SPT6_DEBHA
ID SPT6_DEBHA Reviewed; 1439 AA.
AC Q6BVE1;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 25-MAY-2022, entry version 103.
DE RecName: Full=Transcription elongation factor SPT6;
DE AltName: Full=Chromatin elongation factor SPT6;
GN Name=SPT6; OrderedLocusNames=DEHA2C03344g;
OS Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990
OS / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX NCBI_TaxID=284592;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC 2968;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
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; CR382135; CAG85873.1; -; Genomic_DNA.
DR RefSeq; XP_457828.1; XM_457828.1.
DR AlphaFoldDB; Q6BVE1; -.
DR SMR; Q6BVE1; -.
DR STRING; 4959.XP_457828.1; -.
DR PRIDE; Q6BVE1; -.
DR EnsemblFungi; CAG85873; CAG85873; DEHA2C03344g.
DR GeneID; 2900117; -.
DR KEGG; dha:DEHA2C03344g; -.
DR VEuPathDB; FungiDB:DEHA2C03344g; -.
DR eggNOG; KOG1856; Eukaryota.
DR HOGENOM; CLU_001680_0_1_1; -.
DR InParanoid; Q6BVE1; -.
DR OMA; LCNGFKT; -.
DR OrthoDB; 56990at2759; -.
DR Proteomes; UP000000599; Chromosome C.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0006139; P:nucleobase-containing compound metabolic process; IEA:InterPro.
DR GO; GO:0032968; P:positive regulation of transcription elongation from RNA polymerase II promoter; IEA:InterPro.
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; 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; 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 SMART; SM00252; SH2; 1.
DR SUPFAM; SSF47781; SSF47781; 2.
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..1439
FT /note="Transcription elongation factor SPT6"
FT /id="PRO_0000238574"
FT DOMAIN 1229..1323
FT /note="SH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00191"
FT REGION 1..206
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1417..1439
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..19
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 20..42
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 43..63
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 110..131
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 150..164
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 165..180
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 181..206
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1420..1439
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1439 AA; 165357 MW; A13AF34BE516E104 CRC64;
MAKEDIEEER EIRNDASENS SDEEGDDVLD SSEEDDDDDD EEAIKRVREG FIVDDDEDES
QKRKRRKHKK RKREERTNDD ENNALDQDDL ELLMENSGAR PQPSSNKLKR LKRAYTEDTE
GAEEEEIGAK SGRGGLTDIF SDEDNNEEER ADLGETRVDD DRNILDEFED FIEEDEYSDE
DEERQRKLTQ QRERAQKKGP RLDTSKLSNV DRESLQQLFE VFGNGAEYEW ALEAQEMEDE
GNGENLEPTS LDEVFEHAEL KERMLTEEDN LIRIVDIPER FQKYRANLNY IDLEGEELKS
EQGWVANILF MEKQGSFSGF LEEPFKEAVS KVVEFISKDV YEVPFIWTHR RDFLLYSEEI
KNEDGSVTNS VHKLLFEDDL WRIFQLDIEY HSLYEKRVNI EKLIESLNLD DDLVKDVKSL
ETMVAIQDLQ DYINFTYSTE IRKLYDDKET EGIDANITKK HSKYAIFERI KSNVLYDAVN
AFGISAKEFG ENVQDQSSKK FEVPYRIHAT DDHIESPEDL IERLCEDDEV LFKDPKNALN
AVRKTFAEEI FHNPKIRHEV RTTFKDFASI RVAVTEKGKA IDNHSPYADI KYAINRSPAD
LVRNPDVLLR MLEAEAAGLV VVKVETKDYD SWFQCIFNCL KSDGSSEIFE KWNKEREFVL
NMAFKRLTSM VSMNTKEDLR RECERLIASE VRRRFLARID QAPFTPFGFD KGTKPNVLAL
SFGKGDFDSA VIGAFLRESG KVDEFFKSED NPIRDRESED KFSGQLKEFF DKNLRNQKPD
VIVVSGYNAI SKKLFDSVKS FVETNNVTAN TEELTDVQNP PLIQVIWGQS ETATLFQNSE
RARIEFSDKP TLAKYCVGLA RYVQSPLLEY LSLGEGILSL TFFEHQKLIS TDLVMEAIES
AYVDIINMVG VEINEAIRDP YIAQLLPYVA GLGPRKASGL LRNINSKLGS TLANRSDLIE
NELSTANIFI NCSSFLNIPY DEGLSMRDSS VELLDATRIH PEDYDLARKM AADALDLDEE
DMAHVEEQGG IIYQLMQDGV NKVDDLNLTA YGKELESKFG KKKYATLQSI KEELVNNFEE
IRRSFHILES HEVFHMLTGE TTESFTRNTI VPVTVNKVGQ NFRDFENSKI KFAKVTTSSF
IQGNIEEASI PQGIDLAQGQ VVQAVVLDAY YDSFTASFSL LEADIQKGAA PKFHKDPLKW
NFEAEQADKQ KEMAKERAQL AKTRNIQHPL FHNFSYKQAE EFLAPQAVGD CVLRPSSKGP
NYLTVTWKVS NNLFQHLSIQ ENTQGMGKEY IVEHKKYADL DQLIFQHVQA IAKHVDEMCR
HPKFREGTMS EVNEWLESYT KANPKNSAYV FCFDHKAPGW FLLLFKVNVN TPITTWHVKT
ECDGYRLKGF SYPSMLRLCN GFKQTFKSYV KGIADRSRST KPAPVNNQAQ ASTYGGYGY
