL
LKNRRDIDAE LYEPFQTAVR YVVHFFIRDS LEVPFIWQHR RDYIVHNNRE RNTITPLLSQ
NDLWNIFFLC TKFWSLHSKK QDILKLYSDL GINDDLVVPF CEAASSLDAI DDLNDYIHFT
YSEQIRDRAL LMGTGLRRPQ GSKYSFFEKF RKSSLYNLVK EFGMSAKDFS FNVAQGARLR
FVEDNTLSPE ELSRTYVTNE LSSPEQVLQK ARRVLAEEII HDPQFRKSFR DKLYNAGVVT
VLATQKGVRK IGSEHPYYEF KYLKRKPLGS FELEPILFLK MLKAEEEGLI QLSIEFEDPD
DVFKGLLELF VSDNFSENAM QWNAQRELVL KEVFKRFSAL APDAIRETLR SRYLDELGMR
CRNQLFSRLD QAPYEPSTKN FDRGTIPSVL AVSNGKGESS DAIICVFVDD VGEPTDSLKL
ADLRDLANQA MFAEFVEKVK PDVIGVSGMS VSAHKIRQHV QDSLTSHEPV DLIMVNDEVA
RLYQNSTRAV DEFPTLPTIS CYCVALARYV QNPLFEYAAM GRDLMSLSFD PWQHLLPPDV
LWKYLETALV DISSLVGIDI NEAVTNKYEA NILPYIAGLG PRKADYVLKK IAATGGRIDN
RSDLISKQIM SRKVFINCSS FFIIPNDEYP NMDILDSTRI HNEDYELARK MASDALELDE
EDIEELETNR GVVYHLLEEN ETGKLDELVL EEYADQLERE FHQKKRNTLE KIRLELKDPY
GEQRNVFHKL TPSEIFLMLT GENPEELQAD AIVPVNVRRV TNRFVAVKLD CGIDGNIKAD
EVSDDFIPPP QLLQVGQTVE GVIISLDEAN FMVDLSLRNS VLQSANSKRQ TSSHRTSYWD
TEAEKRDTER MQAETQAEQR VARVIKHPLF KDLNASQAEA YLSKMQVGDL VIRPSSKGSD
HIVVTWKVAE GSYQHIDVLE LEKENEFTIG QKLLVKGRFE KMTYQYSDLD ELIVLHIKAI
AKKIDEMCIH DKFRKGTQAE TEKWLESYSE ANPKRSCYAF CFDHQHPGYF ILCFKASVNS
PVTAWPVKVI PNAFFLQGNV YGDMTALCNG FKLLYAARTK NFRRM
